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P97427 (DPYL1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dihydropyrimidinase-related protein 1

Short name=DRP-1
Alternative name(s):
Collapsin response mediator protein 1
Short name=CRMP-1
Unc-33-like phosphoprotein 3
Short name=ULIP-3
Gene names
Name:Crmp1
Synonyms:Dpysl1, Ulip3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

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

General annotation (Comments)

Function

Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, invasive growth and cell migration. May participate in cytokinesis. Ref.10

Subunit structure

Homotetramer, and heterotetramer with DPYSL2, DPYSL3, DPYSL4 or DPYSL5. Interacts with PLXNA1. Ref.6 Ref.10

Subcellular location

Cytoplasm By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Cytoplasmcytoskeletonspindle By similarity. Note: Associated with centrosomes and the mitotic spindle during metaphase 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 572572Dihydropyrimidinase-related protein 1
PRO_0000165910

Amino acid modifications

Modified residue1011Phosphothreonine; by AURKA By similarity
Modified residue1021Phosphothreonine; by AURKA By similarity
Modified residue3161Nitrated tyrosine Ref.8
Modified residue5041Phosphotyrosine Ref.9
Modified residue5091Phosphothreonine Ref.7 Ref.9

Experimental info

Sequence conflict3381T → I in CAA70300. Ref.2
Sequence conflict4761E → K in BAA21887. Ref.3
Sequence conflict4891F → S in BAA21887. Ref.3
Sequence conflict5201K → E in CAA70300. Ref.2

Secondary structure

................................................................................... 572
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P97427 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: FE17DDCD735CAF8F

FASTA57262,168
        10         20         30         40         50         60 
MSHQGKKSIP HITSDRLLIR GGRIINDDQS FYADVYLEDG LIKQIGENLI VPGGVKTIEA 

        70         80         90        100        110        120 
NGRMVIPGGI DVNTYLQKPS QGMTSADDFF QGTKAALAGG TTMIIDHVVP EPGSSLLTSF 

       130        140        150        160        170        180 
EKWHEAADTK SCCDYSLHVD ITSWYDGVRE ELEVLVQDKG VNSFQVYMAY KDLYQMSDSQ 

       190        200        210        220        230        240 
LYEAFTFLKG LGAVILVHAE NGDLIAQEQK RILEMGITGP EGHALSRPEE LEAEAVFRAI 

       250        260        270        280        290        300 
AIAGRINCPV YITKVMSKSA ADIIALARKK GPLVFGEPIA ASLGTDGTHY WSKNWAKAAA 

       310        320        330        340        350        360 
FVTSPPLSPD PTTPDYLTSL LACGDLQVTG SGHCPYSTAQ KAVGKDNFTL IPEGVNGIEE 

       370        380        390        400        410        420 
RMTVVWDKAV ATGKMDENQF VAVTSTNAAK IFNLYPRKGR IAVGSDADVV IWDPDKMKTI 

       430        440        450        460        470        480 
TAKSHKSTVE YNIFEGMECH GSPLVVISQG KIVFEDGNIS VSKGMGRFIP RKPFPEHLYQ 

       490        500        510        520        530        540 
RVRIRSKVFG LHSVSRGMYD GPVYEVPATP KHAAPAPSAK SSPSKHQPPP IRNLHQSNFS 

       550        560        570 
LSGAQIDDNN PRRTGHRIVA PPGGRSNITS LG 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of the mouse collapsin response mediator protein-1, Crmp1."
Cohen-Salmon M., Crozet F., Rebillard G., Petit C.
Mamm. Genome 8:349-351(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The Ulip family phosphoproteins -- common and specific properties."
Byk T., Ozon S., Sobel A.
Eur. J. Biochem. 254:14-24(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: ICR.
Tissue: Brain.
[3]Hamajima N., Kato Y., Kouwaki M., Wada Y., Sasaski M., Nonaka M.
Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Embryo.
[4]"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].
Strain: C57BL/6.
Tissue: Retina.
[5]Lubec G., Klug S., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 44-56; 150-159; 190-210; 246-254; 259-268; 346-361; 391-397; 401-416; 452-463 AND 472-481, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
[6]"Molecular characterization of CRMP5, a novel member of the collapsin response mediator protein family."
Fukada M., Watakabe I., Yuasa-Kawada J., Kawachi H., Kuroiwa A., Matsuda Y., Noda M.
J. Biol. Chem. 275:37957-37965(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[7]"Phosphoproteomic analysis of the developing mouse brain."
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.
Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-509, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic brain.
[8]"Endogenously nitrated proteins in mouse brain: links to neurodegenerative disease."
Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H., Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J., Squier T.C., Bigelow D.J.
Biochemistry 45:8009-8022(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-316, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[9]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-504 AND THR-509, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[10]"Structural bases for CRMP function in plexin-dependent semaphorin3A signaling."
Deo R.C., Schmidt E.F., Elhabazi A., Togashi H., Burley S.K., Strittmatter S.M.
EMBO J. 23:9-22(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) OF 8-525, FUNCTION, INTERACTION WITH PLEXA1, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U72875 mRNA. Translation: AAB39703.1.
Y09080 mRNA. Translation: CAA70300.1.
AB006714 mRNA. Translation: BAA21887.1.
BC031738 mRNA. Translation: AAH31738.1.
RefSeqNP_031791.3. NM_007765.4.
UniGeneMm.290995.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KCXX-ray2.12A/B8-525[»]
ProteinModelPortalP97427.
SMRP97427. Positions 15-490.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198890. 3 interactions.
IntActP97427. 2 interactions.
MINTMINT-4093514.

Protein family/group databases

MEROPSM38.974.

PTM databases

PhosphoSiteP97427.

Proteomic databases

PaxDbP97427.
PRIDEP97427.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000031004; ENSMUSP00000031004; ENSMUSG00000029121.
GeneID12933.
KEGGmmu:12933.
UCSCuc008xfm.1. mouse.

Organism-specific databases

CTD1400.
MGIMGI:107793. Crmp1.

Phylogenomic databases

eggNOGCOG0044.
GeneTreeENSGT00740000115123.
HOGENOMHOG000219145.
HOVERGENHBG000806.
PhylomeDBP97427.

Gene expression databases

ArrayExpressP97427.
BgeeP97427.
CleanExMM_CRMP1.
GenevestigatorP97427.

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

ChiTaRSCRMP1. mouse.
EvolutionaryTraceP97427.
NextBio282604.
PROP97427.
SOURCESearch...

Entry information

Entry nameDPYL1_MOUSE
AccessionPrimary (citable) accession number: P97427
Secondary accession number(s): O08554, O35097
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 1, 1997
Last modified: April 16, 2014
This is version 119 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot