RET1_HUMAN
ID RET1_HUMAN Reviewed; 135 AA.
AC P09455; A8K2Q0; B7Z7A0; E7EWV0; F2Z2F2; Q6FGX8;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Retinol-binding protein 1;
DE AltName: Full=Cellular retinol-binding protein;
DE Short=CRBP;
DE AltName: Full=Cellular retinol-binding protein I;
DE Short=CRBP-I;
GN Name=RBP1; Synonyms=CRBP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2992469; DOI=10.1016/0006-291x(85)90435-8;
RA Colantuoni V., Cortese R., Nilsson M., Lundvall J., Baavik C.-O.,
RA Eriksson U., Peterson P.A., Sundelin J.;
RT "Cloning and sequencing of a full length cDNA corresponding to human
RT cellular retinol-binding protein.";
RL Biochem. Biophys. Res. Commun. 130:431-439(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3356192; DOI=10.1111/j.1432-1033.1988.tb13963.x;
RA Nilsson M.H.L., Spurr N.K., Lundvall J., Rask L., Peterson P.A.;
RT "Human cellular retinol-binding protein gene organization and chromosomal
RT location.";
RL Eur. J. Biochem. 173:35-44(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Esophagus, Heart, and Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-121 (ISOFORM 1).
RX PubMed=2856408; DOI=10.1210/mend-1-8-526;
RA Wei L.-N., Mertz J.R., Goodman D.S., Nguyen-Huu M.C.;
RT "Cellular retinoic acid- and cellular retinol-binding proteins:
RT complementary deoxyribonucleic acid cloning, chromosomal assignment, and
RT tissue specific expression.";
RL Mol. Endocrinol. 1:526-534(1987).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=11274389; DOI=10.1073/pnas.061455898;
RA Folli C., Calderone V., Ottonello S., Bolchi A., Zanotti G., Stoppini M.,
RA Berni R.;
RT "Identification, retinoid binding and X-ray analysis of a human retinol-
RT binding protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3710-3715(2001).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LEU-30 AND ARG-59.
RX PubMed=15632377; DOI=10.1093/jnci/dji004;
RA Farias E.F., Ong D.E., Ghyselinck N.B., Nakajo S., Kuppumbatti Y.S.,
RA Mira y Lopez R.;
RT "Cellular retinol-binding protein I, a regulator of breast epithelial
RT retinoic acid receptor activity, cell differentiation, and
RT tumorigenicity.";
RL J. Natl. Cancer Inst. 97:21-29(2005).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP FUNCTION, INTERACTION WITH STRA6, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP ARG-22; ARG-31 AND LYS-32.
RX PubMed=22665496; DOI=10.1128/mcb.00505-12;
RA Berry D.C., O'Byrne S.M., Vreeland A.C., Blaner W.S., Noy N.;
RT "Cross talk between signaling and vitamin A transport by the retinol-
RT binding protein receptor STRA6.";
RL Mol. Cell. Biol. 32:3164-3175(2012).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-9 (ISOFORMS 2 AND 3), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [14] {ECO:0007744|PDB:5H8T, ECO:0007744|PDB:5H9A, ECO:0007744|PDB:5HA1, ECO:0007744|PDB:5HBS}
RP X-RAY CRYSTALLOGRAPHY (0.89 ANGSTROMS) IN COMPLEX WITH ALL-TRANS-RETINOL,
RP FUNCTION, AND DOMAIN.
RX PubMed=26900151; DOI=10.1074/jbc.m116.714535;
RA Silvaroli J.A., Arne J.M., Chelstowska S., Kiser P.D., Banerjee S.,
RA Golczak M.;
RT "Ligand Binding Induces Conformational Changes in Human Cellular Retinol-
RT binding Protein 1 (CRBP1) Revealed by Atomic Resolution Crystal
RT Structures.";
RL J. Biol. Chem. 291:8528-8540(2016).
