DPYL1_MOUSE
ID DPYL1_MOUSE Reviewed; 572 AA.
AC P97427; O08554; O35097;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Dihydropyrimidinase-related protein 1;
DE Short=DRP-1;
DE AltName: Full=Collapsin response mediator protein 1;
DE Short=CRMP-1;
DE AltName: Full=Inactive dihydropyrimidinase {ECO:0000305};
DE AltName: Full=Unc-33-like phosphoprotein 3;
DE Short=ULIP-3;
GN Name=Crmp1; Synonyms=Dpysl1, Ulip3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9107681; DOI=10.1007/s003359900438;
RA Cohen-Salmon M., Crozet F., Rebillard G., Petit C.;
RT "Cloning and characterization of the mouse collapsin response mediator
RT protein-1, Crmp1.";
RL Mamm. Genome 8:349-351(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ICR; TISSUE=Brain;
RX PubMed=9652388; DOI=10.1046/j.1432-1327.1998.2540014.x;
RA Byk T., Ozon S., Sobel A.;
RT "The Ulip family phosphoproteins -- common and specific properties.";
RL Eur. J. Biochem. 254:14-24(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo;
RA Hamajima N., Kato Y., Kouwaki M., Wada Y., Sasaski M., Nonaka M.;
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Retina;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 44-56; 150-159; 190-210; 246-254; 259-268; 346-361;
RP 391-397; 401-416; 452-463 AND 472-481, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Klug S., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [6]
RP SUBUNIT.
RX PubMed=10956643; DOI=10.1074/jbc.m003277200;
RA Fukada M., Watakabe I., Yuasa-Kawada J., Kawachi H., Kuroiwa A.,
RA Matsuda Y., Noda M.;
RT "Molecular characterization of CRMP5, a novel member of the collapsin
RT response mediator protein family.";
RL J. Biol. Chem. 275:37957-37965(2000).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-509, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [8]
RP NITRATION [LARGE SCALE ANALYSIS] AT TYR-316, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16800626; DOI=10.1021/bi060474w;
RA Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H., Lacan G.,
RA Melega W.P., Camp D.G. II, Smith R.D., Smith D.J., Squier T.C.,
RA Bigelow D.J.;
RT "Endogenously nitrated proteins in mouse brain: links to neurodegenerative
RT disease.";
RL Biochemistry 45:8009-8022(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-504 AND THR-509, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-509; SER-537; SER-540 AND
RP SER-542, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=25358863; DOI=10.1038/ncomms6325;
RA Nakamura F., Kumeta K., Hida T., Isono T., Nakayama Y.,
RA Kuramata-Matsuoka E., Yamashita N., Uchida Y., Ogura K., Gengyo-Ando K.,
RA Mitani S., Ogino T., Goshima Y.;
RT "Amino- and carboxyl-terminal domains of Filamin-A interact with CRMP1 to
RT mediate Sema3A signalling.";
RL Nat. Commun. 5:5325-5325(2014).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) OF 8-525, FUNCTION, INTERACTION WITH
RP PLEXA1, AND SUBUNIT.
RX PubMed=14685275; DOI=10.1038/sj.emboj.7600021;
RA Deo R.C., Schmidt E.F., Elhabazi A., Togashi H., Burley S.K.,
RA Strittmatter S.M.;
RT "Structural bases for CRMP function in plexin-dependent semaphorin3A
RT signaling.";
RL EMBO J. 23:9-22(2004).
CC -!- FUNCTION: Necessary for signaling by class 3 semaphorins and subsequent
CC remodeling of the cytoskeleton (PubMed:25358863, PubMed:14685275).
CC Plays a role in axon guidance (PubMed:14685275). During the axon
CC guidance process, acts downstream of SEMA3A to promote FLNA
CC dissociation from F-actin which results in the rearrangement of the
CC actin cytoskeleton and the collapse of the growth cone
CC (PubMed:25358863). Involved in invasive growth and cell migration (By
CC similarity). May participate in cytokinesis (By similarity).
