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P97427

- DPYL1_MOUSE

UniProt

P97427 - DPYL1_MOUSE

Protein

Dihydropyrimidinase-related protein 1

Gene

Crmp1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      Previous versions | rss
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    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

    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-SubCell
    2. dendrite Source: MGI
    3. microtubule organizing center Source: UniProtKB-SubCell
    4. neuronal cell body Source: MGI
    5. spindle Source: UniProtKB-SubCell

    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

    ArrayExpressiP97427.
    BgeeiP97427.
    CleanExiMM_CRMP1.
    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 – 215
    Beta strandi23 – 253
    Beta strandi30 – 323
    Beta strandi34 – 385
    Beta strandi41 – 488
    Beta strandi56 – 594
    Beta strandi64 – 674
    Beta strandi69 – 746
    Helixi89 – 9810
    Beta strandi101 – 1088
    Helixi116 – 13015
    Beta strandi132 – 14110
    Helixi148 – 15710
    Beta strandi163 – 1686
    Turni171 – 1744
    Helixi178 – 19013
    Beta strandi194 – 1985
    Helixi202 – 21413
    Helixi221 – 2266
    Helixi230 – 24617
    Beta strandi250 – 2556
    Helixi258 – 27013
    Beta strandi274 – 2796
    Helixi280 – 2845
    Helixi287 – 2915
    Helixi295 – 3006
    Helixi313 – 32210
    Helixi338 – 3414
    Helixi342 – 3443
    Helixi348 – 3503
    Turni358 – 3603
    Helixi361 – 3699
    Turni370 – 3734
    Helixi377 – 3848
    Helixi386 – 3916
    Turni395 – 3973
    Beta strandi409 – 41911
    Turni422 – 4243
    Beta strandi426 – 4305
    Turni433 – 4364
    Beta strandi438 – 44811
    Beta strandi451 – 4555
    Helixi476 – 48813

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    GeneTreeiENSGT00740000115123.
    HOGENOMiHOG000219145.
    HOVERGENiHBG000806.
    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

    MSHQGKKSIP HITSDRLLIR GGRIINDDQS FYADVYLEDG LIKQIGENLI    50
    VPGGVKTIEA NGRMVIPGGI DVNTYLQKPS QGMTSADDFF QGTKAALAGG 100
    TTMIIDHVVP EPGSSLLTSF EKWHEAADTK SCCDYSLHVD ITSWYDGVRE 150
    ELEVLVQDKG VNSFQVYMAY KDLYQMSDSQ LYEAFTFLKG LGAVILVHAE 200
    NGDLIAQEQK RILEMGITGP EGHALSRPEE LEAEAVFRAI AIAGRINCPV 250
    YITKVMSKSA ADIIALARKK GPLVFGEPIA ASLGTDGTHY WSKNWAKAAA 300
    FVTSPPLSPD PTTPDYLTSL LACGDLQVTG SGHCPYSTAQ KAVGKDNFTL 350
    IPEGVNGIEE RMTVVWDKAV ATGKMDENQF VAVTSTNAAK IFNLYPRKGR 400
    IAVGSDADVV IWDPDKMKTI TAKSHKSTVE YNIFEGMECH GSPLVVISQG 450
    KIVFEDGNIS VSKGMGRFIP RKPFPEHLYQ RVRIRSKVFG LHSVSRGMYD 500
    GPVYEVPATP KHAAPAPSAK SSPSKHQPPP IRNLHQSNFS LSGAQIDDNN 550
    PRRTGHRIVA PPGGRSNITS LG 572
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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 ENSGT00740000115123.
    HOGENOMi HOG000219145.
    HOVERGENi HBG000806.
    PhylomeDBi P97427.

    Miscellaneous databases

    ChiTaRSi CRMP1. mouse.
    EvolutionaryTracei P97427.
    NextBioi 282604.
    PROi P97427.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P97427.
    Bgeei P97427.
    CleanExi MM_CRMP1.
    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

    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: October 1, 2014
    This is version 122 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