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Copper-transporting ATPase 1 (EC 3.6.3.54) (Copper pump 1) (Menkes disease-associated protein)

 ATP7A_HUMAN             Reviewed;        1500 AA.
Q04656; B1AT72; O00227; O00745; Q9BYY8;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
10-FEB-2009, sequence version 3.
22-NOV-2017, entry version 207.
RecName: Full=Copper-transporting ATPase 1;
EC=3.6.3.54;
AltName: Full=Copper pump 1;
AltName: Full=Menkes disease-associated protein;
Name=ATP7A; Synonyms=MC1, MNK;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND VARIANT THR-669.
TISSUE=Fibroblast;
PubMed=8490659; DOI=10.1038/ng0193-7;
Vulpe C.D., Levinson B., Whitney S., Packman S., Gitschier J.;
"Isolation of a candidate gene for Menkes disease and evidence that it
encodes a copper-transporting ATPase.";
Nat. Genet. 3:7-13(1993).
[2]
ERRATUM.
Vulpe C.D., Levinson B., Whitney S., Packman S., Gitschier J.;
Nat. Genet. 3:273-273(1993).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 4), AND VARIANT THR-669.
PubMed=7607665; DOI=10.1016/0888-7543(95)80160-N;
Tuemer Z., Vural B., Toennesen T., Chelly J., Monaco A.P., Horn N.;
"Characterization of the exon structure of the Menkes disease gene
using vectorette PCR.";
Genomics 26:437-442(1995).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
TISSUE=Fibroblast;
PubMed=9693104; DOI=10.1042/bj3340071;
Reddy M.C., Harris E.D.;
"Multiple transcripts coding for the menkes gene: evidence for
alternative splicing of Menkes mRNA.";
Biochem. J. 334:71-77(1998).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
TISSUE=Colon carcinoma, and Fibroblast;
PubMed=10079814;
Harris E.D., Reddy M.C., Qian Y., Tiffany-Castiglioni E., Majumdar S.,
Nelson J.;
"Multiple forms of the Menkes Cu-ATPase.";
Adv. Exp. Med. Biol. 448:39-51(1999).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1447 (ISOFORM 4).
PubMed=7490081; DOI=10.1006/geno.1995.1175;
Dierick H.A., Ambrosini L., Spencer J., Glover T.W., Mercer J.F.B.;
"Molecular structure of the Menkes disease gene (ATP7A).";
Genomics 28:462-469(1995).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-626 (ISOFORM 4).
TISSUE=Kidney;
PubMed=8490646; DOI=10.1038/ng0193-14;
Chelly J., Tuemer Z., Toennesen T., Petterson A., Ishikawa-Brush Y.,
Tommerup N., Horn N., Monaco A.P.;
"Isolation of a candidate gene for Menkes disease that encodes a
potential heavy metal binding protein.";
Nat. Genet. 3:14-19(1993).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 12-529 (ISOFORM 4).
TISSUE=Endothelial cell;
PubMed=8490647; DOI=10.1038/ng0193-20;
Mercer J.F.B., Livingston J., Hall B., Paynter J.A., Begy C.,
Chandrasekharappa S., Lockhart P., Grimes A., Bhave M., Siemieniak D.,
Glover T.W.;
"Isolation of a partial candidate gene for Menkes disease by
positional cloning.";
Nat. Genet. 3:20-25(1993).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 213-437.
PubMed=11214319; DOI=10.1038/35054550;
Murphy W.J., Eizirik E., Johnson W.E., Zhang Y.-P., Ryder O.A.,
O'Brien S.J.;
"Molecular phylogenetics and the origins of placental mammals.";
Nature 409:614-618(2001).
[12]
ALTERNATIVE SPLICING (ISOFORM 5), AND SUBCELLULAR LOCATION.
PubMed=9467005; DOI=10.1093/hmg/7.3.465;
Qi M., Byers P.H.;
"Constitutive skipping of alternatively spliced exon 10 in the ATP7A
gene abolishes Golgi localization of the menkes protein and produces
the occipital horn syndrome.";
Hum. Mol. Genet. 7:465-469(1998).
[13]
ALTERNATIVE SPLICING (ISOFORM 6).
TISSUE=Neuroblastoma;
PubMed=10970802; DOI=10.1042/bj3500855;
Reddy M.C., Majumdar S., Harris E.D.;
"Evidence for a Menkes-like protein with a nuclear targeting
sequence.";
Biochem. J. 350:855-863(2000).
[14]
SUBCELLULAR LOCATION.
PubMed=9147644; DOI=10.1093/hmg/6.3.409;
Dierick H.A., Adam A.N., Escara-Wilke J.F., Glover T.W.;
"Immunocytochemical localization of the Menkes copper transport
protein (ATP7A) to the trans-Golgi network.";
Hum. Mol. Genet. 6:409-416(1997).
[15]
SUBCELLULAR LOCATION, AND MUTAGENESIS OF LEUCINE RESIDUES.
PubMed=10484781; DOI=10.1093/hmg/8.11.2107;
Petris M.J., Mercer J.F.B.;
"The Menkes protein (ATP7A; MNK) cycles via the plasma membrane both
in basal and elevated extracellular copper using a C-terminal di-
leucine endocytic signal.";
Hum. Mol. Genet. 8:2107-2115(1999).
[16]
INTERACTION WITH PDZD11.
PubMed=16051599; DOI=10.1074/jbc.M505889200;
Stephenson S.E., Dubach D., Lim C.M., Mercer J.F., La Fontaine S.;
"A single PDZ domain protein interacts with the Menkes copper ATPase,
ATP7A. A new protein implicated in copper homeostasis.";
J. Biol. Chem. 280:33270-33279(2005).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[19]
INTERACTION WITH ATOX1 AND COMMD1, CHARACTERIZATION OF VARIANT OHS
SER-1304, AND CHARACTERIZATION OF VARIANTS MNKD ARG-873; ARG-1000 AND
ASP-1362.
PubMed=21667063; DOI=10.1007/s00018-011-0743-1;
Vonk W.I., de Bie P., Wichers C.G., van den Berghe P.V.,
van der Plaats R., Berger R., Wijmenga C., Klomp L.W.,
van de Sluis B.;
"The copper-transporting capacity of ATP7A mutants associated with
Menkes disease is ameliorated by COMMD1 as a result of improved
protein expression.";
Cell. Mol. Life Sci. 69:149-163(2012).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-152; SER-270; THR-327;
SER-339; SER-357; SER-1460; SER-1463; SER-1466; SER-1469 AND SER-1473,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1430 AND SER-1432, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[22]
STRUCTURE BY NMR OF 375-446.
PubMed=9437429; DOI=10.1038/nsb0198-47;
Gitschier J., Moffat B., Reilly D., Wood W.I., Fairbrother W.J.;
"Solution structure of the fourth metal-binding domain from the Menkes
copper-transporting ATPase.";
Nat. Struct. Biol. 5:47-54(1998).
[23]
REVIEW, AND VARIANTS MNKD.
PubMed=10079817;
Tuemer Z., Moeller L.B., Horn N.;
"Mutation spectrum of ATP7A, the gene defective in Menkes disease.";
Adv. Exp. Med. Biol. 448:83-95(1999).
[24]
VARIANT LEU-767, AND VARIANT MNKD ARG-1302.
PubMed=7977350;
Das S., Levinson B., Whitney S., Vulpe C., Packman S., Gitschier J.;
"Diverse mutations in patients with Menkes disease often lead to exon
skipping.";
Am. J. Hum. Genet. 55:883-889(1994).
