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Probable phospholipid-transporting ATPase IH (EC 3.6.3.1) (ATPase IS) (ATPase class VI type 11A) (P4-ATPase flippase complex alpha subunit ATP11A)

 AT11A_HUMAN             Reviewed;        1134 AA.
P98196; Q5VXT2;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
24-JAN-2006, sequence version 3.
05-DEC-2018, entry version 166.
RecName: Full=Probable phospholipid-transporting ATPase IH;
EC=7.6.2.1;
AltName: Full=ATPase IS;
AltName: Full=ATPase class VI type 11A;
AltName: Full=P4-ATPase flippase complex alpha subunit ATP11A;
Name=ATP11A; Synonyms=ATPIH, ATPIS, KIAA1021;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057823; DOI=10.1038/nature02379;
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
"The DNA sequence and analysis of human chromosome 13.";
Nature 428:522-528(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 33-1134, AND VARIANT
VAL-317.
TISSUE=Brain;
PubMed=10470851; DOI=10.1093/dnares/6.3.197;
Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N.,
Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XIV.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 6:197-205(1999).
[3]
SEQUENCE REVISION.
Ohara O., Nagase T., Kikuno R.;
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
[4]
FUNCTION.
PubMed=15860663; DOI=10.1182/blood-2004-09-3655;
Zhang B., Groffen J., Heisterkamp N.;
"Resistance to farnesyltransferase inhibitors in Bcr/Abl-positive
lymphoblastic leukemia by increased expression of a novel ABC
transporter homolog ATP11a.";
Blood 106:1355-1361(2005).
[5]
INTERACTION WITH TMEM30A, AND SUBCELLULAR LOCATION.
PubMed=21914794; DOI=10.1074/jbc.M111.281006;
Takatsu H., Baba K., Shima T., Umino H., Kato U., Umeda M.,
Nakayama K., Shin H.W.;
"ATP9B, a P4-ATPase (a putative aminophospholipid translocase),
localizes to the trans-Golgi network in a CDC50 protein-independent
manner.";
J. Biol. Chem. 286:38159-38167(2011).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-738, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
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).
-!- FUNCTION: Catalytic component of a P4-ATPase flippase complex
which catalyzes the hydrolysis of ATP coupled to the transport of
aminophospholipids from the outer to the inner leaflet of various
membranes and ensures the maintenance of asymmetric distribution
of phospholipids. Phospholipid translocation seems also to be
implicated in vesicle formation and in uptake of lipid signaling
molecules (Probable). May be involved in the uptake of
farnesyltransferase inhibitor drugs, such as lonafarnib.
{ECO:0000269|PubMed:15860663, ECO:0000305}.
-!- CATALYTIC ACTIVITY:
Reaction=a phospholipid derivative(in) + ATP + H2O = a
phospholipid derivative(out) + ADP + H(+) + phosphate;
Xref=Rhea:RHEA:14989, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:16247, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
ChEBI:CHEBI:456216; EC=7.6.2.1;
-!- SUBUNIT: Component of a P4-ATPase flippase complex which consists
of a catalytic alpha subunit and an accessory beta subunit
(Probable). Interacts with beta subunit TMEM30A.
{ECO:0000269|PubMed:21914794, ECO:0000305}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21914794};
Multi-pass membrane protein {ECO:0000269|PubMed:21914794}. Early
endosome {ECO:0000269|PubMed:21914794}. Recycling endosome
{ECO:0000269|PubMed:21914794}. Endoplasmic reticulum
{ECO:0000269|PubMed:21914794}. Note=Exit from the endoplasmic
reticulum requires the presence of TMEM30A, but not TMEM30B. In
the presence of TMEM30A, predominantly located in the plasma
membrane.
-!- MISCELLANEOUS: Overexpression of ATP11A confers resistance to
lonafarnib.
-!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC
3.A.3) family. Type IV subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AL356740; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL139384; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL356752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AB028944; BAA82973.2; -; mRNA.
CCDS; CCDS32011.1; -.
RefSeq; NP_056020.2; NM_015205.2.
RefSeq; NP_115565.3; NM_032189.3.
RefSeq; XP_005268362.1; XM_005268305.4.
RefSeq; XP_005268363.1; XM_005268306.4.
RefSeq; XP_016875981.1; XM_017020492.1.
UniGene; Hs.29189; -.
ProteinModelPortal; P98196; -.