CC {ECO:0000250|UniProtKB:Q14194, ECO:0000269|PubMed:14685275,
CC ECO:0000269|PubMed:25358863}.
CC -!- SUBUNIT: Homotetramer, and heterotetramer with DPYSL2, DPYSL3, DPYSL4
CC or DPYSL5 (PubMed:10956643, PubMed:14685275). Interacts with PLXNA1
CC (PubMed:14685275). Interacts with FLNA (via calponin-homology (CH)
CC domain 1 and filamin repeat 24); the interaction alters FLNA ternary
CC structure and thus promotes FLNA dissociation from F-actin (By
CC similarity). {ECO:0000250|UniProtKB:Q14194,
CC ECO:0000269|PubMed:10956643, ECO:0000269|PubMed:14685275}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14194}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q14194}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:Q14194}. Cell projection, growth cone
CC {ECO:0000269|PubMed:25358863}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:25358863}. Perikaryon
CC {ECO:0000269|PubMed:14685275}. Note=Associated with centrosomes and the
CC mitotic spindle during metaphase (By similarity). Colocalizes with FLNA
CC and tubulin in the central region of DRG neuron growth cone
CC (PubMed:25358863). Following SEMA3A stimulation of DRG neurons,
CC colocalizes with F-actin (PubMed:25358863).
CC {ECO:0000250|UniProtKB:Q14194, ECO:0000269|PubMed:25358863}.
CC -!- DEVELOPMENTAL STAGE: Expressed in DRG neurons of 12 dpc embryos.
CC {ECO:0000269|PubMed:25358863}.
CC -!- PTM: Phosphorylation at Ser-522 enhances CRMP1-mediated alteration of
CC FLNA ternary structure and FLNA dissociation from F-actin.
CC {ECO:0000250|UniProtKB:Q14194}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Hydantoinase/dihydropyrimidinase family. {ECO:0000305}.
CC -!- CAUTION: Lacks most of the conserved residues that are essential for
CC binding the metal cofactor and hence for dihydropyrimidinase activity.
CC Its enzyme activity is therefore unsure. {ECO:0000305}.
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DR EMBL; U72875; AAB39703.1; -; mRNA.
DR EMBL; Y09080; CAA70300.1; -; mRNA.
DR EMBL; AB006714; BAA21887.1; -; mRNA.
DR EMBL; BC031738; AAH31738.1; -; mRNA.
DR CCDS; CCDS39075.1; -.
DR RefSeq; NP_031791.3; NM_007765.4.
DR PDB; 1KCX; X-ray; 2.12 A; A/B=8-525.
DR PDBsum; 1KCX; -.
DR AlphaFoldDB; P97427; -.
DR SMR; P97427; -.
DR BioGRID; 198890; 29.
DR IntAct; P97427; 5.
DR MINT; P97427; -.
DR STRING; 10090.ENSMUSP00000109795; -.
DR MEROPS; M38.974; -.
DR iPTMnet; P97427; -.
DR PhosphoSitePlus; P97427; -.
DR SwissPalm; P97427; -.
DR EPD; P97427; -.
DR jPOST; P97427; -.
DR MaxQB; P97427; -.
DR PaxDb; P97427; -.
DR PeptideAtlas; P97427; -.
DR PRIDE; P97427; -.
DR ProteomicsDB; 277392; -.
DR Antibodypedia; 9351; 430 antibodies from 36 providers.
DR DNASU; 12933; -.
DR Ensembl; ENSMUST00000031004; ENSMUSP00000031004; ENSMUSG00000029121.
DR GeneID; 12933; -.
DR KEGG; mmu:12933; -.
DR UCSC; uc008xfm.2; mouse.
DR CTD; 1400; -.
DR MGI; MGI:107793; Crmp1.
DR VEuPathDB; HostDB:ENSMUSG00000029121; -.
