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Phospholipid-transporting ATPase IC (EC 3.6.3.1) (ATPase class I type 8B member 1) (Familial intrahepatic cholestasis type 1) (P4-ATPase flippase complex alpha subunit ATP8B1)

 AT8B1_HUMAN             Reviewed;        1251 AA.
O43520; Q9BTP8;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
05-MAY-2009, sequence version 3.
27-SEP-2017, entry version 177.
RecName: Full=Phospholipid-transporting ATPase IC;
EC=3.6.3.1;
AltName: Full=ATPase class I type 8B member 1;
AltName: Full=Familial intrahepatic cholestasis type 1;
AltName: Full=P4-ATPase flippase complex alpha subunit ATP8B1;
Name=ATP8B1; Synonyms=ATPIC, FIC1, PFIC;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], VARIANTS PFIC1 SER-288; VAL-308;
645-ILE--ILE-699 DEL AND ARG-892, VARIANTS BRIC1 THR-661 AND
795-GLY--ARG-797 DEL, AND VARIANT THR-1152.
TISSUE=Intestine, and Liver;
PubMed=9500542; DOI=10.1038/ng0398-219;
Bull L.N., van Eijk M.J.T., Pawlikowska L., DeYoung J.A., Juijn J.A.,
Liao M., Klomp L.W.J., Lomri N., Berger R., Scharschmidt B.F.,
Knisely A.S., Houwen R.H.J., Freimer N.B.;
"A gene encoding a P-type ATPase mutated in two forms of hereditary
cholestasis.";
Nat. Genet. 18:219-223(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16177791; DOI=10.1038/nature03983;
Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D.,
Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S.,
Bloom T., Bugalter B., Butler J., Cook A., DeCaprio D., Engels R.,
Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T.,
Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E.,
Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H.,
O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
"DNA sequence and analysis of human chromosome 18.";
Nature 437:551-555(2005).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 388-661.
TISSUE=Colon tumor;
PubMed=9548971;
Halleck M.S., Pradhan D., Blackman C.F., Berkes C., Williamson P.L.,
Schlegel R.A.;
"Multiple members of a third subfamily of P-type ATPases identified by
genomic sequences and ESTs.";
Genome Res. 8:354-361(1998).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 359-1251, AND VARIANT
THR-1152.
TISSUE=Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=17948906; DOI=10.1002/hep.21950;
Paulusma C.C., Folmer D.E., Ho-Mok K.S., de Waart D.R., Hilarius P.M.,
Verhoeven A.J., Oude Elferink R.P.;
"ATP8B1 requires an accessory protein for endoplasmic reticulum exit
and plasma membrane lipid flippase activity.";
Hepatology 47:268-278(2008).
[6]
FUNCTION.
PubMed=20510206; DOI=10.1016/j.bcp.2010.05.017;
Munoz-Martinez F., Torres C., Castanys S., Gamarro F.;
"CDC50A plays a key role in the uptake of the anticancer drug
perifosine in human carcinoma cells.";
Biochem. Pharmacol. 80:793-800(2010).
[7]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=20512993; DOI=10.1002/hep.23586;
Verhulst P.M., van der Velden L.M., Oorschot V., van Faassen E.E.,
Klumperman J., Houwen R.H., Pomorski T.G., Holthuis J.C., Klomp L.W.;
"A flippase-independent function of ATP8B1, the protein affected in
familial intrahepatic cholestasis type 1, is required for apical
protein expression and microvillus formation in polarized epithelial
cells.";
Hepatology 51:2049-2060(2010).
[8]
INTERACTION WITH TMEM30A AND TMEM30B, AND SUBCELLULAR LOCATION.
PubMed=20947505; DOI=10.1074/jbc.M110.139006;
van der Velden L.M., Wichers C.G., van Breevoort A.E., Coleman J.A.,
Molday R.S., Berger R., Klomp L.W., van de Graaf S.F.;
"Heteromeric interactions required for abundance and subcellular
localization of human CDC50 proteins and class 1 P4-ATPases.";
J. Biol. Chem. 285:40088-40096(2010).
[9]
INTERACTION WITH TMEM30A AND TMEM30B, AND SUBCELLULAR LOCATION.