RN [15] {ECO:0007744|PDB:5LJB, ECO:0007744|PDB:5LJC, ECO:0007744|PDB:5LJD, ECO:0007744|PDB:5LJE, ECO:0007744|PDB:5LJG, ECO:0007744|PDB:5LJH, ECO:0007744|PDB:5LJK}
RP X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) IN COMPLEX WITH ALL-TRANS-RETINOL,
RP FUNCTION, DOMAIN, AND MUTAGENESIS OF LYS-41 AND GLN-109.
RX PubMed=28057518; DOI=10.1016/j.jsb.2016.12.012;
RA Menozzi I., Vallese F., Polverini E., Folli C., Berni R., Zanotti G.;
RT "Structural and molecular determinants affecting the interaction of retinol
RT with human CRBP1.";
RL J. Struct. Biol. 197:330-339(2017).
CC -!- FUNCTION: Cytoplasmic retinol-binding protein (PubMed:22665496,
CC PubMed:26900151, PubMed:28057518). Accepts retinol from the transport
CC protein STRA6, and thereby contributes to retinol uptake, storage and
CC retinoid homeostasis (PubMed:15632377, PubMed:22665496).
CC {ECO:0000269|PubMed:15632377, ECO:0000269|PubMed:22665496,
CC ECO:0000269|PubMed:26900151, ECO:0000269|PubMed:28057518}.
CC -!- SUBUNIT: Interacts (only as retinol-free apoprotein) with STRA6.
CC {ECO:0000269|PubMed:22665496}.
CC -!- INTERACTION:
CC P09455; P49366: DHPS; NbExp=3; IntAct=EBI-2623483, EBI-741925;
CC P09455; Q9UBN6: TNFRSF10D; NbExp=3; IntAct=EBI-2623483, EBI-1044859;
CC P09455; Q6DKK2: TTC19; NbExp=3; IntAct=EBI-2623483, EBI-948354;
CC P09455; Q8N2K1: UBE2J2; NbExp=3; IntAct=EBI-2623483, EBI-2340110;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:22665496}. Lipid
CC droplet {ECO:0000269|PubMed:15632377}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P09455-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P09455-2; Sequence=VSP_046201, VSP_046202;
CC Name=3;
CC IsoId=P09455-3; Sequence=VSP_046201, VSP_046203;
CC -!- TISSUE SPECIFICITY: Detected in nearly all the tissues with higher
CC expression in adult ovary, pancreas, pituitary gland and adrenal gland,
CC and fetal liver. {ECO:0000269|PubMed:11274389}.
CC -!- DOMAIN: Forms a beta-barrel structure that accommodates hydrophobic
CC ligands in its interior. {ECO:0000269|PubMed:26900151,
CC ECO:0000269|PubMed:28057518}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC protein (FABP) family. {ECO:0000305}.
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DR EMBL; M11433; AAA60257.1; -; mRNA.
DR EMBL; X07437; CAA30318.1; -; Genomic_DNA.
DR EMBL; X07438; CAA30318.1; JOINED; Genomic_DNA.
DR EMBL; AK290315; BAF83004.1; -; mRNA.
DR EMBL; AK301684; BAH13536.1; -; mRNA.
DR EMBL; AK309492; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR541979; CAG46776.1; -; mRNA.
DR EMBL; CR542005; CAG46802.1; -; mRNA.
DR EMBL; AC046134; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC121052; AAI21053.1; -; mRNA.
DR EMBL; M36809; AAA35714.1; -; mRNA.
DR CCDS; CCDS46925.1; -. [P09455-2]
DR CCDS; CCDS46926.1; -. [P09455-3]
DR PIR; S00399; RJHUO.
DR RefSeq; NP_001124464.1; NM_001130992.1. [P09455-3]
DR RefSeq; NP_001124465.1; NM_001130993.1. [P09455-2]
DR RefSeq; NP_002890.2; NM_002899.3.
