P29373 (RABP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cellular retinoic acid-binding protein 2

Alternative name(s):
Cellular retinoic acid-binding protein II
Short name=CRABP-II

Gene names

Name:

CRABP2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	138 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Transports retinoic acid to the nucleus. Regulates the access of retinoic acid to the nuclear retinoic acid receptors.
Subunit structure	Interacts with RXR and RARA By similarity. Interacts with importin alpha. Ref.11
Subcellular location	Cytoplasm. Endoplasmic reticulum. Nucleus. Note: Upon ligand binding, a conformation change exposes a nuclear localization motif and the protein is transported into the nucleus. Ref.11 Ref.12
Induction	By retinoic acid.
Domain	Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior.
Post-translational modification	Sumoylated in response to retinoic acid binding, sumoylation is critical for dissociation from ER and subsequent nuclear translocation. Ref.14
Sequence similarities	Belongs to the calycin superfamily. Fatty-acid binding protein (FABP) family.

Ontologies

Keywords
Biological process	Transport
Cellular component	Cytoplasm Endoplasmic reticulum Nucleus
Ligand	Retinol-binding Vitamin A
PTM	Isopeptide bond Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	embryonic forelimb morphogenesis Inferred from electronic annotation. Source: Compara epidermis development Traceable author statement Ref.1. Source: ProtInc regulation of transcription, DNA-dependent Traceable author statement Ref.3. Source: ProtInc retinoic acid metabolic process Inferred from electronic annotation. Source: Compara signal transduction Traceable author statement Ref.1. Source: ProtInc
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay. Source: HPA
Molecular_function	retinal binding Inferred from electronic annotation. Source: UniProtKB-KW retinoic acid binding Inferred from electronic annotation. Source: Compara retinoid binding Traceable author statement Ref.3. Source: ProtInc retinol binding Inferred from electronic annotation. Source: UniProtKB-KW transporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 138

138

Cellular retinoic acid-binding protein 2

PRO_0000067415

Regions

Region

133 – 135

3

Retinoic acid binding

Motif

21 – 31

11

Nuclear localization signal

Amino acid modifications

Cross-link

102

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.14

Experimental info

Mutagenesis

21

1

K → A: Loss of ligand-induced nuclear import; when associated with A-30 and A-31. Ref.12

Mutagenesis

30

1

R → A: Loss of ligand-induced nuclear import; when associated with A-21 and A-31. Ref.12

Mutagenesis

31

1

K → A: Loss of ligand-induced nuclear import; when associated with A-21 and A-30. Ref.12

Secondary structure

1

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138

Helix Strand Turn

Details...

