OSTA_LEUER
ID OSTA_LEUER Reviewed; 352 AA.
AC Q90YM5;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Organic solute transporter subunit alpha {ECO:0000303|PubMed:11470901};
DE Short=OST-alpha {ECO:0000303|PubMed:11470901};
DE AltName: Full=Solute carrier family 51 subunit alpha;
GN Name=slc51a; Synonyms=osta;
OS Leucoraja erinacea (Little skate) (Raja erinacea).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Batoidea; Rajiformes; Rajidae; Leucoraja.
OX NCBI_TaxID=7782;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PROBABLE SUBUNIT, TISSUE SPECIFICITY,
RP AND TRANSPORT ACTIVITY.
RX PubMed=11470901; DOI=10.1073/pnas.161099898;
RA Wang W., Seward D.J., Li L., Boyer J.L., Ballatori N.;
RT "Expression cloning of two genes that together mediate organic solute and
RT steroid transport in the liver of a marine vertebrate.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9431-9436(2001).
CC -!- FUNCTION: Essential component of the Ost-alpha/Ost-beta complex, a
CC heterodimer that acts as the intestinal basolateral transporter
CC responsible for the translocation of bile acids (such as taurocholate),
CC steroids (such as estrone sulfate), and eicosanoids (such as
CC prostaglandin E2). {ECO:0000269|PubMed:11470901}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=taurocholate(out) = taurocholate(in); Xref=Rhea:RHEA:71703,
CC ChEBI:CHEBI:36257; Evidence={ECO:0000269|PubMed:11470901};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=prostaglandin E2(out) = prostaglandin E2(in);
CC Xref=Rhea:RHEA:50984, ChEBI:CHEBI:606564;
CC Evidence={ECO:0000269|PubMed:11470901};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=estrone 3-sulfate(out) = estrone 3-sulfate(in);
CC Xref=Rhea:RHEA:71835, ChEBI:CHEBI:60050;
CC Evidence={ECO:0000250|UniProtKB:Q86UW1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dehydroepiandrosterone 3-sulfate(out) = dehydroepiandrosterone
CC 3-sulfate(in); Xref=Rhea:RHEA:71839, ChEBI:CHEBI:57905;
CC Evidence={ECO:0000250|UniProtKB:Q86UW1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=tauroursodeoxycholate(out) = tauroursodeoxycholate(in);
CC Xref=Rhea:RHEA:71843, ChEBI:CHEBI:132028;
CC Evidence={ECO:0000250|UniProtKB:Q8R000};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycoursodeoxycholate(out) = glycoursodeoxycholate(in);
CC Xref=Rhea:RHEA:71847, ChEBI:CHEBI:132030;
CC Evidence={ECO:0000250|UniProtKB:Q8R000};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycocholate(out) = glycocholate(in); Xref=Rhea:RHEA:71851,
CC ChEBI:CHEBI:29746; Evidence={ECO:0000250|UniProtKB:Q8R000};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=taurochenodeoxycholate(out) = taurochenodeoxycholate(in);
CC Xref=Rhea:RHEA:71855, ChEBI:CHEBI:9407;
CC Evidence={ECO:0000250|UniProtKB:Q8R000};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycochenodeoxycholate(out) = glycochenodeoxycholate(in);
CC Xref=Rhea:RHEA:71859, ChEBI:CHEBI:36252;
CC Evidence={ECO:0000250|UniProtKB:Q8R000};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=taurodeoxycholate(out) = taurodeoxycholate(in);
CC Xref=Rhea:RHEA:71863, ChEBI:CHEBI:36261;
CC Evidence={ECO:0000250|UniProtKB:Q8R000};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycodeoxycholate(out) = glycodeoxycholate(in);
CC Xref=Rhea:RHEA:71867, ChEBI:CHEBI:82982;
CC Evidence={ECO:0000250|UniProtKB:Q8R000};
CC -!- SUBUNIT: Interacts with slc51b. The Ost-alpha/Ost-beta complex is a
CC heterodimer composed of alpha (slc51a) and beta (slc51b) subunit
CC (Probable). {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in liver. {ECO:0000269|PubMed:11470901}.
CC -!- SIMILARITY: Belongs to the OST-alpha family. {ECO:0000305}.
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DR EMBL; AY027664; AAK14805.1; -; mRNA.
DR AlphaFoldDB; Q90YM5; -.
DR TCDB; 2.A.82.1.1; the organic solute transporter (ost) family.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0015721; P:bile acid and bile salt transport; ISS:UniProtKB.
DR InterPro; IPR005178; Ostalpha/TMEM184C.
DR PANTHER; PTHR23423; PTHR23423; 1.
DR Pfam; PF03619; Solute_trans_a; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Endoplasmic reticulum; Glycoprotein; Lipid transport;
KW Membrane; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..352
FT /note="Organic solute transporter subunit alpha"
FT /id="PRO_0000331546"
FT TOPO_DOM 1..45
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..82
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 104..108
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..173
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..210
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 232..250
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 272..294
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 313..352
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 22
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 352 AA; 39345 MW; 874142BD58B232DB CRC64;
MDVAHPEEVT RFSPDILMEK FNVSEACFLP PPISIQLILQ LTWLDIGVFA ALTAMTVLTI
AIYLEIVCYL MDKVKCPIKR KTLMWNSAAP TVIAITSCLG LWVPRAIMFV DMAAAMYFGV
GFYLMLLIIV QGYGGEEAML QHLATHTIRI STGPCCCCCP CLPHIHLTRQ KYKIFVLGAF
QVAFLRPALF LLGVVLWTNG LYDPDDWSST SIFLWLNLFL GVSTILGLWP VNVLFRHSKV
LMADQKLTCK FALFQAILIL SSLQNSIIGT LAGAGHIGCA PPYSARTRGQ QMNNQLLIIE
MFFVGILTRI SYRKRDDRPG HRHVGEVQQI VRECDQPAIA DQQADHSSIS HI
