RET5_HUMAN
ID RET5_HUMAN Reviewed; 135 AA.
AC P82980; Q53FB1;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Retinol-binding protein 5;
DE AltName: Full=Cellular retinol-binding protein III;
DE Short=CRBP-III;
DE AltName: Full=HRBPiso;
GN Name=RBP5;
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], X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS),
RP FUNCTION, AND 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RA Li Y., Wu T., Xu S., Ren S., Chen Z., Han Z.;
RT "A novel gene expressed in human liver non-tumor tissues.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-115.
RC TISSUE=Small intestine;
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], AND VARIANT LEU-115.
RC TISSUE=Spleen;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [6]
RP TISSUE SPECIFICITY.
RX PubMed=17497168; DOI=10.1007/s00432-007-0230-0;
RA Ho J.C.Y., Cheung S.T., Poon W.S., Lee Y.T., Ng I.O.L., Fan S.T.;
RT "Down-regulation of retinol binding protein 5 is associated with aggressive
RT tumor features in hepatocellular carcinoma.";
RL J. Cancer Res. Clin. Oncol. 133:929-936(2007).
RN [7]
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).
CC -!- FUNCTION: Intracellular transport of retinol.
CC {ECO:0000269|PubMed:11274389}.
CC -!- INTERACTION:
CC P82980; O95994: AGR2; NbExp=3; IntAct=EBI-3941274, EBI-712648;
CC P82980; O95273: CCNDBP1; NbExp=3; IntAct=EBI-3941274, EBI-748961;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Higher expression in adult kidney and liver and to
CC a lesser extent in adult and fetal spleen, adult lymph nodes and
CC appendix, and fetal liver and kidney. Strongly decreased in
CC hepatocellular carcinoma tissues (at protein level).
CC {ECO:0000269|PubMed:11274389, ECO:0000269|PubMed:17497168}.
CC -!- DOMAIN: Forms a beta-barrel structure that accommodates hydrophobic
CC ligands in its interior.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC protein (FABP) family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY007436; AAG09617.1; -; mRNA.
DR EMBL; AF212239; AAK14925.1; -; mRNA.
DR EMBL; AK311977; BAG34916.1; -; mRNA.
DR EMBL; AK223378; BAD97098.1; -; mRNA.
DR EMBL; BC029355; AAH29355.1; -; mRNA.
DR CCDS; CCDS8574.1; -.
DR RefSeq; NP_113679.1; NM_031491.3.
DR PDB; 1GGL; X-ray; 2.31 A; A/B=2-134.
DR PDB; 6E5W; X-ray; 2.50 A; A/B/C/D=1-135.
DR PDBsum; 1GGL; -.
DR PDBsum; 6E5W; -.
DR AlphaFoldDB; P82980; -.
DR SMR; P82980; -.
DR BioGRID; 123759; 8.
DR IntAct; P82980; 4.
DR STRING; 9606.ENSP00000266560; -.
DR DrugBank; DB06755; Beta carotene.
DR DrugBank; DB00162; Vitamin A.
DR DrugCentral; P82980; -.
DR SwissLipids; SLP:000001526; -.
DR BioMuta; RBP5; -.
DR DMDM; 14916691; -.
DR jPOST; P82980; -.
DR MassIVE; P82980; -.
DR PaxDb; P82980; -.
DR PeptideAtlas; P82980; -.
DR PRIDE; P82980; -.
DR ProteomicsDB; 57727; -.
DR TopDownProteomics; P82980; -.
DR Antibodypedia; 22880; 199 antibodies from 27 providers.
DR DNASU; 83758; -.
DR Ensembl; ENST00000266560.8; ENSP00000266560.3; ENSG00000139194.8.
DR Ensembl; ENST00000673093.1; ENSP00000500050.1; ENSG00000288369.1.
DR GeneID; 83758; -.
DR KEGG; hsa:83758; -.
DR MANE-Select; ENST00000266560.8; ENSP00000266560.3; NM_031491.4; NP_113679.1.
