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ATP-binding cassette sub-family G member 8 (Sterolin-2)

 ABCG8_HUMAN             Reviewed;         673 AA.
Q9H221; Q53QN8;
05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
12-SEP-2018, entry version 171.
RecName: Full=ATP-binding cassette sub-family G member 8;
AltName: Full=Sterolin-2 {ECO:0000303|PubMed:11452359};
Name=ABCG8;
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 1), FUNCTION, VARIANTS STSL
THR-231; GLN-263; ARG-574 AND ARG-596, AND VARIANT CYS-54.
PubMed=11099417; DOI=10.1126/science.290.5497.1771;
Berge K.E., Tian H., Graf G.A., Yu L., Grishin N.V., Schultz J.,
Kwiterovich P., Shan B., Barnes R., Hobbs H.H.;
"Accumulation of dietary cholesterol in sitosterolemia caused by
mutations in adjacent ABC transporters.";
Science 290:1771-1775(2000).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), FUNCTION,
TISSUE SPECIFICITY, VARIANTS STSL HIS-184; THR-231; LYS-238; GLN-263;
HIS-405; PRO-501; SER-543; PHE-570 DEL; PRO-572; ARG-574; GLU-574 AND
ARG-596, AND VARIANTS HIS-19; CYS-54; VAL-259; LYS-400; ARG-575 AND
ALA-632.
TISSUE=Liver;
PubMed=11452359; DOI=10.1086/321294;
Lu K., Lee M.-H., Hazard S., Brooks-Wilson A., Hidaka H., Kojima H.,
Ose L., Stalenhoef A.F.H., Mietinnen T., Bjorkhem I., Bruckert E.,
Pandya A., Brewer H.B. Jr., Salen G., Dean M., Srivastava A.K.,
Patel S.B.;
"Two genes that map to the STSL locus cause sitosterolemia: genomic
structure and spectrum of mutations involving sterolin-1 and sterolin-
2, encoded by ABCG5 and ABCG8, respectively.";
Am. J. Hum. Genet. 69:278-290(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[4]
REVIEW.
PubMed=11590207;
Schmitz G., Langmann T., Heimerl S.;
"Role of ABCG1 and other ABCG family members in lipid metabolism.";
J. Lipid Res. 42:1513-1520(2001).
[5]
SUBCELLULAR LOCATION.
PubMed=14504269; DOI=10.1074/jbc.M310223200;
Graf G.A., Yu L., Li W.P., Gerard R., Tuma P.L., Cohen J.C.,
Hobbs H.H.;
"ABCG5 and ABCG8 are obligate heterodimers for protein trafficking and
biliary cholesterol excretion.";
J. Biol. Chem. 278:48275-48282(2003).
[6]
FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND GLYCOSYLATION.
PubMed=16893193; DOI=10.1021/bi0608055;
Wang Z., Stalcup L.D., Harvey B.J., Weber J., Chloupkova M.,
Dumont M.E., Dean M., Urbatsch I.L.;
"Purification and ATP hydrolysis of the putative cholesterol
transporters ABCG5 and ABCG8.";
Biochemistry 45:9929-9939(2006).
[7]
FUNCTION, ACTIVITY REGULATION, SUBUNIT, AND GLYCOSYLATION.
PubMed=20210363; DOI=10.1021/bi902064g;
Johnson B.J., Lee J.Y., Pickert A., Urbatsch I.L.;
"Bile acids stimulate ATP hydrolysis in the purified cholesterol
transporter ABCG5/G8.";
Biochemistry 49:3403-3411(2010).
[8]
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).
[9] {ECO:0000244|PDB:5DO7}
X-RAY CRYSTALLOGRAPHY (3.93 ANGSTROMS) IN COMPLEX WITH ABCG5,
FUNCTION, ACTIVITY REGULATION, MUTAGENESIS OF GLY-216, SUBUNIT, AND
TOPOLOGY.
PubMed=27144356; DOI=10.1038/nature17666;
Lee J.Y., Kinch L.N., Borek D.M., Wang J., Wang J., Urbatsch I.L.,
Xie X.S., Grishin N.V., Cohen J.C., Otwinowski Z., Hobbs H.H.,
Rosenbaum D.M.;
"Crystal structure of the human sterol transporter ABCG5/ABCG8.";
Nature 533:561-564(2016).
