ID A0A384AJK1_BALAS Unreviewed; 196 AA.
AC A0A384AJK1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 2.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Retinol-binding protein {ECO:0000256|PIRNR:PIRNR036893};
GN Name=RBP4 {ECO:0000313|RefSeq:XP_007187542.2};
OS Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS (Balaenoptera davidsoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC Balaenopteridae; Balaenoptera.
OX NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007187542.2};
RN [1] {ECO:0000313|RefSeq:XP_007187542.2}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007187542.2};
RG RefSeq;
RL Submitted (JAN-2023) to UniProtKB.
CC -!- FUNCTION: Retinol-binding protein that mediates retinol transport in
CC blood plasma. {ECO:0000256|PIRNR:PIRNR036893}.
CC -!- SUBUNIT: Interacts with TTR. {ECO:0000256|PIRNR:PIRNR036893}.
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 RefSeq; XP_007187542.2; XM_007187480.2.
DR AlphaFoldDB; A0A384AJK1; -.
DR STRING; 310752.A0A384AJK1; -.
DR KEGG; bacu:102997722; -.
DR InParanoid; A0A384AJK1; -.
DR OrthoDB; 5342507at2759; -.
DR Proteomes; UP000261681; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:UniProt.
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 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|PIRSR:PIRSR036893-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000261681};
KW Retinol-binding {ECO:0000256|ARBA:ARBA00023072};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|PIRNR:PIRNR036893};
KW Signal {ECO:0000256|PIRNR:PIRNR036893};
KW Transport {ECO:0000256|PIRNR:PIRNR036893};
KW Vitamin A {ECO:0000256|ARBA:ARBA00022893}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|PIRNR:PIRNR036893"
FT CHAIN 19..196
FT /note="Retinol-binding protein"
FT /evidence="ECO:0000256|PIRNR:PIRNR036893"
FT /id="PRO_5018824591"
FT DOMAIN 39..171
FT /note="Lipocalin/cytosolic fatty-acid binding"
FT /evidence="ECO:0000259|Pfam:PF00061"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036893-51"
FT DISULFID 22..177
FT /evidence="ECO:0000256|PIRSR:PIRSR036893-50"
FT DISULFID 87..191
FT /evidence="ECO:0000256|PIRSR:PIRSR036893-50"
FT DISULFID 137..146
FT /evidence="ECO:0000256|PIRSR:PIRSR036893-50"
SQ SEQUENCE 196 AA; 22628 MW; 625B88540933F6B9 CRC64;
MEWVWALVLL AALGSARAER DCRVSSFRVK ENFDKARFSG TWYAMAKKDP KGLFLQDNIV
AQFMNENGHM TATAKGRVRL FNNWDLCADM LGTFTDTEDP AKFKMKYWGV ASFLQKGNDD
HWIIDTDYDT YAVQYSCRLL NFDGTCADSY SFVFARDLNG FSPEVQKIVR QRQEELCLAR
QYRLIVHNGY CDGESE
//
