UniProtKB - Q62950 (DPYL1_RAT)
Protein
Dihydropyrimidinase-related protein 1
Gene
Crmp1
Organism
Rattus norvegicus (Rat)
Status
Functioni
Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton (By similarity). Plays a role in axon guidance (By similarity). During the axon guidance process, acts downstream of SEMA3A to promote FLNA dissociation from F-actin which results in the rearrangement of the actin cytoskeleton and the collapse of the growth cone (By similarity). Involved in invasive growth and cell migration. May participate in cytokinesis (By similarity).By similarity
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
GO - Molecular functioni
- filamin binding Source: WormBase
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds Source: InterPro
- identical protein binding Source: RGD
- phosphoprotein binding Source: RGD
GO - Biological processi
- axon guidance Source: InterPro
- microtubule cytoskeleton organization Source: InterPro
- negative regulation of actin filament binding Source: RGD
- negative regulation of neuron projection development Source: RGD
- neuron development Source: RGD
- semaphorin-plexin signaling pathway Source: RGD
Enzyme and pathway databases
Reactomei | R-RNO-399956, CRMPs in Sema3A signaling |
Protein family/group databases
MEROPSi | M38.974 |
Names & Taxonomyi
Protein namesi | Recommended name: Dihydropyrimidinase-related protein 1Short name: DRP-1 Alternative name(s): Collapsin response mediator protein 1 Short name: CRMP-1 Inactive dihydropyrimidinaseCurated |
Gene namesi | Name:Crmp1 Synonyms:Dpysl1 |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 2407, Crmp1 |
Subcellular locationi
Cytoskeleton
- centrosome By similarity
- spindle By similarity
- cytoskeleton By similarity
Other locations
- Cytoplasm By similarity
- growth cone By similarity
- Perikaryon By similarity
Note: Associated with centrosomes and the mitotic spindle during metaphase (By similarity). Colocalizes with FLNA and tubulin in the central region of DRG neuron growth cone. Following SEMA3A stimulation of DRG neurons, colocalizes with F-actin (By similarity).By similarity
Cytoskeleton
- actin cytoskeleton Source: RGD
- centrosome Source: Ensembl
- spindle Source: UniProtKB-SubCell
Cytosol
- cytosol Source: Ensembl
Nucleus
- nucleus Source: RGD
Other locations
- cytoplasm Source: RGD
- dendrite Source: RGD
- growth cone Source: RGD
- midbody Source: RGD
- neuronal cell body Source: RGD
- perikaryon Source: UniProtKB-SubCell
Keywords - Cellular componenti
Cell projection, Cytoplasm, CytoskeletonPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000165911 | 1 – 572 | Dihydropyrimidinase-related protein 1Add BLAST | 572 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 8 | PhosphoserineCombined sources | 1 | |
Modified residuei | 101 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 102 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 316 | 3'-nitrotyrosineBy similarity | 1 | |
Modified residuei | 504 | PhosphotyrosineBy similarity | 1 | |
Modified residuei | 509 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 521 | PhosphoserineCombined sources | 1 | |
Modified residuei | 522 | PhosphoserineCombined sources | 1 | |
Modified residuei | 537 | PhosphoserineBy similarity | 1 | |
Modified residuei | 540 | PhosphoserineBy similarity | 1 | |
Modified residuei | 542 | PhosphoserineBy similarity | 1 |
Post-translational modificationi
Phosphorylation at Ser-522 enhances CRMP1-mediated alteration of FLNA ternary structure and FLNA dissociation from F-actin.By similarity
Keywords - PTMi
Nitration, PhosphoproteinProteomic databases
jPOSTi | Q62950 |
PaxDbi | Q62950 |
PRIDEi | Q62950 |
2D gel databases
World-2DPAGEi | 0004:Q62950 |
PTM databases
iPTMneti | Q62950 |
PhosphoSitePlusi | Q62950 |
Expressioni
Developmental stagei
Expressed in the brain of 20 dpc embryos.1 Publication
Gene expression databases
Bgeei | ENSRNOG00000004781, Expressed in frontal cortex and 20 other tissues |
Genevisiblei | Q62950, RN |
Interactioni
Subunit structurei
Homotetramer, and heterotetramer with DPYSL2, DPYSL3, DPYSL4 or DPYSL5 (By similarity).
Interacts with PLXNA1 (By similarity).
Interacts with FLNA (via calponin-homology (CH) domain 1 and filamin repeat 24); the interaction alters FLNA ternary structure and thus promotes FLNA dissociation from F-actin (PubMed:25358863).
