ID   A0A3P8TJ39_AMPPE        Unreviewed;       199 AA.
AC   A0A3P8TJ39;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   28-JAN-2026, entry version 31.
DE   RecName: Full=Plasma retinol-binding protein II {ECO:0000256|ARBA:ARBA00082024};
OS   Amphiprion percula (Orange clownfish) (Lutjanus percula).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Amphiprion.
OX   NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000024631.1, ECO:0000313|Proteomes:UP000265080};
RN   [1] {ECO:0000313|Ensembl:ENSAPEP00000024631.1, ECO:0000313|Proteomes:UP000265080}
RP   NUCLEOTIDE SEQUENCE.
RA   Lehmann R.;
RT   "Finding Nemo's genes: A chromosome-scale reference assembly of the genome
RT   of the orange clownfish Amphiprion percula.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSAPEP00000024631.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [3] {ECO:0000313|Ensembl:ENSAPEP00000024631.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2025) to UniProtKB.
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:0000256|ARBA:ARBA00054865}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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   AlphaFoldDB; A0A3P8TJ39; -.
DR   STRING; 161767.ENSAPEP00000024631; -.
DR   Ensembl; ENSAPET00000025278.1; ENSAPEP00000024631.1; ENSAPEG00000017510.1.
DR   GeneTree; ENSGT00510000047107; -.
DR   OMA; KYWGMAS; -.
DR   Proteomes; UP000265080; Chromosome 19.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-ARBA.
DR   GO; GO:0060417; C:yolk; IEA:UniProtKB-ARBA.
DR   GO; GO:0019841; F:retinol binding; IEA:UniProtKB-KW.
DR   GO; GO:0034632; F:retinol transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0001889; P:liver development; IEA:Ensembl.
DR   GO; GO:0032526; P:response to retinoic acid; IEA:Ensembl.
DR   FunFam; 2.40.128.20:FF:000004; Retinol-binding protein 4; 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; PR01174; RETINOLBNDNG.
DR   SUPFAM; SSF50814; Lipocalins; 1.
DR   PROSITE; PS00213; LIPOCALIN; 1.
PE   3: Inferred from homology;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR036893-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265080};
KW   Retinol-binding {ECO:0000256|ARBA:ARBA00023072};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|PIRNR:PIRNR036893};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|PIRNR:PIRNR036893"
FT   CHAIN           17..199
FT                   /note="Plasma retinol-binding protein II"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR036893"
FT                   /id="PRO_5017856638"
FT   DOMAIN          36..158
FT                   /note="Lipocalin/cytosolic fatty-acid binding"
FT                   /evidence="ECO:0000259|Pfam:PF00061"
FT   BINDING         113
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036893-51"
FT   DISULFID        19..175
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036893-50"
FT   DISULFID        85..189
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036893-50"
FT   DISULFID        135..144
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036893-50"
SQ   SEQUENCE   199 AA;  22502 MW;  1FA616920E4D7A25 CRC64;
     MLRNVVALCL LAMSWAQDCQ VANIQVMQNF DRTRYAGTWY AVGKKDPEGL FLLDNIVANL
     NIGEDGKMTA TAEGRVIILN NWEMCAHMLA TFEDTPDPAK FKMKYWGAAA YLQTGNDDHW
     VIDTDYDNYA VHYSCRLVDS DGTCLDSYSF IFSRHPTGLR PEDQAIVTQR KTELCLLGKY
     RRVPHSGFCQ NSGSVDQPQ
//