[25]
VARIANTS MNKD PRO-629; ARG-727; PRO-1006 AND ASP-1019.
PubMed=8981948;
Tuemer Z., Lund C., Tolshave J., Vural B., Toennesen T., Horn N.;
"Identification of point mutations in 41 unrelated patients affected
with Menkes disease.";
Am. J. Hum. Genet. 60:63-71(1997).
[26]
VARIANT OHS LEU-637.
PubMed=9246006; DOI=10.1086/516852;
Ronce N., Moizard M.P., Robb L., Toutain A., Villard L., Moraine C.;
"A C2055T transition in exon 8 of the ATP7A gene is associated with
exon skipping in an occipital horn syndrome family.";
Am. J. Hum. Genet. 61:233-238(1997).
[27]
VARIANT MNKD VAL-1362.
PubMed=10401004; DOI=10.1093/hmg/8.8.1547;
Ambrosini L., Mercer J.F.B.;
"Defective copper-induced trafficking and localization of the Menkes
protein in patients with mild and copper-treated classical Menkes
disease.";
Hum. Mol. Genet. 8:1547-1555(1999).
[28]
VARIANT MNKD ARG-873.
PubMed=10319589; DOI=10.1007/s100380050144;
Ogawa A., Yamamoto S., Takayanagi M., Kogo T., Kanazawa M., Kohno Y.;
"Identification of three novel mutations in the MNK gene in three
unrelated Japanese patients with classical Menkes disease.";
J. Hum. Genet. 44:206-209(1999).
[29]
INVOLVEMENT IN OCCIPITAL HORN SYNDROME.
PubMed=11431706; DOI=10.1086/321290;
Dagenais S.L., Adam A.N., Innis J.W., Glover T.W.;
"A novel frameshift mutation in exon 23 of ATP7A (MNK) results in
occipital horn syndrome and not in Menkes disease.";
Am. J. Hum. Genet. 69:420-427(2001).
[30]
VARIANTS MNKD ARG-1344 AND PHE-1345.
PubMed=11241493;
DOI=10.1002/1096-8628(2001)9999:9999<::AID-AJMG1167>3.0.CO;2-R;
Gu Y.-H., Kodama H., Murata Y., Mochizuki D., Yanagawa Y.,
Ushijima H., Shiba T., Lee C.-C.;
"ATP7A gene mutations in 16 patients with Menkes disease and a patient
with occipital horn syndrome.";
Am. J. Med. Genet. 99:217-222(2001).
[31]
VARIANTS MNKD ARG-706; ASP-1118 AND ARG-1255.
PubMed=11350187; DOI=10.1006/mgme.2001.3169;
Hahn S., Cho K., Ryu K., Kim J., Pai K., Kim M., Park H., Yoo O.;
"Identification of four novel mutations in classical Menkes disease
and successful prenatal DNA diagnosis.";
Mol. Genet. Metab. 73:86-90(2001).
[32]
VARIANTS MNKD HIS-844; ARG-853; VAL-860; ARG-876; GLU-876; ARG-924;
ARG-1000; VAL-1007; ASP-1015; GLY-1044; PRO-1100; GLU-1282; GLU-1300;
VAL-1302; LYS-1304; ALA-1305; ARG-1315; VAL-1325; ARG-1369 AND
PHE-1397.
PubMed=15981243; DOI=10.1002/humu.20190;
Moeller L.B., Bukrinsky J.T., Moelgaard A., Paulsen M., Lund C.,
Tuemer Z., Larsen S., Horn N.;
"Identification and analysis of 21 novel disease-causing amino acid
substitutions in the conserved part of ATP7A.";
Hum. Mutat. 26:84-93(2005).
[33]
VARIANT OHS SER-1304, AND CHARACTERIZATION OF VARIANT OHS SER-1304.
PubMed=17108763; DOI=10.1097/01.gim.0000245578.94312.1e;
Tang J., Robertson S., Lem K.E., Godwin S.C., Kaler S.G.;
"Functional copper transport explains neurologic sparing in occipital
horn syndrome.";
Genet. Med. 8:711-718(2006).
[34]
VARIANTS DSMAX3 ILE-994 AND SER-1386, AND CHARACTERIZATION OF VARIANTS
DSMAX3 ILE-994 AND SER-1386.
PubMed=20170900; DOI=10.1016/j.ajhg.2010.01.027;
Kennerson M.L., Nicholson G.A., Kaler S.G., Kowalski B.,
Mercer J.F.B., Tang J., Llanos R.M., Chu S., Takata R.I.,
Speck-Martins C.E., Baets J., Almeida-Souza L., Fischer D.,
Timmerman V., Taylor P.E., Scherer S.S., Ferguson T.A., Bird T.D.,
De Jonghe P., Feely S.M.E., Shy M.E., Garbern J.Y.;
"Missense mutations in the copper transporter gene ATP7A cause X-
linked distal hereditary motor neuropathy.";
Am. J. Hum. Genet. 86:343-352(2010).
[35]
VARIANT MNKD ILE-1048.
PubMed=22992316; DOI=10.1186/1471-2431-12-150;
De Leon-Garcia G., Santana A., Villegas-Sepulveda N.,
Perez-Gonzalez C., Henrriquez-Esquiroz J.M., De Leon-Garcia C.,
Wong C., Baeza I.;
"The T1048I mutation in ATP7A gene causes an unusual Menkes disease
presentation.";
BMC Pediatr. 12:150-150(2012).
-!- FUNCTION: May supply copper to copper-requiring proteins within
the secretory pathway, when localized in the trans-Golgi network.
Under conditions of elevated extracellular copper, it relocalized
to the plasma membrane where it functions in the efflux of copper
from cells.
-!- CATALYTIC ACTIVITY: ATP + H(2)O + Cu(+)(Side 1) = ADP + phosphate
+ Cu(+)(Side 2).
-!- SUBUNIT: Monomer. Interacts with PDZD11. Interacts with ATOX1 and
COMMD1 (PubMed:21667063). {ECO:0000269|PubMed:16051599,
ECO:0000269|PubMed:21667063}.
-!- INTERACTION:
Q5EBL8:PDZD11; NbExp=4; IntAct=EBI-7706409, EBI-1644207;
-!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
membrane {ECO:0000269|PubMed:10484781, ECO:0000269|PubMed:9147644,
ECO:0000269|PubMed:9467005}; Multi-pass membrane protein
{ECO:0000255}. Cell membrane {ECO:0000269|PubMed:10484781,
ECO:0000269|PubMed:9147644}; Multi-pass membrane protein
{ECO:0000255}. Note=Cycles constitutively between the trans-Golgi
network (TGN) and the plasma membrane (PubMed:9147644).
Predominantly found in the TGN and relocalized to the plasma
membrane in response to elevated copper levels.
{ECO:0000269|PubMed:9147644}.