Beta strand

6 – 14

9

Helix

16 – 22

7

Helix

27 – 37

11

Beta strand

41 – 47

7

Beta strand

50 – 57

8

Beta strand

60 – 67

8

Beta strand

72 – 75

4

Beta strand

77 – 79

3

Beta strand

81 – 90

10

Beta strand

93 – 103

11

Beta strand

108 – 114

7

Beta strand

116 – 118

3

Beta strand

120 – 126

7

Beta strand

129 – 137

9

Sequences

	Sequence		Length	Mass (Da)
	P29373 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 982833700775B377	FASTA	138	15,693
	10 20 30 40 50 60 MPNFSGNWKI IRSENFEELL KVLGVNVMLR KIAVAAASKP AVEIKQEGDT FYIKTSTTVR 70 80 90 100 110 120 TTEINFKVGE EFEEQTVDGR PCKSLVKWES ENKMVCEQKL LKGEGPKTSW TRELTNDGEL 130 ILTMTADDVV CTRVYVRE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of two human cellular retinoic acid-binding proteins (CRABP). Retinoic acid-induced expression of CRABP-II but not CRABP-I in adult human skin in vivo and in skin fibroblasts in vitro." Astroem A., Tavakkol A., Pettersson U., Cromie M., Elder J.T., Voorhees J.J. J. Biol. Chem. 266:17662-17666(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The molecular cloning and expression of two CRABP cDNAs from human skin." Eller M.S., Oleksiak M.F., McQuaid T.J., McAfee S.G., Gilchrest B.A. Exp. Cell Res. 198:328-336(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Structure of the human cellular retinoic acid-binding protein II gene. Early transcriptional regulation by retinoic acid." Aastroem A., Pettersson U., Voorhees J.J. J. Biol. Chem. 267:25251-25255(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Placenta.
[4]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[7]	"Full-length transcriptome analysis of human retina-derived cell lines ARPE-19 and Y79 using the vector-capping method." Oshikawa M., Tsutsui C., Ikegami T., Fuchida Y., Matsubara M., Toyama S., Usami R., Ohtoko K., Kato S. Invest. Ophthalmol. Vis. Sci. 52:6662-6670(2011) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Colon.
[11]	"Direct channeling of retinoic acid between cellular retinoic acid-binding protein II and retinoic acid receptor sensitizes mammary carcinoma cells to retinoic acid-induced growth arrest." Budhu A.S., Noy N. Mol. Cell. Biol. 22:2632-2641(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NUCLEAR RETINOIC ACID RECEPTORS.
[12]	"A ligand-activated nuclear localization signal in cellular retinoic acid binding protein-II." Sessler R.J., Noy N. Mol. Cell 18:343-353(2005) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-21; ARG-30 AND LYS-31.
[13]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]	"Nuclear translocation of cellular retinoic acid-binding protein II is regulated by retinoic acid-controlled SUMOylation." Majumdar A., Petrescu A.D., Xiong Y., Noy N. J. Biol. Chem. 286:42749-42757(2011) [PubMed] [Europe PMC] [Abstract] Cited for: SUMOYLATION AT LYS-102.
[15]	"Crystal structures of cellular retinoic acid binding proteins I and II in complex with all-trans-retinoic acid and a synthetic retinoid." Kleywegt G.J., Bergfors T., Senn H., le Motte P., Gsell B., Shudo K., Jones T.A. Structure 2:1241-1258(1994) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[16]	"Crystal structure of apo-cellular retinoic acid-binding protein type II (R111M) suggests a mechanism of ligand entry." Chen X., Tordova M., Gilliland G.L., Wang L., Li Y., Yan H., Ji X. J. Mol. Biol. 278:641-653(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[17]	"Structures of cellular retinoic acid binding proteins I and II in complex with synthetic retinoids." Chaudhuri B.N., Kleywegt G.J., Broutin-L'Hermite I., Bergfors T., Senn H., Le Motte P., Partouche O., Jones T.A. Acta Crystallogr. D 55:1850-1857(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[18]	"NMR solution structure of type II human cellular retinoic acid binding protein: implications for ligand binding." Wang L., Li Y., Abildgaard F., Markley J.L., Yan H. Biochemistry 37:12727-12736(1998) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR.
[19]	"NMR study suggests a major role for Arg111 in maintaining the structure and dynamical properties of type II human cellular retinoic acid binding protein." Wang L., Yan H. Biochemistry 37:13021-13032(1998) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR.
[20]	"The structure of apo-wild-type cellular retinoic acid binding protein II at 1.4 A and its relationship to ligand binding and nuclear translocation." Vaezeslami S., Mathes E., Vasileiou C., Borhan B., Geiger J.H. J. Mol. Biol. 363:687-701(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS).
[21]	"Protein design: reengineering cellular retinoic acid binding protein II into a rhodopsin protein mimic." Vasileiou C., Vaezeslami S., Crist R.M., Rabago-Smith M., Geiger J.H., Borhan B. J. Am. Chem. Soc. 129:6140-6148(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.18 ANGSTROMS) IN COMPLEX WITH RETINOIC ACID.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M68867 mRNA. Translation: AAA52068.1.
M97815, M97814 Genomic DNA. Translation: AAA58430.1.
CR450357 mRNA. Translation: CAG29353.1.
BT019827 mRNA. Translation: AAV38630.1.
AK312007 mRNA. Translation: BAG34945.1.
AB593017 mRNA. Translation: BAJ83972.1.
AL590666 Genomic DNA. Translation: CAI16339.1.
CH471121 Genomic DNA. Translation: EAW52921.1.
CH471121 Genomic DNA. Translation: EAW52922.1.
BC001109 mRNA. Translation: AAH01109.1.

IPI

IPI00216088.

