RABP2_HUMAN
ID RABP2_HUMAN Reviewed; 138 AA.
AC P29373; B2R4Z8; D3DVC5; F1T098; Q6ICN6;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Cellular retinoic acid-binding protein 2;
DE AltName: Full=Cellular retinoic acid-binding protein II;
DE Short=CRABP-II;
GN Name=CRABP2;
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=1654334; DOI=10.1016/s0021-9258(19)47422-x;
RA Astroem A., Tavakkol A., Pettersson U., Cromie M., Elder J.T.,
RA Voorhees J.J.;
RT "Molecular cloning of two human cellular retinoic acid-binding proteins
RT (CRABP). Retinoic acid-induced expression of CRABP-II but not CRABP-I in
RT adult human skin in vivo and in skin fibroblasts in vitro.";
RL J. Biol. Chem. 266:17662-17666(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1309505; DOI=10.1016/0014-4827(92)90387-n;
RA Eller M.S., Oleksiak M.F., McQuaid T.J., McAfee S.G., Gilchrest B.A.;
RT "The molecular cloning and expression of two CRABP cDNAs from human skin.";
RL Exp. Cell Res. 198:328-336(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Placenta;
RX PubMed=1334086; DOI=10.1016/s0021-9258(19)74033-2;
RA Aastroem A., Pettersson U., Voorhees J.J.;
RT "Structure of the human cellular retinoic acid-binding protein II gene.
RT Early transcriptional regulation by retinoic acid.";
RL J. Biol. Chem. 267:25251-25255(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=21697133; DOI=10.1167/iovs.11-7479;
RA Oshikawa M., Tsutsui C., Ikegami T., Fuchida Y., Matsubara M., Toyama S.,
RA Usami R., Ohtoko K., Kato S.;
RT "Full-length transcriptome analysis of human retina-derived cell lines
RT ARPE-19 and Y79 using the vector-capping method.";
RL Invest. Ophthalmol. Vis. Sci. 52:6662-6670(2011).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [9]
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 [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
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 [11]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH NUCLEAR RETINOIC ACID RECEPTORS.
RX PubMed=11909957; DOI=10.1128/mcb.22.8.2632-2641.2002;
RA Budhu A.S., Noy N.;
RT "Direct channeling of retinoic acid between cellular retinoic acid-binding
RT protein II and retinoic acid receptor sensitizes mammary carcinoma cells to
RT retinoic acid-induced growth arrest.";
RL Mol. Cell. Biol. 22:2632-2641(2002).
RN [12]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-21; ARG-30 AND LYS-31.
RX PubMed=15866176; DOI=10.1016/j.molcel.2005.03.026;
RA Sessler R.J., Noy N.;
RT "A ligand-activated nuclear localization signal in cellular retinoic acid
RT binding protein-II.";
RL Mol. Cell 18:343-353(2005).
RN [13]
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 [14]
RP SUMOYLATION AT LYS-102.
RX PubMed=21998312; DOI=10.1074/jbc.m111.293464;
RA Majumdar A., Petrescu A.D., Xiong Y., Noy N.;
RT "Nuclear translocation of cellular retinoic acid-binding protein II is
RT regulated by retinoic acid-controlled SUMOylation.";
RL J. Biol. Chem. 286:42749-42757(2011).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=7704533; DOI=10.1016/s0969-2126(94)00125-1;
RA Kleywegt G.J., Bergfors T., Senn H., le Motte P., Gsell B., Shudo K.,
RA Jones T.A.;
RT "Crystal structures of cellular retinoic acid binding proteins I and II in
RT complex with all-trans-retinoic acid and a synthetic retinoid.";
RL Structure 2:1241-1258(1994).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=9600845; DOI=10.1006/jmbi.1998.1734;
RA Chen X., Tordova M., Gilliland G.L., Wang L., Li Y., Yan H., Ji X.;
RT "Crystal structure of apo-cellular retinoic acid-binding protein type II
RT (R111M) suggests a mechanism of ligand entry.";
RL J. Mol. Biol. 278:641-653(1998).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX PubMed=10531482; DOI=10.1107/s0907444999011026;
RA Chaudhuri B.N., Kleywegt G.J., Broutin-L'Hermite I., Bergfors T., Senn H.,
RA Le Motte P., Partouche O., Jones T.A.;
RT "Structures of cellular retinoic acid binding proteins I and II in complex
RT with synthetic retinoids.";
RL Acta Crystallogr. D 55:1850-1857(1999).
