RET4_RAT
ID RET4_RAT Reviewed; 201 AA.
AC P04916;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Retinol-binding protein 4;
DE AltName: Full=Plasma retinol-binding protein;
DE Short=PRBP;
DE Short=RBP {ECO:0000303|PubMed:4708098};
DE Flags: Precursor;
GN Name=Rbp4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=4044565; DOI=10.1016/s0021-9258(17)39053-1;
RA Laurent B.C., Nilsson M.H.L., Bavik C.O., Jones T.A., Sundelin J.,
RA Peterson P.A.;
RT "Characterization of the rat retinol-binding protein gene and its
RT comparison to the three-dimensional structure of the protein.";
RL J. Biol. Chem. 260:11476-11480(1985).
RN [2]
RP PROTEIN SEQUENCE OF 19-59, AND NUCLEOTIDE SEQUENCE OF 30-201.
RX PubMed=3838985; DOI=10.1016/s0021-9258(18)88996-7;
RA Sundelin J., Laurent B.C., Anundi H., Traegaardh L., Larhammar D.,
RA Bjoerck L., Eriksson U., Aakerstroem B., Jones A., Newcomer M.,
RA Peterson P.A., Rask L.;
RT "Amino acid sequence homologies between rabbit, rat, and human serum
RT retinol-binding proteins.";
RL J. Biol. Chem. 260:6472-6480(1985).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TTR, TISSUE SPECIFICITY,
RP AND CIRCULAR DICHROISM ANALYSIS.
RX PubMed=4708098; DOI=10.1016/s0021-9258(19)43832-5;
RA Peterson P.A., Rask L., Ostberg L., Andersson L., Kamwendo F., Pertoft H.;
RT "Studies on the transport and cellular distribution of vitamin A in normal
RT and vitamin A-deficient rats with special reference to the vitamin A-
RT binding plasma protein.";
RL J. Biol. Chem. 248:4009-4022(1973).
CC -!- FUNCTION: Retinol-binding protein that mediates retinol transport in
CC blood plasma. Delivers retinol from the liver stores to the peripheral
CC tissues (PubMed:4708098). Transfers the bound all-trans retinol to
CC STRA6, that then facilitates retinol transport across the cell membrane
CC (By similarity). {ECO:0000250|UniProtKB:P02753,
CC ECO:0000269|PubMed:4708098}.
CC -!- SUBUNIT: Interacts with TTR (PubMed:4708098). Interaction with TTR
CC prevents its loss by filtration through the kidney glomeruli
CC (Probable). Interacts with STRA6 (By similarity).
CC {ECO:0000250|UniProtKB:P02753, ECO:0000269|PubMed:4708098,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:4708098}.
CC -!- TISSUE SPECIFICITY: Detected in blood plasma (at protein level).
CC {ECO:0000269|PubMed:4708098}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC {ECO:0000305}.
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DR EMBL; K03046; AAA42018.1; -; Genomic_DNA.
DR EMBL; M10610; AAA42018.1; JOINED; Genomic_DNA.
DR EMBL; M10934; AAA42020.1; -; mRNA.
DR PIR; A92493; VART.
DR RefSeq; NP_037294.1; NM_013162.1.
DR AlphaFoldDB; P04916; -.
DR SMR; P04916; -.
DR IntAct; P04916; 1.
DR STRING; 10116.ENSRNOP00000021055; -.
DR PaxDb; P04916; -.
DR PRIDE; P04916; -.
DR Ensembl; ENSRNOT00000021055; ENSRNOP00000021055; ENSRNOG00000015518.
DR GeneID; 25703; -.
DR KEGG; rno:25703; -.
DR UCSC; RGD:3546; rat.
DR CTD; 5950; -.
DR RGD; 3546; Rbp4.
DR eggNOG; ENOG502RXEW; Eukaryota.
DR GeneTree; ENSGT00510000047107; -.
DR HOGENOM; CLU_094618_0_0_1; -.
DR InParanoid; P04916; -.
DR OMA; FATFEDT; -.
DR OrthoDB; 1631943at2759; -.
DR PhylomeDB; P04916; -.
DR TreeFam; TF331445; -.
DR Reactome; R-RNO-2453902; The canonical retinoid cycle in rods (twilight vision).
DR Reactome; R-RNO-975634; Retinoid metabolism and transport.
DR PRO; PR:P04916; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000015518; Expressed in liver and 20 other tissues.
DR ExpressionAtlas; P04916; baseline and differential.
