ID G3PZ57_GASAC Unreviewed; 196 AA.
AC G3PZ57;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Retinol binding protein 4, like {ECO:0000313|Ensembl:ENSGACP00000022897.1};
OS Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000022897.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000022897.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000022897.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; G3PZ57; -.
DR Ensembl; ENSGACT00000022940.1; ENSGACP00000022897.1; ENSGACG00000017329.1.
DR GeneTree; ENSGT00510000047107; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000017329; Expressed in camera-type eye and 2 other cell types or tissues.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR036893-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000007635};
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..196
FT /evidence="ECO:0000256|PIRNR:PIRNR036893"
FT /id="PRO_5013436714"
FT DOMAIN 41..176
FT /note="Lipocalin/cytosolic fatty-acid binding"
FT /evidence="ECO:0000259|Pfam:PF00061"
FT DISULFID 24..182
FT /evidence="ECO:0000256|PIRSR:PIRSR036893-50"
FT DISULFID 90..196
FT /evidence="ECO:0000256|PIRSR:PIRSR036893-50"
FT DISULFID 142..151
FT /evidence="ECO:0000256|PIRSR:PIRSR036893-50"
SQ SEQUENCE 196 AA; 21559 MW; 0189C448EE64D30B CRC64;
MTSSKTALLL VLLSCVQHCL SASCVVDSFT VKGDFDPKRY AGKWYALQKK DPEGLFLQDN
ISAEYTIDDD GSMTASSKGR VTLFGFWVVC ADMAAQYSVP DPASPGKMFM NYQGLASYLS
SGGDNYWVID TDYDNYAITY ACRTLKEDGS CEDGYALIFS RNPRGLPPAI QRIVRQKQED
ICLAGEFQPV LQSGAC
//
