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