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   24-NOV-2009, entry version 80.
DE   RecName: Full=Retinol-binding protein 4;
DE   AltName: Full=Plasma retinol-binding protein;
DE            Short=PRBP;
DE            Short=RBP;
DE   Flags: Precursor;
GN   Name=Rbp4;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   MEDLINE=86008182; PubMed=4044565;
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   MEDLINE=85207643; PubMed=3838985;
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).
CC   -!- FUNCTION: Delivers retinol from the liver stores to the peripheral
CC       tissues. In plasma, the RBP-retinol complex interacts with
CC       transthyretin, this prevents its loss by filtration through the
CC       kidney glomeruli.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
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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   IPI; IPI00876581; -.
DR   PIR; A92493; VART.
DR   RefSeq; NP_037294.1; -.
DR   UniGene; Rn.108214; -.
DR   SMR; P04916; 19-192.
DR   STRING; P04916; -.
DR   PRIDE; P04916; -.
DR   Ensembl; ENSRNOT00000021055; ENSRNOP00000021055; ENSRNOG00000015518; Rattus norvegicus.
DR   GeneID; 25703; -.
DR   KEGG; rno:25703; -.
DR   CTD; 25703; -.
DR   RGD; 3546; Rbp4.
DR   HOVERGEN; P04916; -.
DR   OMA; MEWVWAL; -.
DR   OrthoDB; EOG9JT2QV; -.
DR   NextBio; 607739; -.
DR   ArrayExpress; P04916; -.
DR   Genevestigator; P04916; -.
DR   GermOnline; ENSRNOG00000015518; Rattus norvegicus.
DR   GO; GO:0005615; C:extracellular space; IDA:RGD.
DR   GO; GO:0016918; F:retinal binding; IEA:UniProtKB-KW.
DR   GO; GO:0019841; F:retinol binding; TAS:RGD.
DR   GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR   InterPro; IPR012674; Calycin.
DR   InterPro; IPR011038; Calycin-like.
DR   InterPro; IPR002345; Lipocalin.
DR   InterPro; IPR000566; Lipocln_cytFABP.
DR   InterPro; IPR002449; Retinol_bd.
DR   Gene3D; G3DSA:2.40.128.20; Calycin; 1.
DR   PANTHER; PTHR11873; Retinol_bd; 1.
DR   Pfam; PF00061; Lipocalin; 1.
DR   PRINTS; PR00179; LIPOCALIN.
DR   PRINTS; PR01174; RETINOLBNDNG.
DR   PROSITE; PS00213; LIPOCALIN; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Retinol-binding; Secreted;
KW   Signal; Transport; Vitamin A.
FT   SIGNAL        1     18
FT   CHAIN        19    201       Retinol-binding protein 4.
FT                                /FTId=PRO_0000017970.
FT   DISULFID     22    178       By similarity.
FT   DISULFID     88    192       By similarity.
FT   DISULFID    138    147       By similarity.
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
//