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OSTB_BOVIN
ID   OSTB_BOVIN              Reviewed;         130 AA.
AC   A0JNM1;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Organic solute transporter subunit beta;
DE            Short=OST-beta;
DE   AltName: Full=Solute carrier family 51 subunit beta;
GN   Name=SLC51B; Synonyms=OSTB;
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].
RC   STRAIN=Hereford; TISSUE=Testis;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (OCT-2006) 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       The Ost-alpha/Ost-beta complex efficiently transports the major species
CC       of bile acids (taurocholate). Taurine conjugates are transported more
CC       efficiently across the basolateral membrane than glycine-conjugated
CC       bile acids (By similarity). Can also transport steroids such as estrone
CC       3-sulfate and dehydroepiandrosterone 3-sulfate, therefore playing a
CC       role in the enterohepatic circulation of sterols (By similarity). Able
CC       to transport eicosanoids such as prostaglandin E2 (By similarity).
CC       Modulates SLC51A glycosylation, membrane trafficking and stability
CC       activities (By similarity). {ECO:0000250|UniProtKB:Q80WK2,
CC       ECO:0000250|UniProtKB:Q86UW1, 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:Q86UW2};
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:Q86UW2};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=tauroursodeoxycholate(out) = tauroursodeoxycholate(in);
CC         Xref=Rhea:RHEA:71843, ChEBI:CHEBI:132028;
CC         Evidence={ECO:0000250|UniProtKB:Q80WK2};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycoursodeoxycholate(out) = glycoursodeoxycholate(in);
CC         Xref=Rhea:RHEA:71847, ChEBI:CHEBI:132030;
CC         Evidence={ECO:0000250|UniProtKB:Q80WK2};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycocholate(out) = glycocholate(in); Xref=Rhea:RHEA:71851,
CC         ChEBI:CHEBI:29746; Evidence={ECO:0000250|UniProtKB:Q80WK2};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=taurochenodeoxycholate(out) = taurochenodeoxycholate(in);
CC         Xref=Rhea:RHEA:71855, ChEBI:CHEBI:9407;
CC         Evidence={ECO:0000250|UniProtKB:Q80WK2};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycochenodeoxycholate(out) = glycochenodeoxycholate(in);
CC         Xref=Rhea:RHEA:71859, ChEBI:CHEBI:36252;
CC         Evidence={ECO:0000250|UniProtKB:Q80WK2};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=taurodeoxycholate(out) = taurodeoxycholate(in);
CC         Xref=Rhea:RHEA:71863, ChEBI:CHEBI:36261;
CC         Evidence={ECO:0000250|UniProtKB:Q80WK2};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycodeoxycholate(out) = glycodeoxycholate(in);
CC         Xref=Rhea:RHEA:71867, ChEBI:CHEBI:82982;
CC         Evidence={ECO:0000250|UniProtKB:Q80WK2};
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 SLC51A. The Ost-alpha/Ost-beta complex is a
CC       heterodimer composed of alpha (SLC51A) and beta (SLC51B) subunit;
CC       induces the transport of SLC51A from the reticulum endoplasmic to the
CC       plasma membrane (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}. Note=Mainly restricted to the lateral
CC       and basal membranes of ileal enterocytes. {ECO:0000250}.
CC   -!- DOMAIN: The transmembrane domain (TM) is the major site of interaction
CC       with SLC51A. The extracellular-membrane interface is absolutely
CC       required for transport activity. The intracellular-membrane interface
CC       is necessary for establishing the correct membrane orientation that is
CC       essential for the heterodimer Ost-alpha/Ost-beta complex formation and
CC       transport activity at the cell membrane surface (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the OST-beta family. {ECO:0000305}.
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DR   EMBL; BC126778; AAI26779.1; -; mRNA.
DR   RefSeq; NP_001071335.1; NM_001077867.2.
DR   RefSeq; XP_005211336.1; XM_005211279.3.
DR   RefSeq; XP_005211337.1; XM_005211280.3.
DR   AlphaFoldDB; A0JNM1; -.
DR   SMR; A0JNM1; -.
DR   STRING; 9913.ENSBTAP00000004864; -.
DR   PaxDb; A0JNM1; -.
DR   Ensembl; ENSBTAT00000004864; ENSBTAP00000004864; ENSBTAG00000003737.
DR   GeneID; 507185; -.
DR   KEGG; bta:507185; -.
DR   CTD; 123264; -.
DR   VEuPathDB; HostDB:ENSBTAG00000003737; -.
DR   VGNC; VGNC:34901; SLC51B.
DR   eggNOG; ENOG502S380; Eukaryota.
DR   GeneTree; ENSGT00390000010409; -.
DR   HOGENOM; CLU_158049_0_0_1; -.
DR   InParanoid; A0JNM1; -.
DR   OMA; EMLWVFR; -.
DR   OrthoDB; 940161at2759; -.
DR   TreeFam; TF337010; -.
DR   Reactome; R-BTA-159418; Recycling of bile acids and salts.
DR   Proteomes; UP000009136; Chromosome 10.
DR   Bgee; ENSBTAG00000003737; Expressed in cardiac atrium and 58 other tissues.
DR   GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
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:0015721; P:bile acid and bile salt transport; ISS:UniProtKB.
DR   GO; GO:0032782; P:bile acid secretion; IEA:Ensembl.
DR   GO; GO:0070863; P:positive regulation of protein exit from endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0060050; P:positive regulation of protein glycosylation; ISS:UniProtKB.
DR   GO; GO:0090314; P:positive regulation of protein targeting to membrane; ISS:UniProtKB.
DR   GO; GO:0031647; P:regulation of protein stability; ISS:UniProtKB.
DR   InterPro; IPR029387; OSTbeta.
DR   Pfam; PF15048; OSTbeta; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Lipid transport; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..130
FT                   /note="Organic solute transporter subunit beta"
FT                   /id="PRO_0000331553"
FT   TOPO_DOM        1..35
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        36..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        57..130
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          99..130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        114..130
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   130 AA;  14599 MW;  5AD6186D925E6BDB CRC64;
     MNYSEKLTGA PPMTEVPLEL LEEMLWFFRV EDATPWNCSM FVLAALVAII SFILLGRNIQ
     ANRNQKKLPP EKQTPEVLYL AEGGNKDDKN LTSLTETLLS EKPTLAQGEM EAKCSDVPRV
     HLPDPQEPES
 
 
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