PIR

RJHU2. A45057.

RefSeq

NP_001186652.1. NM_001199723.1.
NP_001869.1. NM_001878.3.

UniGene

Hs.405662.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BLR	NMR	-	A	2-138	[»]
1BM5	NMR	-	A	2-138	[»]
1CBQ	X-ray	2.20	A	2-138	[»]
1CBS	X-ray	1.80	A	2-138	[»]
1XCA	X-ray	2.30	A/B	2-138	[»]
2CBS	X-ray	2.10	A	2-138	[»]
2FR3	X-ray	1.48	A	2-138	[»]
2FRS	X-ray	1.51	A/B	2-138	[»]
2FS6	X-ray	1.35	A/B	2-138	[»]
2FS7	X-ray	1.55	A/B	2-138	[»]
2G78	X-ray	1.70	A	2-138	[»]
2G79	X-ray	1.69	A	2-138	[»]
2G7B	X-ray	1.18	A	2-138	[»]
3CBS	X-ray	2.00	A	2-138	[»]
3CR6	X-ray	1.22	A	2-138	[»]
3CWK	X-ray	1.60	A	2-138	[»]
3D95	X-ray	1.20	A/B	2-138	[»]
3D96	X-ray	1.71	A/B	2-138	[»]
3D97	X-ray	1.50	A/B	2-138	[»]
3F8A	X-ray	1.95	A	2-138	[»]
3F9D	X-ray	2.00	A/B	2-138	[»]
3FA6	X-ray	1.54	A/B	2-138	[»]
3FA7	X-ray	1.90	A/B	2-138	[»]
3FA8	X-ray	1.78	A/B	2-138	[»]
3FA9	X-ray	1.94	A/B	2-138	[»]
3FEK	X-ray	1.51	A/B	2-138	[»]
3FEL	X-ray	1.85	A/B	2-138	[»]
3FEN	X-ray	1.56	A/B	2-138	[»]
3FEP	X-ray	2.60	A	2-138	[»]
3I17	X-ray	1.68	A/B	2-138	[»]

ProteinModelPortal

P29373.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000357204.

PTM databases

PhosphoSite

P29373.

Polymorphism databases

DMDM

132401.

2D gel databases

DOSAC-COBS-2DPAGE

P29373.

Proteomic databases

PaxDb

P29373.

PeptideAtlas

P29373.

PRIDE

P29373.

Protocols and materials databases

DNASU

1382.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000368221; ENSP00000357204; ENSG00000143320.
ENST00000368222; ENSP00000357205; ENSG00000143320.

GeneID

1382.

KEGG

hsa:1382.

UCSC

uc001fpr.3. human.

Organism-specific databases

CTD

1382.

GeneCards

GC01M156669.

HGNC

HGNC:2339. CRABP2.

HPA

HPA004135.

MIM

180231. gene.

neXtProt

NX_P29373.

PharmGKB

PA26859.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG300013.

HOGENOM

HOG000004831.

HOVERGEN

HBG005633.

InParanoid

P29373.

OMA

NMMLRKI.

OrthoDB

EOG4KPTC5.

PhylomeDB

P29373.

Gene expression databases

ArrayExpress

P29373.

Bgee

P29373.

CleanEx

HS_CRABP2.

Genevestigator

P29373.

GermOnline

ENSG00000143320. Homo sapiens.

Family and domain databases

Gene3D

2.40.128.20. 1 hit.

InterPro

IPR012674. Calycin.
IPR011038. Calycin-like.
IPR000463. Fatty_acid-bd.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]

Pfam

PF00061. Lipocalin. 1 hit.
[Graphical view]

PRINTS

PR00178. FATTYACIDBP.

SUPFAM

SSF50814. Calycin. 1 hit.

PROSITE

PS00214. FABP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL2692.

DrugBank

DB00523. Alitretinoin.

EvolutionaryTrace

P29373.

GenomeRNAi

1382.

NextBio

5615.

SOURCE

Search...

Entry information

Entry name

RABP2_HUMAN

Accession

Primary (citable) accession number: P29373
Secondary accession number(s): B2R4Z8 , D3DVC5, F1T098, Q6ICN6

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 134 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.