Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Dihydropyrimidinase-related protein 1

Gene

Crmp1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_314392. CRMPs in Sema3A signaling.

Protein family/group databases

MEROPSiM38.974.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Crmp1
Synonyms:Dpysl1, Ulip3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:107793. Crmp1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • dendrite Source: MGI
  • microtubule organizing center Source: UniProtKB-SubCell
  • neuronal cell body Source: MGI
  • spindle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 572572Dihydropyrimidinase-related protein 1PRO_0000165910Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei32 – 321PhosphotyrosineBy similarity
Modified residuei101 – 1011Phosphothreonine; by AURKABy similarity
Modified residuei102 – 1021Phosphothreonine; by AURKABy similarity
Modified residuei258 – 2581N6-succinyllysineBy similarity
Modified residuei259 – 2591PhosphoserineBy similarity
Modified residuei316 – 3161Nitrated tyrosine1 Publication
Modified residuei431 – 4311PhosphotyrosineBy similarity
Modified residuei499 – 4991PhosphotyrosineBy similarity
Modified residuei504 – 5041Phosphotyrosine1 Publication
Modified residuei509 – 5091Phosphothreonine2 Publications
Modified residuei518 – 5181PhosphoserineBy similarity
Modified residuei522 – 5221PhosphoserineBy similarity

Keywords - PTMi

Nitration, Phosphoprotein

Proteomic databases

MaxQBiP97427.
PaxDbiP97427.
PRIDEiP97427.

PTM databases

PhosphoSiteiP97427.

Expressioni

Gene expression databases

BgeeiP97427.
CleanExiMM_CRMP1.
ExpressionAtlasiP97427. baseline and differential.
GenevisibleiP97427. MM.

Interactioni

Subunit structurei

Homotetramer, and heterotetramer with DPYSL2, DPYSL3, DPYSL4 or DPYSL5. Interacts with PLXNA1.2 Publications

Protein-protein interaction databases

BioGridi198890. 3 interactions.
IntActiP97427. 2 interactions.
MINTiMINT-4093514.
STRINGi10090.ENSMUSP00000109795.

Structurei

Secondary structure

1
572
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi17 – 215Combined sources
Beta strandi23 – 253Combined sources
Beta strandi30 – 323Combined sources
Beta strandi34 – 385Combined sources
Beta strandi41 – 488Combined sources
Beta strandi56 – 594Combined sources
Beta strandi64 – 674Combined sources
Beta strandi69 – 746Combined sources
Helixi89 – 9810Combined sources
Beta strandi101 – 1088Combined sources
Helixi116 – 13015Combined sources
Beta strandi132 – 14110Combined sources
Helixi148 – 15710Combined sources
Beta strandi163 – 1686Combined sources
Turni171 – 1744Combined sources
Helixi178 – 19013Combined sources
Beta strandi194 – 1985Combined sources
Helixi202 – 21413Combined sources
Helixi221 – 2266Combined sources
Helixi230 – 24617Combined sources
Beta strandi250 – 2556Combined sources
Helixi258 – 27013Combined sources
Beta strandi274 – 2796Combined sources
Helixi280 – 2845Combined sources
Helixi287 – 2915Combined sources
Helixi295 – 3006Combined sources
Helixi313 – 32210Combined sources
Helixi338 – 3414Combined sources
Helixi342 – 3443Combined sources
Helixi348 – 3503Combined sources
Turni358 – 3603Combined sources
Helixi361 – 3699Combined sources
Turni370 – 3734Combined sources
Helixi377 – 3848Combined sources
Helixi386 – 3916Combined sources
Turni395 – 3973Combined sources
Beta strandi409 – 41911Combined sources
Turni422 – 4243Combined sources
Beta strandi426 – 4305Combined sources
Turni433 – 4364Combined sources
Beta strandi438 – 44811Combined sources
Beta strandi451 – 4555Combined sources
Helixi476 – 48813Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KCXX-ray2.12A/B8-525[»]
ProteinModelPortaliP97427.
SMRiP97427. Positions 15-490.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP97427.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0044.
GeneTreeiENSGT00760000119241.
HOGENOMiHOG000219145.
HOVERGENiHBG000806.
InParanoidiP97427.
PhylomeDBiP97427.

Family and domain databases

Gene3Di2.30.40.10. 2 hits.
InterProiIPR006680. Amidohydro_1.
IPR030624. CRMP1.
IPR011778. Hydantoinase/dihydroPyrase.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
PANTHERiPTHR11647:SF54. PTHR11647:SF54. 1 hit.
PfamiPF01979. Amidohydro_1. 1 hit.
[Graphical view]
SUPFAMiSSF51338. SSF51338. 2 hits.
TIGRFAMsiTIGR02033. D-hydantoinase. 1 hit.

Sequencei

Sequence statusi: Complete.