RN [18]
RP STRUCTURE BY NMR.
RX PubMed=9737849; DOI=10.1021/bi9808924;
RA Wang L., Li Y., Abildgaard F., Markley J.L., Yan H.;
RT "NMR solution structure of type II human cellular retinoic acid binding
RT protein: implications for ligand binding.";
RL Biochemistry 37:12727-12736(1998).
RN [19]
RP STRUCTURE BY NMR.
RX PubMed=9737883; DOI=10.1021/bi981021x;
RA Wang L., Yan H.;
RT "NMR study suggests a major role for Arg111 in maintaining the structure
RT and dynamical properties of type II human cellular retinoic acid binding
RT protein.";
RL Biochemistry 37:13021-13032(1998).
RN [20] {ECO:0007744|PDB:2FR3, ECO:0007744|PDB:2FRS, ECO:0007744|PDB:2FS6, ECO:0007744|PDB:2FS7}
RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF APOPROTEIN AND COMPLEX WITH
RP ALL-TRANS RETINOIC ACID.
RX PubMed=16979656; DOI=10.1016/j.jmb.2006.08.059;
RA Vaezeslami S., Mathes E., Vasileiou C., Borhan B., Geiger J.H.;
RT "The structure of apo-wild-type cellular retinoic acid binding protein II
RT at 1.4 A and its relationship to ligand binding and nuclear
RT translocation.";
RL J. Mol. Biol. 363:687-701(2006).
RN [21] {ECO:0007744|PDB:2G78, ECO:0007744|PDB:2G79}
RP X-RAY CRYSTALLOGRAPHY (1.18 ANGSTROMS) OF MUTANT LYS-133/PHE-135 IN
RP COMPLEXES WITH ALL-TRANS RETINOIC ACID AND ALL-TRANS RETINAL.
RX PubMed=17447762; DOI=10.1021/ja067546r;
RA Vasileiou C., Vaezeslami S., Crist R.M., Rabago-Smith M., Geiger J.H.,
RA Borhan B.;
RT "Protein design: reengineering cellular retinoic acid binding protein II
RT into a rhodopsin protein mimic.";
RL J. Am. Chem. Soc. 129:6140-6148(2007).
CC -!- FUNCTION: Transports retinoic acid to the nucleus. Regulates the access
CC of retinoic acid to the nuclear retinoic acid receptors.
CC -!- SUBUNIT: Interacts with RXR and RARA (By similarity). Interacts with
CC importin alpha. {ECO:0000250, ECO:0000269|PubMed:11909957,
CC ECO:0000269|PubMed:17447762}.
CC -!- INTERACTION:
CC P29373; P35609: ACTN2; NbExp=3; IntAct=EBI-10204806, EBI-77797;
CC P29373; P30281: CCND3; NbExp=3; IntAct=EBI-10204806, EBI-375013;
CC P29373; Q8NFF5-2: FLAD1; NbExp=3; IntAct=EBI-10204806, EBI-11526128;
CC P29373; Q8N6L0: KASH5; NbExp=6; IntAct=EBI-10204806, EBI-749265;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Endoplasmic reticulum. Nucleus.
CC Note=Upon ligand binding, a conformation change exposes a nuclear
CC localization motif and the protein is transported into the nucleus.
CC -!- INDUCTION: By retinoic acid.
CC -!- DOMAIN: Forms a beta-barrel structure that accommodates hydrophobic
CC ligands in its interior.
CC -!- PTM: Sumoylated in response to retinoic acid binding, sumoylation is
CC critical for dissociation from ER and subsequent nuclear translocation.
CC {ECO:0000269|PubMed:21998312}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC protein (FABP) family. {ECO:0000305}.
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DR EMBL; M68867; AAA52068.1; -; mRNA.
DR EMBL; M97815; AAA58430.1; -; Genomic_DNA.
DR EMBL; M97814; AAA58430.1; JOINED; Genomic_DNA.
DR EMBL; CR450357; CAG29353.1; -; mRNA.
DR EMBL; BT019827; AAV38630.1; -; mRNA.
DR EMBL; AK312007; BAG34945.1; -; mRNA.
DR EMBL; AB593017; BAJ83972.1; -; mRNA.
DR EMBL; AL590666; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW52921.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW52922.1; -; Genomic_DNA.
