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   16-JUN-2009, entry version 68.
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;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC   Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=92131004; PubMed=1723146;
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:
RT   molecular cloning and expression in trophectoderm and embryonic
RT   disc.";
RL   Mol. Endocrinol. 5:1533-1540(1991).
RN   [2]
RP   PROTEIN SEQUENCE OF 19-51, AND DEVELOPMENTAL STAGE.
RX   PubMed=2340335;
RA   Harney J.P., Mirando M.A., Smith L.C., Bazer F.W.;
RT   "Retinol-binding protein: a major secretory product of the pig
RT   conceptus.";
RL   Biol. Reprod. 42:523-532(1990).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS), AND SEQUENCE REVISION TO 134
RP   AND 185.
RX   MEDLINE=98437649; 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
RT   resolution.";
RL   Acta Crystallogr. D 54:1049-1052(1998).
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   -!- DEVELOPMENTAL STAGE: Produced between days 10 and 15 of pregnancy
CC       and at day 15 found in both the peri-implantation conceptus
CC       (trophectoderm and yolk sac) and the endometrial surface and
CC       glandular epithelium. Found in allantoic fluid at day 30 of
CC       gestation.
CC   -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
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DR   EMBL; M68860; AAA31113.1; -; mRNA.
DR   PIR; A39486; A39486.
DR   RefSeq; NP_999222.1; -.
DR   UniGene; Ssc.15695; -.
DR   PDB; 1AQB; X-ray; 1.65 A; A=19-201.
DR   PDBsum; 1AQB; -.
DR   GeneID; 397124; -.
DR   KEGG; ssc:397124; -.
DR   HOVERGEN; P27485; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016918; F:retinal binding; IEA:UniProtKB-KW.
DR   GO; GO:0019841; F:retinol binding; IEA:UniProtKB-KW.
DR   GO; GO:0005215; F:transporter activity; IEA:InterPro.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR012674; Calycin.
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   3D-structure; Direct protein sequencing; Disulfide bond;
KW   Retinol-binding; Secreted; Signal; Transport; Vitamin A.
FT   SIGNAL        1     18
FT   CHAIN        19    201       Retinol-binding protein 4.
FT                                /FTId=PRO_0000017968.
FT   DISULFID     22    178
FT   DISULFID     88    192
FT   DISULFID    138    147
FT   CONFLICT    134    134       V -> A (in Ref. 1; AAA31113).
FT   CONFLICT    185    185       I -> L (in Ref. 1; AAA31113).
FT   HELIX        24     26
FT   HELIX        35     38
FT   STRAND       40     48
FT   STRAND       51     53
FT   STRAND       55     65
FT   STRAND       71     80
FT   STRAND       86     97
FT   STRAND      103    112
FT   STRAND      118    127
FT   STRAND      129    141
FT   STRAND      145    158
FT   HELIX       164    176
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
//