-!- SUBCELLULAR LOCATION: Isoform 3: Cytoplasm, cytosol {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Isoform 5: Endoplasmic reticulum
{ECO:0000269|PubMed:9467005}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=4;
IsoId=Q04656-1; Sequence=Displayed;
Name=1;
IsoId=Q04656-2; Sequence=VSP_000419;
Name=2;
IsoId=Q04656-3; Sequence=VSP_000420;
Name=3; Synonyms=2-16;
IsoId=Q04656-4; Sequence=VSP_000424;
Note=Lacks 6 transmembrane regions and 5 heavy-metal-associated
(HMA) domains.;
Name=5;
IsoId=Q04656-5; Sequence=VSP_000425;
Note=Lacks the transmembrane domains 3 and 4. Expressed at a low
level in several tissues of normal individuals and is the only
isoform found in patients with OHS.;
Name=6; Synonyms=NML45;
IsoId=Q04656-6; Sequence=VSP_000421, VSP_000422, VSP_000423;
Note=Lacks all transmembrane regions and 5
heavy-metal-associated (HMA) domains, but has a putative nuclear
localization signal attached at the N-terminus.;
-!- TISSUE SPECIFICITY: Found in most tissues except liver. Isoform 3
is widely expressed including in liver cell lines. Isoform 1 is
expressed in fibroblasts, choriocarcinoma, colon carcinoma and
neuroblastoma cell lines. Isoform 2 is expressed in fibroblasts,
colon carcinoma and neuroblastoma cell lines.
-!- DOMAIN: The C-terminal di-leucine, 1487-Leu-Leu-1488, is an
endocytic targeting signal which functions in retrieving recycling
from the plasma membrane to the TGN. Mutation of the di-leucine
signal results in the accumulation of the protein in the plasma
membrane.
-!- DISEASE: Menkes disease (MNKD) [MIM:309400]: An X-linked recessive
disorder of copper metabolism characterized by generalized copper
deficiency. MNKD results in progressive neurodegeneration and
connective-tissue disturbances: focal cerebral and cerebellar
degeneration, early growth retardation, peculiar hair,
hypopigmentation, cutis laxa, vascular complications and death in
early childhood. The clinical features result from the dysfunction
of several copper-dependent enzymes. A mild form of the disease
has been described, in which cerebellar ataxia and moderate
developmental delay predominate. {ECO:0000269|PubMed:10079817,
ECO:0000269|PubMed:10319589, ECO:0000269|PubMed:10401004,
ECO:0000269|PubMed:11241493, ECO:0000269|PubMed:11350187,
ECO:0000269|PubMed:15981243, ECO:0000269|PubMed:21667063,
ECO:0000269|PubMed:22992316, ECO:0000269|PubMed:7977350,
ECO:0000269|PubMed:8981948}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Occipital horn syndrome (OHS) [MIM:304150]: An X-linked
recessive disorder of copper metabolism. Common features are
unusual facial appearance, skeletal abnormalities, chronic
diarrhea and genitourinary defects. The skeletal abnormalities
include occipital horns, short, broad clavicles, deformed radii,
ulnae and humeri, narrowing of the rib cage, undercalcified long
bones with thin cortical walls and coxa valga.
{ECO:0000269|PubMed:11431706, ECO:0000269|PubMed:17108763,
ECO:0000269|PubMed:21667063, ECO:0000269|PubMed:9246006}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Distal spinal muscular atrophy, X-linked, 3 (DSMAX3)
[MIM:300489]: A neuromuscular disorder. Distal spinal muscular
atrophy, also known as distal hereditary motor neuronopathy,
represents a heterogeneous group of neuromuscular disorders caused
by selective degeneration of motor neurons in the anterior horn of
the spinal cord, without sensory deficit in the posterior horn.
The overall clinical picture consists of a classical distal
muscular atrophy syndrome in the legs without clinical sensory
loss. The disease starts with weakness and wasting of distal
muscles of the anterior tibial and peroneal compartments of the
legs. Later on, weakness and atrophy may expand to the proximal
muscles of the lower limbs and/or to the distal upper limbs.
{ECO:0000269|PubMed:20170900}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC
3.A.3) family. Type IB subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=Protein Spotlight; Note=Heavy metal - Issue 79
of February 2007;
URL="https://web.expasy.org/spotlight/back_issues/079";
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EMBL; L06133; AAA35580.1; -; mRNA.
EMBL; X82336; CAB94714.1; -; Genomic_DNA.
EMBL; X82337; CAB94714.1; JOINED; Genomic_DNA.
EMBL; X82338; CAB94714.1; JOINED; Genomic_DNA.
EMBL; X82339; CAB94714.1; JOINED; Genomic_DNA.
EMBL; X82340; CAB94714.1; JOINED; Genomic_DNA.
EMBL; X82341; CAB94714.1; JOINED; Genomic_DNA.
EMBL; X82342; CAB94714.1; JOINED; Genomic_DNA.
EMBL; X82343; CAB94714.1; JOINED; Genomic_DNA.
EMBL; X82344; CAB94714.1; JOINED; Genomic_DNA.
EMBL; X82345; CAB94714.1; JOINED; Genomic_DNA.
EMBL; X82346; CAB94714.1; JOINED; Genomic_DNA.
EMBL; X82347; CAB94714.1; JOINED; Genomic_DNA.
EMBL; X82348; CAB94714.1; JOINED; Genomic_DNA.
EMBL; X82349; CAB94714.1; JOINED; Genomic_DNA.
EMBL; X82350; CAB94714.1; JOINED; Genomic_DNA.
EMBL; X82351; CAB94714.1; JOINED; Genomic_DNA.
EMBL; X82352; CAB94714.1; JOINED; Genomic_DNA.
EMBL; X82353; CAB94714.1; JOINED; Genomic_DNA.
EMBL; X82354; CAB94714.1; JOINED; Genomic_DNA.
EMBL; X82355; CAB94714.1; JOINED; Genomic_DNA.
EMBL; X82356; CAB94714.1; JOINED; Genomic_DNA.
EMBL; AL645821; CAI42806.1; -; Genomic_DNA.
EMBL; CH471104; EAW98605.1; -; Genomic_DNA.
EMBL; U27381; AAA96010.1; -; Genomic_DNA.
EMBL; U27361; AAA96010.1; JOINED; Genomic_DNA.
EMBL; U27362; AAA96010.1; JOINED; Genomic_DNA.
EMBL; U27363; AAA96010.1; JOINED; Genomic_DNA.
EMBL; U27365; AAA96010.1; JOINED; Genomic_DNA.
EMBL; U27366; AAA96010.1; JOINED; Genomic_DNA.
EMBL; U27367; AAA96010.1; JOINED; Genomic_DNA.
EMBL; U27368; AAA96010.1; JOINED; Genomic_DNA.
EMBL; U27369; AAA96010.1; JOINED; Genomic_DNA.
EMBL; U27370; AAA96010.1; JOINED; Genomic_DNA.
EMBL; U27371; AAA96010.1; JOINED; Genomic_DNA.
EMBL; U27372; AAA96010.1; JOINED; Genomic_DNA.
EMBL; U27373; AAA96010.1; JOINED; Genomic_DNA.
EMBL; U27374; AAA96010.1; JOINED; Genomic_DNA.
EMBL; U27375; AAA96010.1; JOINED; Genomic_DNA.
EMBL; U27376; AAA96010.1; JOINED; Genomic_DNA.
EMBL; U27377; AAA96010.1; JOINED; Genomic_DNA.
EMBL; U27378; AAA96010.1; JOINED; Genomic_DNA.
EMBL; U27379; AAA96010.1; JOINED; Genomic_DNA.
EMBL; U27380; AAA96010.1; JOINED; Genomic_DNA.
EMBL; X69208; CAA49145.1; -; mRNA.
EMBL; L06476; AAA16974.1; -; mRNA.
EMBL; Z94801; CAB08162.2; -; Genomic_DNA.