DR eggNOG; KOG2584; Eukaryota.
DR GeneTree; ENSGT01030000234527; -.
DR HOGENOM; CLU_015572_2_2_1; -.
DR InParanoid; P97427; -.
DR OMA; IKYPMGK; -.
DR PhylomeDB; P97427; -.
DR Reactome; R-MMU-399956; CRMPs in Sema3A signaling.
DR BioGRID-ORCS; 12933; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Crmp1; mouse.
DR EvolutionaryTrace; P97427; -.
DR PRO; PR:P97427; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P97427; protein.
DR Bgee; ENSMUSG00000029121; Expressed in embryonic brain and 194 other tissues.
DR ExpressionAtlas; P97427; baseline and differential.
DR Genevisible; P97427; MM.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:WormBase.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; IDA:MGI.
DR GO; GO:0030426; C:growth cone; IDA:WormBase.
DR GO; GO:0030496; C:midbody; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0031005; F:filamin binding; ISO:MGI.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0051219; F:phosphoprotein binding; IPI:BHF-UCL.
DR GO; GO:0007411; P:axon guidance; IEA:InterPro.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IEA:InterPro.
DR GO; GO:1904530; P:negative regulation of actin filament binding; ISO:MGI.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISO:MGI.
DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; IGI:WormBase.
DR CDD; cd01314; D-HYD; 1.
DR DisProt; DP02621; -.
DR Gene3D; 2.30.40.10; -; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR030624; CRMP1.
DR InterPro; IPR011778; Hydantoinase/dihydroPyrase.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11647:SF54; PTHR11647:SF54; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; SSF51338; 2.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR02033; D-hydantoinase; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell projection; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Nitration; Phosphoprotein; Reference proteome.
FT CHAIN 1..572
FT /note="Dihydropyrimidinase-related protein 1"
FT /id="PRO_0000165910"
FT REGION 509..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 246..247
FT /note="Required for interaction with FLNA"
FT /evidence="ECO:0000250|UniProtKB:Q14194"
FT COMPBIAS 525..549
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62950"
FT MOD_RES 101
FT /note="Phosphothreonine; by AURKA"
FT /evidence="ECO:0000250|UniProtKB:Q14194"
FT MOD_RES 102
FT /note="Phosphothreonine; by AURKA"
FT /evidence="ECO:0000250|UniProtKB:Q14194"
FT MOD_RES 316
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0007744|PubMed:16800626"
FT MOD_RES 504
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 509
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:18034455, ECO:0007744|PubMed:21183079"
FT MOD_RES 521
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62950"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62950"
FT MOD_RES 537
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 540
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 542
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 338
FT /note="T -> I (in Ref. 2; CAA70300)"
FT /evidence="ECO:0000305"
FT CONFLICT 476
FT /note="E -> K (in Ref. 3; BAA21887)"
FT /evidence="ECO:0000305"
FT CONFLICT 489
