RET4_PIG
ID RET4_PIG Reviewed; 201 AA.
AC P27485;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 124.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1723146; DOI=10.1210/mend-5-10-1533;
RA Trout W.E., McDonnell J.J., Kramer K.K., Baumbach G.A., Roberts R.M.;
RT "The retinol-binding protein of the expanding pig blastocyst: molecular
RT cloning and expression in trophectoderm and embryonic disc.";
RL Mol. Endocrinol. 5:1533-1540(1991).
RN [2]
RP PROTEIN SEQUENCE OF 19-51, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=2340335; DOI=10.1095/biolreprod42.3.523;
RA Harney J.P., Mirando M.A., Smith L.C., Bazer F.W.;
RT "Retinol-binding protein: a major secretory product of the pig conceptus.";
RL Biol. Reprod. 42:523-532(1990).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 19-201 IN COMPLEX WITH RETINOL,
RP SEQUENCE REVISION TO 134 AND 185, SUBCELLULAR LOCATION, AND DISULFIDE
RP BONDS.
RX PubMed=9757135; DOI=10.1107/s0907444998002303;
RA Zanotti G., Panzalorto M., Marcato A., Malpeli G., Folli C., Berni R.;
RT "Structure of pig plasma retinol-binding protein at 1.65-A resolution.";
RL Acta Crystallogr. D 54:1049-1052(1998).
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:2340335,
CC ECO:0000269|PubMed:9757135}.
CC -!- DEVELOPMENTAL STAGE: Produced between days 10 and 15 of pregnancy and
CC at day 15 found in both the peri-implantation conceptus (trophectoderm
CC and yolk sac) and the endometrial surface and glandular epithelium.
CC Found in allantoic fluid at day 30 of gestation.
CC {ECO:0000269|PubMed:2340335}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC {ECO:0000305}.
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DR EMBL; M68860; AAA31113.1; -; mRNA.
DR PIR; A39486; A39486.
DR RefSeq; NP_999222.1; NM_214057.1.
DR PDB; 1AQB; X-ray; 1.65 A; A=19-201.
DR PDBsum; 1AQB; -.
DR AlphaFoldDB; P27485; -.
DR SMR; P27485; -.
DR STRING; 9823.ENSSSCP00000011168; -.
DR PaxDb; P27485; -.
DR PeptideAtlas; P27485; -.
DR PRIDE; P27485; -.
DR GeneID; 397124; -.
DR KEGG; ssc:397124; -.
DR CTD; 5950; -.
DR eggNOG; ENOG502RXEW; Eukaryota.
DR InParanoid; P27485; -.
DR EvolutionaryTrace; P27485; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
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; IDA: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 3D-structure; Direct protein sequencing; Disulfide bond; Methylation;
KW Reference proteome; Retinol-binding; Secreted; Signal; Transport;
KW Vitamin A.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:2340335"
FT CHAIN 19..201
FT /note="Retinol-binding protein 4"
FT /id="PRO_0000017968"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:9757135,
FT ECO:0007744|PDB:1AQB"
FT MOD_RES 139
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q00724"
FT DISULFID 22..178
FT /evidence="ECO:0000269|PubMed:9757135,
FT ECO:0007744|PDB:1AQB"
FT DISULFID 88..192
FT /evidence="ECO:0000269|PubMed:9757135,
FT ECO:0007744|PDB:1AQB"
FT DISULFID 138..147
FT /evidence="ECO:0000269|PubMed:9757135,
FT ECO:0007744|PDB:1AQB"
FT CONFLICT 134
FT /note="V -> A (in Ref. 1; AAA31113)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="I -> L (in Ref. 1; AAA31113)"
FT /evidence="ECO:0000305"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:1AQB"
FT HELIX 35..38
FT /evidence="ECO:0007829|PDB:1AQB"
FT STRAND 40..48
FT /evidence="ECO:0007829|PDB:1AQB"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:1AQB"
FT STRAND 55..65
FT /evidence="ECO:0007829|PDB:1AQB"
FT STRAND 71..80
FT /evidence="ECO:0007829|PDB:1AQB"
FT STRAND 86..97
FT /evidence="ECO:0007829|PDB:1AQB"
FT STRAND 103..112
FT /evidence="ECO:0007829|PDB:1AQB"
FT STRAND 118..127
FT /evidence="ECO:0007829|PDB:1AQB"
FT STRAND 129..141
FT /evidence="ECO:0007829|PDB:1AQB"
FT STRAND 145..158
FT /evidence="ECO:0007829|PDB:1AQB"
FT HELIX 164..176
FT /evidence="ECO:0007829|PDB:1AQB"
SQ SEQUENCE 201 AA; 23067 MW; A20E39D3C9471DC8 CRC64;
MEWVWALVLL AALGSAQAER DCRVSSFRVK ENFDKARFSG TWYAMAKKDP EGLFLQDNIV
AEFSVDENGH MSATAKGRVR LLNNWDVCAD MVGTFTDTED PAKFKMKYWG VASFLQKGND
DHWIIDTDYD TYAVQYSCRL QNLDGTCADS YSFVFARDPH GFSPEVQKIV RQRQEELCLA
RQYRIITHNG YCDGKSERNI L