DR EMBL; BC001109; AAH01109.1; -; mRNA.
DR CCDS; CCDS1152.1; -.
DR PIR; A45057; RJHU2.
DR RefSeq; NP_001186652.1; NM_001199723.1.
DR RefSeq; NP_001869.1; NM_001878.3.
DR RefSeq; XP_016855832.1; XM_017000343.1.
DR PDB; 1BLR; NMR; -; A=2-138.
DR PDB; 1BM5; NMR; -; A=2-138.
DR PDB; 1CBQ; X-ray; 2.20 A; A=2-138.
DR PDB; 1CBS; X-ray; 1.80 A; A=2-138.
DR PDB; 1XCA; X-ray; 2.30 A; A/B=2-138.
DR PDB; 2CBS; X-ray; 2.10 A; A=2-138.
DR PDB; 2FR3; X-ray; 1.48 A; A=2-138.
DR PDB; 2FRS; X-ray; 1.51 A; A/B=2-138.
DR PDB; 2FS6; X-ray; 1.35 A; A/B=2-138.
DR PDB; 2FS7; X-ray; 1.55 A; A/B=2-138.
DR PDB; 2G78; X-ray; 1.70 A; A=2-138.
DR PDB; 2G79; X-ray; 1.69 A; A=2-138.
DR PDB; 2G7B; X-ray; 1.18 A; A=2-138.
DR PDB; 3CBS; X-ray; 2.00 A; A=2-138.
DR PDB; 3CR6; X-ray; 1.22 A; A=2-138.
DR PDB; 3CWK; X-ray; 1.60 A; A=2-138.
DR PDB; 3D95; X-ray; 1.20 A; A/B=2-138.
DR PDB; 3D96; X-ray; 1.71 A; A/B=2-138.
DR PDB; 3D97; X-ray; 1.50 A; A/B=2-138.
DR PDB; 3F8A; X-ray; 1.95 A; A=2-138.
DR PDB; 3F9D; X-ray; 2.00 A; A/B=2-138.
DR PDB; 3FA6; X-ray; 1.54 A; A/B=2-138.
DR PDB; 3FA7; X-ray; 1.90 A; A/B=2-138.
DR PDB; 3FA8; X-ray; 1.78 A; A/B=2-138.
DR PDB; 3FA9; X-ray; 1.94 A; A/B=2-138.
DR PDB; 3FEK; X-ray; 1.51 A; A/B=2-138.
DR PDB; 3FEL; X-ray; 1.85 A; A/B=2-138.
DR PDB; 3FEN; X-ray; 1.56 A; A/B=2-138.
DR PDB; 3FEP; X-ray; 2.60 A; A=2-138.
DR PDB; 3I17; X-ray; 1.68 A; A/B=2-138.
DR PDB; 4I9R; X-ray; 2.60 A; A=2-138.
DR PDB; 4I9S; X-ray; 2.58 A; A=2-138.
DR PDB; 4M6S; X-ray; 2.47 A; A=2-138.
DR PDB; 4M7M; X-ray; 2.57 A; A=2-138.
DR PDB; 4QGV; X-ray; 1.73 A; A/B=2-138.
DR PDB; 4QGW; X-ray; 1.77 A; A/B=2-138.
DR PDB; 4QGX; X-ray; 1.47 A; A/B=2-138.
DR PDB; 4YBP; X-ray; 1.83 A; A=2-138.
DR PDB; 4YBU; X-ray; 1.92 A; A=2-138.
DR PDB; 4YCE; X-ray; 1.95 A; A=2-138.
DR PDB; 4YCH; X-ray; 1.96 A; A=2-138.
DR PDB; 4YDA; X-ray; 1.95 A; A=2-138.
DR PDB; 4YDB; X-ray; 2.03 A; A=2-138.
DR PDB; 4YFP; X-ray; 1.95 A; A=2-138.
DR PDB; 4YFQ; X-ray; 1.62 A; A=2-138.
DR PDB; 4YFR; X-ray; 1.95 A; A=2-138.
DR PDB; 4YGG; X-ray; 1.90 A; A=2-138.
DR PDB; 4YGH; X-ray; 2.10 A; A=2-138.
DR PDB; 4YGZ; X-ray; 2.06 A; A=2-138.
DR PDB; 4YH0; X-ray; 2.14 A; A=2-138.
DR PDB; 4YKM; X-ray; 1.58 A; A/B=2-138.
