Q14194 (DPYL1_HUMAN) 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

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

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.11
Subunit structure	Homotetramer, and heterotetramer with DPYSL2, DPYSL3, DPYSL4 or DPYSL5. Interacts with PLXNA1 By similarity. Ref.10
Subcellular location	Cytoplasm. Cytoplasm › cytoskeleton › centrosome. Cytoplasm › cytoskeleton › spindle. Note: Associated with centrosomes and the mitotic spindle during metaphase. Ref.11
Tissue specificity	Brain.
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
Coding sequence diversity	Alternative splicing Polymorphism
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	axon guidance Traceable author statement. Source: Reactome nucleobase-containing compound metabolic process Traceable author statement Ref.1. Source: ProtInc pyrimidine nucleobase catabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytosol Traceable author statement. Source: Reactome dendrite Inferred from electronic annotation. Source: Compara intracellular membrane-bounded organelle Inferred from direct assay. Source: HPA microtubule organizing center Inferred from electronic annotation. Source: UniProtKB-SubCell neuronal cell body Inferred from electronic annotation. Source: Compara 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...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AXIN1	O15169	2	EBI-473101,EBI-710484
HTT	P42858	2	EBI-473101,EBI-466029
VIM	P08670	2	EBI-473101,EBI-353844

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q14194-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform LCRMP-1 (identifier: Q14194-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-13: MSYQGKKSIPHIT → MADRRRAWNT...DLPLGRDNGQ

