RET4_FELCA
ID RET4_FELCA Reviewed; 201 AA.
AC M5AXY1; M3WVN1;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Retinol binding protein 4 {ECO:0000303|PubMed:23719693, ECO:0000312|EMBL:BAN13410.1};
DE AltName: Full=Feline conceptus protein 1 {ECO:0000303|PubMed:2015342};
DE Short=fCP1 {ECO:0000303|PubMed:23719693};
DE AltName: Full=Plasma retinol-binding protein {ECO:0000305};
DE Short=PRBP {ECO:0000305};
DE Short=RBP {ECO:0000303|PubMed:2015342};
DE Flags: Precursor;
GN Name=RBP4 {ECO:0000303|PubMed:23719693, ECO:0000312|EMBL:BAN13410.1};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000312|EMBL:BAN13410.1};
RN [1] {ECO:0000312|EMBL:BAN13410.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Liver {ECO:0000303|PubMed:23719693, ECO:0000312|EMBL:BAN13410.1};
RX PubMed=23719693; DOI=10.1292/jvms.13-0131;
RA Sasaki N., Ishibashi M., Soeta S.;
RT "Molecular characterization and tissue distribution of feline retinol-
RT binding protein 4.";
RL J. Vet. Med. Sci. 75:1383-1387(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian;
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [3]
RP PROTEIN SEQUENCE OF 19-46, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=2015342; DOI=10.1095/biolreprod44.1.108;
RA Thatcher M.D., Shille V.M., Fliss M.F., Bazer F.W., Sisum W., Randal S.;
RT "Characterization of feline conceptus proteins during pregnancy.";
RL Biol. Reprod. 44:108-120(1991).
CC -!- FUNCTION: Retinol-binding protein that mediates retinol transport in
CC blood plasma. Delivers retinol from the liver stores to the peripheral
CC tissues. Transfers the bound all-trans retinol to STRA6, that then
CC facilitates retinol transport across the cell membrane.
CC {ECO:0000250|UniProtKB:P02753}.
CC -!- SUBUNIT: Interacts with TTR. Interaction with TTR prevents its loss by
CC filtration through the kidney glomeruli. Interacts with STRA6.
CC {ECO:0000250|UniProtKB:P02753}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2015342}.
CC -!- TISSUE SPECIFICITY: Highly expressed in liver. Also expressed in
CC adipose tissue (PubMed:23719693). Expressed by endometrium from days
CC 16-25 and by unattached chorioallantois from days 30-36 during
CC pregnancy (PubMed:2015342). {ECO:0000269|PubMed:2015342,
CC ECO:0000269|PubMed:23719693}.
CC -!- DEVELOPMENTAL STAGE: Secreted in fetal fluids. Present on day 25,
CC decreases from days 30-39, and disappears by day 50. Expressed by
CC blastocysts on days 10-25 during prenatal development, but disappears
CC by day 50. {ECO:0000269|PubMed:2015342}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC {ECO:0000255, ECO:0000255|RuleBase:RU003695, ECO:0000305}.
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DR EMBL; AB771450; BAN13410.1; -; mRNA.
DR RefSeq; NP_001277178.1; NM_001290249.1.
DR AlphaFoldDB; M5AXY1; -.
DR SMR; M5AXY1; -.
DR STRING; 9685.ENSFCAP00000018418; -.
DR Ensembl; ENSFCAT00000064276; ENSFCAP00000045095; ENSFCAG00000045563.
DR GeneID; 101094377; -.
DR KEGG; fca:101094377; -.
DR CTD; 5950; -.
DR eggNOG; ENOG502RXEW; Eukaryota.
DR GeneTree; ENSGT00510000047107; -.
DR OrthoDB; 1631943at2759; -.
DR Proteomes; UP000011712; Chromosome D2.
DR Bgee; ENSFCAG00000045563; Expressed in liver and 10 other tissues.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0016918; F:retinal binding; IEA:UniProtKB-KW.
DR GO; GO:0019841; F:retinol binding; ISS:UniProtKB.
DR GO; GO:0034632; F:retinol transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0034633; P:retinol transport; IBA:GO_Central.
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:2015342"
FT CHAIN 19..201
FT /note="Retinol binding protein 4"
FT /evidence="ECO:0000250|UniProtKB:P02753,
FT ECO:0000305|PubMed:2015342"
FT /id="PRO_5004063033"
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; 22898 MW; 10F45F15081EE0F5 CRC64;
MAWVWALVLL AALGSARAER DCRVSSFRVK ENFDKARFSG TWYAMAKKDP EGLFLQDNIV
AEFSVDENGQ MSATAKGRVR LLNNWDVCAD MVGTFTDTED SAKFKMKYWG VASFLQKGND
DHWIIDTDYD TYAVQYSCRL LNLDGTCADS YSFVFARDPN GLPPDVQKIV RQRQDELCLA
RQYRLIVHNG YCDGKSEQNI L