DR PDB; 4YKO; X-ray; 1.57 A; A/B=2-138.
DR PDB; 5HZQ; X-ray; 1.75 A; A/B=1-138.
DR PDB; 5OGB; X-ray; 1.80 A; A=1-138.
DR PDB; 6HKR; X-ray; 1.50 A; A=1-138.
DR PDB; 6MOP; X-ray; 1.90 A; A=2-138.
DR PDB; 6MOQ; X-ray; 2.20 A; A=2-138.
DR PDB; 6MOR; X-ray; 1.79 A; A=2-138.
DR PDB; 6MOV; X-ray; 1.75 A; A=2-138.
DR PDB; 6MOW; X-ray; 2.35 A; A=2-138.
DR PDB; 6MOX; X-ray; 2.18 A; A=2-138.
DR PDB; 6MPK; X-ray; 1.58 A; A=2-138.
DR PDB; 6MQI; X-ray; 1.87 A; A=2-138.
DR PDB; 6MQJ; X-ray; 2.12 A; A=2-138.
DR PDB; 6MQW; X-ray; 2.09 A; A=2-138.
DR PDB; 6MQX; X-ray; 2.01 A; A=2-138.
DR PDB; 6MQY; X-ray; 1.90 A; A=2-138.
DR PDB; 6MQZ; X-ray; 2.07 A; A=2-138.
DR PDB; 6MR0; X-ray; 2.65 A; A=2-138.
DR PDB; 6NNX; X-ray; 1.87 A; A=2-138.
DR PDB; 6NNY; X-ray; 1.67 A; A=2-138.
DR PDB; 6NOE; X-ray; 1.97 A; A=2-138.
DR PDB; 6Z2U; X-ray; 2.40 A; A=1-138.
DR PDB; 6Z2Z; X-ray; 2.55 A; A=1-138.
DR PDB; 6ZSW; X-ray; 2.08 A; A=1-138.
DR PDB; 6ZSX; X-ray; 2.40 A; A=1-138.
DR PDB; 7AA0; X-ray; 1.82 A; AAA/BBB=1-138.
DR PDB; 7AA1; X-ray; 1.71 A; AAA=1-138.
DR PDB; 7RY5; X-ray; 2.00 A; AAA/BBB=2-138.
DR PDBsum; 1BLR; -.
DR PDBsum; 1BM5; -.
DR PDBsum; 1CBQ; -.
DR PDBsum; 1CBS; -.
DR PDBsum; 1XCA; -.
DR PDBsum; 2CBS; -.
DR PDBsum; 2FR3; -.
DR PDBsum; 2FRS; -.
DR PDBsum; 2FS6; -.
DR PDBsum; 2FS7; -.
DR PDBsum; 2G78; -.
DR PDBsum; 2G79; -.
DR PDBsum; 2G7B; -.
DR PDBsum; 3CBS; -.
DR PDBsum; 3CR6; -.
DR PDBsum; 3CWK; -.
DR PDBsum; 3D95; -.
DR PDBsum; 3D96; -.
DR PDBsum; 3D97; -.
DR PDBsum; 3F8A; -.
DR PDBsum; 3F9D; -.
DR PDBsum; 3FA6; -.
DR PDBsum; 3FA7; -.
DR PDBsum; 3FA8; -.
DR PDBsum; 3FA9; -.
DR PDBsum; 3FEK; -.
DR PDBsum; 3FEL; -.
DR PDBsum; 3FEN; -.
DR PDBsum; 3FEP; -.
DR PDBsum; 3I17; -.
DR PDBsum; 4I9R; -.
DR PDBsum; 4I9S; -.
DR PDBsum; 4M6S; -.
DR PDBsum; 4M7M; -.
DR PDBsum; 4QGV; -.
DR PDBsum; 4QGW; -.
DR PDBsum; 4QGX; -.
DR PDBsum; 4YBP; -.
DR PDBsum; 4YBU; -.
DR PDBsum; 4YCE; -.
DR PDBsum; 4YCH; -.
DR PDBsum; 4YDA; -.
DR PDBsum; 4YDB; -.
DR PDBsum; 4YFP; -.
DR PDBsum; 4YFQ; -.
DR PDBsum; 4YFR; -.
DR PDBsum; 4YGG; -.
DR PDBsum; 4YGH; -.
DR PDBsum; 4YGZ; -.
DR PDBsum; 4YH0; -.
DR PDBsum; 4YKM; -.
