ID   A0A3Q1JCW1_ANATE        Unreviewed;       257 AA.
AC   A0A3Q1JCW1;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Retinol binding protein 4, plasma {ECO:0000313|Ensembl:ENSATEP00000030825.1};
OS   Anabas testudineus (Climbing perch) (Anthias testudineus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX   NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000030825.1, ECO:0000313|Proteomes:UP000265040};
RN   [1] {ECO:0000313|Ensembl:ENSATEP00000030825.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC       {ECO:0000256|ARBA:ARBA00006889, ECO:0000256|RuleBase:RU003695}.
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DR   AlphaFoldDB; A0A3Q1JCW1; -.
DR   STRING; 64144.ENSATEP00000030825; -.
DR   Ensembl; ENSATET00000031287.2; ENSATEP00000030825.1; ENSATEG00000021293.2.
DR   GeneTree; ENSGT00510000047107; -.
DR   InParanoid; A0A3Q1JCW1; -.
DR   OMA; NIKTMEN; -.
DR   Proteomes; UP000265040; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProt.
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   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   Disulfide bond {ECO:0000256|PIRSR:PIRSR036893-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265040};
KW   Retinol-binding {ECO:0000256|ARBA:ARBA00023072};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          96..216
FT                   /note="Lipocalin/cytosolic fatty-acid binding"
FT                   /evidence="ECO:0000259|Pfam:PF00061"
FT   BINDING         172
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036893-51"
FT   DISULFID        79..234
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036893-50"
FT   DISULFID        144..248
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036893-50"
FT   DISULFID        194..203
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036893-50"
SQ   SEQUENCE   257 AA;  28976 MW;  FF63E946C3487E93 CRC64;
     MQMFVQWKAS CGKSMGGTGL QKSLCKSSGV YIRPKPDRKP EDLCDLPASF CTSFSFLCGK
     MLRCVVALCL LGLSWAQDCQ VANIKTMENF DKTRYAGTWY AVGKKDPEGL FLIDNIVAQF
     TIEGDQMTAK AVGRVNILNN WELCAEMFGT FESTIDPAKF KMKYWGIASY LQSGNDDHWV
     VDTDYDNYAI HYSCRLVDSD GTCLDSYSLI FSRHPTGLRP EDQPIVTQKK MDLCLLGKYR
     RVAHTGYCPN NGFINFQ
//