P97427 (DPYL1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	Crmp1
Synonyms:	Dpysl1, Ulip3

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	572 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, invasive growth and cell migration. Ref.10
Subunit structure	Homotetramer, and heterotetramer with DPYSL2, DPYSL3, DPYSL4 or DPYSL5. Interacts with PLXNA1. Ref.8 Ref.10
Subcellular location	Cytoplasm By similarity. Cytoplasm › cytoskeleton › centrosome By similarity. Cytoplasm › cytoskeleton › spindle By similarity. Note: Associated with centrosomes and the mitotic spindle during metaphase By similarity.
Sequence similarities	Belongs to the DHOase family. Hydantoinase/dihydropyrimidinase subfamily.
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.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
PTM	Nitration Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	pyrimidine nucleobase catabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell dendrite Inferred from direct assay PubMed 15834957. Source: MGI microtubule organizing center Inferred from electronic annotation. Source: UniProtKB-SubCell neuronal cell body Inferred from direct assay PubMed 15834957. Source: MGI spindle Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 572

572

Dihydropyrimidinase-related protein 1

PRO_0000165910

Amino acid modifications

Modified residue

316

1

Nitrated tyrosine Ref.7

Modified residue

431

1

Phosphotyrosine Ref.9

Modified residue

504

1

Phosphotyrosine Ref.9

Modified residue

509

1

Phosphothreonine Ref.6 Ref.9

Experimental info

Sequence conflict

338

1

T → I in CAA70300. Ref.2

Sequence conflict

476

1

E → K in BAA21887. Ref.3

Sequence conflict

489

1

F → S in BAA21887. Ref.3

Sequence conflict

520

1

K → E in CAA70300. Ref.2

Secondary structure

1

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572

Helix Strand Turn

Details...

