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P97427

- DPYL1_MOUSE

UniProt

P97427 - DPYL1_MOUSE

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Protein

Dihydropyrimidinase-related protein 1

Gene

Crmp1

Organism
Mus musculus (Mouse)
Status
Reviewed - 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

  1. hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides Source: InterPro
  2. phosphoprotein binding Source: BHF-UCL

GO - Biological processi

  1. pyrimidine nucleobase catabolic process Source: InterPro
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_244852. 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: Chromosome 5

Organism-specific databases

MGIiMGI:107793. Crmp1.

Subcellular locationi

Cytoplasm By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Cytoplasmcytoskeletonspindle By similarity
Note: Associated with centrosomes and the mitotic spindle during metaphase.By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. cytoskeleton Source: UniProtKB-KW
  3. dendrite Source: MGI
  4. neuronal cell body Source: MGI
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 residuei101 – 1011Phosphothreonine; by AURKABy similarity
Modified residuei102 – 1021Phosphothreonine; by AURKABy similarity
Modified residuei316 – 3161Nitrated tyrosine1 Publication
Modified residuei504 – 5041Phosphotyrosine1 Publication
Modified residuei509 – 5091Phosphothreonine2 Publications

Keywords - PTMi

Nitration, Phosphoprotein

Proteomic databases

MaxQBiP97427.
PaxDbiP97427.
PRIDEiP97427.

PTM databases

PhosphoSiteiP97427.

Expressioni

Gene expression databases

BgeeiP97427.
CleanExiMM_CRMP1.
ExpressionAtlasiP97427. baseline and differential.
GenevestigatoriP97427.

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.

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.
IPR011778. Hydantoinase/dihydroPyrase.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
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. 1 PublicationCurated
Sequence conflicti489 – 4891F → S in BAA21887. 1 PublicationCurated
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.1. 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 .
CCDSi CCDS39075.1.
RefSeqi NP_031791.3. NM_007765.4.
UniGenei Mm.290995.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1KCX X-ray 2.12 A/B 8-525 [» ]
ProteinModelPortali P97427.
SMRi P97427. Positions 15-490.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198890. 3 interactions.
IntActi P97427. 2 interactions.
MINTi MINT-4093514.

Protein family/group databases

MEROPSi M38.974.

PTM databases

PhosphoSitei P97427.

Proteomic databases

MaxQBi P97427.
PaxDbi P97427.
PRIDEi P97427.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000031004 ; ENSMUSP00000031004 ; ENSMUSG00000029121 .
GeneIDi 12933.
KEGGi mmu:12933.
UCSCi uc008xfm.1. mouse.

Organism-specific databases

CTDi 1400.
MGIi MGI:107793. Crmp1.

Phylogenomic databases

eggNOGi COG0044.
GeneTreei ENSGT00760000119241.
HOGENOMi HOG000219145.
HOVERGENi HBG000806.
InParanoidi P97427.
PhylomeDBi P97427.

Enzyme and pathway databases

Reactomei REACT_244852. CRMPs in Sema3A signaling.

Miscellaneous databases

ChiTaRSi Crmp1. mouse.
EvolutionaryTracei P97427.
NextBioi 282604.
PROi P97427.
SOURCEi Search...

Gene expression databases

Bgeei P97427.
CleanExi MM_CRMP1.
ExpressionAtlasi P97427. baseline and differential.
Genevestigatori P97427.

Family and domain databases

Gene3Di 2.30.40.10. 2 hits.
InterProi IPR006680. Amidohydro_1.
IPR011778. Hydantoinase/dihydroPyrase.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view ]
Pfami PF01979. Amidohydro_1. 1 hit.
[Graphical view ]
SUPFAMi SSF51338. SSF51338. 2 hits.
TIGRFAMsi TIGR02033. D-hydantoinase. 1 hit.
ProtoNeti Search...

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: November 26, 2014
This is version 124 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