BioGrid; 116854; 5.
STRING; 9606.ENSP00000283558; -.
TCDB; 3.A.3.8.17; the p-type atpase (p-atpase) superfamily.
iPTMnet; P98196; -.
PhosphoSitePlus; P98196; -.
SwissPalm; P98196; -.
BioMuta; ATP11A; -.
DMDM; 85700404; -.
EPD; P98196; -.
MaxQB; P98196; -.
PaxDb; P98196; -.
PeptideAtlas; P98196; -.
PRIDE; P98196; -.
ProteomicsDB; 57826; -.
DNASU; 23250; -.
Ensembl; ENST00000375645; ENSP00000364796; ENSG00000068650.
Ensembl; ENST00000487903; ENSP00000420387; ENSG00000068650.
GeneID; 23250; -.
KEGG; hsa:23250; -.
UCSC; uc001vsi.4; human.
CTD; 23250; -.
DisGeNET; 23250; -.
EuPathDB; HostDB:ENSG00000068650.18; -.
GeneCards; ATP11A; -.
HGNC; HGNC:13552; ATP11A.
HPA; HPA035583; -.
HPA; HPA035584; -.
MalaCards; ATP11A; -.
MIM; 605868; gene.
neXtProt; NX_P98196; -.
OpenTargets; ENSG00000068650; -.
Orphanet; 2032; Idiopathic pulmonary fibrosis.
PharmGKB; PA25101; -.
eggNOG; KOG0206; Eukaryota.
eggNOG; COG0474; LUCA.
GeneTree; ENSGT00940000157849; -.
HOGENOM; HOG000202528; -.
HOVERGEN; HBG050601; -.
InParanoid; P98196; -.
KO; K01530; -.
PhylomeDB; P98196; -.
TreeFam; TF326897; -.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-936837; Ion transport by P-type ATPases.
ChiTaRS; ATP11A; human.
GenomeRNAi; 23250; -.
PRO; PR:P98196; -.
Proteomes; UP000005640; Chromosome 13.
Bgee; ENSG00000068650; Expressed in 207 organ(s), highest expression level in visceral pleura.
CleanEx; HS_ATP11A; -.
ExpressionAtlas; P98196; baseline and differential.
Genevisible; P98196; HS.
GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0004012; F:phospholipid-translocating ATPase activity; IBA:GO_Central.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0045332; P:phospholipid translocation; IBA:GO_Central.
Gene3D; 3.40.1110.10; -; 1.
Gene3D; 3.40.50.1000; -; 1.
InterPro; IPR030361; ATP11A.
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; IPR006539; P-type_ATPase_IV.
InterPro; IPR032631; P-type_ATPase_N.
InterPro; IPR001757; P_typ_ATPase.
InterPro; IPR032630; P_typ_ATPase_c.
PANTHER; PTHR24092; PTHR24092; 1.
PANTHER; PTHR24092:SF33; PTHR24092:SF33; 1.
Pfam; PF16212; PhoLip_ATPase_C; 1.
Pfam; PF16209; PhoLip_ATPase_N; 1.
SUPFAM; SSF56784; SSF56784; 1.
SUPFAM; SSF81653; SSF81653; 1.
SUPFAM; SSF81660; SSF81660; 1.
SUPFAM; SSF81665; SSF81665; 1.
TIGRFAMs; TIGR01652; ATPase-Plipid; 1.
TIGRFAMs; TIGR01494; ATPase_P-type; 3.
PROSITE; PS00154; ATPASE_E1_E2; 1.
1: Evidence at protein level;
ATP-binding; Cell membrane; Complete proteome; Endoplasmic reticulum;
Endosome; Lipid transport; Magnesium; Membrane; Metal-binding;
Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome;
Translocase; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 1134 Probable phospholipid-transporting ATPase
IH.
/FTId=PRO_0000046369.
TOPO_DOM 1 61 Cytoplasmic. {ECO:0000255}.
TRANSMEM 62 82 Helical. {ECO:0000255}.
TOPO_DOM 83 88 Extracellular. {ECO:0000255}.
TRANSMEM 89 110 Helical. {ECO:0000255}.
TOPO_DOM 111 296 Cytoplasmic. {ECO:0000255}.
TRANSMEM 297 318 Helical. {ECO:0000255}.
TOPO_DOM 319 349 Extracellular. {ECO:0000255}.
