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Retinol-binding protein 2 (Cellular retinol-binding protein II) (CRBP-II)

 RET2_HUMAN              Reviewed;         134 AA.
P50120; A8K7G3; Q6ISQ9; Q6ISS7;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
12-SEP-2018, entry version 157.
RecName: Full=Retinol-binding protein 2;
AltName: Full=Cellular retinol-binding protein II;
Short=CRBP-II;
Name=RBP2; Synonyms=CRBP2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7657783; DOI=10.1093/oxfordjournals.humrep.a136137;
Loughney A.D., Kumarendran M.K., Thomas E.J., Redfern C.P.F.;
"Variation in the expression of cellular retinoid binding proteins in
human endometrium throughout the menstrual cycle.";
Hum. Reprod. 10:1297-1304(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Small intestine;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
TISSUE SPECIFICITY.
PubMed=11274389; DOI=10.1073/pnas.061455898;
Folli C., Calderone V., Ottonello S., Bolchi A., Zanotti G.,
Stoppini M., Berni R.;
"Identification, retinoid binding and X-ray analysis of a human
retinol-binding protein.";
Proc. Natl. Acad. Sci. U.S.A. 98:3710-3715(2001).
[6]
X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) IN COMPLEX WITH RETINOL.
PubMed=18076076; DOI=10.1002/prot.21848;
Tarter M., Capaldi S., Carrizo M.E., Ambrosi E., Perduca M.,
Monaco H.L.;
"Crystal structure of human cellular retinol-binding protein II to 1.2
A resolution.";
Proteins 70:1626-1630(2008).
-!- FUNCTION: Intracellular transport of retinol.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- TISSUE SPECIFICITY: Higher expression in adult small intestine and
to a much lesser extent in fetal kidney.
{ECO:0000269|PubMed:11274389}.
-!- DOMAIN: Forms a beta-barrel structure that accommodates
hydrophobic ligands in its interior.
-!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
protein (FABP) family. {ECO:0000305}.
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EMBL; U13831; AAC50162.1; -; mRNA.
EMBL; AK291978; BAF84667.1; -; mRNA.
EMBL; CH471052; EAW79036.1; -; Genomic_DNA.
EMBL; BC069296; AAH69296.1; -; mRNA.
EMBL; BC069361; AAH69361.1; -; mRNA.
EMBL; BC069396; AAH69396.1; -; mRNA.
EMBL; BC069424; AAH69424.1; -; mRNA.
EMBL; BC069447; AAH69447.1; -; mRNA.
EMBL; BC069513; AAH69513.1; -; mRNA.
EMBL; BC069522; AAH69522.1; -; mRNA.
CCDS; CCDS3109.1; -.
RefSeq; NP_004155.2; NM_004164.2.
UniGene; Hs.655516; -.
PDB; 2RCQ; X-ray; 1.20 A; A=2-134.
PDB; 2RCT; X-ray; 1.20 A; A=2-134.
PDB; 4EDE; X-ray; 1.40 A; A/B=2-134.
PDB; 4EEJ; X-ray; 1.50 A; A/B=2-134.
PDB; 4EFG; X-ray; 1.58 A; A/B=2-134.
PDB; 4EXZ; X-ray; 1.61 A; A/B=2-134.
PDB; 4GKC; X-ray; 1.30 A; A/B=2-134.
PDB; 4QYN; X-ray; 1.19 A; A/B=2-134.
PDB; 4QYP; X-ray; 1.62 A; A/B/C/D=2-134.
PDB; 4QZT; X-ray; 1.90 A; A/B/C/D=2-134.
PDB; 4QZU; X-ray; 1.50 A; A/B/C/D=2-134.
PDB; 4RUU; X-ray; 1.40 A; A/B=2-134.
PDB; 4ZCB; X-ray; 1.70 A; A/B=2-134.
PDB; 4ZGU; X-ray; 1.49 A; A/B/C/D=2-134.
PDB; 4ZH6; X-ray; 1.55 A; A=2-134.
PDB; 4ZH9; X-ray; 2.66 A; A=2-134.
PDB; 4ZJ0; X-ray; 1.50 A; A/B=2-134.
PDB; 4ZR2; X-ray; 1.80 A; A/B=2-134.
PDB; 5DG4; X-ray; 1.50 A; A/B/C/D=2-134.
PDB; 5DPQ; X-ray; 1.77 A; A/B=2-134.
PDB; 5F58; X-ray; 1.54 A; A/B=2-134.
PDB; 5F6B; X-ray; 1.31 A; A/B=2-134.
PDB; 5F7G; X-ray; 1.48 A; A/B=2-134.
PDB; 5FAZ; X-ray; 1.40 A; A/B=2-134.
PDB; 5FEN; X-ray; 1.55 A; A/B=2-134.
PDB; 5FFH; X-ray; 1.68 A; A/B=2-134.
PDB; 5U6G; X-ray; 2.60 A; A/B/C/D/E/F/G/H/I/J/K/L=2-134.
PDB; 6C7Z; X-ray; 1.42 A; A/B=2-134.
PDBsum; 2RCQ; -.
PDBsum; 2RCT; -.
PDBsum; 4EDE; -.
PDBsum; 4EEJ; -.
PDBsum; 4EFG; -.
PDBsum; 4EXZ; -.
PDBsum; 4GKC; -.
PDBsum; 4QYN; -.
PDBsum; 4QYP; -.
PDBsum; 4QZT; -.
PDBsum; 4QZU; -.
PDBsum; 4RUU; -.
PDBsum; 4ZCB; -.
PDBsum; 4ZGU; -.
