ID A0A3Q1IWK3_ANATE Unreviewed; 213 AA.
AC A0A3Q1IWK3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Purpurin-like {ECO:0000313|Ensembl:ENSATEP00000023589.1};
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:ENSATEP00000023589.1, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000023589.1}
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 AlphaFoldDB; A0A3Q1IWK3; -.
DR Ensembl; ENSATET00000023971.2; ENSATEP00000023589.1; ENSATEG00000016316.2.
DR GeneTree; ENSGT00510000047107; -.
DR InParanoid; A0A3Q1IWK3; -.
DR OMA; MMLLACV; -.
DR OrthoDB; 5342507at2759; -.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000265040};
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..213
FT /evidence="ECO:0000256|PIRNR:PIRNR036893"
FT /id="PRO_5018384078"
FT DOMAIN 40..176
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 213 AA; 23882 MW; F09889B0A6E3BFC6 CRC64;
MDFQLFALVM LFLACMEQSL ATCVVDSFTV KEDFDAKRYA GKWYALQKKD PEGLFLDDNI
SAEYTVGDDG AMVASSRGRV TLFGFWVVCA DMAAQYSVPN PSTPGKMFMD YQGLASYLSS
GGDNYWVIDT DYDHYAITYA CRTLKEDGSC EDGYALVFSR NPRGLPPAIQ RIVRQKQEEI
CMAGQFKPVL QSGTCSVFHI HLNKQMKRGS RLT
//