ID A0A2K6GTT1_PROCO Unreviewed; 187 AA.
AC A0A2K6GTT1;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 28-JAN-2026, entry version 27.
DE RecName: Full=Retinol-binding protein {ECO:0000256|PIRNR:PIRNR036893};
GN Name=RBP4 {ECO:0000313|Ensembl:ENSPCOP00000029604.1};
OS Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS coquereli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Indriidae; Propithecus.
OX NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000029604.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000029604.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSPCOP00000029604.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- FUNCTION: Retinol-binding protein that mediates retinol transport in
CC blood plasma. Delivers retinol from the liver stores to the peripheral
CC tissues. Transfers the bound all-trans retinol to STRA6, that then
CC facilitates retinol transport across the cell membrane.
CC {ECO:0000256|ARBA:ARBA00045232}.
CC -!- SUBUNIT: Interacts with TTR. Interaction with TTR prevents its loss by
CC filtration through the kidney glomeruli. Interacts with STRA6.
CC {ECO:0000256|ARBA:ARBA00046762}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613,
CC ECO:0000256|PIRNR:PIRNR036893}.
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; A0A2K6GTT1; -.
DR Ensembl; ENSPCOT00000040548.1; ENSPCOP00000029604.1; ENSPCOG00000027515.1.
DR GeneTree; ENSGT00510000047107; -.
DR Proteomes; UP000233160; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR GO; GO:0016918; F:retinal binding; IEA:UniProtKB-KW.
DR GO; GO:0019841; F:retinol binding; IEA:UniProtKB-KW.
DR GO; GO:0034632; F:retinol transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR CDD; cd00743; lipocalin_RBP_like; 1.
DR FunFam; 2.40.128.20:FF:000004; Retinol-binding protein 4; 1.
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; 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|ARBA:ARBA00023157};
KW Reference proteome {ECO:0000313|Proteomes:UP000233160};
KW Retinol-binding {ECO:0000256|ARBA:ARBA00023072};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|PIRNR:PIRNR036893};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR036893};
KW Vitamin A {ECO:0000256|ARBA:ARBA00022893}.
FT DOMAIN 25..158
FT /note="Lipocalin/cytosolic fatty-acid binding"
FT /evidence="ECO:0000259|Pfam:PF00061"
FT BINDING 102
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036893-51"
SQ SEQUENCE 187 AA; 21337 MW; DFCFE3BCEF9F9931 CRC64;
KNYSKTPAQL ALRGRRGQFG MARFAGTWYA MAKKDPEGLF LQDNIVAEFS VDENGQMSAT
AKGRVRLLNN WDVCADMVGT FTDTEDSAKF KMKYWGVASF LQKGNDDHWI IDTDYDTYAV
QYSCRLLNLD GTCADSYSFV FARDPNGLPP DVQRIVRQRQ EELCLARQYR LITHNGYCDG
KSERNIL
//