PubMed=20961850; DOI=10.1074/jbc.M110.139543;
Bryde S., Hennrich H., Verhulst P.M., Devaux P.F., Lenoir G.,
Holthuis J.C.;
"CDC50 proteins are critical components of the human class-1 P4-ATPase
transport machinery.";
J. Biol. Chem. 285:40562-40572(2010).
[10]
INTERACTION WITH TMEM30A AND TMEM30B, 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).
[11]
VARIANT BRIC1 THR-661.
PubMed=9918928; DOI=10.1002/hep.510290214;
Tygstrup N., Steig B.A., Juijn J.A., Bull L.N., Houwen R.H.J.;
"Recurrent familial intrahepatic cholestasis in the Faeroe Islands.
Phenotypic heterogeneity but genetic homogeneity.";
Hepatology 29:506-508(1999).
[12]
VARIANT PFIC1 ASN-554.
PubMed=11093741; DOI=10.1053/jhep.2000.20520;
Klomp L.W.J., Bull L.N., Knisely A.S., van Der Doelen M.A.,
Juijn J.A., Berger R., Forget S., Nielsen I.-M., Eiberg H.,
Houwen R.H.J.;
"A missense mutation in FIC1 is associated with Greenland familial
cholestasis.";
Hepatology 32:1337-1341(2000).
[13]
VARIANTS PFIC1 PRO-127; TYR-403; PRO-412; MET-456; HIS-500; PHE-529
DEL; LEU-535; ASN-554; THR-661; GLY-688; ARG-733; SER-853; ARG-892 AND
ARG-1040, VARIANTS BRIC1 ASN-70; ASP-308; PHE-344; TYR-453; GLY-454;
TRP-600; GLN-600; TRP-628; THR-661; THR-694 AND ARG-892, AND VARIANT
ALA-429.
PubMed=15239083; DOI=10.1002/hep.20285;
Klomp L.W.J., Vargas J.C., van Mil S.W.C., Pawlikowska L.,
Strautnieks S.S., van Eijk M.J.T., Juijn J.A., Pabon-Pena C.,
Smith L.B., DeYoung J.A., Byrne J.A., Gombert J., van der Brugge G.,
Berger R., Jankowska I., Pawlowska J., Villa E., Knisely A.S.,
Thompson R.J., Freimer N.B., Houwen R.H.J., Bull L.N.;
"Characterization of mutations in ATP8B1 associated with hereditary
cholestasis.";
Hepatology 40:27-38(2004).
[14]
VARIANTS ICP1 THR-45 AND GLU-203, AND VARIANT GLN-952.
PubMed=15657619; DOI=10.1038/sj.ejhg.5201355;
Painter J.N., Savander M., Ropponen A., Nupponen N., Riikonen S.,
Ylikorkala O., Lehesjoki A.E., Aittomaki K.;
"Sequence variation in the ATP8B1 gene and intrahepatic cholestasis of
pregnancy.";
Eur. J. Hum. Genet. 13:435-439(2005).
[15]
VARIANT ICP1 CYS-867, AND VARIANTS ASN-70; ILE-305 AND GLN-952.
PubMed=15888793; DOI=10.1136/gut.2004.058115;
Muellenbach R., Bennett A., Tetlow N., Patel N., Hamilton G.,
Cheng F., Chambers J., Howard R., Taylor-Robinson S.D., Williamson C.;
"ATP8B1 mutations in British cases with intrahepatic cholestasis of
pregnancy.";
Gut 54:829-834(2005).
[16]
VARIANTS [LARGE SCALE ANALYSIS] VAL-886 AND MET-1178.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[17]
CHARACTERIZATION OF VARIANTS PFIC1 VAL-308; ASN-554; THR-661 AND
ARG-1040, CHARACTERIZATION OF VARIANTS BRIC1 ASN-70 AND THR-661,
CHARACTERIZATION OF VARIANT ICP1 CYS-867, AND MUTAGENESIS OF ASP-454.
