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OSTB_LEUER
ID   OSTB_LEUER              Reviewed;         182 AA.
AC   Q90YM4;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 42.
DE   RecName: Full=Organic solute transporter subunit beta;
DE            Short=OST-beta;
DE   AltName: Full=Solute carrier family 51 subunit beta;
DE   Flags: Precursor;
GN   Name=slc51b; Synonyms=ostb;
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, AND TISSUE
RP   SPECIFICITY.
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 bile acid export from enterocytes into portal blood.
CC       Efficiently transports the major species of bile acids. May modulate
CC       slc51a glycosylation, membrane trafficking and stability activities (By
CC       similarity). Able to transport taurocholate, estrone sulfate, digoxin,
CC       and prostaglandin E(2), but not p-aminohippurate or S-dinitrophenyl
CC       glutathione. {ECO:0000250, ECO:0000269|PubMed:11470901}.
CC   -!- SUBUNIT: Interacts with slc51a. The Ost-alpha/Ost-beta complex is a
CC       heterodimer composed of alpha (slc51a) and beta (slc51b) subunit; may
CC       induce the transport of slc51a from the reticulum endoplasmic to the
CC       plasma membrane (Probable). {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in liver. {ECO:0000269|PubMed:11470901}.
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; AY027665; AAK14806.1; -; mRNA.
DR   AlphaFoldDB; Q90YM4; -.
DR   SMR; Q90YM4; -.
DR   TCDB; 2.A.82.1.1; the organic solute transporter (ost) family.
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:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015721; P:bile acid and bile salt transport; ISS:UniProtKB.
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   1: Evidence at protein level;
KW   Cell membrane; Glycoprotein; Membrane; Signal; Transmembrane;
KW   Transmembrane helix; Transport.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..182
FT                   /note="Organic solute transporter subunit beta"
FT                   /id="PRO_0000331556"
FT   TOPO_DOM        21..64
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        65..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        86..182
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        42
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        48
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   182 AA;  20343 MW;  0A3758892D350120 CRC64;
     MSGLLKYLFG CFILCLLLQG KTHMTSATIS KPHETIDIEK QNMTGERNST LAQQLSFPME
     DPTNWNYAIL ALAFVVLFLA FLILAQNSRA NRTRKMKALN GAGGRNETEA DSTQKAMMQY
     VVEVDNLAET DQMLQSKPTY ISLNQVAQTS SPKVLPKEGQ ILVEWKDGNI GFLYTDSKED
     DV
 
 
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