EMBL; Z94753; CAB08160.1; -; Genomic_DNA.
EMBL; AY011418; AAG47452.1; -; Genomic_DNA.
CCDS; CCDS35339.1; -. [Q04656-1]
CCDS; CCDS75997.1; -. [Q04656-5]
PIR; S36149; S36149.
RefSeq; NP_000043.4; NM_000052.6.
RefSeq; NP_001269153.1; NM_001282224.1.
UniGene; Hs.496414; -.
UniGene; Hs.733232; -.
PDB; 1AW0; NMR; -; A=375-446.
PDB; 1KVI; NMR; -; A=1-79.
PDB; 1KVJ; NMR; -; A=1-79.
PDB; 1Q8L; NMR; -; A=164-246.
PDB; 1S6O; NMR; -; A=169-240.
PDB; 1S6U; NMR; -; A=169-240.
PDB; 1Y3J; NMR; -; A=486-558.
PDB; 1Y3K; NMR; -; A=486-558.
PDB; 1YJR; NMR; -; A=562-633.
PDB; 1YJT; NMR; -; A=562-633.
PDB; 1YJU; NMR; -; A=562-633.
PDB; 1YJV; NMR; -; A=562-633.
PDB; 2AW0; NMR; -; A=375-446.
PDB; 2G9O; NMR; -; A=275-352.
PDB; 2GA7; NMR; -; A=275-352.
PDB; 2K1R; NMR; -; A=5-77.
PDB; 2KIJ; NMR; -; A=806-924.
PDB; 2KMV; NMR; -; A=1051-1231.
PDB; 2KMX; NMR; -; A=1051-1231.
PDB; 3CJK; X-ray; 1.80 A; B=7-77.
PDB; 5T7L; X-ray; 2.83 A; B=7-77.
PDBsum; 1AW0; -.
PDBsum; 1KVI; -.
PDBsum; 1KVJ; -.
PDBsum; 1Q8L; -.
PDBsum; 1S6O; -.
PDBsum; 1S6U; -.
PDBsum; 1Y3J; -.
PDBsum; 1Y3K; -.
PDBsum; 1YJR; -.
PDBsum; 1YJT; -.
PDBsum; 1YJU; -.
PDBsum; 1YJV; -.
PDBsum; 2AW0; -.
PDBsum; 2G9O; -.
PDBsum; 2GA7; -.
PDBsum; 2K1R; -.
PDBsum; 2KIJ; -.
PDBsum; 2KMV; -.
PDBsum; 2KMX; -.
PDBsum; 3CJK; -.
PDBsum; 5T7L; -.
DisProt; DP00282; -.
ProteinModelPortal; Q04656; -.
SMR; Q04656; -.
BioGrid; 107020; 38.
ELM; Q04656; -.
IntAct; Q04656; 4.
MINT; MINT-106053; -.
STRING; 9606.ENSP00000345728; -.
DrugBank; DB00958; Carboplatin.
DrugBank; DB00515; Cisplatin.
DrugBank; DB00526; Oxaliplatin.
TCDB; 3.A.3.5.6; the p-type atpase (p-atpase) superfamily.
iPTMnet; Q04656; -.
PhosphoSitePlus; Q04656; -.
DMDM; 223590241; -.
MaxQB; Q04656; -.
PaxDb; Q04656; -.
PeptideAtlas; Q04656; -.
PRIDE; Q04656; -.
DNASU; 538; -.
Ensembl; ENST00000341514; ENSP00000345728; ENSG00000165240.
Ensembl; ENST00000343533; ENSP00000343026; ENSG00000165240.
Ensembl; ENST00000350425; ENSP00000343678; ENSG00000165240.
GeneID; 538; -.
KEGG; hsa:538; -.
UCSC; uc004ecx.6; human. [Q04656-1]
CTD; 538; -.
DisGeNET; 538; -.
EuPathDB; HostDB:ENSG00000165240.17; -.
GeneCards; ATP7A; -.
GeneReviews; ATP7A; -.
HGNC; HGNC:869; ATP7A.
HPA; HPA012887; -.
HPA; HPA048107; -.
MalaCards; ATP7A; -.
MIM; 300011; gene.
MIM; 300489; phenotype.
MIM; 304150; phenotype.
MIM; 309400; phenotype.
neXtProt; NX_Q04656; -.
Orphanet; 565; Menkes disease.
Orphanet; 198; Occipital horn syndrome.
Orphanet; 139557; X-linked distal spinal muscular atrophy.
PharmGKB; PA72; -.
eggNOG; KOG0207; Eukaryota.
eggNOG; COG2217; LUCA.
HOGENOM; HOG000250397; -.
HOVERGEN; HBG050616; -.
InParanoid; Q04656; -.
KO; K17686; -.
OrthoDB; EOG091G022E; -.
PhylomeDB; Q04656; -.
TreeFam; TF300460; -.
BRENDA; 3.6.3.4; 2681.
Reactome; R-HSA-3299685; Detoxification of Reactive Oxygen Species.
Reactome; R-HSA-6803544; Ion influx/efflux at host-pathogen interface.
Reactome; R-HSA-936837; Ion transport by P-type ATPases.
SABIO-RK; Q04656; -.
ChiTaRS; ATP7A; human.
EvolutionaryTrace; Q04656; -.
GeneWiki; ATP7A; -.
GenomeRNAi; 538; -.
PRO; PR:Q04656; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000165240; -.
CleanEx; HS_ATP7A; -.
Genevisible; Q04656; HS.
GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
GO; GO:0031526; C:brush border membrane; IEA:Ensembl.
GO; GO:0031252; C:cell leading edge; IEA:Ensembl.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005770; C:late endosome; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0005902; C:microvillus; IEA:Ensembl.
GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0043204; C:perikaryon; IEA:Ensembl.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0030141; C:secretory granule; IEA:Ensembl.
GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
GO; GO:0030140; C:trans-Golgi network transport vesicle; IMP:HGNC.
GO; GO:0005524; F:ATP binding; TAS:HGNC.
GO; GO:0051087; F:chaperone binding; IEA:Ensembl.
GO; GO:0005507; F:copper ion binding; IDA:UniProtKB.
GO; GO:0005375; F:copper ion transmembrane transporter activity; ISS:UniProtKB.
GO; GO:0032767; F:copper-dependent protein binding; IPI:UniProtKB.
GO; GO:0004008; F:copper-exporting ATPase activity; ISS:UniProtKB.
GO; GO:1903136; F:cuprous ion binding; IMP:CAFA.
GO; GO:0048365; F:Rac GTPase binding; IEA:Ensembl.
GO; GO:0016532; F:superoxide dismutase copper chaperone activity; ISS:UniProtKB.
GO; GO:0019730; P:antimicrobial humoral response; TAS:Reactome.
GO; GO:0001568; P:blood vessel development; ISS:UniProtKB.
GO; GO:0001974; P:blood vessel remodeling; ISS:UniProtKB.
GO; GO:0051216; P:cartilage development; ISS:UniProtKB.
GO; GO:0006584; P:catecholamine metabolic process; ISS:UniProtKB.
GO; GO:0006878; P:cellular copper ion homeostasis; IMP:UniProtKB.
GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
GO; GO:0071236; P:cellular response to antibiotic; IEA:Ensembl.
GO; GO:0071276; P:cellular response to cadmium ion; IEA:Ensembl.
GO; GO:0071279; P:cellular response to cobalt ion; IEA:Ensembl.
