OSTA_XENTR
ID OSTA_XENTR Reviewed; 339 AA.
AC A9ULC7;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 75.
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 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=N6; TISSUE=Intestine;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2007) 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 the translocation of bile acids (such as taurocholate),
CC steroids (such as estrone sulfate), and eicosanoids (such as
CC prostaglandin E2). {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:Q90YM5};
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 -!- 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 (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}.
CC -!- SIMILARITY: Belongs to the OST-alpha family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI57206.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC157205; AAI57206.1; ALT_INIT; mRNA.
DR RefSeq; NP_001107358.1; NM_001113886.1.
DR RefSeq; XP_017946555.1; XM_018091066.1.
DR AlphaFoldDB; A9ULC7; -.
DR SMR; A9ULC7; -.
DR STRING; 8364.ENSXETP00000009505; -.
DR PaxDb; A9ULC7; -.
DR GeneID; 100135183; -.
DR KEGG; xtr:100135183; -.
DR CTD; 100135183; -.
DR Xenbase; XB-GENE-5838770; slc51a-like.1.
DR eggNOG; ENOG502QVWH; Eukaryota.
DR HOGENOM; CLU_054316_0_1_1; -.
DR InParanoid; A9ULC7; -.
DR OMA; GAVMWIN; -.
DR OrthoDB; 1374406at2759; -.
DR TreeFam; TF316050; -.
DR Proteomes; UP000008143; Chromosome 2.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000024712; Expressed in intestine and 8 other tissues.
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 2: Evidence at transcript level;
KW Cell membrane; Endoplasmic reticulum; Glycoprotein; Lipid transport;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..339
FT /note="Organic solute transporter subunit alpha"
FT /id="PRO_0000331547"
FT TOPO_DOM 1..32
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 54..70
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 92..97
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..165
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 187..202
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224..254
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 276..283
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 302..339
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 6
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 339 AA; 38291 MW; DD874974EA7D5AE7 CRC64;
MDPEQNDTKP PFNPICATRQ APYSHEILEN LDITGILLFA ILTFMTLVSL LVFLEEAYYM
YRKIPNPKNS IIIWINAGAM MIATTSCFGM WIPRSTMFTD FTASVFLAVL IHKFQLMLVN
ECGGRREFLS TFGDTKLKIS TGPFCCCCLC LPHKDINRKT LFILKLGTFQ FAFLRPVLMF
LAVVLWTNGT YMIGNSSAEK ATIWINIGVG ITTITALWAV GIMFNLVKDN LKEKNIIGKF
AVYQFTVILS QLQTSIINIL GTTGVISCVP PLPGPSRASY MNQQLLIMEM FLVTVICRVL
YRRRYDDKNL LENQETNDNL RNSMMHLNGK ALEDGPQSV
