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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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 572572Dihydropyrimidinase-related protein 1PRO_0000165910Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei8 – 81PhosphoserineBy similarity
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 tyrosineCombined sources
Modified residuei431 – 4311PhosphotyrosineBy similarity
Modified residuei499 – 4991PhosphotyrosineBy similarity
Modified residuei504 – 5041PhosphotyrosineCombined sources
Modified residuei509 – 5091PhosphothreonineCombined sources
Modified residuei518 – 5181PhosphoserineBy similarity
Modified residuei521 – 5211PhosphoserineBy similarity
Modified residuei522 – 5221PhosphoserineBy similarity
Modified residuei537 – 5371PhosphoserineCombined sources
Modified residuei540 – 5401PhosphoserineCombined sources
Modified residuei542 – 5421PhosphoserineCombined sources

Keywords - PTMi

Nitration, Phosphoprotein

Proteomic databases

EPDiP97427.
MaxQBiP97427.
PaxDbiP97427.
PeptideAtlasiP97427.
PRIDEiP97427.

PTM databases

iPTMnetiP97427.
PhosphoSiteiP97427.
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 interactions.
IntActiP97427. 3 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

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

Family and domain databases

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)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.
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
EntryMethodResolution (Å)ChainPositionsPDBsum
1KCXX-ray2.12A/B8-525[»]
ProteinModelPortaliP97427.
SMRiP97427. Positions 15-490.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Protein family/group databases

MEROPSiM38.974.

PTM databases

iPTMnetiP97427.
PhosphoSiteiP97427.
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

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: September 7, 2016
This is version 143 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.