DR PDBsum; 4YKO; -.
DR PDBsum; 5HZQ; -.
DR PDBsum; 5OGB; -.
DR PDBsum; 6HKR; -.
DR PDBsum; 6MOP; -.
DR PDBsum; 6MOQ; -.
DR PDBsum; 6MOR; -.
DR PDBsum; 6MOV; -.
DR PDBsum; 6MOW; -.
DR PDBsum; 6MOX; -.
DR PDBsum; 6MPK; -.
DR PDBsum; 6MQI; -.
DR PDBsum; 6MQJ; -.
DR PDBsum; 6MQW; -.
DR PDBsum; 6MQX; -.
DR PDBsum; 6MQY; -.
DR PDBsum; 6MQZ; -.
DR PDBsum; 6MR0; -.
DR PDBsum; 6NNX; -.
DR PDBsum; 6NNY; -.
DR PDBsum; 6NOE; -.
DR PDBsum; 6Z2U; -.
DR PDBsum; 6Z2Z; -.
DR PDBsum; 6ZSW; -.
DR PDBsum; 6ZSX; -.
DR PDBsum; 7AA0; -.
DR PDBsum; 7AA1; -.
DR PDBsum; 7RY5; -.
DR AlphaFoldDB; P29373; -.
DR BMRB; P29373; -.
DR SMR; P29373; -.
DR BioGRID; 107773; 38.
DR IntAct; P29373; 14.
DR STRING; 9606.ENSP00000482841; -.
DR BindingDB; P29373; -.
DR ChEMBL; CHEMBL2692; -.
DR DrugBank; DB08127; 1,3,3-trimethyl-2-[(1E,3E)-3-methylpenta-1,3-dien-1-yl]cyclohexene.
DR DrugBank; DB08467; 6-(2,3,4,5,6,7-HEXAHYDRO-2,4,4-TRIMETHYL-1-METYLENEINDEN-2-YL)-3-METHYLHEXA-2,4-DIENOIC ACID.
DR DrugBank; DB00523; Alitretinoin.
DR DrugBank; DB08455; Ro 12-7310.
DR DrugBank; DB00755; Tretinoin.
DR iPTMnet; P29373; -.
DR MetOSite; P29373; -.
DR PhosphoSitePlus; P29373; -.
DR BioMuta; CRABP2; -.
DR DMDM; 132401; -.
DR DOSAC-COBS-2DPAGE; P29373; -.
DR CPTAC; CPTAC-51; -.
DR CPTAC; CPTAC-52; -.
DR EPD; P29373; -.
DR jPOST; P29373; -.
DR MassIVE; P29373; -.
DR MaxQB; P29373; -.
DR PaxDb; P29373; -.
DR PeptideAtlas; P29373; -.
DR PRIDE; P29373; -.
DR ProteomicsDB; 54555; -.
DR Antibodypedia; 20440; 716 antibodies from 39 providers.
DR CPTC; P29373; 2 antibodies.
DR DNASU; 1382; -.
DR Ensembl; ENST00000368221.1; ENSP00000357204.1; ENSG00000143320.9.
DR Ensembl; ENST00000368222.8; ENSP00000357205.3; ENSG00000143320.9.
DR Ensembl; ENST00000621784.4; ENSP00000482841.1; ENSG00000143320.9.
DR GeneID; 1382; -.
DR KEGG; hsa:1382; -.
DR MANE-Select; ENST00000368222.8; ENSP00000357205.3; NM_001878.4; NP_001869.1.
DR UCSC; uc001fpr.4; human.
DR CTD; 1382; -.
DR DisGeNET; 1382; -.
DR GeneCards; CRABP2; -.
DR HGNC; HGNC:2339; CRABP2.
DR HPA; ENSG00000143320; Group enriched (esophagus, vagina).
DR MIM; 180231; gene.
DR neXtProt; NX_P29373; -.
DR OpenTargets; ENSG00000143320; -.
DR PharmGKB; PA26859; -.
DR VEuPathDB; HostDB:ENSG00000143320; -.
DR eggNOG; KOG4015; Eukaryota.
DR GeneTree; ENSGT00940000157619; -.
DR HOGENOM; CLU_113772_0_2_1; -.
DR InParanoid; P29373; -.
DR OMA; ISTWEGD; -.
DR OrthoDB; 1443155at2759; -.
DR PhylomeDB; P29373; -.
