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 27-MAR-2024, entry version 214. 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}. 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; 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; 7OXW; X-ray; 1.16 A; A=1-138. DR PDB; 7OXX; X-ray; 1.33 A; A/B/C/D=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; 7OXW; -. DR PDBsum; 7OXX; -. DR PDBsum; 7RY5; -. DR AlphaFoldDB; P29373; -. DR BMRB; P29373; -. DR SMR; P29373; -. DR BioGRID; 107773; 49. 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 SwissPalm; 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; 9606-ENSP00000482841; -. DR PeptideAtlas; P29373; -. DR ProteomicsDB; 54555; -. DR Pumba; P29373; -. DR Antibodypedia; 20440; 780 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 AGR; HGNC:2339; -. DR CTD; 1382; -. DR DisGeNET; 1382; -. DR GeneCards; CRABP2; -. DR HGNC; HGNC:2339; CRABP2. DR HPA; ENSG00000143320; Tissue enhanced (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; WETDCKI; -. DR OrthoDB; 46617at2759; -. 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; 22 hits in 1159 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 146 other cell types or tissues. DR ExpressionAtlas; P29373; baseline and differential. 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 DNA-templated transcription; TAS:ProtInc. DR GO; GO:0042573; P:retinoic acid metabolic process; IEA:Ensembl. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR CDD; cd19461; CRABP2; 1. 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:SF152; CELLULAR RETINOIC ACID-BINDING PROTEIN 2; 1. DR PANTHER; PTHR11955; FATTY ACID BINDING PROTEIN; 1. DR Pfam; PF00061; Lipocalin; 1. DR PRINTS; PR00178; FATTYACIDBP. DR SUPFAM; SSF50814; Lipocalins; 1. DR PROSITE; PS00214; FABP; 1. DR Genevisible; P29373; HS. 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..15 FT /evidence="ECO:0007829|PDB:7OXW" FT HELIX 16..23 FT /evidence="ECO:0007829|PDB:7OXW" FT HELIX 24..26 FT /evidence="ECO:0007829|PDB:7OXW" FT HELIX 29..32 FT /evidence="ECO:0007829|PDB:7OXW" FT TURN 33..35 FT /evidence="ECO:0007829|PDB:7OXW" FT STRAND 38..40 FT /evidence="ECO:0007829|PDB:7OXW" FT STRAND 42..47 FT /evidence="ECO:0007829|PDB:7OXW" FT STRAND 50..56 FT /evidence="ECO:0007829|PDB:7OXW" FT STRAND 57..59 FT /evidence="ECO:0007829|PDB:1BLR" FT STRAND 61..67 FT /evidence="ECO:0007829|PDB:7OXW" FT STRAND 72..76 FT /evidence="ECO:0007829|PDB:7OXW" FT STRAND 77..79 FT /evidence="ECO:0007829|PDB:1BM5" FT STRAND 81..90 FT /evidence="ECO:0007829|PDB:7OXW" FT STRAND 93..103 FT /evidence="ECO:0007829|PDB:7OXW" FT STRAND 108..114 FT /evidence="ECO:0007829|PDB:7OXW" FT STRAND 116..118 FT /evidence="ECO:0007829|PDB:4M7M" FT STRAND 120..126 FT /evidence="ECO:0007829|PDB:7OXW" FT STRAND 129..137 FT /evidence="ECO:0007829|PDB:7OXW" SQ SEQUENCE 138 AA; 15693 MW; 982833700775B377 CRC64; MPNFSGNWKI IRSENFEELL KVLGVNVMLR KIAVAAASKP AVEIKQEGDT FYIKTSTTVR TTEINFKVGE EFEEQTVDGR PCKSLVKWES ENKMVCEQKL LKGEGPKTSW TRELTNDGEL ILTMTADDVV CTRVYVRE //