P97427-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSHQGKKSIP HITSDRLLIR GGRIINDDQS FYADVYLEDG LIKQIGENLI
60 70 80 90 100
VPGGVKTIEA NGRMVIPGGI DVNTYLQKPS QGMTSADDFF QGTKAALAGG
110 120 130 140 150
TTMIIDHVVP EPGSSLLTSF EKWHEAADTK SCCDYSLHVD ITSWYDGVRE
160 170 180 190 200
ELEVLVQDKG VNSFQVYMAY KDLYQMSDSQ LYEAFTFLKG LGAVILVHAE
210 220 230 240 250
NGDLIAQEQK RILEMGITGP EGHALSRPEE LEAEAVFRAI AIAGRINCPV
260 270 280 290 300
YITKVMSKSA ADIIALARKK GPLVFGEPIA ASLGTDGTHY WSKNWAKAAA
310 320 330 340 350
FVTSPPLSPD PTTPDYLTSL LACGDLQVTG SGHCPYSTAQ KAVGKDNFTL
360 370 380 390 400
IPEGVNGIEE RMTVVWDKAV ATGKMDENQF VAVTSTNAAK IFNLYPRKGR
410 420 430 440 450
IAVGSDADVV IWDPDKMKTI TAKSHKSTVE YNIFEGMECH GSPLVVISQG
460 470 480 490 500
KIVFEDGNIS VSKGMGRFIP RKPFPEHLYQ RVRIRSKVFG LHSVSRGMYD
510 520 530 540 550
GPVYEVPATP KHAAPAPSAK SSPSKHQPPP IRNLHQSNFS LSGAQIDDNN
560 570
PRRTGHRIVA PPGGRSNITS LG
Length:572
Mass (Da):62,168
Last modified:May 1, 1997 - v1
Checksum:iFE17DDCD735CAF8F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti338 – 3381T → I in CAA70300 (PubMed:9652388).Curated
Sequence conflicti476 – 4761E → K in BAA21887 (Ref. 3) Curated
Sequence conflicti489 – 4891F → S in BAA21887 (Ref. 3) Curated
Sequence conflicti520 – 5201K → E in CAA70300 (PubMed:9652388).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U72875 mRNA. Translation: AAB39703.1.
Y09080 mRNA. Translation: CAA70300.1.
AB006714 mRNA. Translation: BAA21887.1.
BC031738 mRNA. Translation: AAH31738.1.
CCDSiCCDS39075.1.
RefSeqiNP_031791.3. NM_007765.4.
UniGeneiMm.290995.

Genome annotation databases

EnsembliENSMUST00000031004; ENSMUSP00000031004; ENSMUSG00000029121.
GeneIDi12933.
UCSCiuc008xfm.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U72875 mRNA. Translation: AAB39703.1.
Y09080 mRNA. Translation: CAA70300.1.
AB006714 mRNA. Translation: BAA21887.1.
BC031738 mRNA. Translation: AAH31738.1.
CCDSiCCDS39075.1.
RefSeqiNP_031791.3. NM_007765.4.
UniGeneiMm.290995.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KCXX-ray2.12A/B8-525[»]
ProteinModelPortaliP97427.
SMRiP97427. Positions 15-490.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198890. 3 interactions.
IntActiP97427. 2 interactions.
MINTiMINT-4093514.
STRINGi10090.ENSMUSP00000109795.

Protein family/group databases

MEROPSiM38.974.

PTM databases

PhosphoSiteiP97427.

Proteomic databases

MaxQBiP97427.
PaxDbiP97427.
PRIDEiP97427.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031004; ENSMUSP00000031004; ENSMUSG00000029121.
GeneIDi12933.
UCSCiuc008xfm.2. mouse.

Organism-specific databases

CTDi1400.
MGIiMGI:107793. Crmp1.

Phylogenomic databases

eggNOGiCOG0044.
GeneTreeiENSGT00760000119241.
HOGENOMiHOG000219145.
HOVERGENiHBG000806.
InParanoidiP97427.
PhylomeDBiP97427.

Enzyme and pathway databases

ReactomeiREACT_314392. CRMPs in Sema3A signaling.

Miscellaneous databases

ChiTaRSiCrmp1. mouse.
EvolutionaryTraceiP97427.
NextBioi282604.
PROiP97427.
SOURCEiSearch...

Gene expression databases

BgeeiP97427.
CleanExiMM_CRMP1.
ExpressionAtlasiP97427. baseline and differential.
GenevisibleiP97427. MM.

Family and domain databases

Gene3Di2.30.40.10. 2 hits.
InterProiIPR006680. Amidohydro_1.
IPR030624. CRMP1.
IPR011778. Hydantoinase/dihydroPyrase.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
PANTHERiPTHR11647:SF54. PTHR11647:SF54. 1 hit.
PfamiPF01979. Amidohydro_1. 1 hit.
[Graphical view]
SUPFAMiSSF51338. SSF51338. 2 hits.
TIGRFAMsiTIGR02033. D-hydantoinase. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-509, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  8. 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.

Entry informationi

Entry nameiDPYL1_MOUSE
AccessioniPrimary (citable) accession number: P97427
Secondary accession number(s): O08554, O35097
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 1, 1997
Last modified: July 22, 2015
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.