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Protein

Dihydropyrimidinase-related protein 1

Gene

Crmp1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 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 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

  • axon guidance Source: InterPro
  • microtubule cytoskeleton organization Source: InterPro
  • neuron development Source: RGD
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-RNO-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
Gene namesi
Name:Crmp1
Synonyms:Dpysl1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 14

Organism-specific databases

RGDi2407. Crmp1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 572572Dihydropyrimidinase-related protein 1PRO_0000165911Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei8 – 81PhosphoserineCombined sources
Modified residuei32 – 321PhosphotyrosineBy similarity
Modified residuei101 – 1011PhosphothreonineBy similarity
Modified residuei102 – 1021PhosphothreonineBy similarity
Modified residuei258 – 2581N6-succinyllysineBy similarity
Modified residuei259 – 2591PhosphoserineBy similarity
Modified residuei316 – 3161Nitrated tyrosineBy similarity
Modified residuei431 – 4311PhosphotyrosineBy similarity
Modified residuei499 – 4991PhosphotyrosineBy similarity
Modified residuei504 – 5041PhosphotyrosineBy similarity
Modified residuei509 – 5091PhosphothreonineBy similarity
Modified residuei518 – 5181PhosphoserineBy similarity
Modified residuei521 – 5211PhosphoserineCombined sources
Modified residuei522 – 5221PhosphoserineCombined sources
Modified residuei537 – 5371PhosphoserineBy similarity
Modified residuei540 – 5401PhosphoserineBy similarity
Modified residuei542 – 5421PhosphoserineBy similarity

Keywords - PTMi

Nitration, Phosphoprotein

Proteomic databases

PaxDbiQ62950.
PRIDEiQ62950.

2D gel databases

World-2DPAGE0004:Q62950.

PTM databases

iPTMnetiQ62950.
PhosphoSiteiQ62950.

Expressioni

Gene expression databases

GenevisibleiQ62950. RN.

Interactioni

Subunit structurei

Homotetramer, and heterotetramer with DPYSL2, DPYSL3, DPYSL4 or DPYSL5. Interacts with PLXNA1 (By similarity).By similarity

GO - Molecular functioni

  • filamin binding Source: WormBase

Protein-protein interaction databases

BioGridi247450. 2 interactions.
IntActiQ62950. 2 interactions.
MINTiMINT-4051102.
STRINGi10116.ENSRNOP00000063671.

Structurei

3D structure databases

ProteinModelPortaliQ62950.
SMRiQ62950. Positions 15-490.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2584. Eukaryota.
COG0044. LUCA.
GeneTreeiENSGT00760000119241.
HOGENOMiHOG000219145.
HOVERGENiHBG000806.
InParanoidiQ62950.
OMAiGINSFQV.
OrthoDBiEOG7SJD48.
PhylomeDBiQ62950.

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.

Q62950-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSHQGKKSIP HITSDRLLIR GGRIINDDQS FYADVYLEDG LIKQIGENLI
60 70 80 90 100
VPGGVKTIEA NGRMVIPGGI DVNTYLQKPS QGMTSADDFF 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
Length:572
Mass (Da):62,196
Last modified:November 1, 1996 - v1
Checksum:iED63BD8C751CCFDF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31H → Y in AAB07042 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U52102 mRNA. Translation: AAB03280.1.
U52095 mRNA. Translation: AAB07042.1.
RefSeqiNP_037064.1. NM_012932.2.
UniGeneiRn.11379.

Genome annotation databases

EnsembliENSRNOT00000065334; ENSRNOP00000063671; ENSRNOG00000004781.
GeneIDi25415.
KEGGirno:25415.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U52102 mRNA. Translation: AAB03280.1.
U52095 mRNA. Translation: AAB07042.1.
RefSeqiNP_037064.1. NM_012932.2.
UniGeneiRn.11379.

3D structure databases

ProteinModelPortaliQ62950.
SMRiQ62950. Positions 15-490.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247450. 2 interactions.
IntActiQ62950. 2 interactions.
MINTiMINT-4051102.
STRINGi10116.ENSRNOP00000063671.

Protein family/group databases

MEROPSiM38.974.

PTM databases

iPTMnetiQ62950.
PhosphoSiteiQ62950.

2D gel databases

World-2DPAGE0004:Q62950.

Proteomic databases

PaxDbiQ62950.
PRIDEiQ62950.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000065334; ENSRNOP00000063671; ENSRNOG00000004781.
GeneIDi25415.
KEGGirno:25415.

Organism-specific databases

CTDi1400.
RGDi2407. Crmp1.

Phylogenomic databases

eggNOGiKOG2584. Eukaryota.
COG0044. LUCA.
GeneTreeiENSGT00760000119241.
HOGENOMiHOG000219145.
HOVERGENiHBG000806.
InParanoidiQ62950.
OMAiGINSFQV.
OrthoDBiEOG7SJD48.
PhylomeDBiQ62950.

Enzyme and pathway databases

ReactomeiR-RNO-399956. CRMPs in Sema3A signaling.

Miscellaneous databases

PROiQ62950.

Gene expression databases

GenevisibleiQ62950. RN.

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...

Publicationsi

« Hide 'large scale' publications
  1. "A family of rat CRMP genes is differentially expressed in the nervous system."
    Wang L., Strittmatter S.M.
    J. Neurosci. 16:6197-6207(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. Quach T.T., Honnorat J., Aguera M., Belin M.-F., Kolattukudy P.E., Antoine J.-C.
    Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Brain.
  3. "Brain CRMP forms heterotetramers similar to liver dihydropyrimidinase."
    Wang L.H., Strittmatter S.M.
    J. Neurochem. 69:2261-2269(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, INTERACTION WITH DPYSL2; DPYSL3 AND DPYSL4.
  4. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-521 AND SER-522, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiDPYL1_RAT
AccessioniPrimary (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: June 8, 2016
This is version 125 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

Complete proteome, Reference proteome

Documents

  1. 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.