PubMed=19731236; DOI=10.1002/hep.23158;
Folmer D.E., van der Mark V.A., Ho-Mok K.S., Oude Elferink R.P.,
Paulusma C.C.;
"Differential effects of progressive familial intrahepatic cholestasis
type 1 and benign recurrent intrahepatic cholestasis type 1 mutations
on canalicular localization of ATP8B1.";
Hepatology 50:1597-1605(2009).
[18]
VARIANT PFIC1 THR-209.
PubMed=20038848; DOI=10.1097/MPG.0b013e3181c1b368;
Liu L.Y., Wang X.H., Wang Z.L., Zhu Q.R., Wang J.S.;
"Characterization of ATP8B1 gene mutations and a hot-linked mutation
found in Chinese children with progressive intrahepatic cholestasis
and low GGT.";
J. Pediatr. Gastroenterol. Nutr. 50:179-183(2010).
[19]
VARIANT PFIC1 ILE-1012.
PubMed=23197899; DOI=10.3748/wjg.v18.i44.6504;
Deng B.C., Lv S., Cui W., Zhao R., Lu X., Wu J., Liu P.;
"Novel ATP8B1 mutation in an adult male with progressive familial
intrahepatic cholestasis.";
World J. Gastroenterol. 18:6504-6509(2012).
-!- 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. May play a role in asymmetric distribution of
phospholipids in the canicular membrane. May have a role in
transport of bile acids into the canaliculus, uptake of bile acids
from intestinal contents into intestinal mucosa or both. In
cooperation with ABCB4 may be involved in establishing integrity
of the canalicular membrane thus protecting hepatocytes from bile
salts. Together with TMEM30A is involved in uptake of the
synthetic drug alkylphospholipid perifosine. Involved in the
microvillus formation in polarized epithelial cells; the function
seems to be independent from its flippase activity. Required for
the preservation of cochlear hair cells in the inner ear. May act
as cardiolipin transporter during inflammatory injury.
{ECO:0000269|PubMed:17948906, ECO:0000269|PubMed:20510206,
ECO:0000269|PubMed:20512993}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O + phospholipid(Side 1) = ADP +
phosphate + phospholipid(Side 2).
-!- SUBUNIT: Component of a P4-ATPase flippase complex which consists
of a catalytic alpha subunit and an accessory beta subunit
(Probable). The probable flippase ATP8B1:TMEM30A complex can form
an intermediate phosphoenzyme in vitro. Also interacts with beta
subunit TMEM30B. {ECO:0000269|PubMed:17948906,
ECO:0000269|PubMed:20947505, ECO:0000269|PubMed:20961850,
ECO:0000269|PubMed:21914794, ECO:0000305}.
-!- INTERACTION:
Q9NV96:TMEM30A; NbExp=3; IntAct=EBI-9524729, EBI-2836942;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17948906,
ECO:0000269|PubMed:20947505, ECO:0000269|PubMed:20961850,
ECO:0000269|PubMed:21914794}; Multi-pass membrane protein. Apical
cell membrane {ECO:0000269|PubMed:20512993}. Cell projection,
stereocilium {ECO:0000250|UniProtKB:Q148W0}. Endoplasmic reticulum
{ECO:0000269|PubMed:17948906, ECO:0000269|PubMed:20947505,
ECO:0000269|PubMed:20961850, ECO:0000269|PubMed:21914794}. Golgi
apparatus {ECO:0000269|PubMed:20961850}. Note=Exit from the
endoplasmic reticulum requires the presence of TMEM30A or TMEM30B
(PubMed:20947505). Localizes to apical membranes in epithelial
cells (PubMed:20512993). {ECO:0000269|PubMed:20512993,
ECO:0000269|PubMed:20947505}.
-!- TISSUE SPECIFICITY: Found in most tissues except brain and
skeletal muscle. Most abundant in pancreas and small intestine.
-!- DISEASE: Cholestasis, progressive familial intrahepatic, 1 (PFIC1)
[MIM:211600]: A disorder characterized by early onset of
cholestasis that progresses to hepatic fibrosis, cirrhosis, and
end-stage liver disease before adulthood.