GO; GO:0071280; P:cellular response to copper ion; IEA:Ensembl.
GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
GO; GO:0071281; P:cellular response to iron ion; IEA:Ensembl.
GO; GO:0071284; P:cellular response to lead ion; IEA:Ensembl.
GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IEA:Ensembl.
GO; GO:0021954; P:central nervous system neuron development; ISS:UniProtKB.
GO; GO:0021702; P:cerebellar Purkinje cell differentiation; ISS:UniProtKB.
GO; GO:0030199; P:collagen fibril organization; ISS:UniProtKB.
GO; GO:0060003; P:copper ion export; ISS:UniProtKB.
GO; GO:0015677; P:copper ion import; ISS:UniProtKB.
GO; GO:0006825; P:copper ion transport; IMP:UniProtKB.
GO; GO:0010273; P:detoxification of copper ion; ISS:UniProtKB.
GO; GO:0042417; P:dopamine metabolic process; ISS:UniProtKB.
GO; GO:0048251; P:elastic fiber assembly; ISS:UniProtKB.
GO; GO:0051542; P:elastin biosynthetic process; ISS:UniProtKB.
GO; GO:0042414; P:epinephrine metabolic process; ISS:UniProtKB.
GO; GO:0030198; P:extracellular matrix organization; ISS:UniProtKB.
GO; GO:0031069; P:hair follicle morphogenesis; ISS:UniProtKB.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
GO; GO:0007595; P:lactation; IEA:Ensembl.
GO; GO:0001889; P:liver development; IEA:Ensembl.
GO; GO:0007626; P:locomotory behavior; ISS:UniProtKB.
GO; GO:0048286; P:lung alveolus development; ISS:UniProtKB.
GO; GO:0007005; P:mitochondrion organization; ISS:UniProtKB.
GO; GO:0043086; P:negative regulation of catalytic activity; ISS:UniProtKB.
GO; GO:0034760; P:negative regulation of iron ion transmembrane transport; IEA:Ensembl.
GO; GO:0048812; P:neuron projection morphogenesis; ISS:UniProtKB.
GO; GO:0042415; P:norepinephrine metabolic process; ISS:UniProtKB.
GO; GO:0018205; P:peptidyl-lysine modification; ISS:UniProtKB.
GO; GO:0043473; P:pigmentation; ISS:UniProtKB.
GO; GO:0015679; P:plasma membrane copper ion transport; IEA:Ensembl.
GO; GO:0043085; P:positive regulation of catalytic activity; ISS:UniProtKB.
GO; GO:0045793; P:positive regulation of cell size; IEA:Ensembl.
GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IEA:Ensembl.
GO; GO:0010592; P:positive regulation of lamellipodium assembly; IEA:Ensembl.
GO; GO:0051353; P:positive regulation of oxidoreductase activity; IDA:UniProtKB.
GO; GO:1903036; P:positive regulation of response to wounding; IEA:Ensembl.
GO; GO:1904754; P:positive regulation of vascular associated smooth muscle cell migration; IEA:Ensembl.
GO; GO:0021860; P:pyramidal neuron development; ISS:UniProtKB.
GO; GO:1904959; P:regulation of cytochrome-c oxidase activity; IEA:Ensembl.
GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl.
GO; GO:0002082; P:regulation of oxidative phosphorylation; ISS:UniProtKB.
GO; GO:0019430; P:removal of superoxide radicals; ISS:UniProtKB.
GO; GO:0010041; P:response to iron(III) ion; IEA:Ensembl.
GO; GO:0010042; P:response to manganese ion; IEA:Ensembl.
GO; GO:0010043; P:response to zinc ion; IEA:Ensembl.
GO; GO:0042428; P:serotonin metabolic process; ISS:UniProtKB.
GO; GO:0043588; P:skin development; ISS:UniProtKB.
GO; GO:0042093; P:T-helper cell differentiation; ISS:UniProtKB.
GO; GO:0006568; P:tryptophan metabolic process; ISS:UniProtKB.
CDD; cd00371; HMA; 6.
Gene3D; 3.40.1110.10; -; 1.
Gene3D; 3.40.50.1000; -; 1.
InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
InterPro; IPR018303; ATPase_P-typ_P_site.
InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
InterPro; IPR036412; HAD-like_sf.
InterPro; IPR023214; HAD_sf.
InterPro; IPR017969; Heavy-metal-associated_CS.
InterPro; IPR006122; HMA_Cu_ion-bd.
InterPro; IPR006121; HMA_dom.
InterPro; IPR036163; HMA_dom_sf.
InterPro; IPR027256; P-typ_ATPase_IB.
InterPro; IPR001757; P_typ_ATPase.
Pfam; PF00403; HMA; 6.
SUPFAM; SSF55008; SSF55008; 6.
SUPFAM; SSF56784; SSF56784; 2.
SUPFAM; SSF81653; SSF81653; 1.
SUPFAM; SSF81660; SSF81660; 2.
SUPFAM; SSF81665; SSF81665; 3.
TIGRFAMs; TIGR01525; ATPase-IB_hvy; 1.
TIGRFAMs; TIGR01494; ATPase_P-type; 2.
TIGRFAMs; TIGR00003; TIGR00003; 6.
PROSITE; PS00154; ATPASE_E1_E2; 1.
PROSITE; PS01047; HMA_1; 6.
PROSITE; PS50846; HMA_2; 6.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Cell membrane;
Complete proteome; Copper; Copper transport; Cytoplasm;
Disease mutation; Endoplasmic reticulum; Glycoprotein;
Golgi apparatus; Hydrolase; Ion transport; Magnesium; Membrane;
Metal-binding; Neurodegeneration; Nucleotide-binding; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 1500 Copper-transporting ATPase 1.
/FTId=PRO_0000046311.
TOPO_DOM 1 653 Cytoplasmic. {ECO:0000255}.
TRANSMEM 654 675 Helical. {ECO:0000255}.
TOPO_DOM 676 714 Extracellular. {ECO:0000255}.
TRANSMEM 715 734 Helical. {ECO:0000255}.
TOPO_DOM 735 741 Cytoplasmic. {ECO:0000255}.
TRANSMEM 742 762 Helical. {ECO:0000255}.
TOPO_DOM 763 781 Extracellular. {ECO:0000255}.
TRANSMEM 782 802 Helical. {ECO:0000255}.
TOPO_DOM 803 936 Cytoplasmic. {ECO:0000255}.
TRANSMEM 937 959 Helical. {ECO:0000255}.
TOPO_DOM 960 989 Extracellular. {ECO:0000255}.
TRANSMEM 990 1011 Helical. {ECO:0000255}.
TOPO_DOM 1012 1356 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1357 1374 Helical. {ECO:0000255}.
TOPO_DOM 1375 1385 Extracellular. {ECO:0000255}.
TRANSMEM 1386 1405 Helical. {ECO:0000255}.
TOPO_DOM 1406 1500 Cytoplasmic. {ECO:0000255}.
DOMAIN 9 75 HMA 1. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
DOMAIN 172 238 HMA 2. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
DOMAIN 278 344 HMA 3. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
DOMAIN 378 444 HMA 4. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
DOMAIN 489 555 HMA 5. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
DOMAIN 565 631 HMA 6. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
REGION 1486 1500 PDZD11-binding.
MOTIF 1487 1488 Endocytosis signal.
COMPBIAS 355 362 Poly-Ser.
