RET2_HUMAN
ID RET2_HUMAN Reviewed; 134 AA.
AC P50120; A8K7G3; Q6ISQ9; Q6ISS7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Retinol-binding protein 2;
DE AltName: Full=Cellular retinol-binding protein II;
DE Short=CRBP-II;
GN Name=RBP2; Synonyms=CRBP2;
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].
RX PubMed=7657783; DOI=10.1093/oxfordjournals.humrep.a136137;
RA Loughney A.D., Kumarendran M.K., Thomas E.J., Redfern C.P.F.;
RT "Variation in the expression of cellular retinoid binding proteins in human
RT endometrium throughout the menstrual cycle.";
RL Hum. Reprod. 10:1297-1304(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
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 [6] {ECO:0007744|PDB:2RCQ, ECO:0007744|PDB:2RCT}
RP X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) IN COMPLEX WITH ALL-TRANS-RETINOL.
RX PubMed=18076076; DOI=10.1002/prot.21848;
RA Tarter M., Capaldi S., Carrizo M.E., Ambrosi E., Perduca M., Monaco H.L.;
RT "Crystal structure of human cellular retinol-binding protein II to 1.2 A
RT resolution.";
RL Proteins 70:1626-1630(2008).
CC -!- FUNCTION: Intracellular transport of retinol.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Higher expression in adult small intestine and to a
CC much lesser extent in fetal kidney. {ECO:0000269|PubMed:11274389}.
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}.
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DR EMBL; U13831; AAC50162.1; -; mRNA.
DR EMBL; AK291978; BAF84667.1; -; mRNA.
DR EMBL; CH471052; EAW79036.1; -; Genomic_DNA.
DR EMBL; BC069296; AAH69296.1; -; mRNA.
DR EMBL; BC069361; AAH69361.1; -; mRNA.
DR EMBL; BC069396; AAH69396.1; -; mRNA.
DR EMBL; BC069424; AAH69424.1; -; mRNA.
DR EMBL; BC069447; AAH69447.1; -; mRNA.
DR EMBL; BC069513; AAH69513.1; -; mRNA.
DR EMBL; BC069522; AAH69522.1; -; mRNA.
DR CCDS; CCDS3109.1; -.
DR RefSeq; NP_004155.2; NM_004164.2.
DR PDB; 2RCQ; X-ray; 1.20 A; A=2-134.
DR PDB; 2RCT; X-ray; 1.20 A; A=2-134.
DR PDB; 4EDE; X-ray; 1.40 A; A/B=2-134.
DR PDB; 4EEJ; X-ray; 1.50 A; A/B=2-134.
DR PDB; 4EFG; X-ray; 1.58 A; A/B=2-134.
DR PDB; 4EXZ; X-ray; 1.61 A; A/B=2-134.
DR PDB; 4GKC; X-ray; 1.30 A; A/B=2-134.
DR PDB; 4QYN; X-ray; 1.19 A; A/B=2-134.
DR PDB; 4QYP; X-ray; 1.62 A; A/B/C/D=2-134.
DR PDB; 4QZT; X-ray; 1.90 A; A/B/C/D=2-134.
DR PDB; 4QZU; X-ray; 1.50 A; A/B/C/D=2-134.
DR PDB; 4RUU; X-ray; 1.40 A; A/B=2-134.
DR PDB; 4ZCB; X-ray; 1.70 A; A/B=2-134.
DR PDB; 4ZGU; X-ray; 1.49 A; A/B/C/D=2-134.
DR PDB; 4ZH6; X-ray; 1.55 A; A=2-134.
DR PDB; 4ZH9; X-ray; 2.66 A; A=2-134.
DR PDB; 4ZJ0; X-ray; 1.50 A; A/B=2-134.
DR PDB; 4ZR2; X-ray; 1.80 A; A/B=2-134.
DR PDB; 5DG4; X-ray; 1.50 A; A/B/C/D=2-134.
DR PDB; 5DPQ; X-ray; 1.77 A; A/B=2-134.
DR PDB; 5F58; X-ray; 1.54 A; A/B=2-134.
DR PDB; 5F6B; X-ray; 1.31 A; A/B=2-134.
DR PDB; 5F7G; X-ray; 1.48 A; A/B=2-134.