[10]
VARIANTS HIS-19; CYS-54; LYS-400; ALA-632 AND PHE-641.
PubMed=11668628; DOI=10.1002/humu.1206;
Hubacek J.A., Berge K.E., Cohen J.C., Hobbs H.H.;
"Mutations in ATP-cassette binding proteins G5 (ABCG5) and G8 (ABCG8)
causing sitosterolemia.";
Hum. Mutat. 18:359-360(2001).
[11]
VARIANTS CYS-54 AND LYS-400.
PubMed=12111378; DOI=10.1007/s100380200041;
Iida A., Saito S., Sekine A., Mishima C., Kitamura Y., Kondo K.,
Harigae S., Osawa S., Nakamura Y.;
"Catalog of 605 single-nucleotide polymorphisms (SNPs) among 13 genes
encoding human ATP-binding cassette transporters: ABCA4, ABCA7, ABCA8,
ABCD1, ABCD3, ABCD4, ABCE1, ABCF1, ABCG1, ABCG2, ABCG4, ABCG5, and
ABCG8.";
J. Hum. Genet. 47:285-310(2002).
[12]
CHARACTERIZATION OF VARIANTS STSL HIS-184; THR-231; GLN-263; PRO-501;
SER-543; GLU-574 AND ARG-596, AND FUNCTION.
PubMed=15054092; DOI=10.1074/jbc.M402634200;
Graf G.A., Cohen J.C., Hobbs H.H.;
"Missense mutations in ABCG5 and ABCG8 disrupt heterodimerization and
trafficking.";
J. Biol. Chem. 279:24881-24888(2004).
[13]
VARIANT HIS-19, AND INVOLVEMENT IN GBD4.
PubMed=17632509; DOI=10.1038/ng2101;
Buch S., Schafmayer C., Voelzke H., Becker C., Franke A.,
von Eller-Eberstein H., Kluck C., Baessmann I., Brosch M., Lammert F.,
Miquel J.F., Nervi F., Wittig M., Rosskopf D., Timm B., Hoell C.,
Seeger M., ElSharawy A., Lu T., Egberts J., Faendrich F.,
Foelsch U.R., Krawczak M., Schreiber S., Nuernberg P., Tepel J.,
Hampe J.;
"A genome-wide association scan identifies the hepatic cholesterol
transporter ABCG8 as a susceptibility factor for human gallstone
disease.";
Nat. Genet. 39:995-999(2007).
-!- FUNCTION: ABCG5 and ABCG8 form an obligate heterodimer that
mediates Mg(2+)- and ATP-dependent sterol transport across the
cell membrane. Plays an essential role in the selective transport
of the dietary cholesterol in and out of the enterocytes and in
the selective sterol excretion by the liver into bile
(PubMed:11099417, PubMed:11452359, PubMed:27144356,
PubMed:15054092). Required for normal sterol homeostasis
(PubMed:11099417, PubMed:11452359, PubMed:15054092). The
heterodimer with ABCG5 has ATPase activity (PubMed:16893193,
PubMed:20210363, PubMed:27144356). {ECO:0000269|PubMed:11099417,
ECO:0000269|PubMed:11452359, ECO:0000269|PubMed:15054092,
ECO:0000269|PubMed:16893193, ECO:0000269|PubMed:27144356}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:Q9DBM0};
-!- ACTIVITY REGULATION: The ATPase activity of the heterodimer is
stimulated by cholate. Taurocholate, glycocholate,
taurochenodeoxycholate, glycochenodeoxycholate and
taurodeoxycholate also stimulate ATPase activity, but to a lower
degree. Glycodeoxycholate has no significant effect on ATPase
activity. ATPase activity is inhibited by vanadate and by
berillium fluoride. {ECO:0000269|PubMed:20210363,
ECO:0000269|PubMed:27144356}.
-!- SUBUNIT: Heterodimer with ABCG8. {ECO:0000269|PubMed:16893193,
ECO:0000269|PubMed:20210363, ECO:0000269|PubMed:27144356}.