ACT_SITE 1044 1044 4-aspartylphosphate intermediate.
{ECO:0000250}.
METAL 1301 1301 Magnesium. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 1305 1305 Magnesium. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
MOD_RES 152 152 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 270 270 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 327 327 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 339 339 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 353 353 Phosphoserine.
{ECO:0000250|UniProtKB:P70705}.
MOD_RES 357 357 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 362 362 Phosphoserine.
{ECO:0000250|UniProtKB:Q64430}.
MOD_RES 1212 1212 Phosphothreonine.
{ECO:0000250|UniProtKB:P70705}.
MOD_RES 1430 1430 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1432 1432 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1460 1460 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1463 1463 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1466 1466 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1469 1469 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1473 1473 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1476 1476 Phosphoserine.
{ECO:0000250|UniProtKB:Q64430}.
MOD_RES 1486 1486 Phosphoserine.
{ECO:0000250|UniProtKB:Q64430}.
CARBOHYD 686 686 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 975 975 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 1 M -> MRKLSIRKRDNNLLK (in isoform 1).
{ECO:0000303|PubMed:10079814}.
/FTId=VSP_000419.
VAR_SEQ 1 1 M -> MRKLSIRKRDNNLLKPSSASSLGIAVSLGRPVLSRS
SSGTVNLLEEVGLHIRDTAFSSTKLLEAISTVSAQVEELAV
HNECY (in isoform 2).
{ECO:0000303|PubMed:10079814}.
/FTId=VSP_000420.
VAR_SEQ 1 1 M -> MRKLSIRKRDNNLLKECNEEIK (in isoform
6). {ECO:0000305}.
/FTId=VSP_000421.
VAR_SEQ 42 1038 Missing (in isoform 3).
{ECO:0000303|PubMed:10079814,
ECO:0000303|PubMed:9693104}.
/FTId=VSP_000424.
VAR_SEQ 53 81 DPKLQTPKTLQEAIDDMGFDAVIHNPDPL -> AHWFGFAA
LDGICSNGCFICFCSTFFSSL (in isoform 6).
{ECO:0000305}.
/FTId=VSP_000422.
VAR_SEQ 82 1499 Missing (in isoform 6). {ECO:0000305}.
/FTId=VSP_000423.
VAR_SEQ 725 802 Missing (in isoform 5). {ECO:0000305}.
/FTId=VSP_000425.
VARIANT 629 629 A -> P (in MNKD).
{ECO:0000269|PubMed:8981948}.
/FTId=VAR_000699.
VARIANT 637 637 S -> L (in OHS; dbSNP:rs28936068).
{ECO:0000269|PubMed:9246006}.
/FTId=VAR_009999.
VARIANT 669 669 I -> T (in dbSNP:rs2234935).
{ECO:0000269|PubMed:7607665,
ECO:0000269|PubMed:8490659}.
/FTId=VAR_016119.
VARIANT 703 703 R -> H (in dbSNP:rs2234936).
/FTId=VAR_016120.
VARIANT 706 706 L -> R (in MNKD).
{ECO:0000269|PubMed:11350187}.
/FTId=VAR_023261.
VARIANT 727 727 G -> R (in MNKD).
{ECO:0000269|PubMed:8981948}.
/FTId=VAR_000700.
VARIANT 767 767 V -> L (in dbSNP:rs2227291).
{ECO:0000269|PubMed:7977350}.
/FTId=VAR_010000.
VARIANT 844 844 R -> H (in MNKD).
{ECO:0000269|PubMed:15981243}.
/FTId=VAR_023262.
VARIANT 853 853 G -> R (in MNKD).
{ECO:0000269|PubMed:15981243}.
/FTId=VAR_023263.
VARIANT 860 860 G -> V (in MNKD).
{ECO:0000269|PubMed:15981243}.
/FTId=VAR_023264.
VARIANT 873 873 L -> R (in MNKD; increased protein
abundance; does not affect interaction
with ATOX1; does not affect interaction
with COMMD1; increased localization at
the plasma membrane; does not cycle back
to TGN under conditions of copper
depletion). {ECO:0000269|PubMed:10319589,
ECO:0000269|PubMed:21667063}.
/FTId=VAR_010001.
VARIANT 876 876 G -> E (in MNKD).
{ECO:0000269|PubMed:15981243}.
/FTId=VAR_010002.
VARIANT 876 876 G -> R (in MNKD).
{ECO:0000269|PubMed:15981243}.
/FTId=VAR_023265.
VARIANT 924 924 Q -> R (in MNKD).
{ECO:0000269|PubMed:15981243}.
/FTId=VAR_023266.
VARIANT 994 994 T -> I (in DSMAX3; demonstrates impaired
intracellular trafficking compared to
control with some of the mutant protein
remaining in the Golgi apparatus after
exposure to copper).
{ECO:0000269|PubMed:20170900}.
/FTId=VAR_063882.
VARIANT 1000 1000 C -> R (in MNKD; decreased protein
abundance; increased protein degradation;
does not affect interaction with ATOX1;
does not affect interaction with COMMD1;
subcellular location restricted to TGN;
does not localizes to the plasma membrane
in response to elevated copper levels).
{ECO:0000269|PubMed:15981243,
ECO:0000269|PubMed:21667063}.
/FTId=VAR_010003.
VARIANT 1006 1006 L -> P (in MNKD).
{ECO:0000269|PubMed:8981948}.
/FTId=VAR_000701.
VARIANT 1007 1007 A -> V (in MNKD).
{ECO:0000269|PubMed:15981243}.
/FTId=VAR_023267.
VARIANT 1015 1015 G -> D (in MNKD).
{ECO:0000269|PubMed:15981243}.
/FTId=VAR_023268.
VARIANT 1019 1019 G -> D (in MNKD).
{ECO:0000269|PubMed:8981948}.
/FTId=VAR_000702.
VARIANT 1044 1044 D -> G (in MNKD).
{ECO:0000269|PubMed:15981243}.
/FTId=VAR_023269.
VARIANT 1048 1048 T -> I (in MNKD).
{ECO:0000269|PubMed:22992316}.
/FTId=VAR_068831.
VARIANT 1100 1100 L -> P (in MNKD).
{ECO:0000269|PubMed:15981243}.
/FTId=VAR_023270.
VARIANT 1118 1118 G -> D (in MNKD).
{ECO:0000269|PubMed:11350187}.
/FTId=VAR_023271.
VARIANT 1255 1255 G -> R (in MNKD).
{ECO:0000269|PubMed:11350187}.
/FTId=VAR_023272.
VARIANT 1282 1282 K -> E (in MNKD).
{ECO:0000269|PubMed:15981243}.
/FTId=VAR_023273.
VARIANT 1300 1300 G -> E (in MNKD).
{ECO:0000269|PubMed:15981243}.
/FTId=VAR_010004.
VARIANT 1302 1302 G -> R (in MNKD).
{ECO:0000269|PubMed:7977350}.
/FTId=VAR_010005.
VARIANT 1302 1302 G -> V (in MNKD).
{ECO:0000269|PubMed:15981243}.
/FTId=VAR_010006.
VARIANT 1304 1304 N -> K (in MNKD).
{ECO:0000269|PubMed:15981243}.
/FTId=VAR_023274.
VARIANT 1304 1304 N -> S (in OHS; has approximately 33%
residual copper transport; increased
protein abundance; increased localization
at the plasma membrane; does not cycle
back to TGN under conditions of copper
depletion; does not affect interaction
with ATOX1; does not affect interaction
with COMMD1).