DR PDB; 5FAZ; X-ray; 1.40 A; A/B=2-134.
DR PDB; 5FEN; X-ray; 1.55 A; A/B=2-134.
DR PDB; 5FFH; X-ray; 1.68 A; A/B=2-134.
DR PDB; 5U6G; X-ray; 2.60 A; A/B/C/D/E/F/G/H/I/J/K/L=2-134.
DR PDB; 6BTH; X-ray; 1.35 A; A/B=1-134.
DR PDB; 6BTI; X-ray; 1.45 A; A/B=1-134.
DR PDB; 6C7Z; X-ray; 1.42 A; A/B=2-134.
DR PDB; 6E50; X-ray; 1.97 A; A=2-134.
DR PDB; 6E51; X-ray; 2.26 A; A=2-134.
DR PDB; 6E5E; X-ray; 1.70 A; A=2-134.
DR PDB; 6E5Q; X-ray; 1.99 A; A=2-134.
DR PDB; 6E5R; X-ray; 2.59 A; A/B=2-134.
DR PDB; 6E5S; X-ray; 2.06 A; A/B/C/D/E/F/G/H/I/J/K/L=2-134.
DR PDB; 6E6L; X-ray; 2.08 A; A=2-134.
DR PDB; 6E7M; X-ray; 2.70 A; A/B/C/D=2-134.
DR PDB; 6MCU; X-ray; 2.57 A; A/B/C/D/E/F/G/H/I/J/K/L=2-134.
DR PDB; 6MCV; X-ray; 3.30 A; A/B/C/D/E/F/G/H/I/J/K/L=2-134.
DR PDB; 6MKV; X-ray; 2.11 A; A/B/C/D=2-134.
DR PDB; 6MLB; X-ray; 2.15 A; A/B/C/D=2-134.
DR PDB; 6ON5; X-ray; 1.64 A; A/B=2-134.
DR PDB; 6ON7; X-ray; 1.98 A; A/B=2-134.
DR PDB; 6ON8; X-ray; 2.40 A; A=2-134.
DR PDB; 6VID; X-ray; 2.89 A; A/B/C/D/E/F=2-134.
DR PDB; 6VIS; X-ray; 2.79 A; A/B/C=2-134.
DR PDB; 6VIT; X-ray; 3.20 A; A/B=2-134.
DR PDB; 6WNF; X-ray; 1.67 A; A/B=2-134.
DR PDB; 6WNJ; X-ray; 2.10 A; A/B/C=2-134.
DR PDB; 6WP0; X-ray; 2.78 A; A/B/C/D/E/F/G/H/I/J/K/L=2-134.
DR PDB; 6WP1; X-ray; 2.99 A; A/B/C/D/E/F=2-134.
DR PDB; 6WP2; X-ray; 2.48 A; A/B/C=2-134.
DR PDB; 7JVG; X-ray; 1.40 A; A/B=1-134.
DR PDB; 7JVY; X-ray; 1.30 A; A/B=1-134.
DR PDB; 7JWD; X-ray; 1.35 A; A/B=1-134.
DR PDB; 7JWR; X-ray; 1.30 A; A/B=1-134.
DR PDB; 7JX2; X-ray; 1.80 A; A=1-134.
DR PDB; 7JZ5; X-ray; 1.57 A; A/B=1-134.
DR PDB; 7K3I; X-ray; 1.20 A; A=1-134.
DR PDB; 7LHJ; X-ray; 1.26 A; A/B=2-134.
DR PDB; 7LHM; X-ray; 1.50 A; A/B=2-134.
DR PDB; 7LHN; X-ray; 2.11 A; A/B=2-134.
DR PDB; 7LHO; X-ray; 1.40 A; A/B=2-134.
DR PDB; 7LSQ; X-ray; 1.67 A; A/B/C/D=2-134.
DR PDB; 7MFX; X-ray; 1.59 A; A/B/C/D=2-134.
DR PDB; 7MFY; X-ray; 1.26 A; A=2-134.
DR PDB; 7MFZ; X-ray; 2.49 A; A/B/C=2-134.
DR PDBsum; 2RCQ; -.
DR PDBsum; 2RCT; -.
DR PDBsum; 4EDE; -.
DR PDBsum; 4EEJ; -.
DR PDBsum; 4EFG; -.