DR TreeFam; TF316894; -.
DR PathwayCommons; P29373; -.
DR Reactome; R-HSA-5362517; Signaling by Retinoic Acid.
DR SignaLink; P29373; -.
DR SIGNOR; P29373; -.
DR BioGRID-ORCS; 1382; 20 hits in 1081 CRISPR screens.
DR EvolutionaryTrace; P29373; -.
DR GeneWiki; CRABP2; -.
DR GenomeRNAi; 1382; -.
DR Pharos; P29373; Tchem.
DR PRO; PR:P29373; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P29373; protein.
DR Bgee; ENSG00000143320; Expressed in lower esophagus mucosa and 144 other tissues.
DR ExpressionAtlas; P29373; baseline and differential.
DR Genevisible; P29373; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0030332; F:cyclin binding; IDA:MGI.
DR GO; GO:0005504; F:fatty acid binding; IBA:GO_Central.
DR GO; GO:0016918; F:retinal binding; IEA:UniProtKB-KW.
DR GO; GO:0001972; F:retinoic acid binding; IBA:GO_Central.
DR GO; GO:0005501; F:retinoid binding; TAS:ProtInc.
DR GO; GO:0019841; F:retinol binding; IEA:UniProtKB-KW.
DR GO; GO:0035115; P:embryonic forelimb morphogenesis; IEA:Ensembl.
DR GO; GO:0008544; P:epidermis development; TAS:ProtInc.
DR GO; GO:0015908; P:fatty acid transport; IBA:GO_Central.
DR GO; GO:0048672; P:positive regulation of collateral sprouting; IEA:Ensembl.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:ProtInc.
DR GO; GO:0002138; P:retinoic acid biosynthetic process; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; 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; Endoplasmic reticulum; Isopeptide bond; Nucleus;
KW Reference proteome; Retinol-binding; Transport; Ubl conjugation; Vitamin A.
FT CHAIN 1..138
FT /note="Cellular retinoic acid-binding protein 2"
FT /id="PRO_0000067415"
FT MOTIF 21..31
FT /note="Nuclear localization signal"
FT BINDING 133..135
FT /ligand="all-trans-retinoate"
FT /ligand_id="ChEBI:CHEBI:35291"
FT /evidence="ECO:0000269|PubMed:16979656,
FT ECO:0007744|PDB:2FR3"
FT CROSSLNK 102
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:21998312"
FT MUTAGEN 21
FT /note="K->A: Loss of ligand-induced nuclear import; when
FT associated with A-30 and A-31."
FT /evidence="ECO:0000269|PubMed:15866176"
FT MUTAGEN 30
FT /note="R->A: Loss of ligand-induced nuclear import; when
FT associated with A-21 and A-31."
FT /evidence="ECO:0000269|PubMed:15866176"
FT MUTAGEN 31
FT /note="K->A: Loss of ligand-induced nuclear import; when
FT associated with A-21 and A-30."
FT /evidence="ECO:0000269|PubMed:15866176"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:6Z2U"
FT STRAND 6..14
FT /evidence="ECO:0007829|PDB:2G7B"
FT HELIX 16..22
FT /evidence="ECO:0007829|PDB:2G7B"
FT HELIX 27..37
FT /evidence="ECO:0007829|PDB:2G7B"
FT STRAND 41..47
FT /evidence="ECO:0007829|PDB:2G7B"
FT STRAND 50..57
FT /evidence="ECO:0007829|PDB:2G7B"
FT STRAND 60..67
FT /evidence="ECO:0007829|PDB:2G7B"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:2G7B"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:1BM5"
FT STRAND 81..90
FT /evidence="ECO:0007829|PDB:2G7B"
FT STRAND 93..103
FT /evidence="ECO:0007829|PDB:2G7B"
FT STRAND 108..114
FT /evidence="ECO:0007829|PDB:2G7B"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:4M7M"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:2G7B"
FT STRAND 129..137
FT /evidence="ECO:0007829|PDB:2G7B"
SQ SEQUENCE 138 AA; 15693 MW; 982833700775B377 CRC64;
MPNFSGNWKI IRSENFEELL KVLGVNVMLR KIAVAAASKP AVEIKQEGDT FYIKTSTTVR
TTEINFKVGE EFEEQTVDGR PCKSLVKWES ENKMVCEQKL LKGEGPKTSW TRELTNDGEL
ILTMTADDVV CTRVYVRE
