ID   RET4A_ONCMY             Reviewed;         176 AA.
AC   P24774; P80066;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 2.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Retinol-binding protein 4-A;
DE   AltName: Full=Plasma retinol-binding protein 1;
DE            Short=PRBP-1;
DE   AltName: Full=Plasma retinol-binding protein II;
DE            Short=PRBP-I;
GN   Name=rbp4a;
OS   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8022;
RN   [1]
RP   PROTEIN SEQUENCE, AND 3D-STRUCTURE MODELING.
RX   PubMed=1483476; DOI=10.1111/j.1432-1033.1992.tb17498.x;
RA   Zapponi M.C., Zanotti G., Stoppini M., Berni R.;
RT   "The primary structure of piscine (Oncorhynchus mykiss) retinol-binding
RT   protein and a comparison with the three-dimensional structure of mammalian
RT   retinol-binding protein.";
RL   Eur. J. Biochem. 210:937-943(1992).
RN   [2]
RP   PARTIAL PROTEIN SEQUENCE, ACETYLATION AT SER-1, AND SUBCELLULAR LOCATION.
RX   PubMed=1740159; DOI=10.1111/j.1432-1033.1992.tb16610.x;
RA   Berni R., Stoppini M., Zapponi M.C.;
RT   "The piscine plasma retinol-binding protein. Purification, partial amino
RT   acid sequence and interaction with mammalian transthyretin of rainbow trout
RT   (Oncorhynchus mykiss) retinol-binding protein.";
RL   Eur. J. Biochem. 204:99-106(1992).
CC   -!- FUNCTION: RBP 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 kidney
CC       glomeruli. {ECO:0000250|UniProtKB:P04916}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1740159}.
CC   -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC       {ECO:0000305}.
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DR   PIR; S27192; S27192.
DR   AlphaFoldDB; P24774; -.
DR   SMR; P24774; -.
DR   iPTMnet; P24774; -.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0060417; C:yolk; IDA:AgBase.
DR   GO; GO:0019841; F:retinol binding; IEA:UniProtKB-KW.
DR   GO; GO:0034632; F:retinol transmembrane transporter activity; IEA:InterPro.
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   Acetylation; Direct protein sequencing; Disulfide bond; Retinol-binding;
KW   Secreted; Transport.
FT   CHAIN           1..176
FT                   /note="Retinol-binding protein 4-A"
FT                   /id="PRO_0000201029"
FT   BINDING         97
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P27485"
FT   MOD_RES         1
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000305|PubMed:1740159"
FT   DISULFID        3..159
FT                   /evidence="ECO:0000250|UniProtKB:P02753"
FT   DISULFID        69..173
FT                   /evidence="ECO:0000250|UniProtKB:P02753"
FT   DISULFID        119..128
FT                   /evidence="ECO:0000250|UniProtKB:P02753"
SQ   SEQUENCE   176 AA;  20139 MW;  02A4F2C496CDCD49 CRC64;
     SDCQVSNIQV MQNFDRSRYT GRWYAVAKKD PVGLFLLDNV VAQFSVDESG KVTATAHGRV
     IILNNWEMCA NMFGTFEDTP DPAKFKMRYW GAASYLQTGN DDHWVIDTDY DNYAIHYSCR
     EVDLDGTCLD GYSFIFSRHP TGLRPEDQKI VTDKKKEICF LGKYRRVGHT GFCESS