Beta strand

17 – 21

5

Beta strand

23 – 25

3

Beta strand

30 – 32

3

Beta strand

34 – 38

5

Beta strand

41 – 48

8

Beta strand

56 – 59

4

Beta strand

64 – 67

4

Beta strand

69 – 74

6

Helix

89 – 98

10

Beta strand

101 – 108

8

Helix

116 – 130

15

Beta strand

132 – 141

10

Helix

148 – 157

10

Beta strand

163 – 168

6

Turn

171 – 174

4

Helix

178 – 190

13

Beta strand

194 – 198

5

Helix

202 – 214

13

Helix

221 – 226

6

Helix

230 – 246

17

Beta strand

250 – 255

6

Helix

258 – 270

13

Beta strand

274 – 279

6

Helix

280 – 284

5

Helix

287 – 291

5

Helix

295 – 300

6

Helix

313 – 322

10

Helix

338 – 341

4

Helix

342 – 344

3

Helix

348 – 350

3

Turn

358 – 360

3

Helix

361 – 369

9

Turn

370 – 373

4

Helix

377 – 384

8

Helix

386 – 391

6

Turn

395 – 397

3

Beta strand

409 – 419

11

Turn

422 – 424

3

Beta strand

426 – 430

5

Turn

433 – 436

4

Beta strand

438 – 448

11

Beta strand

451 – 455

5

Helix

476 – 488

13

Sequences

	Sequence		Length	Mass (Da)
	P97427 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: FE17DDCD735CAF8F	FASTA	572	62,168
	10 20 30 40 50 60 MSHQGKKSIP HITSDRLLIR GGRIINDDQS FYADVYLEDG LIKQIGENLI VPGGVKTIEA 70 80 90 100 110 120 NGRMVIPGGI DVNTYLQKPS QGMTSADDFF QGTKAALAGG TTMIIDHVVP EPGSSLLTSF 130 140 150 160 170 180 EKWHEAADTK SCCDYSLHVD ITSWYDGVRE ELEVLVQDKG VNSFQVYMAY KDLYQMSDSQ 190 200 210 220 230 240 LYEAFTFLKG LGAVILVHAE NGDLIAQEQK RILEMGITGP EGHALSRPEE LEAEAVFRAI 250 260 270 280 290 300 AIAGRINCPV YITKVMSKSA ADIIALARKK GPLVFGEPIA ASLGTDGTHY WSKNWAKAAA 310 320 330 340 350 360 FVTSPPLSPD PTTPDYLTSL LACGDLQVTG SGHCPYSTAQ KAVGKDNFTL IPEGVNGIEE 370 380 390 400 410 420 RMTVVWDKAV ATGKMDENQF VAVTSTNAAK IFNLYPRKGR IAVGSDADVV IWDPDKMKTI 430 440 450 460 470 480 TAKSHKSTVE YNIFEGMECH GSPLVVISQG KIVFEDGNIS VSKGMGRFIP RKPFPEHLYQ 490 500 510 520 530 540 RVRIRSKVFG LHSVSRGMYD GPVYEVPATP KHAAPAPSAK SSPSKHQPPP IRNLHQSNFS 550 560 570 LSGAQIDDNN PRRTGHRIVA PPGGRSNITS LG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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, MASS SPECTROMETRY. Strain: OF1. Tissue: Hippocampus.
[6]	"Phosphoproteomic analysis of the developing mouse brain." Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P. Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-509, MASS SPECTROMETRY. Tissue: Embryonic brain.
[7]	"Endogenously nitrated proteins in mouse brain: links to neurodegenerative disease." Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H., Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J., Squier T.C., Bigelow D.J. Biochemistry 45:8009-8022(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-316, MASS SPECTROMETRY. Tissue: Brain.
[8]	"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.
[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-431; TYR-504 AND THR-509, MASS SPECTROMETRY. 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U72875 mRNA. Translation: AAB39703.1.
Y09080 mRNA. Translation: CAA70300.1.
AB006714 mRNA. Translation: BAA21887.1.
BC031738 mRNA. Translation: AAH31738.1.

IPI

IPI00875117.

RefSeq

NP_031791.3. NM_007765.4.

UniGene

Mm.290995.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KCX	X-ray	2.12	A/B	8-525	[»]

ProteinModelPortal

P97427.

SMR

P97427. Positions 15-490.

ModBase

Search...

Protein-protein interaction databases

IntAct

P97427. 1 interaction.

Protein family/group databases

MEROPS

M38.974.

PTM databases

PhosphoSite

P97427.

Proteomic databases

PaxDb

P97427.

PRIDE

P97427.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000031004; ENSMUSP00000031004; ENSMUSG00000029121.

GeneID

12933.

KEGG

mmu:12933.

UCSC

uc008xfm.1. mouse.

Organism-specific databases

CTD

1400.

MGI

MGI:107793. Crmp1.

Phylogenomic databases

eggNOG

COG0044.

GeneTree

ENSGT00550000074371.

HOGENOM

HOG000219145.

HOVERGEN

HBG000806.

Gene expression databases

ArrayExpress

P97427.

Bgee

P97427.

CleanEx

MM_CRMP1.

Genevestigator

P97427.

GermOnline

ENSMUSG00000029121. Mus musculus.

Family and domain databases

InterPro

IPR006680. Amidohydro_1.
IPR011778. Hydantoinase/dihydroPyrase.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]

Pfam

PF01979. Amidohydro_1. 1 hit.
[Graphical view]

SUPFAM

SSF51338. Metalo_hydrolase. 2 hits.

TIGRFAMs

TIGR02033. D-hydantoinase. 1 hit.

ProtoNet

Search...

Other

ChiTaRS

CRMP1. mouse.

EvolutionaryTrace

P97427.

NextBio

282604.

SOURCE

Search...

Entry information

Entry name

DPYL1_MOUSE

Accession

Primary (citable) accession number: P97427
Secondary accession number(s): O08554, O35097

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	May 1, 1997
Last modified:	May 1, 2013
This is version 111 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program