DR PDBsum; 4EXZ; -.
DR PDBsum; 4GKC; -.
DR PDBsum; 4QYN; -.
DR PDBsum; 4QYP; -.
DR PDBsum; 4QZT; -.
DR PDBsum; 4QZU; -.
DR PDBsum; 4RUU; -.
DR PDBsum; 4ZCB; -.
DR PDBsum; 4ZGU; -.
DR PDBsum; 4ZH6; -.
DR PDBsum; 4ZH9; -.
DR PDBsum; 4ZJ0; -.
DR PDBsum; 4ZR2; -.
DR PDBsum; 5DG4; -.
DR PDBsum; 5DPQ; -.
DR PDBsum; 5F58; -.
DR PDBsum; 5F6B; -.
DR PDBsum; 5F7G; -.
DR PDBsum; 5FAZ; -.
DR PDBsum; 5FEN; -.
DR PDBsum; 5FFH; -.
DR PDBsum; 5U6G; -.
DR PDBsum; 6BTH; -.
DR PDBsum; 6BTI; -.
DR PDBsum; 6C7Z; -.
DR PDBsum; 6E50; -.
DR PDBsum; 6E51; -.
DR PDBsum; 6E5E; -.
DR PDBsum; 6E5Q; -.
DR PDBsum; 6E5R; -.
DR PDBsum; 6E5S; -.
DR PDBsum; 6E6L; -.
DR PDBsum; 6E7M; -.
DR PDBsum; 6MCU; -.
DR PDBsum; 6MCV; -.
DR PDBsum; 6MKV; -.
DR PDBsum; 6MLB; -.
DR PDBsum; 6ON5; -.
DR PDBsum; 6ON7; -.
DR PDBsum; 6ON8; -.
DR PDBsum; 6VID; -.
DR PDBsum; 6VIS; -.
DR PDBsum; 6VIT; -.
DR PDBsum; 6WNF; -.
DR PDBsum; 6WNJ; -.
DR PDBsum; 6WP0; -.
DR PDBsum; 6WP1; -.
DR PDBsum; 6WP2; -.
DR PDBsum; 7JVG; -.
DR PDBsum; 7JVY; -.
DR PDBsum; 7JWD; -.
DR PDBsum; 7JWR; -.
DR PDBsum; 7JX2; -.
DR PDBsum; 7JZ5; -.
DR PDBsum; 7K3I; -.
DR PDBsum; 7LHJ; -.
DR PDBsum; 7LHM; -.
DR PDBsum; 7LHN; -.
DR PDBsum; 7LHO; -.
DR PDBsum; 7LSQ; -.
DR PDBsum; 7MFX; -.
DR PDBsum; 7MFY; -.
DR PDBsum; 7MFZ; -.
DR AlphaFoldDB; P50120; -.
DR SMR; P50120; -.
DR BioGRID; 111882; 9.
DR IntAct; P50120; 3.
DR STRING; 9606.ENSP00000232217; -.
DR DrugBank; DB06755; Beta carotene.
DR DrugBank; DB00162; Vitamin A.
DR DrugCentral; P50120; -.
DR TCDB; 8.A.33.1.3; the fatty acid binding protein (fabp) family.
DR GlyConnect; 2069; 1 N-Linked glycan (1 site).
DR GlyGen; P50120; 1 site, 2 N-linked glycans (1 site).
DR iPTMnet; P50120; -.
DR PhosphoSitePlus; P50120; -.
DR BioMuta; RBP2; -.
DR DMDM; 62297500; -.
DR jPOST; P50120; -.
DR MassIVE; P50120; -.
DR MaxQB; P50120; -.
DR PaxDb; P50120; -.
DR PeptideAtlas; P50120; -.
DR PRIDE; P50120; -.
DR ProteomicsDB; 56194; -.
DR Antibodypedia; 33461; 252 antibodies from 27 providers.
DR DNASU; 5948; -.
DR Ensembl; ENST00000232217.6; ENSP00000232217.2; ENSG00000114113.6.
DR GeneID; 5948; -.
DR KEGG; hsa:5948; -.
DR MANE-Select; ENST00000232217.6; ENSP00000232217.2; NM_004164.3; NP_004155.2.
DR UCSC; uc003eth.4; human.