{ECO:0000269|PubMed:11093741, ECO:0000269|PubMed:15239083,
ECO:0000269|PubMed:19731236, ECO:0000269|PubMed:20038848,
ECO:0000269|PubMed:23197899, ECO:0000269|PubMed:9500542}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Cholestasis, benign recurrent intrahepatic, 1 (BRIC1)
[MIM:243300]: A disorder characterized by intermittent episodes of
cholestasis without progression to liver failure. There is initial
elevation of serum bile acids, followed by cholestatic jaundice
which generally spontaneously resolves after periods of weeks to
months. The cholestatic attacks vary in severity and duration.
Patients are asymptomatic between episodes, both clinically and
biochemically. {ECO:0000269|PubMed:15239083,
ECO:0000269|PubMed:19731236, ECO:0000269|PubMed:9500542,
ECO:0000269|PubMed:9918928}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Cholestasis of pregnancy, intrahepatic 1 (ICP1)
[MIM:147480]: A liver disorder of pregnancy. It presents during
the second or, more commonly, the third trimester of pregnancy
with intense pruritus which becomes more severe with advancing
gestation and cholestasis. Cholestasis results from abnormal
biliary transport from the liver into the small intestine. ICP1
causes fetal distress, spontaneous premature delivery and
intrauterine death. ICP1 patients have spontaneous and progressive
disappearance of cholestasis after delivery.
{ECO:0000269|PubMed:15657619, ECO:0000269|PubMed:15888793,
ECO:0000269|PubMed:19731236}. Note=The disease may be 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 IV subfamily. {ECO:0000305}.
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EMBL; AF038007; AAC63461.1; -; mRNA.
EMBL; AC027097; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF032442; AAC04328.1; -; mRNA.
EMBL; BC003534; AAH03534.1; -; mRNA.
CCDS; CCDS11965.1; -.
RefSeq; NP_005594.1; NM_005603.4.
RefSeq; XP_006722544.1; XM_006722481.3.
RefSeq; XP_011524324.1; XM_011526022.2.
UniGene; Hs.216623; -.
ProteinModelPortal; O43520; -.
SMR; O43520; -.
BioGrid; 111227; 2.
IntAct; O43520; 2.
STRING; 9606.ENSP00000283684; -.
SwissLipids; SLP:000000342; -.
TCDB; 3.A.3.8.11; the p-type atpase (p-atpase) superfamily.
iPTMnet; O43520; -.
PhosphoSitePlus; O43520; -.
BioMuta; ATP8B1; -.
MaxQB; O43520; -.
PaxDb; O43520; -.
PeptideAtlas; O43520; -.
PRIDE; O43520; -.
Ensembl; ENST00000283684; ENSP00000283684; ENSG00000081923.
GeneID; 5205; -.
KEGG; hsa:5205; -.
UCSC; uc002lgw.5; human.
CTD; 5205; -.
DisGeNET; 5205; -.
EuPathDB; HostDB:ENSG00000081923.10; -.
GeneCards; ATP8B1; -.
GeneReviews; ATP8B1; -.
HGNC; HGNC:3706; ATP8B1.
HPA; HPA018673; -.
HPA; HPA018674; -.
MalaCards; ATP8B1; -.
MIM; 147480; phenotype.
MIM; 211600; phenotype.
MIM; 243300; phenotype.
MIM; 602397; gene.
neXtProt; NX_O43520; -.
OpenTargets; ENSG00000081923; -.
Orphanet; 99960; Benign recurrent intrahepatic cholestasis type 1.
Orphanet; 69665; Intrahepatic cholestasis of pregnancy.
Orphanet; 79306; Progressive familial intrahepatic cholestasis type 1.
PharmGKB; PA265; -.
eggNOG; ENOG410ITKD; Eukaryota.
eggNOG; ENOG410XPYK; LUCA.
GeneTree; ENSGT00870000136387; -.
HOGENOM; HOG000202528; -.
HOVERGEN; HBG050601; -.
