OSTA_BOVIN
ID OSTA_BOVIN Reviewed; 340 AA.
AC Q3T124; Q56K15;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Organic solute transporter subunit alpha;
DE Short=OST-alpha;
DE AltName: Full=Solute carrier family 51 subunit alpha;
GN Name=SLC51A; Synonyms=OSTA;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lymphoid epithelium;
RA Yu J., Meng Y., Wang Z., Hansen C., Li C., Moore S.S.;
RT "Analysis of sequences obtained from constructed full-length bovine cDNA
RT libraries.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Essential component of the Ost-alpha/Ost-beta complex, a
CC heterodimer that acts as the intestinal basolateral transporter
CC responsible for bile acid export from enterocytes into portal blood.
CC Efficiently transports the major species of bile acids (taurocholate)
CC (By similarity). Taurine conjugates are transported more efficiently
CC across the basolateral membrane than glycine-conjugated bile acids (By
CC similarity). Can also transport steroids such as estrone 3-sulfate and
CC dehydroepiandrosterone 3-sulfate, therefore playing a role in the
CC enterohepatic circulation of sterols (By similarity). Able to transport
CC eicosanoids such as prostaglandin E2 (By similarity).
CC {ECO:0000250|UniProtKB:Q86UW1, ECO:0000250|UniProtKB:Q8R000,
CC ECO:0000250|UniProtKB:Q90YM5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=taurocholate(out) = taurocholate(in); Xref=Rhea:RHEA:71703,
CC ChEBI:CHEBI:36257; Evidence={ECO:0000250|UniProtKB:Q86UW1};
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 -!- CATALYTIC ACTIVITY:
CC Reaction=prostaglandin E2(out) = prostaglandin E2(in);
CC Xref=Rhea:RHEA:50984, ChEBI:CHEBI:606564;
CC Evidence={ECO:0000250|UniProtKB:Q90YM5};
CC -!- SUBUNIT: Interacts with SLC51B. The Ost-alpha/Ost-beta complex is a
CC heterodimer composed of alpha (SLC51A) and beta (SLC51B) subunit (By
CC similarity). {ECO:0000250}.
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}. Note=Transported from the
CC endoplasmic reticulum to the plasma membrane upon interacting with
CC SLC51B. Mainly restricted to the lateral and basal membranes of ileal
CC enterocytes (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3T124-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3T124-2; Sequence=VSP_033256;
CC -!- SIMILARITY: Belongs to the OST-alpha family. {ECO:0000305}.
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DR EMBL; AY911312; AAW82080.1; -; mRNA.
DR EMBL; BC102154; AAI02155.1; -; mRNA.
DR RefSeq; NP_001020504.1; NM_001025333.2. [Q3T124-2]
DR RefSeq; XP_005201455.1; XM_005201398.3. [Q3T124-1]
DR AlphaFoldDB; Q3T124; -.
DR STRING; 9913.ENSBTAP00000016384; -.
DR PaxDb; Q3T124; -.
DR Ensembl; ENSBTAT00000016384; ENSBTAP00000016384; ENSBTAG00000012347. [Q3T124-1]
DR GeneID; 516626; -.
DR KEGG; bta:516626; -.
DR CTD; 200931; -.
DR VEuPathDB; HostDB:ENSBTAG00000012347; -.
DR eggNOG; ENOG502R3BX; Eukaryota.
DR GeneTree; ENSGT00940000160780; -.
DR HOGENOM; CLU_054316_0_0_1; -.
DR InParanoid; Q3T124; -.
DR OMA; YLEDAVY; -.
DR OrthoDB; 1374406at2759; -.
DR TreeFam; TF316050; -.
DR Reactome; R-BTA-159418; Recycling of bile acids and salts.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000012347; Expressed in cortex of kidney and 34 other tissues.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
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:0015125; F:bile acid transmembrane transporter activity; IEA:Ensembl.
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 GO; GO:0032782; P:bile acid secretion; IEA:Ensembl.
DR InterPro; IPR005178; Ostalpha/TMEM184C.
DR PANTHER; PTHR23423; PTHR23423; 1.
DR Pfam; PF03619; Solute_trans_a; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Endoplasmic reticulum; Glycoprotein;
KW Lipid transport; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..340
FT /note="Organic solute transporter subunit alpha"
FT /id="PRO_0000331542"
FT TOPO_DOM 1..52
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..87
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 109..110
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132..186
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 208..219
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 241..255
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 277..295
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 317..340
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R000"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 45..65
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_033256"
SQ SEQUENCE 340 AA; 37858 MW; C9EB139D53E909B9 CRC64;
MEPDRTQIRL DPRYTADLLE ILKTNYSVPS ACFSYPPTAA QLLRALGPVD ISLMVIMTLF
VLGSIAIFLE AAVYLHKNTR CPIKRKTLIW CSSSPTIVSA FSCFGLWIPR ALTLVEMAIT
TFYSMCFYLL MQAMVEGFGG KEAVLRTLKD TPVMIHTGPC CCCCPCCPRI KITRKRLQLL
LLGPIQYAFF KISLTLVGLF LIPDGIFDPS DISEGSTALW INTFLGVSTL SALWTIGIIF
RQARLHLGEQ NIGAKFVLFQ ALLILSALQP SIFSVLASGG QIACSPPFSS KIRSQVMNCH
LLILESFLIT VLTRIYYRRK DDKLGYEPFS SPDQDLNLKA