DR CTD; 5948; -.
DR DisGeNET; 5948; -.
DR GeneCards; RBP2; -.
DR HGNC; HGNC:9920; RBP2.
DR HPA; ENSG00000114113; Tissue enriched (intestine).
DR MIM; 180280; gene.
DR neXtProt; NX_P50120; -.
DR OpenTargets; ENSG00000114113; -.
DR PharmGKB; PA34287; -.
DR VEuPathDB; HostDB:ENSG00000114113; -.
DR eggNOG; KOG4015; Eukaryota.
DR GeneTree; ENSGT00940000160165; -.
DR HOGENOM; CLU_113772_5_1_1; -.
DR InParanoid; P50120; -.
DR OMA; HWIEGDI; -.
DR OrthoDB; 1417203at2759; -.
DR PhylomeDB; P50120; -.
DR TreeFam; TF316894; -.
DR BioCyc; MetaCyc:ENSG00000114113-MON; -.
DR PathwayCommons; P50120; -.
DR Reactome; R-HSA-975634; Retinoid metabolism and transport.
DR SignaLink; P50120; -.
DR SIGNOR; P50120; -.
DR BioGRID-ORCS; 5948; 11 hits in 1075 CRISPR screens.
DR EvolutionaryTrace; P50120; -.
DR GeneWiki; RBP2; -.
DR GenomeRNAi; 5948; -.
DR Pharos; P50120; Tbio.
DR PRO; PR:P50120; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P50120; protein.
DR Bgee; ENSG00000114113; Expressed in jejunal mucosa and 126 other tissues.
DR ExpressionAtlas; P50120; baseline and differential.
DR Genevisible; P50120; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:ProtInc.
DR GO; GO:0019841; F:retinol binding; IEA:UniProtKB-KW.
DR GO; GO:0008544; P:epidermis development; TAS:ProtInc.
DR GO; GO:0015908; P:fatty acid transport; IBA:GO_Central.
DR GO; GO:0006776; P:vitamin A metabolic process; TAS:ProtInc.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR000463; Fatty_acid-bd.
DR InterPro; IPR031259; ILBP.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR PANTHER; PTHR11955; PTHR11955; 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; Cytoplasm; Reference proteome; Retinol-binding; Transport;
KW Vitamin A.
FT CHAIN 1..134
FT /note="Retinol-binding protein 2"
FT /id="PRO_0000067395"
FT BINDING 41
FT /ligand="all-trans-retinol"
FT /ligand_id="ChEBI:CHEBI:17336"
FT /evidence="ECO:0000269|PubMed:18076076"
FT BINDING 109
FT /ligand="all-trans-retinol"
FT /ligand_id="ChEBI:CHEBI:17336"
FT /evidence="ECO:0000269|PubMed:18076076"
FT CONFLICT 31
FT /note="R -> P (in Ref. 1; AAC50162)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="D -> G (in Ref. 4; AAH69396)"
FT /evidence="ECO:0000305"
FT STRAND 7..16
FT /evidence="ECO:0007829|PDB:4QYN"
FT HELIX 17..23
FT /evidence="ECO:0007829|PDB:4QYN"
FT HELIX 28..34
FT /evidence="ECO:0007829|PDB:4QYN"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:4QYN"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:4QYN"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:4QYN"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:4QYN"
FT TURN 76..79
FT /evidence="ECO:0007829|PDB:4QYN"
FT STRAND 82..90
FT /evidence="ECO:0007829|PDB:4QYN"
FT STRAND 93..104
FT /evidence="ECO:0007829|PDB:4QYN"
FT STRAND 106..112
FT /evidence="ECO:0007829|PDB:4QYN"
FT STRAND 115..122
FT /evidence="ECO:0007829|PDB:4QYN"
FT STRAND 125..133
FT /evidence="ECO:0007829|PDB:4QYN"
SQ SEQUENCE 134 AA; 15707 MW; A4A7FB157B099A7D CRC64;
MTRDQNGTWE MESNENFEGY MKALDIDFAT RKIAVRLTQT KVIDQDGDNF KTKTTSTFRN
YDVDFTVGVE FDEYTKSLDN RHVKALVTWE GDVLVCVQKG EKENRGWKQW IEGDKLYLEL
TCGDQVCRQV FKKK