-!- INTERACTION:
Q9H222:ABCG5; NbExp=2; IntAct=EBI-3908684, EBI-1761423;
Q9H222-1:ABCG5; NbExp=5; IntAct=EBI-16205990, EBI-16205983;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:16893193};
Multi-pass membrane protein {ECO:0000269|PubMed:27144356}. Apical
cell membrane {ECO:0000269|PubMed:14504269}; Multi-pass membrane
protein {ECO:0000269|PubMed:27144356}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9H221-1; Sequence=Displayed;
Name=2;
IsoId=Q9H221-2; Sequence=VSP_000052;
Note=Minor form detected in approximately 10% of the cDNA
clones.;
-!- TISSUE SPECIFICITY: Predominantly expressed in the liver
(PubMed:11099417, PubMed:11452359). Low expression levels in the
small intestine and colon (PubMed:11099417). Very low levels in
other tissues, including brain, heart and spleen
(PubMed:11452359). {ECO:0000269|PubMed:11099417,
ECO:0000269|PubMed:11452359}.
-!- DOMAIN: A functional Walker motif (consensus sequence G-X-X-G-X-G-
K-[ST]-T) is expected to bind ATP. The essential Lys in this
region is not conserved in ABCG8 (G-S-S-G-C-R-A-S) and is not
required for transport activity mediated by the heterodimer with
ABCG5. {ECO:0000250|UniProtKB:Q9DBM0}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:16893193,
ECO:0000269|PubMed:20210363}.
-!- DISEASE: Gallbladder disease 4 (GBD4) [MIM:611465]: One of the
major digestive diseases. Gallstones composed of cholesterol
(cholelithiasis) are the common manifestations in western
countries. Most people with gallstones, however, remain
asymptomatic through their lifetimes.
{ECO:0000269|PubMed:17632509}. Note=Disease susceptibility may be
associated with variations affecting the gene represented in this
entry.
-!- DISEASE: Sitosterolemia (STSL) [MIM:210250]: Rare autosomal
recessive disorder characterized by increased intestinal
absorption of all sterols including cholesterol, plant and
shellfish sterols, and decreased biliary excretion of dietary
sterols into bile. Sitosterolemia patients have
hypercholesterolemia, very high levels of plant sterols in the
plasma, and frequently develop tendon and tuberous xanthomas,
accelerated atherosclerosis and premature coronary artery disease.
{ECO:0000269|PubMed:11099417, ECO:0000269|PubMed:11452359,
ECO:0000269|PubMed:15054092}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG
family. Eye pigment precursor importer (TC 3.A.1.204) subfamily.
{ECO:0000305}.
-!- CAUTION: Seems to have a defective ATP-binding region.
{ECO:0000305}.
-!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC
proteins;
URL="http://abcmutations.hegelab.org/proteinDetails?uniprot_id=Q9H221";
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EMBL; AF320294; AAG40004.1; -; mRNA.
EMBL; AF324494; AAK84078.1; -; mRNA.
EMBL; AF351824; AAK84663.1; -; Genomic_DNA.
EMBL; AF351812; AAK84663.1; JOINED; Genomic_DNA.
EMBL; AF351813; AAK84663.1; JOINED; Genomic_DNA.
EMBL; AF351814; AAK84663.1; JOINED; Genomic_DNA.
EMBL; AF351815; AAK84663.1; JOINED; Genomic_DNA.
EMBL; AF351816; AAK84663.1; JOINED; Genomic_DNA.
EMBL; AF351817; AAK84663.1; JOINED; Genomic_DNA.
EMBL; AF351818; AAK84663.1; JOINED; Genomic_DNA.
EMBL; AF351819; AAK84663.1; JOINED; Genomic_DNA.
EMBL; AF351820; AAK84663.1; JOINED; Genomic_DNA.
EMBL; AF351821; AAK84663.1; JOINED; Genomic_DNA.
EMBL; AF351822; AAK84663.1; JOINED; Genomic_DNA.
EMBL; AF351823; AAK84663.1; JOINED; Genomic_DNA.
EMBL; AC108476; AAY24011.1; -; Genomic_DNA.