InParanoid; O43520; -.
KO; K01530; -.
OMA; ARTQNTI; -.
OrthoDB; EOG091G0139; -.
PhylomeDB; O43520; -.
TreeFam; TF300654; -.
BRENDA; 3.6.3.1; 2681.
Reactome; R-HSA-936837; Ion transport by P-type ATPases.
GeneWiki; ATP8B1; -.
GenomeRNAi; 5205; -.
PRO; PR:O43520; -.
Proteomes; UP000005640; Chromosome 18.
Bgee; ENSG00000081923; -.
CleanEx; HS_ATP8B1; -.
ExpressionAtlas; O43520; baseline and differential.
Genevisible; O43520; HS.
GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
GO; GO:0031526; C:brush border membrane; IEA:Ensembl.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0032420; C:stereocilium; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:1901612; F:cardiolipin binding; IEA:Ensembl.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0004012; F:phospholipid-translocating ATPase activity; TAS:UniProtKB.
GO; GO:0015721; P:bile acid and bile salt transport; NAS:UniProtKB.
GO; GO:0008206; P:bile acid metabolic process; IEA:Ensembl.
GO; GO:0006855; P:drug transmembrane transport; IDA:UniProtKB.
GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
GO; GO:0060119; P:inner ear receptor cell development; IEA:Ensembl.
GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0045332; P:phospholipid translocation; IDA:UniProtKB.
GO; GO:0032534; P:regulation of microvillus assembly; IMP:UniProtKB.
GO; GO:0007605; P:sensory perception of sound; IEA:UniProtKB-KW.
GO; GO:0021650; P:vestibulocochlear nerve formation; IEA:Ensembl.
Gene3D; 3.40.1110.10; -; 2.
Gene3D; 3.40.50.1000; -; 1.
InterPro; IPR030346; ATP8B1.
InterPro; IPR023299; ATPase_P-typ_cyto_domN.
InterPro; IPR018303; ATPase_P-typ_P_site.
InterPro; IPR023298; ATPase_P-typ_TM_dom.
InterPro; IPR008250; ATPase_P-typ_transduc_dom_A.
InterPro; IPR023214; HAD-like_dom.
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:SF109; PTHR24092:SF109; 1.
Pfam; PF16212; PhoLip_ATPase_C; 1.
Pfam; PF16209; PhoLip_ATPase_N; 1.
SUPFAM; SSF56784; SSF56784; 3.
SUPFAM; SSF81653; SSF81653; 2.
SUPFAM; SSF81660; SSF81660; 2.
SUPFAM; SSF81665; SSF81665; 3.
TIGRFAMs; TIGR01652; ATPase-Plipid; 1.
TIGRFAMs; TIGR01494; ATPase_P-type; 1.
PROSITE; PS00154; ATPASE_E1_E2; 1.
1: Evidence at protein level;
ATP-binding; Cell membrane; Cell projection; Complete proteome;
Disease mutation; Endoplasmic reticulum; Golgi apparatus; Hearing;
Hydrolase; Intrahepatic cholestasis; Lipid transport; Magnesium;
Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
Polymorphism; Reference proteome; Transmembrane; Transmembrane helix;
Transport.
CHAIN 1 1251 Phospholipid-transporting ATPase IC.
/FTId=PRO_0000046364.
TOPO_DOM 1 108 Cytoplasmic. {ECO:0000255}.
TRANSMEM 109 130 Helical. {ECO:0000255}.
TOPO_DOM 131 136 Exoplasmic loop. {ECO:0000255}.
TRANSMEM 137 156 Helical. {ECO:0000255}.
TOPO_DOM 157 340 Cytoplasmic. {ECO:0000255}.
TRANSMEM 341 362 Helical. {ECO:0000255}.
TOPO_DOM 363 389 Exoplasmic loop. {ECO:0000255}.
TRANSMEM 390 411 Helical. {ECO:0000255}.
TOPO_DOM 412 949 Cytoplasmic. {ECO:0000255}.
TRANSMEM 950 970 Helical. {ECO:0000255}.
