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P47942 (DPYL2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dihydropyrimidinase-related protein 2

Short name=DRP-2
Alternative name(s):
Collapsin response mediator protein 2
Short name=CRMP-2
Turned on after division 64 kDa protein
Short name=TOAD-64
Gene names
Name:Dpysl2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length572 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role in neuronal development and polarity, as well as in axon growth and guidance, neuronal growth cone collapse and cell migration. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. May play a role in endocytosis By similarity.

Subunit structure

Homotetramer, and heterotetramer with CRMP1, DPYSL3, DPYSL4 or DPYSL5. Interacts through its C-terminus with the C-terminus of CYFIP1/SRA1. Interacts with HTR4. Interacts with CLN6. Interacts with MICALL1. Ref.3

Subcellular location

Cytoplasmcytosol By similarity. Cytoplasmcytoskeleton By similarity. Membrane By similarity. Note: Tightly but noncovalently associated with membranes. Ref.1

Developmental stage

Expressed immediately after neuronal birth and is dramatically down-regulated in the adult.

Post-translational modification

Phosphorylation by DYRK2 at Ser-522 is required for subsequent phosphorylation by GSK3B. Phosphorylation at Thr-514 by GSK3B abolishes tubulin-binding leading to destabilization of microtubule assembly in axons and neurodegeneration By similarity.

Sequence similarities

Belongs to the DHOase family. Hydantoinase/dihydropyrimidinase subfamily.

Caution

Lacks most of the conserved residues that are essential for binding the metal cofactor and hence for dihydropyrimidinase activity. Its enzyme activity is therefore unsure.

Ontologies

Keywords
   Biological processDifferentiation
Neurogenesis
   Cellular componentCytoplasm
Cytoskeleton
Membrane
   Molecular functionDevelopmental protein
   PTMPhosphoprotein
S-nitrosylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processbrain development

Inferred from expression pattern PubMed 8946055. Source: RGD

cytoskeleton organization

Inferred from sequence or structural similarity. Source: UniProtKB

endocytosis

Inferred from sequence or structural similarity. Source: UniProtKB

olfactory bulb development

Inferred from expression pattern PubMed 14751288. Source: RGD

positive regulation of glutamate secretion

Inferred from direct assay PubMed 19755421. Source: RGD

pyrimidine nucleobase catabolic process

Inferred from electronic annotation. Source: InterPro

regulation of axon extension

Non-traceable author statement Ref.1. Source: RGD

regulation of neuron differentiation

Inferred from mutant phenotype PubMed 18218617. Source: RGD

response to amphetamine

Inferred from expression pattern PubMed 20058175. Source: RGD

response to cocaine

Inferred from expression pattern PubMed 19457111. Source: RGD

response to drug

Inferred from expression pattern PubMed 12188101. Source: RGD

spinal cord development

Inferred from expression pattern PubMed 8946055. Source: RGD

synaptic vesicle transport

Inferred from direct assay PubMed 19755421. Source: RGD

   Cellular_componentaxon

Inferred from electronic annotation. Source: Ensembl

cytosol

Inferred from direct assay PubMed 11741937. Source: RGD

dendrite

Inferred from direct assay PubMed 19755421. Source: RGD

growth cone

Inferred from direct assay Ref.1. Source: RGD

membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

microtubule

Inferred from electronic annotation. Source: Ensembl

mitochondrion

Inferred from electronic annotation. Source: Ensembl

neuron projection

Inferred from direct assay PubMed 19755421. Source: RGD

neuronal cell body

Inferred from direct assay PubMed 19457111. Source: RGD

protein complex

Inferred from direct assay PubMed 19755421. Source: RGD

   Molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction PubMed 20220019. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Ppp2caP633312EBI-917570,EBI-7050205

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 572572Dihydropyrimidinase-related protein 2
PRO_0000165915

Sites

Site4861Not phosphorylated

Amino acid modifications

Modified residue321Phosphotyrosine; by FYN By similarity
Modified residue2581N6-succinyllysine By similarity
Modified residue4311Phosphotyrosine By similarity
Modified residue4651Phosphoserine By similarity
Modified residue4991Phosphotyrosine By similarity
Modified residue5041S-nitrosocysteine Ref.5
Modified residue5091Phosphothreonine Ref.4 Ref.6
Modified residue5141Phosphothreonine; by GSK3-beta By similarity
Modified residue5171Phosphoserine By similarity
Modified residue5181Phosphoserine Ref.4
Modified residue5221Phosphoserine; alternate Ref.4
Modified residue5221Phosphoserine; by DYRK2; alternate By similarity
Modified residue5551Phosphothreonine; by ROCK2 By similarity

Sequences

Sequence LengthMass (Da)Tools
P47942 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: C031F3BC038AA737

FASTA57262,278
        10         20         30         40         50         60 
MSYQGKKNIP RITSDRLLIK GGKIVNDDQS FYADIYMEDG LIKQIGENLI VPGGVKTIEA 

        70         80         90        100        110        120 
HSRMVIPGGI DVHTRFQMPD QGMTSADDFF QGTKAALAGG TTMIIDHVVP EPGTSLLAAF 