{ECO:0000269|PubMed:17108763,
ECO:0000269|PubMed:21667063}.
/FTId=VAR_063883.
VARIANT 1305 1305 D -> A (in MNKD).
{ECO:0000269|PubMed:15981243}.
/FTId=VAR_010007.
VARIANT 1315 1315 G -> R (in MNKD).
{ECO:0000269|PubMed:15981243}.
/FTId=VAR_023275.
VARIANT 1325 1325 A -> V (in MNKD).
{ECO:0000269|PubMed:15981243}.
/FTId=VAR_023276.
VARIANT 1344 1344 S -> R (in MNKD).
{ECO:0000269|PubMed:11241493}.
/FTId=VAR_023277.
VARIANT 1345 1345 I -> F (in MNKD).
{ECO:0000269|PubMed:11241493}.
/FTId=VAR_023278.
VARIANT 1362 1362 A -> V (in MNKD; decreased protein
abundance; increased protein degradation;
does not affect interaction with ATOX1;
does not affect interaction with COMMD1;
subcellular location restricted to TGN;
does not localizes to the plasma membrane
in response to elevated copper levels).
{ECO:0000269|PubMed:10401004,
ECO:0000269|PubMed:21667063}.
/FTId=VAR_010008.
VARIANT 1369 1369 G -> R (in MNKD).
{ECO:0000269|PubMed:15981243}.
/FTId=VAR_023279.
VARIANT 1386 1386 P -> S (in DSMAX3; demonstrates impaired
intracellular trafficking compared to
control with some mutant protein
remaining in the Golgi apparatus after
exposure to copper).
{ECO:0000269|PubMed:20170900}.
/FTId=VAR_063884.
VARIANT 1397 1397 S -> F (in MNKD).
{ECO:0000269|PubMed:15981243}.
/FTId=VAR_023280.
VARIANT 1464 1464 I -> V (in dbSNP:rs2234938).
/FTId=VAR_016121.
MUTAGEN 1487 1488 LL->AA: Loss of relocalization to the
trans-Golgi.
{ECO:0000269|PubMed:10484781}.
CONFLICT 10 10 V -> A (in Ref. 4; no nucleotide entry).
{ECO:0000305}.
CONFLICT 36 36 V -> E (in Ref. 10; AAA16974).
{ECO:0000305}.
CONFLICT 336 336 E -> V (in Ref. 1; AAA35580 and 8;
AAA96010). {ECO:0000305}.
CONFLICT 446 446 D -> G (in Ref. 6; CAB08162).
{ECO:0000305}.
CONFLICT 624 624 S -> G (in Ref. 6; CAB08162).
{ECO:0000305}.
CONFLICT 725 725 F -> V (in Ref. 6; CAB08162).
{ECO:0000305}.
CONFLICT 833 833 S -> R (in Ref. 6; CAB08162).
{ECO:0000305}.
CONFLICT 1099 1099 E -> K (in Ref. 4; no nucleotide entry).
{ECO:0000305}.
CONFLICT 1171 1171 N -> S (in Ref. 6; CAB08162).
{ECO:0000305}.
CONFLICT 1178 1178 Y -> C (in Ref. 4; no nucleotide entry).
{ECO:0000305}.
CONFLICT 1178 1178 Y -> H (in Ref. 1; AAA35580, 3; CAB94714
and 8; AAA96010). {ECO:0000305}.
CONFLICT 1220 1220 D -> G (in Ref. 6; CAB08162).
{ECO:0000305}.
CONFLICT 1295 1295 R -> W (in Ref. 4; no nucleotide entry).
{ECO:0000305}.
CONFLICT 1313 1313 N -> D (in Ref. 4; no nucleotide entry).
{ECO:0000305}.
CONFLICT 1336 1336 N -> D (in Ref. 6; CAB08162).
{ECO:0000305}.
CONFLICT 1350 1350 E -> K (in Ref. 1; AAA35580, 3; CAB94714
and 8; AAA96010). {ECO:0000305}.
CONFLICT 1376 1376 V -> M (in Ref. 6; CAB08162).
{ECO:0000305}.
CONFLICT 1396 1396 S -> P (in Ref. 4; no nucleotide entry).
{ECO:0000305}.
CONFLICT 1409 1409 L -> R (in Ref. 6; CAB08160).
{ECO:0000305}.
CONFLICT 1455 1455 R -> W (in Ref. 4; no nucleotide entry).
{ECO:0000305}.
TURN 4 6 {ECO:0000244|PDB:1KVI}.
STRAND 8 14 {ECO:0000244|PDB:3CJK}.
HELIX 20 31 {ECO:0000244|PDB:3CJK}.
STRAND 33 35 {ECO:0000244|PDB:1KVI}.
STRAND 36 42 {ECO:0000244|PDB:3CJK}.
TURN 43 46 {ECO:0000244|PDB:3CJK}.
STRAND 47 52 {ECO:0000244|PDB:3CJK}.
TURN 54 56 {ECO:0000244|PDB:3CJK}.
HELIX 59 68 {ECO:0000244|PDB:3CJK}.
STRAND 73 77 {ECO:0000244|PDB:3CJK}.
STRAND 165 169 {ECO:0000244|PDB:1Q8L}.
STRAND 171 177 {ECO:0000244|PDB:1Q8L}.
TURN 180 182 {ECO:0000244|PDB:1Q8L}.
HELIX 187 194 {ECO:0000244|PDB:1Q8L}.
STRAND 199 204 {ECO:0000244|PDB:1Q8L}.
TURN 207 209 {ECO:0000244|PDB:1Q8L}.
STRAND 210 215 {ECO:0000244|PDB:1Q8L}.
TURN 217 219 {ECO:0000244|PDB:1S6O}.
HELIX 222 231 {ECO:0000244|PDB:1Q8L}.
STRAND 236 238 {ECO:0000244|PDB:1S6U}.
TURN 242 244 {ECO:0000244|PDB:1Q8L}.
STRAND 277 285 {ECO:0000244|PDB:2G9O}.
HELIX 288 299 {ECO:0000244|PDB:2G9O}.
STRAND 305 311 {ECO:0000244|PDB:2G9O}.
TURN 312 315 {ECO:0000244|PDB:2G9O}.
STRAND 316 321 {ECO:0000244|PDB:2G9O}.
STRAND 324 326 {ECO:0000244|PDB:2GA7}.
HELIX 329 336 {ECO:0000244|PDB:2G9O}.
TURN 340 342 {ECO:0000244|PDB:2G9O}.
STRAND 344 346 {ECO:0000244|PDB:2G9O}.
STRAND 377 384 {ECO:0000244|PDB:1AW0}.
HELIX 388 400 {ECO:0000244|PDB:1AW0}.
STRAND 408 411 {ECO:0000244|PDB:1AW0}.
TURN 412 415 {ECO:0000244|PDB:1AW0}.
STRAND 416 421 {ECO:0000244|PDB:1AW0}.
TURN 423 425 {ECO:0000244|PDB:1AW0}.
HELIX 428 438 {ECO:0000244|PDB:1AW0}.
STRAND 441 446 {ECO:0000244|PDB:1AW0}.
STRAND 488 495 {ECO:0000244|PDB:1Y3J}.
HELIX 497 499 {ECO:0000244|PDB:1Y3J}.
HELIX 502 510 {ECO:0000244|PDB:1Y3J}.