TOPO_DOM 971 982 Exoplasmic loop. {ECO:0000255}.
TRANSMEM 983 1002 Helical. {ECO:0000255}.
TOPO_DOM 1003 1032 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1033 1054 Helical. {ECO:0000255}.
TOPO_DOM 1055 1068 Exoplasmic loop. {ECO:0000255}.
TRANSMEM 1069 1091 Helical. {ECO:0000255}.
TOPO_DOM 1092 1097 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1098 1118 Helical. {ECO:0000255}.
TOPO_DOM 1119 1138 Exoplasmic loop. {ECO:0000255}.
TRANSMEM 1139 1163 Helical. {ECO:0000255}.
TOPO_DOM 1164 1251 Cytoplasmic. {ECO:0000255}.
ACT_SITE 454 454 4-aspartylphosphate intermediate.
{ECO:0000250}.
METAL 893 893 Magnesium. {ECO:0000250}.
METAL 897 897 Magnesium. {ECO:0000250}.
MOD_RES 1223 1223 Phosphoserine.
{ECO:0000250|UniProtKB:Q148W0}.
VARIANT 45 45 N -> T (in ICP1; dbSNP:rs146599962).
{ECO:0000269|PubMed:15657619}.
/FTId=VAR_043044.
VARIANT 70 70 D -> N (in BRIC1; compound heterozygote
with Q-600; uncertain pathological
significance; may be associated with ICP;
reduces interaction with TMEM30A;
dbSNP:rs34719006).
{ECO:0000269|PubMed:15239083,
ECO:0000269|PubMed:15888793,
ECO:0000269|PubMed:19731236}.
/FTId=VAR_043045.
VARIANT 78 78 H -> Q (in dbSNP:rs3745079).
/FTId=VAR_029271.
VARIANT 127 127 L -> P (in PFIC1).
{ECO:0000269|PubMed:15239083}.
/FTId=VAR_043046.
VARIANT 203 203 K -> E (in ICP1; dbSNP:rs56355310).
{ECO:0000269|PubMed:15657619}.
/FTId=VAR_043047.
VARIANT 209 209 P -> T (in PFIC1; dbSNP:rs515726138).
{ECO:0000269|PubMed:20038848}.
/FTId=VAR_071045.
VARIANT 288 288 L -> S (in PFIC1; dbSNP:rs121909099).
{ECO:0000269|PubMed:9500542}.
/FTId=VAR_008809.
VARIANT 305 305 F -> I (in dbSNP:rs150860808).
{ECO:0000269|PubMed:15888793}.
/FTId=VAR_043048.
VARIANT 308 308 G -> D (in BRIC1; dbSNP:rs28939685).
{ECO:0000269|PubMed:15239083}.
/FTId=VAR_043049.
VARIANT 308 308 G -> V (in PFIC1; greatly reduced
expression due to proteosomal
degradation; abolishes interaction with
TMEM30A; dbSNP:rs28939685).
{ECO:0000269|PubMed:19731236,
ECO:0000269|PubMed:9500542}.
/FTId=VAR_008810.
VARIANT 344 344 I -> F (in BRIC1; dbSNP:rs140665115).
{ECO:0000269|PubMed:15239083}.
/FTId=VAR_043050.
VARIANT 384 384 R -> H (in dbSNP:rs2271260).
/FTId=VAR_043051.
VARIANT 393 393 I -> V (in dbSNP:rs34315917).
/FTId=VAR_043052.
VARIANT 403 403 S -> Y (in PFIC1).
{ECO:0000269|PubMed:15239083}.
/FTId=VAR_043053.
VARIANT 412 412 R -> P (in PFIC1).
{ECO:0000269|PubMed:15239083}.
/FTId=VAR_043054.
VARIANT 429 429 E -> A (in dbSNP:rs34018205).
{ECO:0000269|PubMed:15239083}.
/FTId=VAR_043055.
VARIANT 453 453 S -> Y (in BRIC1).
{ECO:0000269|PubMed:15239083}.
/FTId=VAR_043056.
VARIANT 454 454 D -> G (in BRIC1).