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 572	572	Dihydropyrimidinase-related protein 1		PRO_0000165909
Amino acid modifications
	Modified residue	431	1	Phosphotyrosine By similarity
	Modified residue	504	1	Phosphotyrosine By similarity
	Modified residue	509	1	Phosphothreonine By similarity
Natural variations
	Alternative sequence	1 – 13	13	MSYQG…IPHIT → MADRRRAWNTEDDLPVYLAR PGSAAQTPRQKYGGMFAAVE GAYENKTIDFDAYSVGRRGS ARTPRSAGRPDAVGLPGPGG SEDTASDVSEPSGSAVSSPG ERDERPPTLRIRRPAPRDLP LGRDNGQ in isoform LCRMP-1.		VSP_042545
	Natural variant	461	1	V → I. Corresponds to variant rs34611001 [ dbSNP | Ensembl ].		VAR_037745
Experimental info
	Sequence conflict	351 – 370	20	Missing in AAK55500. Ref.7
	Sequence conflict	504	1	Y → H in AAA93201. Ref.8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: A5385FCC79328A30	FASTA	572	62,184
	10 20 30 40 50 60 MSYQGKKSIP HITSDRLLIK GGRIINDDQS LYADVYLEDG LIKQIGENLI VPGGVKTIEA 70 80 90 100 110 120 NGRMVIPGGI DVNTYLQKPS QGMTAADDFF QGTRAALVGG TTMIIDHVVP EPGSSLLTSF 130 140 150 160 170 180 EKWHEAADTK SCCDYSLHVD ITSWYDGVRE ELEVLVQDKG VNSFQVYMAY KDVYQMSDSQ 190 200 210 220 230 240 LYEAFTFLKG LGAVILVHAE NGDLIAQEQK RILEMGITGP EGHALSRPEE LEAEAVFRAI 250 260 270 280 290 300 TIAGRINCPV 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 IWDPDKLKTI 430 440 450 460 470 480 TAKSHKSAVE YNIFEGMECH GSPLVVISQG KIVFEDGNIN VNKGMGRFIP RKAFPEHLYQ 490 500 510 520 530 540 RVKIRNKVFG LQGVSRGMYD GPVYEVPATP KYATPAPSAK SSPSKHQPPP IRNLHQSNFS 550 560 570 LSGAQIDDNN PRRTGHRIVA PPGGRSNITS LG
	Isoform LCRMP-1 [UniParc]. Checksum: 2C897F656E5F34FA	FASTA	686	74,262
	10 20 30 40 50 60 MADRRRAWNT EDDLPVYLAR PGSAAQTPRQ KYGGMFAAVE GAYENKTIDF DAYSVGRRGS 70 80 90 100 110 120 ARTPRSAGRP DAVGLPGPGG SEDTASDVSE PSGSAVSSPG ERDERPPTLR IRRPAPRDLP 130 140 150 160 170 180 LGRDNGQSDR LLIKGGRIIN DDQSLYADVY LEDGLIKQIG ENLIVPGGVK TIEANGRMVI 190 200 210 220 230 240 PGGIDVNTYL QKPSQGMTAA DDFFQGTRAA LVGGTTMIID HVVPEPGSSL LTSFEKWHEA 250 260 270 280 290 300 ADTKSCCDYS LHVDITSWYD GVREELEVLV QDKGVNSFQV YMAYKDVYQM SDSQLYEAFT 310 320 330 340 350 360 FLKGLGAVIL VHAENGDLIA QEQKRILEMG ITGPEGHALS RPEELEAEAV FRAITIAGRI 370 380 390 400 410 420 NCPVYITKVM SKSAADIIAL ARKKGPLVFG EPIAASLGTD GTHYWSKNWA KAAAFVTSPP 430 440 450 460 470 480 LSPDPTTPDY LTSLLACGDL QVTGSGHCPY STAQKAVGKD NFTLIPEGVN GIEERMTVVW 490 500 510 520 530 540 DKAVATGKMD ENQFVAVTST NAAKIFNLYP RKGRIAVGSD ADVVIWDPDK LKTITAKSHK 550 560 570 580 590 600 SAVEYNIFEG MECHGSPLVV ISQGKIVFED GNINVNKGMG RFIPRKAFPE HLYQRVKIRN 610 620 630 640 650 660 KVFGLQGVSR GMYDGPVYEV PATPKYATPA PSAKSSPSKH QPPPIRNLHQ SNFSLSGAQI 670 680 DDNNPRRTGH RIVAPPGGRS NITSLG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel gene family defined by human dihydropyrimidinase and three related proteins with differential tissue distribution." Hamajima N., Matsuda K., Sakata S., Tamaki N., Sasaki M., Nonaka M. Gene 180:157-163(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Brain.
[2]	"Long form collapsin response mediator protein-1 (LCRMP-1) expression is associated with clinical outcome and lymph node metastasis in non-small cell lung cancer patients." Pan S.-H., Chao Y.-C., Chen H.Y., Hung P.F., Lin P.Y., Lin C.W., Chang Y.L., Wu C.T., Lee Y.C., Yang S.-C., Hong T.-M., Yang P.-C. Lung Cancer 67:93-100(2010) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LCRMP-1), ALTERNATIVE SPLICING. Tissue: Lung adenocarcinoma.
[3]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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] (ISOFORM 1). Tissue: Eye.
[7]	"Genomic organization and localization of the human CRMP-1 gene." Torres R., Polymeropoulos M.H. DNA Res. 5:393-395(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 14-572 (ISOFORM 1).
[8]	"Collapsin-induced growth cone collapse mediated by an intracellular protein related to UNC-33." Goshima Y., Nakamura F., Strittmatter P., Strittmatter S.M. Nature 376:509-514(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 64-572 (ISOFORM 1). Tissue: Brain.
[9]	Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 44-56; 190-210; 246-254; 259-268; 346-361; 391-397; 452-463; 472-481; 488-511 AND 533-552, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[10]	"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 AND DPYSL4.
[11]	"Collapsin response mediator protein-1 and the invasion and metastasis of cancer cells." Shih J.-Y., Yang S.-C., Hong T.-M., Yuan A., Chen J.J.W., Yu C.-J., Chang Y.-L., Lee Y.-C., Peck K., Wu C.-W., Yang P.-C. J. Natl. Cancer Inst. 93:1392-1400(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D78012 mRNA. Translation: BAA11190.1. DQ206871 mRNA. Translation: ABB22046.1. BT006806 mRNA. Translation: AAP35452.1. AC105915 Genomic DNA. Translation: AAY40959.1. CH471131 Genomic DNA. Translation: EAW82405.1. CH471131 Genomic DNA. Translation: EAW82407.1. BC000252 mRNA. Translation: AAH00252.1. BC007613 mRNA. Translation: AAH07613.1. AH010780 Genomic DNA. Translation: AAK55500.1. U17278 mRNA. Translation: AAA93201.1.
IPI	IPI00414123. IPI00556376.
PIR	JC5316.
RefSeq	NP_001014809.1. NM_001014809.1. NP_001304.1. NM_001313.3.
UniGene	Hs.135270.
3D structure databases
ProteinModelPortal	Q14194.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q14194. 54 interactions.
MINT	MINT-1423114.
STRING	9606.ENSP00000321606.
Protein family/group databases
MEROPS	M38.974.
PTM databases
PhosphoSite	Q14194.
Polymorphism databases
DMDM	3122031.
Proteomic databases
PaxDb	Q14194.
PRIDE	Q14194.
Protocols and materials databases
DNASU	1400.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000324989; ENSP00000321606; ENSG00000072832. ENST00000397890; ENSP00000380987; ENSG00000072832. ENST00000534845; ENSP00000441150; ENSG00000072832.
GeneID	1400.
KEGG	hsa:1400.
UCSC	uc003giq.3. human.
Organism-specific databases
CTD	1400.
GeneCards	GC04M005815.
HGNC	HGNC:2365. CRMP1.
HPA	HPA035640.
MIM	602462. gene.
neXtProt	NX_Q14194.
PharmGKB	PA26885.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0044.
HOGENOM	HOG000219145.
HOVERGEN	HBG000806.
OMA	GINTPFT.
PhylomeDB	Q14194.
Enzyme and pathway databases
Reactome	REACT_111045. Developmental Biology.
Gene expression databases
ArrayExpress	Q14194.
Bgee	Q14194.
CleanEx	HS_CRMP1.
Genevestigator	Q14194.
GermOnline	ENSG00000072832. Homo sapiens.
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. 1 hit.
TIGRFAMs	TIGR02033. D-hydantoinase. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	CRMP1. human.
GenomeRNAi	1400.
NextBio	5731.
SOURCE	Search...

Entry information

Entry name

DPYL1_HUMAN

Accession

Primary (citable) accession number: Q14194
Secondary accession number(s): A0EJG6 , Q13024, Q4W5F1, Q96TC8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 131 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.