ID F1SC80_PIG Unreviewed; 201 AA.
AC F1SC80;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=Retinol-binding protein {ECO:0000256|PIRNR:PIRNR036893};
GN Name=RBP4 {ECO:0000313|Ensembl:ENSSSCP00000011168.2,
GN ECO:0000313|VGNC:VGNC:92164};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000011168.2, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000011168.2, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000011168.2,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:HDB72539.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=30723633; DOI=.7717/peerj.6374;
RA Gilbert D.G.;
RT "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL PeerJ 7:E6374-E6374(2019).
RN [3] {ECO:0000313|Ensembl:ENSSSCP00000011168.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Retinol-binding protein that mediates retinol transport in
CC blood plasma. {ECO:0000256|PIRNR:PIRNR036893}.
CC -!- SUBUNIT: Interacts with TTR. {ECO:0000256|PIRNR:PIRNR036893}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613,
CC ECO:0000256|PIRNR:PIRNR036893}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC {ECO:0000256|ARBA:ARBA00006889, ECO:0000256|PIRNR:PIRNR036893,
CC ECO:0000256|RuleBase:RU003695}.
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DR EMBL; DQIR01217062; HDB72539.1; -; Transcribed_RNA.
DR Ensembl; ENSSSCT00000011467.5; ENSSSCP00000011168.2; ENSSSCG00000010479.5.
DR VGNC; VGNC:92164; RBP4.
DR GeneTree; ENSGT00510000047107; -.
DR HOGENOM; CLU_094618_0_0_1; -.
DR OMA; KYWGMAS; -.
DR TreeFam; TF331445; -.
DR Proteomes; UP000008227; Chromosome 14.
DR Bgee; ENSSSCG00000010479; Expressed in liver and 32 other cell types or tissues.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0016918; F:retinal binding; IEA:UniProtKB-KW.
DR GO; GO:0019841; F:retinol binding; IEA:UniProtKB-KW.
DR GO; GO:0034632; F:retinol transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0001654; P:eye development; IEA:Ensembl.
DR GO; GO:0006094; P:gluconeogenesis; IEA:Ensembl.
DR GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
DR GO; GO:0030277; P:maintenance of gastrointestinal epithelium; IEA:Ensembl.
DR GO; GO:0032024; P:positive regulation of insulin secretion; IEA:Ensembl.
DR GO; GO:0032526; P:response to retinoic acid; IEA:Ensembl.
DR GO; GO:0042572; P:retinol metabolic process; IEA:Ensembl.
DR CDD; cd00743; lipocalin_RBP_like; 1.
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; RETINOL-BINDING PROTEIN 4; 1.
DR PANTHER; PTHR11873:SF2; RETINOL-BINDING PROTEIN 4; 1.
DR Pfam; PF00061; Lipocalin; 1.
DR PIRSF; PIRSF036893; Lipocalin_ApoD; 1.
DR PIRSF; PIRSF500204; RBP_purpurin; 1.
DR PRINTS; PR00179; LIPOCALIN.
DR PRINTS; PR01174; RETINOLBNDNG.
DR SUPFAM; SSF50814; Lipocalins; 1.
DR PROSITE; PS00213; LIPOCALIN; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR036893-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Retinol-binding {ECO:0000256|ARBA:ARBA00023072};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|PIRNR:PIRNR036893};
KW Signal {ECO:0000256|PIRNR:PIRNR036893};
KW Transport {ECO:0000256|PIRNR:PIRNR036893};
KW Vitamin A {ECO:0000256|ARBA:ARBA00022893}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|PIRNR:PIRNR036893"
FT CHAIN 19..201
FT /note="Retinol-binding protein"
FT /evidence="ECO:0000256|PIRNR:PIRNR036893"
FT /id="PRO_5014494850"
FT DOMAIN 39..171
FT /note="Lipocalin/cytosolic fatty-acid binding"
FT /evidence="ECO:0000259|Pfam:PF00061"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036893-51"
FT DISULFID 22..178
FT /evidence="ECO:0000256|PIRSR:PIRSR036893-50"
FT DISULFID 88..192
FT /evidence="ECO:0000256|PIRSR:PIRSR036893-50"
FT DISULFID 138..147
FT /evidence="ECO:0000256|PIRSR:PIRSR036893-50"
SQ SEQUENCE 201 AA; 23067 MW; A4B889D3C9471DC8 CRC64;
MEWVWALVLL AALGSAQAER DCRVSSFRVK ENFDKARFSG TWYAMAKKDP EGLFLQDNIV
AEFSVDENGH MSATAKGRVR LLNNWDVCAD MVGTFTDTED PAKFKMKYWG VASFLQKGND
DHWIIDTDYD TYAVQYSCRL QNLDGTCADS YSFVFARDPH GFSPEVQKIV RQRQEELCLA
RQYRLITHNG YCDGKSERNI L
//
