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Database: UniProt
Entry: A0A3B3VL20_9TELE
LinkDB: A0A3B3VL20_9TELE
Original site: A0A3B3VL20_9TELE 
ID   A0A3B3VL20_9TELE        Unreviewed;       195 AA.
AC   A0A3B3VL20;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Purpurin-like {ECO:0000313|Ensembl:ENSPLAP00000026500.1};
OS   Poecilia latipinna (sailfin molly).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000026500.1, ECO:0000313|Proteomes:UP000261500};
RN   [1] {ECO:0000313|Ensembl:ENSPLAP00000026500.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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_014883639.1; XM_015028153.1.
DR   AlphaFoldDB; A0A3B3VL20; -.
DR   Ensembl; ENSPLAT00000018566.1; ENSPLAP00000026500.1; ENSPLAG00000014357.1.
DR   GeneID; 106944867; -.
DR   KEGG; plai:106944867; -.
DR   GeneTree; ENSGT00510000047107; -.
DR   OrthoDB; 5342507at2759; -.
DR   Proteomes; UP000261500; 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   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:SF1; PURPURIN; 1.
DR   PANTHER; PTHR11873; RETINOL-BINDING PROTEIN 4; 1.
DR   Pfam; PF00061; Lipocalin; 1.
DR   PIRSF; PIRSF036893; Lipocalin_ApoD; 1.
DR   PRINTS; PR00179; LIPOCALIN.
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   Retinol-binding {ECO:0000256|ARBA:ARBA00023072};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|PIRNR:PIRNR036893}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|PIRNR:PIRNR036893"
FT   CHAIN           22..195
FT                   /evidence="ECO:0000256|PIRNR:PIRNR036893"
FT                   /id="PRO_5017106883"
FT   DOMAIN          40..175
FT                   /note="Lipocalin/cytosolic fatty-acid binding"
FT                   /evidence="ECO:0000259|Pfam:PF00061"
FT   DISULFID        23..181
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036893-50"
FT   DISULFID        89..195
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036893-50"
FT   DISULFID        141..150
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036893-50"
SQ   SEQUENCE   195 AA;  21803 MW;  379AA5EBF493803B CRC64;
     MDFQLFGLMM LFLACVEQSL ASCVVDRFTV KQDFDPQRYA GKWYALQKKD PEGLFLQDNI
     SAEYTVGDDG SMVASSRGRV TLFGFWVVCA DMAAQYSVPD PNTPGKMFMN YQGLASYLSS
     GGDNYWVIDT DYDNYAITYA CRTLKEDGSC EDGYALVFSR NPRGLPPAIQ RVVRQKQEEI
     CMAGQFQPVL QSGAC
//
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