DR PDB; 5H8T; X-ray; 1.21 A; A=2-135.
DR PDB; 5H9A; X-ray; 1.38 A; A=2-135.
DR PDB; 5HA1; X-ray; 1.35 A; A=2-135.
DR PDB; 5HBS; X-ray; 0.89 A; A=2-135.
DR PDB; 5LJB; X-ray; 1.26 A; A=1-135.
DR PDB; 5LJC; X-ray; 1.43 A; A=1-135.
DR PDB; 5LJD; X-ray; 1.61 A; A=1-135.
DR PDB; 5LJE; X-ray; 1.40 A; A=1-135.
DR PDB; 5LJG; X-ray; 1.15 A; A=1-135.
DR PDB; 5LJH; X-ray; 1.52 A; A=1-135.
DR PDB; 5LJK; X-ray; 1.70 A; A=1-135.
DR PDB; 6E5L; X-ray; 1.17 A; A=2-135.
DR PDB; 6E5T; X-ray; 1.55 A; A=2-135.
DR PDB; 6E6M; X-ray; 1.55 A; A/B/C=2-135.
DR PDBsum; 5H8T; -.
DR PDBsum; 5H9A; -.
DR PDBsum; 5HA1; -.
DR PDBsum; 5HBS; -.
DR PDBsum; 5LJB; -.
DR PDBsum; 5LJC; -.
DR PDBsum; 5LJD; -.
DR PDBsum; 5LJE; -.
DR PDBsum; 5LJG; -.
DR PDBsum; 5LJH; -.
DR PDBsum; 5LJK; -.
DR PDBsum; 6E5L; -.
DR PDBsum; 6E5T; -.
DR PDBsum; 6E6M; -.
DR AlphaFoldDB; P09455; -.
DR SMR; P09455; -.
DR BioGRID; 111881; 28.
DR IntAct; P09455; 10.
DR MINT; P09455; -.
DR STRING; 9606.ENSP00000232219; -.
DR DrugBank; DB00459; Acitretin.
DR DrugBank; DB06755; Beta carotene.
DR DrugBank; DB00162; Vitamin A.
DR DrugCentral; P09455; -.
DR iPTMnet; P09455; -.
DR PhosphoSitePlus; P09455; -.
DR BioMuta; RBP1; -.
DR DMDM; 132387; -.
DR EPD; P09455; -.
DR jPOST; P09455; -.
DR MassIVE; P09455; -.
DR MaxQB; P09455; -.
DR PaxDb; P09455; -.
DR PeptideAtlas; P09455; -.
DR PRIDE; P09455; -.
DR ProteomicsDB; 18915; -.
DR ProteomicsDB; 23698; -.
DR ProteomicsDB; 52219; -. [P09455-1]
DR Antibodypedia; 17981; 497 antibodies from 36 providers.
DR DNASU; 5947; -.
DR Ensembl; ENST00000492918.1; ENSP00000429166.1; ENSG00000114115.10. [P09455-3]
DR Ensembl; ENST00000617459.4; ENSP00000477621.1; ENSG00000114115.10. [P09455-2]
DR Ensembl; ENST00000619087.4; ENSP00000482165.1; ENSG00000114115.10. [P09455-1]
DR GeneID; 5947; -.
DR KEGG; hsa:5947; -.
DR UCSC; uc011bmx.2; human. [P09455-1]
DR CTD; 5947; -.
DR DisGeNET; 5947; -.
DR GeneCards; RBP1; -.
DR HGNC; HGNC:9919; RBP1.
DR HPA; ENSG00000114115; Tissue enhanced (ovary, pancreas).
DR MIM; 180260; gene.
DR neXtProt; NX_P09455; -.
DR OpenTargets; ENSG00000114115; -.
DR PharmGKB; PA34286; -.
DR VEuPathDB; HostDB:ENSG00000114115; -.
DR eggNOG; KOG4015; Eukaryota.
DR GeneTree; ENSGT00940000159675; -.