CCDS; CCDS1815.1; -. [Q9H221-1]
RefSeq; NP_071882.1; NM_022437.2. [Q9H221-1]
RefSeq; XP_005264540.1; XM_005264483.3.
UniGene; Hs.413931; -.
PDB; 5DO7; X-ray; 3.93 A; B/D=2-673.
PDBsum; 5DO7; -.
ProteinModelPortal; Q9H221; -.
SMR; Q9H221; -.
BioGrid; 122125; 13.
DIP; DIP-42631N; -.
IntAct; Q9H221; 9.
MINT; Q9H221; -.
STRING; 9606.ENSP00000272286; -.
DrugBank; DB00973; Ezetimibe.
TCDB; 3.A.1.204.5; the atp-binding cassette (abc) superfamily.
iPTMnet; Q9H221; -.
PhosphoSitePlus; Q9H221; -.
BioMuta; ABCG8; -.
DMDM; 17432916; -.
PaxDb; Q9H221; -.
PeptideAtlas; Q9H221; -.
PRIDE; Q9H221; -.
ProteomicsDB; 80473; -.
ProteomicsDB; 80474; -. [Q9H221-2]
DNASU; 64241; -.
Ensembl; ENST00000272286; ENSP00000272286; ENSG00000143921. [Q9H221-1]
Ensembl; ENST00000645013; ENSP00000496450; ENSG00000143921. [Q9H221-1]
GeneID; 64241; -.
KEGG; hsa:64241; -.
UCSC; uc002rtq.3; human. [Q9H221-1]
CTD; 64241; -.
DisGeNET; 64241; -.
EuPathDB; HostDB:ENSG00000143921.6; -.
GeneCards; ABCG8; -.
GeneReviews; ABCG8; -.
HGNC; HGNC:13887; ABCG8.
HPA; HPA019556; -.
MalaCards; ABCG8; -.
MIM; 210250; phenotype.
MIM; 605460; gene.
MIM; 611465; phenotype.
neXtProt; NX_Q9H221; -.
OpenTargets; ENSG00000143921; -.
Orphanet; 2882; Sitosterolemia.
PharmGKB; PA24412; -.
eggNOG; KOG0061; Eukaryota.
eggNOG; COG1131; LUCA.
GeneTree; ENSGT00920000149166; -.
HOGENOM; HOG000033764; -.
HOVERGEN; HBG050444; -.
InParanoid; Q9H221; -.
KO; K05684; -.
OMA; LLPTFHM; -.
OrthoDB; EOG091G0E38; -.
PhylomeDB; Q9H221; -.
TreeFam; TF105212; -.
Reactome; R-HSA-1369062; ABC transporters in lipid homeostasis.
Reactome; R-HSA-5679090; Defective ABCG8 causes gallbladder disease 4 and sitosterolemia.
Reactome; R-HSA-5679096; Defective ABCG5 causes sitosterolemia.
SIGNOR; Q9H221; -.
GeneWiki; ABCG8; -.
GenomeRNAi; 64241; -.
PRO; PR:Q9H221; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000143921; Expressed in 30 organ(s), highest expression level in right lobe of liver.
CleanEx; HS_ABCG8; -.
Genevisible; Q9H221; HS.
GO; GO:0016324; C:apical plasma membrane; IMP:BHF-UCL.
GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0043235; C:receptor complex; IDA:BHF-UCL.
GO; GO:0005524; F:ATP binding; IEA:InterPro.
GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0046982; F:protein heterodimerization activity; IPI:BHF-UCL.
GO; GO:0033344; P:cholesterol efflux; IMP:UniProtKB.
GO; GO:0042632; P:cholesterol homeostasis; IMP:UniProtKB.
GO; GO:0007588; P:excretion; IGI:BHF-UCL.
GO; GO:0030299; P:intestinal cholesterol absorption; IC:BHF-UCL.
GO; GO:0045796; P:negative regulation of intestinal cholesterol absorption; IMP:BHF-UCL.
GO; GO:0010949; P:negative regulation of intestinal phytosterol absorption; IMP:BHF-UCL.
InterPro; IPR013525; ABC_2_trans.
InterPro; IPR003439; ABC_transporter-like.
