RET4_CHICK
ID RET4_CHICK Reviewed; 196 AA.
AC P41263;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 158.
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 Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7748490; DOI=10.1089/dna.1995.14.403;
RA Vieira A.V., Kuchler K., Schneider W.J.;
RT "Retinol in avian oogenesis: molecular properties of the carrier protein.";
RL DNA Cell Biol. 14:403-410(1995).
RN [2] {ECO:0007744|PDB:1IIU}
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 24-196 IN COMPLEX WITH RETINOL,
RP SUBCELLULAR LOCATION, AND DISULFIDE BONDS.
RX PubMed=11738088; DOI=10.1016/s0167-4838(01)00268-0;
RA Zanotti G., Calderone V., Beda M., Malpeli G., Folli C., Berni R.;
RT "Structure of chicken plasma retinol-binding protein.";
RL Biochim. Biophys. Acta 1550:64-69(2001).
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 -!- INTERACTION:
CC P41263; P27731: TTR; NbExp=4; IntAct=EBI-6622456, EBI-6622511;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11738088}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC {ECO:0000305}.
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DR EMBL; X77960; CAA54922.1; -; mRNA.
DR PIR; I50675; I50675.
DR RefSeq; NP_990569.1; NM_205238.1.
DR PDB; 1IIU; X-ray; 2.50 A; A=24-196.
DR PDBsum; 1IIU; -.
DR AlphaFoldDB; P41263; -.
DR SMR; P41263; -.
DR IntAct; P41263; 1.
DR STRING; 9031.ENSGALP00000010694; -.
DR PaxDb; P41263; -.
DR Ensembl; ENSGALT00000010708; ENSGALP00000010694; ENSGALG00000006629.
DR Ensembl; ENSGALT00000061509; ENSGALP00000057089; ENSGALG00000006629.
DR GeneID; 396166; -.
DR KEGG; gga:396166; -.
DR CTD; 396166; -.
DR VEuPathDB; HostDB:geneid_396166; -.
DR eggNOG; ENOG502RXEW; Eukaryota.
DR GeneTree; ENSGT00510000047107; -.
DR HOGENOM; CLU_094618_0_0_1; -.
DR InParanoid; P41263; -.
DR OMA; FATFEDT; -.
DR OrthoDB; 1631943at2759; -.
DR PhylomeDB; P41263; -.
DR TreeFam; TF331445; -.
DR Reactome; R-GGA-2453902; The canonical retinoid cycle in rods (twilight vision).
DR Reactome; R-GGA-975634; Retinoid metabolism and transport.
DR EvolutionaryTrace; P41263; -.
DR PRO; PR:P41263; -.
DR Proteomes; UP000000539; Chromosome 6.
DR Bgee; ENSGALG00000006629; Expressed in liver and 10 other tissues.
DR ExpressionAtlas; P41263; baseline.
DR GO; GO:0030136; C:clathrin-coated vesicle; IDA:AgBase.
DR GO; GO:0070062; C:extracellular exosome; ISM:AgBase.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR GO; GO:0060417; C:yolk; IDA:AgBase.
DR GO; GO:0060418; C:yolk plasma; IDA:AgBase.
DR GO; GO:0019904; F:protein domain specific binding; IPI:AgBase.
DR GO; GO:0016918; F:retinal binding; IEA:UniProtKB-KW.
DR GO; GO:0019841; F:retinol binding; IDA:AgBase.
DR GO; GO:0034632; F:retinol transmembrane transporter activity; IC:AgBase.
DR GO; GO:0005102; F:signaling receptor binding; IDA:AgBase.
DR GO; GO:0001654; P:eye development; ISM:AgBase.
DR GO; GO:0006094; P:gluconeogenesis; ISM:AgBase.
DR GO; GO:0042593; P:glucose homeostasis; ISM:AgBase.
DR GO; GO:0030277; P:maintenance of gastrointestinal epithelium; ISM:AgBase.
DR GO; GO:0001555; P:oocyte growth; IEP:AgBase.
DR GO; GO:0032024; P:positive regulation of insulin secretion; ISM:AgBase.
DR GO; GO:0065003; P:protein-containing complex assembly; IDA:AgBase.
DR GO; GO:0043627; P:response to estrogen; IDA:AgBase.
DR GO; GO:0032526; P:response to retinoic acid; ISM:AgBase.
DR GO; GO:0009615; P:response to virus; IDA:AgBase.
DR GO; GO:0033189; P:response to vitamin A; IDA:AgBase.
DR GO; GO:0042572; P:retinol metabolic process; ISM:AgBase.
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 3D-structure; Disulfide bond; Reference proteome; Retinol-binding;
KW Secreted; Signal; Transport; Vitamin A.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..196
FT /note="Retinol-binding protein 4"
FT /id="PRO_0000017971"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11738088,
FT ECO:0007744|PDB:1IIU"
FT DISULFID 25..181
FT /evidence="ECO:0000269|PubMed:11738088,
FT ECO:0007744|PDB:1IIU"
FT DISULFID 91..195
FT /evidence="ECO:0000269|PubMed:11738088,
FT ECO:0007744|PDB:1IIU"
FT DISULFID 141..150
FT /evidence="ECO:0000269|PubMed:11738088,
FT ECO:0007744|PDB:1IIU"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:1IIU"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:1IIU"
FT STRAND 43..51
FT /evidence="ECO:0007829|PDB:1IIU"
FT STRAND 60..68
FT /evidence="ECO:0007829|PDB:1IIU"
FT STRAND 74..83
FT /evidence="ECO:0007829|PDB:1IIU"
FT STRAND 89..99
FT /evidence="ECO:0007829|PDB:1IIU"
FT STRAND 106..118
FT /evidence="ECO:0007829|PDB:1IIU"
FT STRAND 121..130
FT /evidence="ECO:0007829|PDB:1IIU"
FT STRAND 132..144
FT /evidence="ECO:0007829|PDB:1IIU"
FT STRAND 148..161
FT /evidence="ECO:0007829|PDB:1IIU"
FT HELIX 167..178
FT /evidence="ECO:0007829|PDB:1IIU"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:1IIU"
SQ SEQUENCE 196 AA; 22515 MW; 5E9423A14578DA75 CRC64;
MAYTWRALLL LALAFLGSSM AERDCRVSSF KVKENFDKNR YSGTWYAMAK KDPEGLFLQD
NVVAQFTVDE NGQMSATAKG RVRLFNNWDV CADMIGSFTD TEDPAKFKMK YWGVASFLQK
GNDDHWVVDT DYDTYALHYS CRELNEDGTC ADSYSFVFSR DPKGLPPEAQ KIVRQRQIDL
CLDRKYRVIV HNGFCS