{ECO:0000269|PubMed:15239083}.
/FTId=VAR_043057.
VARIANT 456 456 T -> M (in PFIC1; dbSNP:rs121909104).
{ECO:0000269|PubMed:15239083}.
/FTId=VAR_043058.
VARIANT 500 500 Y -> H (in PFIC1; dbSNP:rs147642236).
{ECO:0000269|PubMed:15239083}.
/FTId=VAR_043059.
VARIANT 529 529 Missing (in PFIC1).
{ECO:0000269|PubMed:15239083}.
/FTId=VAR_043060.
VARIANT 535 535 H -> L (in PFIC1).
{ECO:0000269|PubMed:15239083}.
/FTId=VAR_043061.
VARIANT 554 554 D -> N (in PFIC1; greatly reduced
expression due to proteosomal
degradation; abolishes interaction with
TMEM30A; dbSNP:rs121909101).
{ECO:0000269|PubMed:11093741,
ECO:0000269|PubMed:15239083,
ECO:0000269|PubMed:19731236}.
/FTId=VAR_015423.
VARIANT 577 577 I -> V (in dbSNP:rs3745078).
/FTId=VAR_029272.
VARIANT 580 580 S -> N (in dbSNP:rs33963153).
/FTId=VAR_043062.
VARIANT 600 600 R -> Q (in BRIC1; compound heterozygote
with N-70).
{ECO:0000269|PubMed:15239083}.
/FTId=VAR_043063.
VARIANT 600 600 R -> W (in BRIC1).
{ECO:0000269|PubMed:15239083}.
/FTId=VAR_043064.
VARIANT 628 628 R -> W (in BRIC1; dbSNP:rs752045131).
{ECO:0000269|PubMed:15239083}.
/FTId=VAR_043065.
VARIANT 645 699 Missing (in PFIC1).
{ECO:0000269|PubMed:9500542}.
/FTId=VAR_008811.
VARIANT 661 661 I -> T (in BRIC1 and PFIC1; common
mutation; reduces interaction with
TMEM30A; dbSNP:rs28939686).
{ECO:0000269|PubMed:15239083,
ECO:0000269|PubMed:19731236,
ECO:0000269|PubMed:9500542,
ECO:0000269|PubMed:9918928}.
/FTId=VAR_008812.
VARIANT 674 674 M -> T (in dbSNP:rs35470719).
/FTId=VAR_043066.
VARIANT 688 688 D -> G (in PFIC1).
{ECO:0000269|PubMed:15239083}.
/FTId=VAR_043067.
VARIANT 694 694 I -> T (in BRIC1; dbSNP:rs541474497).
{ECO:0000269|PubMed:15239083}.
/FTId=VAR_043068.
VARIANT 733 733 G -> R (in PFIC1).
{ECO:0000269|PubMed:15239083}.
/FTId=VAR_043069.
VARIANT 795 797 Missing (in BRIC1).
{ECO:0000269|PubMed:9500542}.
/FTId=VAR_008814.
VARIANT 814 814 K -> N (in dbSNP:rs34018300).
/FTId=VAR_043070.
VARIANT 853 853 F -> S (in PFIC1; dbSNP:rs773092889).
{ECO:0000269|PubMed:15239083}.
/FTId=VAR_043071.
VARIANT 867 867 R -> C (in ICP1; reduces interaction with
TMEM30A; dbSNP:rs121909103).
{ECO:0000269|PubMed:15888793,
ECO:0000269|PubMed:19731236}.
/FTId=VAR_043072.
VARIANT 886 886 A -> V (in a breast cancer sample;
somatic mutation; dbSNP:rs767398921).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036499.
VARIANT 892 892 G -> R (in PFIC1 and BRIC1;
dbSNP:rs121909098).
{ECO:0000269|PubMed:15239083,
ECO:0000269|PubMed:9500542}.
/FTId=VAR_008813.
VARIANT 952 952 R -> Q (in dbSNP:rs12968116).
{ECO:0000269|PubMed:15657619,
ECO:0000269|PubMed:15888793}.