InterPro; IPR017871; ABC_transporter_CS.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF01061; ABC2_membrane; 1.
Pfam; PF00005; ABC_tran; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Disease mutation; Glycoprotein; Lipid transport; Magnesium; Membrane;
Metal-binding; Polymorphism; Reference proteome; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 673 ATP-binding cassette sub-family G member
8.
/FTId=PRO_0000093396.
TOPO_DOM 1 416 Cytoplasmic.
{ECO:0000269|PubMed:27144356}.
TRANSMEM 417 437 Helical; Name=1.
{ECO:0000269|PubMed:27144356}.
TOPO_DOM 438 447 Extracellular.
{ECO:0000269|PubMed:27144356}.
TRANSMEM 448 468 Helical; Name=2.
{ECO:0000269|PubMed:27144356}.
TOPO_DOM 469 497 Cytoplasmic.
{ECO:0000269|PubMed:27144356}.
TRANSMEM 498 518 Helical; Name=3.
{ECO:0000269|PubMed:27144356}.
TOPO_DOM 519 527 Extracellular.
{ECO:0000269|PubMed:27144356}.
TRANSMEM 528 548 Helical; Name=4.
{ECO:0000269|PubMed:27144356}.
TOPO_DOM 549 555 Cytoplasmic.
{ECO:0000269|PubMed:27144356}.
TRANSMEM 556 576 Helical; Name=5.
{ECO:0000269|PubMed:27144356}.
TOPO_DOM 577 639 Extracellular.
{ECO:0000269|PubMed:27144356}.
TRANSMEM 640 660 Helical; Name=6.
{ECO:0000269|PubMed:27144356}.
TOPO_DOM 661 673 Cytoplasmic.
{ECO:0000269|PubMed:27144356}.
DOMAIN 47 313 ABC transporter. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
DOMAIN 411 665 ABC transmembrane type-2.
CARBOHYD 619 619 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 376 376 Missing (in isoform 2).
{ECO:0000303|PubMed:11452359}.
/FTId=VSP_000052.
VARIANT 19 19 D -> H (associated significantly with
GBD4; dbSNP:rs11887534).
{ECO:0000269|PubMed:11452359,
ECO:0000269|PubMed:11668628,
ECO:0000269|PubMed:17632509}.
/FTId=VAR_012250.
VARIANT 54 54 Y -> C (in dbSNP:rs4148211).
{ECO:0000269|PubMed:11099417,
ECO:0000269|PubMed:11452359,
ECO:0000269|PubMed:11668628,
ECO:0000269|PubMed:12111378}.
/FTId=VAR_012251.
VARIANT 184 184 R -> H (in STSL; strongly decreased
maturation of glycan chains;
dbSNP:rs766212636).
{ECO:0000269|PubMed:11452359,
ECO:0000269|PubMed:15054092}.
/FTId=VAR_012252.
VARIANT 210 210 V -> M (in dbSNP:rs9282574).
/FTId=VAR_022074.
VARIANT 231 231 P -> T (in STSL; strongly decreased
maturation of glycan chains;
dbSNP:rs137852993).
{ECO:0000269|PubMed:11099417,
ECO:0000269|PubMed:11452359,
ECO:0000269|PubMed:15054092}.
/FTId=VAR_012253.
VARIANT 238 238 E -> K (in STSL; unknown pathological
significance; dbSNP:rs34754243).
{ECO:0000269|PubMed:11452359}.
/FTId=VAR_012254.
VARIANT 259 259 A -> V (in dbSNP:rs35518570).
{ECO:0000269|PubMed:11452359}.
/FTId=VAR_012255.
VARIANT 263 263 R -> Q (in STSL; strongly decreased
maturation of glycan chains;
dbSNP:rs137852990).
{ECO:0000269|PubMed:11099417,
ECO:0000269|PubMed:11452359,
ECO:0000269|PubMed:15054092}.
/FTId=VAR_012256.
VARIANT 400 400 T -> K (in dbSNP:rs4148217).
{ECO:0000269|PubMed:11452359,
ECO:0000269|PubMed:11668628,
ECO:0000269|PubMed:12111378}.
/FTId=VAR_012257.