DR HOGENOM; CLU_113772_5_1_1; -.
DR InParanoid; P09455; -.
DR OrthoDB; 1377380at2759; -.
DR PhylomeDB; P09455; -.
DR TreeFam; TF316894; -.
DR BioCyc; MetaCyc:ENSG00000114115-MON; -.
DR PathwayCommons; P09455; -.
DR Reactome; R-HSA-2453864; Retinoid cycle disease events.
DR Reactome; R-HSA-2453902; The canonical retinoid cycle in rods (twilight vision).
DR Reactome; R-HSA-975634; Retinoid metabolism and transport.
DR SignaLink; P09455; -.
DR SIGNOR; P09455; -.
DR BioGRID-ORCS; 5947; 11 hits in 1077 CRISPR screens.
DR ChiTaRS; RBP1; human.
DR GeneWiki; RBP1; -.
DR GenomeRNAi; 5947; -.
DR Pharos; P09455; Tbio.
DR PRO; PR:P09455; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P09455; protein.
DR Bgee; ENSG00000114115; Expressed in pigmented layer of retina and 182 other tissues.
DR ExpressionAtlas; P09455; baseline and differential.
DR Genevisible; P09455; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005811; C:lipid droplet; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:1904768; F:all-trans-retinol binding; IDA:UniProtKB.
DR GO; GO:0005504; F:fatty acid binding; IBA:GO_Central.
DR GO; GO:0016918; F:retinal binding; IEA:UniProtKB-KW.
DR GO; GO:0005501; F:retinoid binding; TAS:ProtInc.
DR GO; GO:0015908; P:fatty acid transport; IBA:GO_Central.
DR GO; GO:0055088; P:lipid homeostasis; IMP:UniProtKB.
DR GO; GO:0002138; P:retinoic acid biosynthetic process; IEA:InterPro.
DR GO; GO:0006776; P:vitamin A metabolic process; IMP:UniProtKB.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR031264; CRBP1.
DR InterPro; IPR000463; Fatty_acid-bd.
DR InterPro; IPR031259; ILBP.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR PANTHER; PTHR11955; PTHR11955; 1.
DR PANTHER; PTHR11955:SF56; PTHR11955:SF56; 1.
DR Pfam; PF00061; Lipocalin; 1.
DR PRINTS; PR00178; FATTYACIDBP.
DR SUPFAM; SSF50814; SSF50814; 1.
DR PROSITE; PS00214; FABP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Lipid droplet; Methylation;
KW Reference proteome; Retinol-binding; Transport; Vitamin A.
FT CHAIN 1..135
FT /note="Retinol-binding protein 1"
FT /id="PRO_0000067392"
FT REGION 22..32
FT /note="Important for interaction with STRA6"
FT /evidence="ECO:0000269|PubMed:22665496"
FT BINDING 41
FT /ligand="all-trans-retinol"
FT /ligand_id="ChEBI:CHEBI:17336"
FT /evidence="ECO:0000269|PubMed:26900151,
FT ECO:0007744|PDB:5H8T, ECO:0007744|PDB:5HBS,
FT ECO:0007744|PDB:5LJB, ECO:0007744|PDB:5LJC"
FT BINDING 63
FT /ligand="all-trans-retinol"
FT /ligand_id="ChEBI:CHEBI:17336"
FT /evidence="ECO:0000269|PubMed:28057518,
FT ECO:0007744|PDB:5LJC, ECO:0007744|PDB:5LJE"
FT BINDING 109
FT /ligand="all-trans-retinol"
FT /ligand_id="ChEBI:CHEBI:17336"
FT /evidence="ECO:0000269|PubMed:26900151,
FT ECO:0000269|PubMed:28057518, ECO:0007744|PDB:5H8T,
FT ECO:0007744|PDB:5HBS, ECO:0007744|PDB:5LJB,
FT ECO:0007744|PDB:5LJC, ECO:0007744|PDB:5LJD,
FT ECO:0007744|PDB:5LJE"
FT VAR_SEQ 1
FT /note="M -> MDPPAGFVRAGNPAVAAPQSPLSPEGAHFRAAHHPRSTGSRCPGSLQ
FT PSRPLVANWLQSLPEM (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046201"
FT VAR_SEQ 85..135
FT /note="TTVSWDGDKLQCVQKGEKEGRGWTQWIEGDELHLEMRVEGVVCKQVFKKVQ
FT -> SETGFSS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046202"
FT VAR_SEQ 85..135
FT /note="TTVSWDGDKLQCVQKGEKEGRGWTQWIEGDELHLEMRVEGVVCKQVFKKVQ
FT -> AGVQSRDLSSL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046203"
FT MUTAGEN 22
FT /note="R->A: No effect on retinol binding. Abolishes
FT interaction with STA6 and the ability to enhance STA6-
FT mediated vitamin A uptake."