By similarity1 PublicationGO - Molecular functioni
- filamin binding Source: WormBase
- identical protein binding Source: RGD
- phosphoprotein binding Source: RGD
Protein-protein interaction databases
BioGRIDi | 247450, 4 interactors |
IntActi | Q62950, 3 interactors |
MINTi | Q62950 |
STRINGi | 10116.ENSRNOP00000063671 |
Family & Domainsi
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 246 – 247 | Required for interaction with FLNABy similarity | 2 |
Sequence similaritiesi
Belongs to the metallo-dependent hydrolases superfamily. Hydantoinase/dihydropyrimidinase family.Curated
Phylogenomic databases
eggNOGi | KOG2584, Eukaryota |
GeneTreei | ENSGT00990000203659 |
HOGENOMi | CLU_015572_2_2_1 |
InParanoidi | Q62950 |
OMAi | HICHVSH |
OrthoDBi | 719800at2759 |
PhylomeDBi | Q62950 |
Family and domain databases
CDDi | cd01314, D-HYD, 1 hit |
Gene3Di | 2.30.40.10, 1 hit |
InterProi | View protein in InterPro IPR006680, Amidohydro-rel IPR030624, CRMP1 IPR011778, Hydantoinase/dihydroPyrase IPR011059, Metal-dep_hydrolase_composite IPR032466, Metal_Hydrolase |
PANTHERi | PTHR11647:SF54, PTHR11647:SF54, 1 hit |
Pfami | View protein in Pfam PF01979, Amidohydro_1, 1 hit |
SUPFAMi | SSF51338, SSF51338, 2 hits SSF51556, SSF51556, 1 hit |
TIGRFAMsi | TIGR02033, D-hydantoinase, 1 hit |
i Sequence
Sequence statusi: Complete.
Q62950-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MSHQGKKSIP HITSDRLLIR GGRIINDDQS FYADVYLEDG LIKQIGENLI
60 70 80 90 100
VPGGVKTIEA NGRMVIPGGI DVNTYLQKPS QGMTSADDFF QGTRAALAGG
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 IWDPDKMKTL 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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 3 | H → Y in AAB07042 (Ref. 2) Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U52102 mRNA Translation: AAB03280.1 U52095 mRNA Translation: AAB07042.1 |
RefSeqi | NP_037064.1, NM_012932.2 |
Genome annotation databases
Ensembli | ENSRNOT00000065334; ENSRNOP00000063671; ENSRNOG00000004781 |
GeneIDi | 25415 |
KEGGi | rno:25415 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U52102 mRNA Translation: AAB03280.1 U52095 mRNA Translation: AAB07042.1 |
RefSeqi | NP_037064.1, NM_012932.2 |
3D structure databases
SMRi | Q62950 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 247450, 4 interactors |
IntActi | Q62950, 3 interactors |
MINTi | Q62950 |
STRINGi | 10116.ENSRNOP00000063671 |
Protein family/group databases
MEROPSi | M38.974 |
PTM databases
iPTMneti | Q62950 |
PhosphoSitePlusi | Q62950 |
2D gel databases
World-2DPAGEi | 0004:Q62950 |
Proteomic databases
jPOSTi | Q62950 |
PaxDbi | Q62950 |
PRIDEi | Q62950 |
Genome annotation databases
Ensembli | ENSRNOT00000065334; ENSRNOP00000063671; ENSRNOG00000004781 |
GeneIDi | 25415 |
KEGGi | rno:25415 |
Organism-specific databases
CTDi | 1400 |
RGDi | 2407, Crmp1 |
Phylogenomic databases
eggNOGi | KOG2584, Eukaryota |
GeneTreei | ENSGT00990000203659 |
HOGENOMi | CLU_015572_2_2_1 |
InParanoidi | Q62950 |
OMAi | HICHVSH |
OrthoDBi | 719800at2759 |
PhylomeDBi | Q62950 |
Enzyme and pathway databases
Reactomei | R-RNO-399956, CRMPs in Sema3A signaling |
Miscellaneous databases
PROi | PR:Q62950 |
Gene expression databases
Bgeei | ENSRNOG00000004781, Expressed in frontal cortex and 20 other tissues |
Genevisiblei | Q62950, RN |
Family and domain databases
CDDi | cd01314, D-HYD, 1 hit |
Gene3Di | 2.30.40.10, 1 hit |
InterProi | View protein in InterPro IPR006680, Amidohydro-rel IPR030624, CRMP1 IPR011778, Hydantoinase/dihydroPyrase IPR011059, Metal-dep_hydrolase_composite IPR032466, Metal_Hydrolase |
PANTHERi | PTHR11647:SF54, PTHR11647:SF54, 1 hit |
Pfami | View protein in Pfam PF01979, Amidohydro_1, 1 hit |
SUPFAMi | SSF51338, SSF51338, 2 hits SSF51556, SSF51556, 1 hit |
TIGRFAMsi | TIGR02033, D-hydantoinase, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | DPYL1_RAT | |
Accessioni | Q62950Primary (citable) accession number: Q62950 Secondary accession number(s): P70546 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 15, 1998 |
Last sequence update: | November 1, 1996 | |
Last modified: | February 10, 2021 | |
This is version 159 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families