/FTId=VAR_029273.
VARIANT 1012 1012 S -> I (in PFIC1).
{ECO:0000269|PubMed:23197899}.
/FTId=VAR_071046.
VARIANT 1040 1040 G -> R (in PFIC1; greatly reduces
interaction with TMEM30A).
{ECO:0000269|PubMed:15239083,
ECO:0000269|PubMed:19731236}.
/FTId=VAR_043073.
VARIANT 1152 1152 A -> T (in dbSNP:rs222581).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9500542}.
/FTId=VAR_055045.
VARIANT 1178 1178 I -> M (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036500.
MUTAGEN 454 454 D->A: Greatly reduced expression due to
proteosomal degradation; abolishes
interaction with TMEM30A.
{ECO:0000269|PubMed:19731236}.
CONFLICT 1016 1016 P -> L (in Ref. 4; AAH03534).
{ECO:0000305}.
SEQUENCE 1251 AA; 143695 MW; 770FEF3946CB579F CRC64;
MSTERDSETT FDEDSQPNDE VVPYSDDETE DELDDQGSAV EPEQNRVNRE AEENREPFRK
ECTWQVKAND RKYHEQPHFM NTKFLCIKES KYANNAIKTY KYNAFTFIPM NLFEQFKRAA
NLYFLALLIL QAVPQISTLA WYTTLVPLLV VLGVTAIKDL VDDVARHKMD KEINNRTCEV
IKDGRFKVAK WKEIQVGDVI RLKKNDFVPA DILLLSSSEP NSLCYVETAE LDGETNLKFK
MSLEITDQYL QREDTLATFD GFIECEEPNN RLDKFTGTLF WRNTSFPLDA DKILLRGCVI
RNTDFCHGLV IFAGADTKIM KNSGKTRFKR TKIDYLMNYM VYTIFVVLIL LSAGLAIGHA
YWEAQVGNSS WYLYDGEDDT PSYRGFLIFW GYIIVLNTMV PISLYVSVEV IRLGQSHFIN
WDLQMYYAEK DTPAKARTTT LNEQLGQIHY IFSDKTGTLT QNIMTFKKCC INGQIYGDHR
DASQHNHNKI EQVDFSWNTY ADGKLAFYDH YLIEQIQSGK EPEVRQFFFL LAVCHTVMVD
RTDGQLNYQA ASPDEGALVN AARNFGFAFL ARTQNTITIS ELGTERTYNV LAILDFNSDR
KRMSIIVRTP EGNIKLYCKG ADTVIYERLH RMNPTKQETQ DALDIFANET LRTLCLCYKE
IEEKEFTEWN KKFMAASVAS TNRDEALDKV YEEIEKDLIL LGATAIEDKL QDGVPETISK
LAKADIKIWV LTGDKKETAE NIGFACELLT EDTTICYGED INSLLHARME NQRNRGGVYA
KFAPPVQESF FPPGGNRALI ITGSWLNEIL LEKKTKRNKI LKLKFPRTEE ERRMRTQSKR
RLEAKKEQRQ KNFVDLACEC SAVICCRVTP KQKAMVVDLV KRYKKAITLA IGDGANDVNM
IKTAHIGVGI SGQEGMQAVM SSDYSFAQFR YLQRLLLVHG RWSYIRMCKF LRYFFYKNFA
FTLVHFWYSF FNGYSAQTAY EDWFITLYNV LYTSLPVLLM GLLDQDVSDK LSLRFPGLYI
VGQRDLLFNY KRFFVSLLHG VLTSMILFFI PLGAYLQTVG QDGEAPSDYQ SFAVTIASAL
VITVNFQIGL DTSYWTFVNA FSIFGSIALY FGIMFDFHSA GIHVLFPSAF QFTGTASNAL
RQPYIWLTII LAVAVCLLPV VAIRFLSMTI WPSESDKIQK HRKRLKAEEQ WQRRQQVFRR
GVSTRRSAYA FSHQRGYADL ISSGRSIRKK RSPLDAIVAD GTAEYRRTGD S


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