FT /note="F -> S (in Ref. 3; BAA21887)"
FT /evidence="ECO:0000305"
FT CONFLICT 520
FT /note="K -> E (in Ref. 2; CAA70300)"
FT /evidence="ECO:0000305"
FT STRAND 17..21
FT /evidence="ECO:0007829|PDB:1KCX"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:1KCX"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:1KCX"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:1KCX"
FT STRAND 41..48
FT /evidence="ECO:0007829|PDB:1KCX"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:1KCX"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:1KCX"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:1KCX"
FT HELIX 89..98
FT /evidence="ECO:0007829|PDB:1KCX"
FT STRAND 101..108
FT /evidence="ECO:0007829|PDB:1KCX"
FT HELIX 116..130
FT /evidence="ECO:0007829|PDB:1KCX"
FT STRAND 132..141
FT /evidence="ECO:0007829|PDB:1KCX"
FT HELIX 148..157
FT /evidence="ECO:0007829|PDB:1KCX"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:1KCX"
FT TURN 171..174
FT /evidence="ECO:0007829|PDB:1KCX"
FT HELIX 178..190
FT /evidence="ECO:0007829|PDB:1KCX"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:1KCX"
FT HELIX 202..214
FT /evidence="ECO:0007829|PDB:1KCX"
FT HELIX 221..226
FT /evidence="ECO:0007829|PDB:1KCX"
FT HELIX 230..246
FT /evidence="ECO:0007829|PDB:1KCX"
FT STRAND 250..255
FT /evidence="ECO:0007829|PDB:1KCX"
FT HELIX 258..270
FT /evidence="ECO:0007829|PDB:1KCX"
FT STRAND 274..279
FT /evidence="ECO:0007829|PDB:1KCX"
FT HELIX 280..284
FT /evidence="ECO:0007829|PDB:1KCX"
FT HELIX 287..291
FT /evidence="ECO:0007829|PDB:1KCX"
FT HELIX 295..300
FT /evidence="ECO:0007829|PDB:1KCX"
FT HELIX 313..322
FT /evidence="ECO:0007829|PDB:1KCX"
FT HELIX 338..341
FT /evidence="ECO:0007829|PDB:1KCX"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:1KCX"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:1KCX"
FT TURN 358..360
FT /evidence="ECO:0007829|PDB:1KCX"
FT HELIX 361..369
FT /evidence="ECO:0007829|PDB:1KCX"
FT TURN 370..373
FT /evidence="ECO:0007829|PDB:1KCX"
FT HELIX 377..384
FT /evidence="ECO:0007829|PDB:1KCX"
FT HELIX 386..391
FT /evidence="ECO:0007829|PDB:1KCX"
FT TURN 395..397
FT /evidence="ECO:0007829|PDB:1KCX"
FT STRAND 409..419
FT /evidence="ECO:0007829|PDB:1KCX"
FT TURN 422..424
FT /evidence="ECO:0007829|PDB:1KCX"
FT STRAND 426..430
FT /evidence="ECO:0007829|PDB:1KCX"
FT TURN 433..436
FT /evidence="ECO:0007829|PDB:1KCX"
FT STRAND 438..448
FT /evidence="ECO:0007829|PDB:1KCX"
FT STRAND 451..455
FT /evidence="ECO:0007829|PDB:1KCX"
FT HELIX 476..488
FT /evidence="ECO:0007829|PDB:1KCX"
SQ SEQUENCE 572 AA; 62168 MW; FE17DDCD735CAF8F CRC64;
MSHQGKKSIP HITSDRLLIR GGRIINDDQS FYADVYLEDG LIKQIGENLI VPGGVKTIEA
NGRMVIPGGI DVNTYLQKPS QGMTSADDFF QGTKAALAGG TTMIIDHVVP EPGSSLLTSF
EKWHEAADTK SCCDYSLHVD ITSWYDGVRE ELEVLVQDKG VNSFQVYMAY KDLYQMSDSQ
LYEAFTFLKG LGAVILVHAE NGDLIAQEQK RILEMGITGP EGHALSRPEE LEAEAVFRAI
AIAGRINCPV YITKVMSKSA ADIIALARKK GPLVFGEPIA ASLGTDGTHY WSKNWAKAAA
FVTSPPLSPD PTTPDYLTSL LACGDLQVTG SGHCPYSTAQ KAVGKDNFTL IPEGVNGIEE
RMTVVWDKAV ATGKMDENQF VAVTSTNAAK IFNLYPRKGR IAVGSDADVV IWDPDKMKTI
TAKSHKSTVE YNIFEGMECH GSPLVVISQG KIVFEDGNIS VSKGMGRFIP RKPFPEHLYQ
RVRIRSKVFG LHSVSRGMYD GPVYEVPATP KHAAPAPSAK SSPSKHQPPP IRNLHQSNFS
LSGAQIDDNN PRRTGHRIVA PPGGRSNITS LG