DR UCSC; uc001qsq.4; human.
DR CTD; 83758; -.
DR DisGeNET; 83758; -.
DR GeneCards; RBP5; -.
DR HGNC; HGNC:15847; RBP5.
DR HPA; ENSG00000139194; Tissue enhanced (kidney, liver).
DR MIM; 611866; gene.
DR neXtProt; NX_P82980; -.
DR OpenTargets; ENSG00000139194; -.
DR PharmGKB; PA164742366; -.
DR VEuPathDB; HostDB:ENSG00000139194; -.
DR eggNOG; KOG4015; Eukaryota.
DR GeneTree; ENSGT00940000162526; -.
DR HOGENOM; CLU_113772_5_1_1; -.
DR InParanoid; P82980; -.
DR OMA; HWLEGDR; -.
DR OrthoDB; 1377380at2759; -.
DR PhylomeDB; P82980; -.
DR TreeFam; TF316894; -.
DR PathwayCommons; P82980; -.
DR SignaLink; P82980; -.
DR BioGRID-ORCS; 83758; 14 hits in 1076 CRISPR screens.
DR ChiTaRS; RBP5; human.
DR EvolutionaryTrace; P82980; -.
DR GenomeRNAi; 83758; -.
DR Pharos; P82980; Tbio.
DR PRO; PR:P82980; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P82980; protein.
DR Bgee; ENSG00000139194; Expressed in adult mammalian kidney and 98 other tissues.
DR ExpressionAtlas; P82980; baseline and differential.
DR Genevisible; P82980; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:UniProtKB.
DR GO; GO:0019841; F:retinol binding; IEA:UniProtKB-KW.
DR GO; GO:0015908; P:fatty acid transport; IBA:GO_Central.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR031270; CRBP-III.
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:SF74; PTHR11955:SF74; 1.
DR Pfam; PF00061; Lipocalin; 1.
DR PRINTS; PR00178; FATTYACIDBP.
DR SUPFAM; SSF50814; SSF50814; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Reference proteome; Retinol-binding; Transport;
KW Vitamin A.
FT CHAIN 1..135
FT /note="Retinol-binding protein 5"
FT /id="PRO_0000067400"
FT VARIANT 19
FT /note="D -> N (in dbSNP:rs10963)"
FT /id="VAR_049013"
FT VARIANT 70
FT /note="E -> Q (in dbSNP:rs7969705)"
FT /id="VAR_034445"
FT VARIANT 115
FT /note="M -> L (in dbSNP:rs2290237)"
FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.4"
FT /id="VAR_034446"
FT STRAND 7..15
FT /evidence="ECO:0007829|PDB:1GGL"
FT HELIX 17..23
FT /evidence="ECO:0007829|PDB:1GGL"
FT TURN 28..33
FT /evidence="ECO:0007829|PDB:1GGL"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:1GGL"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:1GGL"
FT STRAND 47..55
FT /evidence="ECO:0007829|PDB:1GGL"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:1GGL"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:1GGL"
FT TURN 76..79
FT /evidence="ECO:0007829|PDB:1GGL"
FT STRAND 82..89
FT /evidence="ECO:0007829|PDB:1GGL"
FT STRAND 91..102
FT /evidence="ECO:0007829|PDB:1GGL"
FT STRAND 106..112
FT /evidence="ECO:0007829|PDB:1GGL"
FT STRAND 115..122
FT /evidence="ECO:0007829|PDB:1GGL"
FT STRAND 125..133
FT /evidence="ECO:0007829|PDB:1GGL"
SQ SEQUENCE 135 AA; 15931 MW; B9D059DCCC0A88ED CRC64;
MPPNLTGYYR FVSQKNMEDY LQALNISLAV RKIALLLKPD KEIEHQGNHM TVRTLSTFRN
YTVQFDVGVE FEEDLRSVDG RKCQTIVTWE EEHLVCVQKG EVPNRGWRHW LEGEMLYLEL
TARDAVCEQV FRKVR
