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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

ReactomeiR-MMU-399956. 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
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:107793. Crmp1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • dendrite Source: MGI
  • growth cone Source: WormBase
  • 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)DescriptionActionsGraphical viewLength
ChainiPRO_00001659101 – 572Dihydropyrimidinase-related protein 1Add BLAST572

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei8PhosphoserineBy similarity1
Modified residuei32PhosphotyrosineBy similarity1
Modified residuei101Phosphothreonine; by AURKABy similarity1
Modified residuei102Phosphothreonine; by AURKABy similarity1
Modified residuei258N6-succinyllysineBy similarity1
Modified residuei259PhosphoserineBy similarity1
Modified residuei316Nitrated tyrosineCombined sources1
Modified residuei431PhosphotyrosineBy similarity1
Modified residuei499PhosphotyrosineBy similarity1
Modified residuei504PhosphotyrosineCombined sources1
Modified residuei509PhosphothreonineCombined sources1
Modified residuei518PhosphoserineBy similarity1
Modified residuei521PhosphoserineBy similarity1
Modified residuei522PhosphoserineBy similarity1
Modified residuei537PhosphoserineCombined sources1
Modified residuei540PhosphoserineCombined sources1
Modified residuei542PhosphoserineCombined sources1
Modified residuei565Asymmetric dimethylarginineBy similarity1

Keywords - PTMi

Methylation, Nitration, Phosphoprotein

Proteomic databases

EPDiP97427.
MaxQBiP97427.
PaxDbiP97427.
PeptideAtlasiP97427.
PRIDEiP97427.

PTM databases

iPTMnetiP97427.
PhosphoSitePlusiP97427.
SwissPalmiP97427.

Expressioni

Gene expression databases

BgeeiENSMUSG00000029121.
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

GO - Molecular functioni

  • filamin binding Source: MGI
  • phosphoprotein binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi198890. 3 interactors.
IntActiP97427. 3 interactors.
MINTiMINT-4093514.
STRINGi10090.ENSMUSP00000109795.

Structurei

Secondary structure

1572
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi17 – 21Combined sources5
Beta strandi23 – 25Combined sources3
Beta strandi30 – 32Combined sources3
Beta strandi34 – 38Combined sources5
Beta strandi41 – 48Combined sources8
Beta strandi56 – 59Combined sources4
Beta strandi64 – 67Combined sources4
Beta strandi69 – 74Combined sources6
Helixi89 – 98Combined sources10
Beta strandi101 – 108Combined sources8
Helixi116 – 130Combined sources15
Beta strandi132 – 141Combined sources10
Helixi148 – 157Combined sources10
Beta strandi163 – 168Combined sources6
Turni171 – 174Combined sources4
Helixi178 – 190Combined sources13
Beta strandi194 – 198Combined sources5
Helixi202 – 214Combined sources13
Helixi221 – 226Combined sources6
Helixi230 – 246Combined sources17
Beta strandi250 – 255Combined sources6
Helixi258 – 270Combined sources13
Beta strandi274 – 279Combined sources6
Helixi280 – 284Combined sources5
Helixi287 – 291Combined sources5
Helixi295 – 300Combined sources6
Helixi313 – 322Combined sources10
Helixi338 – 341Combined sources4
Helixi342 – 344Combined sources3
Helixi348 – 350Combined sources3
Turni358 – 360Combined sources3
Helixi361 – 369Combined sources9
Turni370 – 373Combined sources4
Helixi377 – 384Combined sources8
Helixi386 – 391Combined sources6
Turni395 – 397Combined sources3
Beta strandi409 – 419Combined sources11
Turni422 – 424Combined sources3
Beta strandi426 – 430Combined sources5
Turni433 – 436Combined sources4
Beta strandi438 – 448Combined sources11
Beta strandi451 – 455Combined sources5
Helixi476 – 488Combined sources13

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP97427.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2584. Eukaryota.
COG0044. LUCA.
GeneTreeiENSGT00760000119241.
HOGENOMiHOG000219145.
HOVERGENiHBG000806.
InParanoidiP97427.
PhylomeDBiP97427.

Family and domain databases

CDDicd01314. D-HYD. 1 hit.
Gene3Di2.30.40.10. 2 hits.
InterProiIPR006680. Amidohydro-rel.
IPR030624. CRMP1.
IPR011778. Hydantoinase/dihydroPyrase.
IPR011059. Metal-dep_hydrolase_composite.
IPR032466. Metal_Hydrolase.
[Graphical view]
PANTHERiPTHR11647:SF54. PTHR11647:SF54. 1 hit.
PfamiPF01979. Amidohydro_1. 1 hit.
[Graphical view]
SUPFAMiSSF51338. SSF51338. 2 hits.
SSF51556. SSF51556. 1 hit.
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)DescriptionActionsGraphical viewLength
Sequence conflicti338T → I in CAA70300 (PubMed:9652388).Curated1
Sequence conflicti476E → K in BAA21887 (Ref. 3) Curated1
Sequence conflicti489F → S in BAA21887 (Ref. 3) Curated1
Sequence conflicti520K → E in CAA70300 (PubMed:9652388).Curated1

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.
KEGGimmu:12933.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KCXX-ray2.12A/B8-525[»]
ProteinModelPortaliP97427.
SMRiP97427.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198890. 3 interactors.
IntActiP97427. 3 interactors.
MINTiMINT-4093514.
STRINGi10090.ENSMUSP00000109795.

Protein family/group databases

MEROPSiM38.974.

PTM databases

iPTMnetiP97427.
PhosphoSitePlusiP97427.
SwissPalmiP97427.

Proteomic databases

EPDiP97427.
MaxQBiP97427.
PaxDbiP97427.
PeptideAtlasiP97427.
PRIDEiP97427.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031004; ENSMUSP00000031004; ENSMUSG00000029121.
GeneIDi12933.
KEGGimmu:12933.
UCSCiuc008xfm.2. mouse.

Organism-specific databases

CTDi1400.
MGIiMGI:107793. Crmp1.

Phylogenomic databases

eggNOGiKOG2584. Eukaryota.
COG0044. LUCA.
GeneTreeiENSGT00760000119241.
HOGENOMiHOG000219145.
HOVERGENiHBG000806.
InParanoidiP97427.
PhylomeDBiP97427.

Enzyme and pathway databases

ReactomeiR-MMU-399956. CRMPs in Sema3A signaling.

Miscellaneous databases

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

Gene expression databases

BgeeiENSMUSG00000029121.
CleanExiMM_CRMP1.
ExpressionAtlasiP97427. baseline and differential.
GenevisibleiP97427. MM.

Family and domain databases

CDDicd01314. D-HYD. 1 hit.
Gene3Di2.30.40.10. 2 hits.
InterProiIPR006680. Amidohydro-rel.
IPR030624. CRMP1.
IPR011778. Hydantoinase/dihydroPyrase.
IPR011059. Metal-dep_hydrolase_composite.
IPR032466. Metal_Hydrolase.
[Graphical view]
PANTHERiPTHR11647:SF54. PTHR11647:SF54. 1 hit.
PfamiPF01979. Amidohydro_1. 1 hit.
[Graphical view]
SUPFAMiSSF51338. SSF51338. 2 hits.
SSF51556. SSF51556. 1 hit.
TIGRFAMsiTIGR02033. D-hydantoinase. 1 hit.
ProtoNetiSearch...

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: November 2, 2016
This is version 145 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

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 one 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.