VARIANT 405 405 R -> H (in STSL).
{ECO:0000269|PubMed:11452359}.
/FTId=VAR_012258.
VARIANT 501 501 L -> P (in STSL; strongly decreased
maturation of glycan chains).
{ECO:0000269|PubMed:11452359,
ECO:0000269|PubMed:15054092}.
/FTId=VAR_012259.
VARIANT 543 543 R -> S (in STSL; decreased maturation of
glycan chains; dbSNP:rs201690654).
{ECO:0000269|PubMed:11452359,
ECO:0000269|PubMed:15054092}.
/FTId=VAR_012260.
VARIANT 570 570 Missing (in STSL).
{ECO:0000269|PubMed:11452359}.
/FTId=VAR_012261.
VARIANT 572 572 L -> P (in STSL; dbSNP:rs769576789).
{ECO:0000269|PubMed:11452359}.
/FTId=VAR_012262.
VARIANT 574 574 G -> E (in STSL; strongly decreased
maturation of glycan chains).
{ECO:0000269|PubMed:11452359,
ECO:0000269|PubMed:15054092}.
/FTId=VAR_012263.
VARIANT 574 574 G -> R (in STSL; decreased maturation of
glycan chains; dbSNP:rs137852988).
{ECO:0000269|PubMed:11099417,
ECO:0000269|PubMed:11452359,
ECO:0000269|PubMed:15054092}.
/FTId=VAR_012264.
VARIANT 575 575 G -> R. {ECO:0000269|PubMed:11452359}.
/FTId=VAR_012265.
VARIANT 596 596 L -> R (in STSL; strongly decreased
maturation of glycan chains;
dbSNP:rs137852992).
{ECO:0000269|PubMed:11099417,
ECO:0000269|PubMed:11452359,
ECO:0000269|PubMed:15054092}.
/FTId=VAR_012266.
VARIANT 632 632 V -> A (in dbSNP:rs6544718).
{ECO:0000269|PubMed:11452359,
ECO:0000269|PubMed:11668628}.
/FTId=VAR_012267.
VARIANT 641 641 Y -> F (in dbSNP:rs145125968).
{ECO:0000269|PubMed:11668628}.
/FTId=VAR_020785.
VARIANT 655 655 M -> V (in dbSNP:rs9282573).
/FTId=VAR_022075.
MUTAGEN 216 216 G->D: Loss of ATPase activity.
{ECO:0000269|PubMed:27144356}.
SEQUENCE 673 AA; 75679 MW; 594AFD1D6C1BB50F CRC64;
MAGKAAEERG LPKGATPQDT SGLQDRLFSS ESDNSLYFTY SGQPNTLEVR DLNYQVDLAS
QVPWFEQLAQ FKMPWTSPSC QNSCELGIQN LSFKVRSGQM LAIIGSSGCG RASLLDVITG
RGHGGKIKSG QIWINGQPSS PQLVRKCVAH VRQHNQLLPN LTVRETLAFI AQMRLPRTFS
QAQRDKRVED VIAELRLRQC ADTRVGNMYV RGLSGGERRR VSIGVQLLWN PGILILDEPT
SGLDSFTAHN LVKTLSRLAK GNRLVLISLH QPRSDIFRLF DLVLLMTSGT PIYLGAAQHM
VQYFTAIGYP CPRYSNPADF YVDLTSIDRR SREQELATRE KAQSLAALFL EKVRDLDDFL
WKAETKDLDE DTCVESSVTP LDTNCLPSPT KMPGAVQQFT TLIRRQISND FRDLPTLLIH
GAEACLMSMT IGFLYFGHGS IQLSFMDTAA LLFMIGALIP FNVILDVISK CYSERAMLYY
ELEDGLYTTG PYFFAKILGE LPEHCAYIII YGMPTYWLAN LRPGLQPFLL HFLLVWLVVF
CCRIMALAAA ALLPTFHMAS FFSNALYNSF YLAGGFMINL SSLWTVPAWI SKVSFLRWCF
EGLMKIQFSR RTYKMPLGNL TIAVSGDKIL SVMELDSYPL YAIYLIVIGL SGGFMVLYYV
SLRFIKQKPS QDW


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