STRAND 513 518 {ECO:0000244|PDB:1Y3J}.
TURN 523 526 {ECO:0000244|PDB:1Y3J}.
STRAND 527 532 {ECO:0000244|PDB:1Y3J}.
TURN 534 536 {ECO:0000244|PDB:1Y3J}.
HELIX 539 549 {ECO:0000244|PDB:1Y3J}.
STRAND 553 557 {ECO:0000244|PDB:1Y3J}.
STRAND 566 571 {ECO:0000244|PDB:1YJR}.
TURN 575 577 {ECO:0000244|PDB:1YJR}.
HELIX 578 586 {ECO:0000244|PDB:1YJR}.
STRAND 592 598 {ECO:0000244|PDB:1YJR}.
TURN 599 602 {ECO:0000244|PDB:1YJR}.
STRAND 603 608 {ECO:0000244|PDB:1YJR}.
TURN 610 613 {ECO:0000244|PDB:1YJR}.
HELIX 614 626 {ECO:0000244|PDB:1YJR}.
STRAND 628 633 {ECO:0000244|PDB:1YJR}.
HELIX 808 814 {ECO:0000244|PDB:2KIJ}.
STRAND 818 824 {ECO:0000244|PDB:2KIJ}.
STRAND 826 828 {ECO:0000244|PDB:2KIJ}.
STRAND 833 838 {ECO:0000244|PDB:2KIJ}.
TURN 839 841 {ECO:0000244|PDB:2KIJ}.
STRAND 847 849 {ECO:0000244|PDB:2KIJ}.
STRAND 860 862 {ECO:0000244|PDB:2KIJ}.
STRAND 868 870 {ECO:0000244|PDB:2KIJ}.
TURN 872 875 {ECO:0000244|PDB:2KIJ}.
STRAND 887 889 {ECO:0000244|PDB:2KIJ}.
STRAND 894 898 {ECO:0000244|PDB:2KIJ}.
STRAND 901 904 {ECO:0000244|PDB:2KIJ}.
TURN 908 910 {ECO:0000244|PDB:2KIJ}.
HELIX 912 919 {ECO:0000244|PDB:2KIJ}.
TURN 920 923 {ECO:0000244|PDB:2KIJ}.
STRAND 1055 1061 {ECO:0000244|PDB:2KMV}.
TURN 1065 1067 {ECO:0000244|PDB:2KMV}.
HELIX 1070 1079 {ECO:0000244|PDB:2KMV}.
HELIX 1080 1082 {ECO:0000244|PDB:2KMV}.
STRAND 1083 1085 {ECO:0000244|PDB:2KMV}.
HELIX 1087 1100 {ECO:0000244|PDB:2KMV}.
STRAND 1112 1114 {ECO:0000244|PDB:2KMV}.
TURN 1115 1117 {ECO:0000244|PDB:2KMV}.
STRAND 1118 1123 {ECO:0000244|PDB:2KMV}.
HELIX 1127 1129 {ECO:0000244|PDB:2KMV}.
TURN 1135 1139 {ECO:0000244|PDB:2KMX}.
TURN 1150 1153 {ECO:0000244|PDB:2KMV}.
STRAND 1161 1166 {ECO:0000244|PDB:2KMX}.
TURN 1167 1171 {ECO:0000244|PDB:2KMV}.
HELIX 1172 1174 {ECO:0000244|PDB:2KMV}.
STRAND 1178 1183 {ECO:0000244|PDB:2KMV}.
HELIX 1185 1191 {ECO:0000244|PDB:2KMV}.
HELIX 1197 1208 {ECO:0000244|PDB:2KMV}.
STRAND 1212 1218 {ECO:0000244|PDB:2KMV}.
STRAND 1221 1229 {ECO:0000244|PDB:2KMV}.
SEQUENCE 1500 AA; 163374 MW; CF8FF9EA061D463B CRC64;
MDPSMGVNSV TISVEGMTCN SCVWTIEQQI GKVNGVHHIK VSLEEKNATI IYDPKLQTPK
TLQEAIDDMG FDAVIHNPDP LPVLTDTLFL TVTASLTLPW DHIQSTLLKT KGVTDIKIYP
QKRTVAVTII PSIVNANQIK ELVPELSLDT GTLEKKSGAC EDHSMAQAGE VVLKMKVEGM
TCHSCTSTIE GKIGKLQGVQ RIKVSLDNQE ATIVYQPHLI SVEEMKKQIE AMGFPAFVKK
QPKYLKLGAI DVERLKNTPV KSSEGSQQRS PSYTNDSTAT FIIDGMHCKS CVSNIESTLS
ALQYVSSIVV SLENRSAIVK YNASSVTPES LRKAIEAVSP GLYRVSITSE VESTSNSPSS
SSLQKIPLNV VSQPLTQETV INIDGMTCNS CVQSIEGVIS KKPGVKSIRV SLANSNGTVE
YDPLLTSPET LRGAIEDMGF DATLSDTNEP LVVIAQPSSE MPLLTSTNEF YTKGMTPVQD
KEEGKNSSKC YIQVTGMTCA SCVANIERNL RREEGIYSIL VALMAGKAEV RYNPAVIQPP
MIAEFIRELG FGATVIENAD EGDGVLELVV RGMTCASCVH KIESSLTKHR GILYCSVALA
TNKAHIKYDP EIIGPRDIIH TIESLGFEAS LVKKDRSASH LDHKREIRQW RRSFLVSLFF
CIPVMGLMIY MMVMDHHFAT LHHNQNMSKE EMINLHSSMF LERQILPGLS VMNLLSFLLC
VPVQFFGGWY FYIQAYKALK HKTANMDVLI VLATTIAFAY SLIILLVAMY ERAKVNPITF
FDTPPMLFVF IALGRWLEHI AKGKTSEALA KLISLQATEA TIVTLDSDNI LLSEEQVDVE
LVQRGDIIKV VPGGKFPVDG RVIEGHSMVD ESLITGEAMP VAKKPGSTVI AGSINQNGSL
LICATHVGAD TTLSQIVKLV EEAQTSKAPI QQFADKLSGY FVPFIVFVSI ATLLVWIVIG
FLNFEIVETY FPGYNRSISR TETIIRFAFQ ASITVLCIAC PCSLGLATPT AVMVGTGVGA
QNGILIKGGE PLEMAHKVKV VVFDKTGTIT HGTPVVNQVK VLTESNRISH HKILAIVGTA
ESNSEHPLGT AITKYCKQEL DTETLGTCID FQVVPGCGIS CKVTNIEGLL HKNNWNIEDN
NIKNASLVQI DASNEQSSTS SSMIIDAQIS NALNAQQYKV LIGNREWMIR NGLVINNDVN
DFMTEHERKG RTAVLVAVDD ELCGLIAIAD TVKPEAELAI HILKSMGLEV VLMTGDNSKT
ARSIASQVGI TKVFAEVLPS HKVAKVKQLQ EEGKRVAMVG DGINDSPALA MANVGIAIGT
GTDVAIEAAD VVLIRNDLLD VVASIDLSRE TVKRIRINFV FALIYNLVGI PIAAGVFMPI
GLVLQPWMGS AAMAASSVSV VLSSLFLKLY RKPTYESYEL PARSQIGQKS PSEISVHVGI
DDTSRNSPKL GLLDRIVNYS RASINSLLSD KRSLNSVVTS EPDKHSLLVG DFREDDDTAL


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