PDBsum; 4ZH6; -.
PDBsum; 4ZH9; -.
PDBsum; 4ZJ0; -.
PDBsum; 4ZR2; -.
PDBsum; 5DG4; -.
PDBsum; 5DPQ; -.
PDBsum; 5F58; -.
PDBsum; 5F6B; -.
PDBsum; 5F7G; -.
PDBsum; 5FAZ; -.
PDBsum; 5FEN; -.
PDBsum; 5FFH; -.
PDBsum; 5U6G; -.
PDBsum; 6C7Z; -.
ProteinModelPortal; P50120; -.
SMR; P50120; -.
BioGrid; 111882; 3.
IntAct; P50120; 3.
STRING; 9606.ENSP00000232217; -.
DrugBank; DB00162; Vitamin A.
TCDB; 8.A.33.1.3; the fatty acid binding protein (fabp) family.
iPTMnet; P50120; -.
PhosphoSitePlus; P50120; -.
BioMuta; RBP2; -.
DMDM; 62297500; -.
EPD; P50120; -.
MaxQB; P50120; -.
PaxDb; P50120; -.
PeptideAtlas; P50120; -.
PRIDE; P50120; -.
ProteomicsDB; 56194; -.
DNASU; 5948; -.
Ensembl; ENST00000232217; ENSP00000232217; ENSG00000114113.
GeneID; 5948; -.
KEGG; hsa:5948; -.
UCSC; uc003eth.4; human.
CTD; 5948; -.
DisGeNET; 5948; -.
EuPathDB; HostDB:ENSG00000114113.6; -.
GeneCards; RBP2; -.
HGNC; HGNC:9920; RBP2.
HPA; HPA035866; -.
MIM; 180280; gene.
neXtProt; NX_P50120; -.
OpenTargets; ENSG00000114113; -.
PharmGKB; PA34287; -.
eggNOG; KOG4015; Eukaryota.
eggNOG; ENOG4111US8; LUCA.
GeneTree; ENSGT00760000118898; -.
HOGENOM; HOG000004831; -.
HOVERGEN; HBG005633; -.
InParanoid; P50120; -.
KO; K14622; -.
OMA; ENRGWKQ; -.
OrthoDB; EOG091G0QSV; -.
PhylomeDB; P50120; -.
TreeFam; TF316894; -.
BioCyc; MetaCyc:ENSG00000114113-MONOMER; -.
Reactome; R-HSA-975634; Retinoid metabolism and transport.
EvolutionaryTrace; P50120; -.
GeneWiki; RBP2; -.
GenomeRNAi; 5948; -.
PRO; PR:P50120; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000114113; Expressed in 105 organ(s), highest expression level in duodenum.
CleanEx; HS_RBP2; -.
ExpressionAtlas; P50120; baseline and differential.
Genevisible; P50120; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0016918; F:retinal binding; IEA:UniProtKB-KW.
GO; GO:0005501; F:retinoid binding; TAS:ProtInc.
GO; GO:0019841; F:retinol binding; IEA:UniProtKB-KW.
GO; GO:0008544; P:epidermis development; TAS:ProtInc.
GO; GO:0001523; P:retinoid metabolic process; TAS:Reactome.
GO; GO:0006776; P:vitamin A metabolic process; TAS:ProtInc.
Gene3D; 2.40.128.20; -; 1.
InterPro; IPR012674; Calycin.
InterPro; IPR000463; Fatty_acid-bd.
InterPro; IPR031259; ILBP.
InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
PANTHER; PTHR11955; PTHR11955; 1.
Pfam; PF00061; Lipocalin; 1.
PRINTS; PR00178; FATTYACIDBP.
SUPFAM; SSF50814; SSF50814; 1.
PROSITE; PS00214; FABP; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Reference proteome;
Retinol-binding; Transport; Vitamin A.
CHAIN 1 134 Retinol-binding protein 2.
/FTId=PRO_0000067395.
BINDING 41 41 Retinoic acid.
BINDING 109 109 Retinoic acid. {ECO:0000250}.
CONFLICT 31 31 R -> P (in Ref. 1; AAC50162).
{ECO:0000305}.
CONFLICT 114 114 D -> G (in Ref. 4; AAH69396).
{ECO:0000305}.
STRAND 7 16 {ECO:0000244|PDB:4QYN}.
HELIX 17 23 {ECO:0000244|PDB:4QYN}.
HELIX 28 34 {ECO:0000244|PDB:4QYN}.
STRAND 40 46 {ECO:0000244|PDB:4QYN}.
STRAND 49 55 {ECO:0000244|PDB:4QYN}.
STRAND 61 66 {ECO:0000244|PDB:4QYN}.
STRAND 71 74 {ECO:0000244|PDB:4QYN}.
TURN 76 79 {ECO:0000244|PDB:4QYN}.
STRAND 82 90 {ECO:0000244|PDB:4QYN}.
STRAND 93 104 {ECO:0000244|PDB:4QYN}.
STRAND 106 112 {ECO:0000244|PDB:4QYN}.
STRAND 115 122 {ECO:0000244|PDB:4QYN}.
STRAND 125 133 {ECO:0000244|PDB:4QYN}.
SEQUENCE 134 AA; 15707 MW; A4A7FB157B099A7D CRC64;
MTRDQNGTWE MESNENFEGY MKALDIDFAT RKIAVRLTQT KVIDQDGDNF KTKTTSTFRN
YDVDFTVGVE FDEYTKSLDN RHVKALVTWE GDVLVCVQKG EKENRGWKQW IEGDKLYLEL
TCGDQVCRQV FKKK


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