DR Genevisible; P04916; RN.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0016918; F:retinal binding; IEA:UniProtKB-KW.
DR GO; GO:0019841; F:retinol binding; IDA:UniProtKB.
DR GO; GO:0034632; F:retinol transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0048738; P:cardiac muscle tissue development; ISO:RGD.
DR GO; GO:0050908; P:detection of light stimulus involved in visual perception; ISO:RGD.
DR GO; GO:0048562; P:embryonic organ morphogenesis; ISO:RGD.
DR GO; GO:0060059; P:embryonic retina morphogenesis in camera-type eye; ISO:RGD.
DR GO; GO:0048706; P:embryonic skeletal system development; ISO:RGD.
DR GO; GO:0001654; P:eye development; ISO:RGD.
DR GO; GO:0048807; P:female genitalia morphogenesis; ISO:RGD.
DR GO; GO:0006094; P:gluconeogenesis; ISO:RGD.
DR GO; GO:0042593; P:glucose homeostasis; ISO:RGD.
DR GO; GO:0007507; P:heart development; ISO:RGD.
DR GO; GO:0060347; P:heart trabecula formation; ISO:RGD.
DR GO; GO:0030324; P:lung development; ISO:RGD.
DR GO; GO:0030277; P:maintenance of gastrointestinal epithelium; ISO:RGD.
DR GO; GO:0008584; P:male gonad development; ISO:RGD.
DR GO; GO:0060044; P:negative regulation of cardiac muscle cell proliferation; ISO:RGD.
DR GO; GO:0002639; P:positive regulation of immunoglobulin production; ISO:RGD.
DR GO; GO:0032024; P:positive regulation of insulin secretion; ISO:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0032868; P:response to insulin; ISO:RGD.
DR GO; GO:0032526; P:response to retinoic acid; ISO:RGD.
DR GO; GO:0060041; P:retina development in camera-type eye; ISO:RGD.
DR GO; GO:0042574; P:retinal metabolic process; ISO:RGD.
DR GO; GO:0042572; P:retinol metabolic process; ISO:RGD.
DR GO; GO:0034633; P:retinol transport; IDA:RGD.
DR GO; GO:0007283; P:spermatogenesis; ISO:RGD.
DR GO; GO:0060157; P:urinary bladder development; ISO:RGD.
DR GO; GO:0060065; P:uterus development; ISO:RGD.
DR GO; GO:0060068; P:vagina development; ISO:RGD.
DR GO; GO:0071939; P:vitamin A import into cell; ISO:RGD.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR022271; Lipocalin_ApoD.
DR InterPro; IPR022272; Lipocalin_CS.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR InterPro; IPR002449; Retinol-bd/Purpurin.
DR PANTHER; PTHR11873; PTHR11873; 1.
DR Pfam; PF00061; Lipocalin; 1.
DR PIRSF; PIRSF036893; Lipocalin_ApoD; 1.
DR PIRSF; PIRSF500204; RBP_purpurin; 1.
DR PRINTS; PR01174; RETINOLBNDNG.
DR SUPFAM; SSF50814; SSF50814; 1.
DR PROSITE; PS00213; LIPOCALIN; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Methylation; Reference proteome;
KW Retinol-binding; Secreted; Signal; Transport; Vitamin A.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:3838985"
FT CHAIN 19..201
FT /note="Retinol-binding protein 4"
FT /evidence="ECO:0000250|UniProtKB:P02753,
FT ECO:0000305|PubMed:3838985"
FT /id="PRO_0000017970"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P27485"
FT MOD_RES 139
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q00724"
FT DISULFID 22..178
FT /evidence="ECO:0000250|UniProtKB:P02753"
FT DISULFID 88..192
FT /evidence="ECO:0000250|UniProtKB:P02753"
FT DISULFID 138..147
FT /evidence="ECO:0000250|UniProtKB:P02753"
SQ SEQUENCE 201 AA; 23220 MW; E6737E293B37A30A CRC64;
MEWVWALVLL AALGGGSAER DCRVSSFRVK ENFDKARFSG LWYAIAKKDP EGLFLQDNII
AEFSVDEKGH MSATAKGRVR LLSNWEVCAD MVGTFTDTED PAKFKMKYWG VASFLQRGND
DHWIIDTDYD TFALQYSCRL QNLDGTCADS YSFVFSRDPN GLTPETRRLV RQRQEELCLE
RQYRWIEHNG YCQSRPSRNS L