FT /evidence="ECO:0000269|PubMed:28057518"
FT MUTAGEN 30
FT /note="L->A: Decreases cellular retinol uptake and impairs
FT retinol storage."
FT /evidence="ECO:0000269|PubMed:15632377"
FT MUTAGEN 31
FT /note="R->A: No effect on retinol binding. Abolishes
FT interaction with STA6 and the ability to enhance STA6-
FT mediated vitamin A uptake."
FT /evidence="ECO:0000269|PubMed:28057518"
FT MUTAGEN 32
FT /note="K->A: No effect on retinol binding. Abolishes
FT interaction with STA6 and the ability to enhance STA6-
FT mediated vitamin A uptake."
FT /evidence="ECO:0000269|PubMed:28057518"
FT MUTAGEN 41
FT /note="K->L: Strongly decreased affinity for retinol.
FT Further decrease in affinity for retinol; when associated
FT with L-109."
FT /evidence="ECO:0000269|PubMed:28057518"
FT MUTAGEN 59
FT /note="R->E: Decreases cellular retinol uptake and impairs
FT retinol storage."
FT /evidence="ECO:0000269|PubMed:15632377"
FT MUTAGEN 109
FT /note="Q->L: Strongly decreased affinity for retinol.
FT Further decrease in for retinol; when associated with L-
FT 41."
FT /evidence="ECO:0000269|PubMed:28057518"
FT STRAND 7..16
FT /evidence="ECO:0007829|PDB:5HBS"
FT HELIX 17..23
FT /evidence="ECO:0007829|PDB:5HBS"
FT HELIX 28..34
FT /evidence="ECO:0007829|PDB:5HBS"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:5HBS"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:5HBS"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:5HBS"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:5HBS"
FT TURN 76..79
FT /evidence="ECO:0007829|PDB:5HBS"
FT STRAND 82..90
FT /evidence="ECO:0007829|PDB:5HBS"
FT STRAND 93..102
FT /evidence="ECO:0007829|PDB:5HBS"
FT STRAND 106..112
FT /evidence="ECO:0007829|PDB:5HBS"
FT STRAND 115..122
FT /evidence="ECO:0007829|PDB:5HBS"
FT STRAND 125..134
FT /evidence="ECO:0007829|PDB:5HBS"
FT MOD_RES P09455-2:9
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CONFLICT P09455-2:18
FT /note="P -> L (in Ref. 3; BAH13536)"
FT /evidence="ECO:0000305"
FT MOD_RES P09455-3:9
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
SQ SEQUENCE 135 AA; 15850 MW; FA47545761AFA3A2 CRC64;
MPVDFTGYWK MLVNENFEEY LRALDVNVAL RKIANLLKPD KEIVQDGDHM IIRTLSTFRN
YIMDFQVGKE FEEDLTGIDD RKCMTTVSWD GDKLQCVQKG EKEGRGWTQW IEGDELHLEM
RVEGVVCKQV FKKVQ
