ID A0A3Q3BIN0_KRYMA Unreviewed; 197 AA.
AC A0A3Q3BIN0;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Retinol binding protein 4 {ECO:0000313|Ensembl:ENSKMAP00000024659.1};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000024659.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000024659.1}
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|PIRNR:PIRNR036893,
CC ECO:0000256|RuleBase:RU003695}.
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DR RefSeq; XP_017291988.1; XM_017436499.1.
DR AlphaFoldDB; A0A3Q3BIN0; -.
DR STRING; 37003.ENSKMAP00000024659; -.
DR Ensembl; ENSKMAT00000024967.1; ENSKMAP00000024659.1; ENSKMAG00000018276.1.
DR GeneID; 108248035; -.
DR KEGG; kmr:108248035; -.
DR CTD; 5950; -.
DR GeneTree; ENSGT00510000047107; -.
DR OMA; KYWGMAS; -.
DR OrthoDB; 5342507at2759; -.
DR Proteomes; UP000264800; 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:UP000264800};
KW Retinol-binding {ECO:0000256|ARBA:ARBA00023072};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|PIRNR:PIRNR036893}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|PIRNR:PIRNR036893"
FT CHAIN 17..197
FT /evidence="ECO:0000256|PIRNR:PIRNR036893"
FT /id="PRO_5018383880"
FT DOMAIN 36..159
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 197 AA; 22392 MW; 1DB8910B29125333 CRC64;
MLRFAVALCL LALSLAQECQ VANIQVMQNF TKTRYAGTWY AVGKKDPEGL FLLDNVVAQF
TIDSDLKMTA TAKGRVIILN NWEMCAHMFA TFEETPEPAK FRMNYWGAAS YLQTGNDEHW
VIDTDYDNYA IHYSCRVVDS DSTCLDSYSF IFSRHPTGLR PEDQAIVTQK KMELCLLGKY
RRVAHNGFCE NSGSIQP
//
