ID A0A4U1FP85_MONMO Unreviewed; 196 AA.
AC A0A4U1FP85;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 28-JAN-2026, entry version 24.
DE RecName: Full=Retinol-binding protein {ECO:0000256|PIRNR:PIRNR036893};
GN Name=RBP4 {ECO:0000313|Ensembl:ENSMMNP00015022893.1};
GN ORFNames=EI555_005711 {ECO:0000313|EMBL:TKC52011.1};
OS Monodon monoceros (Narwhal) (Ceratodon monodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Monodon.
OX NCBI_TaxID=40151 {ECO:0000313|EMBL:TKC52011.1, ECO:0000313|Proteomes:UP000308365};
RN [1] {ECO:0000313|Proteomes:UP000308365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=31054839; DOI=10.1016/j.isci.2019.03.023;
RA Westbury M.V., Petersen B., Garde E., Heide-Jorgensen M.P., Lorenzen E.D.;
RT "Narwhal Genome Reveals Long-Term Low Genetic Diversity despite Current
RT Large Abundance Size.";
RL IScience 15:592-599(2019).
RN [2] {ECO:0000313|EMBL:TKC52011.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MVW {ECO:0000313|EMBL:TKC52011.1};
RC TISSUE=Liver {ECO:0000313|EMBL:TKC52011.1};
RA Westbury M.V., Petersen B., Garde E., Heide-Jorgensen M.P., Lorenzen E.D.;
RT "Narwhal Genome Reveals Long-Term Low Genetic Diversity despite Current
RT Large Abundance Size.";
RL IScience 0:0-0(2019).
RN [3] {ECO:0000313|Ensembl:ENSMMNP00015022893.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAY-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 EMBL; RWIC01000041; TKC52011.1; -; Genomic_DNA.
DR RefSeq; XP_029057033.1; XM_029201200.1.
DR AlphaFoldDB; A0A4U1FP85; -.
DR Ensembl; ENSMMNT00015025158.1; ENSMMNP00015022893.1; ENSMMNG00015016831.1.
DR GeneID; 114883417; -.
DR CTD; 5950; -.
DR GeneTree; ENSGT00510000047107; -.
DR OrthoDB; 9923952at2759; -.
DR Proteomes; UP000308365; Unassembled WGS sequence.
DR Proteomes; UP000694561; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0140104; F:molecular carrier activity; IEA:Ensembl.
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 GO; GO:0048738; P:cardiac muscle tissue development; IEA:Ensembl.
DR GO; GO:0050908; P:detection of light stimulus involved in visual perception; IEA:Ensembl.
DR GO; GO:0048562; P:embryonic organ morphogenesis; IEA:Ensembl.
DR GO; GO:0060059; P:embryonic retina morphogenesis in camera-type eye; IEA:Ensembl.
DR GO; GO:0048706; P:embryonic skeletal system development; IEA:Ensembl.
DR GO; GO:0048807; P:female genitalia morphogenesis; IEA:Ensembl.
DR GO; GO:0006094; P:gluconeogenesis; IEA:Ensembl.
DR GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
DR GO; GO:0060347; P:heart trabecula formation; IEA:Ensembl.
DR GO; GO:0030324; P:lung development; IEA:Ensembl.
DR GO; GO:0030277; P:maintenance of gastrointestinal epithelium; IEA:Ensembl.
DR GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR GO; GO:0060044; P:negative regulation of cardiac muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0007603; P:phototransduction, visible light; IEA:Ensembl.
DR GO; GO:0002639; P:positive regulation of immunoglobulin production; IEA:Ensembl.
DR GO; GO:0032024; P:positive regulation of insulin secretion; IEA:Ensembl.
DR GO; GO:0032868; P:response to insulin; IEA:Ensembl.
DR GO; GO:0032526; P:response to retinoic acid; IEA:Ensembl.
DR GO; GO:0042574; P:retinal metabolic process; IEA:Ensembl.
DR GO; GO:0042572; P:retinol metabolic process; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR GO; GO:0060157; P:urinary bladder development; IEA:Ensembl.
DR GO; GO:0060065; P:uterus development; IEA:Ensembl.
DR GO; GO:0060068; P:vagina development; IEA:Ensembl.
DR GO; GO:0071939; P:vitamin A import into cell; IEA:Ensembl.
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 ECO:0000256|PIRSR:PIRSR036893-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000694561};
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|ARBA:ARBA00022448, 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_5044535890"
FT DOMAIN 39..170
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; 22610 MW; A41B6C2D031548B7 CRC64;
MQWVWALVLL AALGSARAER DCRVSSFRVK ENFDKDRFSG TWYAMAKKDP KGLFLQDNIV
AQFMNENGHM TATAKGRVRL FNSWDLCADM LGTFTDTEDP AKFKMKYWGV ASFLQKGNDD
HWIIDTDYDT YAVQYSCRLL NLDGTCADSY SFVFARDLNG FSPEVQRIVR QRQEELCLAR
QYRLIAHNGY CDGESE
//