       130        140        150        160        170        180 
DQWREWADSK SCCDYSLHVD ITEWHKGIQE EMEALVKDHG VNSFLVYMAF KDRFQLTDSQ 

       190        200        210        220        230        240 
IYEVLSVIRD IGAIAQVHAE NGDIIAEEQQ RILDLGITGP EGHVLSRPEE VEAEAVNRSI 

       250        260        270        280        290        300 
TIANQTNCPL YVTKVMSKSA AEVIAQARKK GTVVYGEPIT ASLGTDGSHY WSKNWAKAAA 

       310        320        330        340        350        360 
FVTSPPLSPD PTTPDFLNSL LSCGDLQVTG SAHCTFNTAQ KAVGKDNFTL IPEGTNGTEE 

       370        380        390        400        410        420 
RMSVIWDKAV VTGKMDENQF VAVTSTNAAK VFNLYPRKGR ISVGSDADLV IWDPDSVKTI 

       430        440        450        460        470        480 
SAKTHNSALE YNIFEGMECR GSPLVVISQG KIVLEDGTLH VTEGSGRYIP RKPFPDFVYK 

       490        500        510        520        530        540 
RIKARSRLAE LRGVPRGLYD GPVCEVSVTP KTVTPASSAK TSPAKQQAPP VRNLHQSGFS 

       550        560        570 
LSGAQIDDNI PRRTTQRIVA PPGGRANITS LG 

« Hide

References

« Hide 'large scale' references
[1]"TOAD-64, a gene expressed early in neuronal differentiation in the rat, is related to unc-33, a C. elegans gene involved in axon outgrowth."
Minturn J.E., Fryer H.J.L., Geschwind D.H., Hockfield S.
J. Neurosci. 15:6757-6766(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 136-142; 402-418; 441-450 AND 499-511, SUBCELLULAR LOCATION.
Strain: Sprague-Dawley.
Tissue: Brain.
[2]Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 44-56; 76-94; 147-157; 174-238; 259-268; 375-397; 424-467; 472-480; 533-552 AND 558-565, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Brain, Hippocampus and Spinal cord.
[3]"Brain CRMP forms heterotetramers similar to liver dihydropyrimidinase."
Wang L.H., Strittmatter S.M.
J. Neurochem. 69:2261-2269(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CRMP1; DPYSL3 AND DPYSL4, SUBUNIT.
[4]"Neurofibrillary tangle-associated collapsin response mediator protein-2 (CRMP-2) is highly phosphorylated on Thr-509, Ser-518, and Ser-522."
Gu Y., Hamajima N., Ihara Y.
Biochemistry 39:4267-4275(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-509; SER-518 AND SER-522, IDENTIFICATION BY MASS SPECTROMETRY.
[5]"SNOSID, a proteomic method for identification of cysteine S-nitrosylation sites in complex protein mixtures."
Hao G., Derakhshan B., Shi L., Campagne F., Gross S.S.
Proc. Natl. Acad. Sci. U.S.A. 103:1012-1017(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: S-NITROSYLATION [LARGE SCALE ANALYSIS] AT CYS-504, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]Lubec G., Chen W.-Q.
Submitted (FEB-2007) to UniProtKB
Cited for: PHOSPHORYLATION AT THR-509, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z46882 mRNA. Translation: CAA86981.1.
PIRS49985. A59280.
RefSeqNP_001099187.1. NM_001105717.2.
UniGeneRn.2889.

3D structure databases

ProteinModelPortalP47942.
SMRP47942. Positions 14-490.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid247451. 6 interactions.
IntActP47942. 4 interactions.
MINTMINT-224453.
STRING10116.ENSRNOP00000012996.

Protein family/group databases

MEROPSM38.975.

PTM databases

PhosphoSiteP47942.

2D gel databases

World-2DPAGE0004:P47942.

Proteomic databases

PaxDbP47942.
PRIDEP47942.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000012996; ENSRNOP00000012996; ENSRNOG00000009625.
GeneID25416.
KEGGrno:25416.
UCSCRGD:2517. rat.

Organism-specific databases

CTD1808.
RGD2517. Dpysl2.

Phylogenomic databases

eggNOGCOG0044.
GeneTreeENSGT00740000115123.
HOGENOMHOG000219145.
HOVERGENHBG000806.
InParanoidP47942.
KOK07528.
OMAEVPAFFK.
OrthoDBEOG7SJD48.
PhylomeDBP47942.
TreeFamTF314706.

Gene expression databases

GenevestigatorP47942.

Family and domain databases

Gene3D2.30.40.10. 2 hits.
InterProIPR006680. Amidohydro_1.
IPR011778. Hydantoinase/dihydroPyrase.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
PfamPF01979. Amidohydro_1. 1 hit.
[Graphical view]
SUPFAMSSF51338. SSF51338. 2 hits.
TIGRFAMsTIGR02033. D-hydantoinase. 1 hit.
ProtoNetSearch...

Other

NextBio606559.
PROP47942.

Entry information

Entry nameDPYL2_RAT
AccessionPrimary (citable) accession number: P47942
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: June 11, 2014
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families