TRANSMEM 350 372 Helical. {ECO:0000255}.
TOPO_DOM 373 881 Cytoplasmic. {ECO:0000255}.
TRANSMEM 882 902 Helical. {ECO:0000255}.
TOPO_DOM 903 914 Extracellular. {ECO:0000255}.
TRANSMEM 915 934 Helical. {ECO:0000255}.
TOPO_DOM 935 964 Cytoplasmic. {ECO:0000255}.
TRANSMEM 965 986 Helical. {ECO:0000255}.
TOPO_DOM 987 1000 Extracellular. {ECO:0000255}.
TRANSMEM 1001 1023 Helical. {ECO:0000255}.
TOPO_DOM 1024 1029 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1030 1050 Helical. {ECO:0000255}.
TOPO_DOM 1051 1068 Extracellular. {ECO:0000255}.
TRANSMEM 1069 1093 Helical. {ECO:0000255}.
TOPO_DOM 1094 1134 Cytoplasmic. {ECO:0000255}.
ACT_SITE 414 414 4-aspartylphosphate intermediate.
{ECO:0000250}.
METAL 825 825 Magnesium. {ECO:0000250}.
METAL 829 829 Magnesium. {ECO:0000250}.
MOD_RES 738 738 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VARIANT 317 317 M -> V (in dbSNP:rs368865).
{ECO:0000269|PubMed:10470851}.
/FTId=VAR_059139.
VARIANT 1091 1091 V -> I (in dbSNP:rs11616795).
/FTId=VAR_048379.
SEQUENCE 1134 AA; 129756 MW; A486BDFC85D6D3B2 CRC64;
MDCSLVRTLV HRYCAGEENW VDSRTIYVGH REPPPGAEAY IPQRYPDNRI VSSKYTFWNF
IPKNLFEQFR RVANFYFLII FLVQLIIDTP TSPVTSGLPL FFVITVTAIK QGYEDWLRHK
ADNAMNQCPV HFIQHGKLVR KQSRKLRVGD IVMVKEDETF PCDLIFLSSN RGDGTCHVTT
ASLDGESSHK THYAVQDTKG FHTEEDIGGL HATIECEQPQ PDLYKFVGRI NVYSDLNDPV
VRPLGSENLL LRGATLKNTE KIFGVAIYTG METKMALNYQ SKSQKRSAVE KSMNAFLIVY
LCILISKALI NTVLKYMWQS EPFRDEPWYN QKTESERQRN LFLKAFTDFL AFMVLFNYII
PVSMYVTVEM QKFLGSYFIT WDEDMFDEET GEGPLVNTSD LNEELGQVEY IFTDKTGTLT
ENNMEFKECC IEGHVYVPHV ICNGQVLPES SGIDMIDSSP SVNGREREEL FFRALCLCHT
VQVKDDDSVD GPRKSPDGGK SCVYISSSPD EVALVEGVQR LGFTYLRLKD NYMEILNREN
HIERFELLEI LSFDSVRRRM SVIVKSATGE IYLFCKGADS SIFPRVIEGK VDQIRARVER
NAVEGLRTLC VAYKRLIQEE YEGICKLLQA AKVALQDREK KLAEAYEQIE KDLTLLGATA
VEDRLQEKAA DTIEALQKAG IKVWVLTGDK METAAATCYA CKLFRRNTQL LELTTKRIEE
QSLHDVLFEL SKTVLRHSGS LTRDNLSGLS ADMQDYGLII DGAALSLIMK PREDGSSGNY
RELFLEICRS CSAVLCCRMA PLQKAQIVKL IKFSKEHPIT LAIGDGANDV SMILEAHVGI
GVIGKEGRQA ARNSDYAIPK FKHLKKMLLV HGHFYYIRIS ELVQYFFYKN VCFIFPQFLY
QFFCGFSQQT LYDTAYLTLY NISFTSLPIL LYSLMEQHVG IDVLKRDPTL YRDVAKNALL
RWRVFIYWTL LGLFDALVFF FGAYFVFENT TVTSNGQIFG NWTFGTLVFT VMVFTVTLKL
ALDTHYWTWI NHFVIWGSLL FYVVFSLLWG GVIWPFLNYQ RMYYVFIQML SSGPAWLAIV
LLVTISLLPD VLKKVLCRQL WPTATERVQT KSQCLSVEQS TIFMLSQTSS SLSF


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