[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Brain; DOI=10.1016/S0378-1119(96)00445-3; PubMed=8973361 [NCBI, ExPASy, EBI, Israel, Japan] Hamajima N., Matsuda K., Sakata S., Tamaki N., Sasaki M., Nonaka M.; "A novel gene family defined by human dihydropyrimidinase and three related proteins with differential tissue distribution."; Gene 180:157-163(1996).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Brain; DOI=10.1074/jbc.272.18.12195; PubMed=9115293 [NCBI, ExPASy, EBI, Israel, Japan] Gaetano C., Matsuo T., Thiele C.J.; "Identification and characterization of a retinoic acid-regulated human homologue of the unc-33-like phosphoprotein gene (hUlip) from neuroblastoma cells."; J. Biol. Chem. 272:12195-12201(1997).
[3]	PROTEIN SEQUENCE OF 24-56; 82-122; 131-157; 239-254; 259-268; 346-368; 375-397; 401-418; 424-440; 452-480; 488-511 AND 532-550, AND MASS SPECTROMETRY. TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex; Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.; Submitted (DEC-2008) to UniProtKB.
[4]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-522 AND SER-551, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan] Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."; Cell 127:635-648(2006).
[5]	IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. Colinge J., Superti-Furga G., Bennett K.L.; Submitted (OCT-2008) to UniProtKB.

Comments

FUNCTION: Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, neuronal growth cone collapse and cell migration (By similarity).
SUBUNIT: Homotetramer, and heterotetramer with CRMP1, DPYSL2, DPYSL4 or DPYSL5 (By similarity). Interacts with synaptic vesicle protein 2 and SH3A domain of intersectin (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell projection, growth cone (By similarity). Note=Colocalizes with synaptic vesicle protein 2 in the central region of the growth cone (By similarity).
TISSUE SPECIFICITY: Mainly in heart and skeletal muscle. Also expressed strongly in fetal brain and spinal cord.
SIMILARITY: Belongs to the DHOase family. Hydantoinase/dihydropyrimidinase subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

D78014; BAA11192.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Y07818; CAA69153.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00872788; -.

JC5318; JC5318.

NP_001378.1; -.

3D structure databases

HSSP

Q45515; 1K1D. [HSSP ENTRY / PDB]

SMR

Q14195; 15-488.

ModBase

Q14195.

Protein-protein interaction databases

IntAct

Q14195; 1.

Protein family/group databases

MEROPS

M38.976; -.

2D gel databases

REPRODUCTION-2DPAGE

Q14195; -.

Organism-specific databases

GC05M146750; -.

HIX0024842; -.

HGNC:3015; DPYSL3.

HPA010948; -.

601168; gene. [NCBI / EBI]

PharmGKB

PA27473; -.

Gene expression databases

Q14195; -.

Q14195; -.

HS_DPYSL3; -.

ENSG00000113657; Homo sapiens.

Ontologies

GO:0042995;	Cellular component: cell projection (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-SubCell).
GO:0030426;	Cellular component: growth cone (inferred from electronic annotation from UniProtKB-SubCell).
GO:0004157;	Molecular function: dihydropyrimidinase activity (traceable author statement from ProtInc).
GO:0007399;	Biological process: nervous system development (traceable author statement from ProtInc).
GO:0006139;	Biological process: nucleobase, nucleoside, nucleotide and nucleic acid metabolic process (traceable author statement from ProtInc).
GO:0007165;	Biological process: signal transduction (traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR006680; Amidohydro_1.
IPR011778; D-hydantoinase.
Graphical view of domain structure.

Pfam

PF01979; Amidohydro_1; 1.
Pfam graphical view of domain structure.

ProDom

PD000518; DHOase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR02033; D-hydantoinase; 1.

Proteomic databases

PRIDE

Q14195; -.

Genome annotation databases

Ensembl

ENSG00000113657; Homo sapiens. [Contig view]

GeneID

1809; -.

KEGG

hsa:1809; -.

Phylogenomic databases

HOVERGEN

Q14195; -.

Other

NextBio

7373; -.

SOURCE

DPYSL3; Homo sapiens.

ProtoNet

Q14195.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cell projection; Cytoplasm; Direct protein sequencing; Phosphoprotein; Polymorphism.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 570`	`570`	`Dihydropyrimidinase-related protein 3.`	`PRO_0000165917`
`MOD_RES`	`499 499`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`509 509`		`Phosphothreonine (By similarity).`
`MOD_RES`	`514 514`		`Phosphothreonine (By similarity).`
`MOD_RES`	`518 518`		`Phosphoserine (By similarity).`
`MOD_RES`	`522 522`		`Phosphoserine.`
`MOD_RES`	`551 551`		`Phosphoserine.`
`VARIANT`	`442 442`	`1`	`A -> S (in dbSNP:rs2304044 [NCBI]).`	`VAR_020485 [3D]`
`CONFLICT`	`49 49`		`L -> V (in Ref. 2; CAA69153).`
`CONFLICT`	`142 142`		`T -> A (in Ref. 2; CAA69153).`

Sequence information

Length: 570 AA [This is the length of the unprocessed precursor]

Molecular weight: 61963 Da [This is the MW of the unprocessed precursor]

CRC64: 9D6AFE86CBB33AD5 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSYQGKKNIP RITSDRLLIK GGRIVNDDQS FYADIYMEDG LIKQIGDNLI VPGGVKTIEA 

        70         80         90        100        110        120 
NGKMVIPGGI DVHTHFQMPY KGMTTVDDFF QGTKAALAGG TTMIIDHVVP EPESSLTEAY 

       130        140        150        160        170        180 
EKWREWADGK SCCDYALHVD ITHWNDSVKQ EVQNLIKDKG VNSFMVYMAY KDLYQVSNTE 

       190        200        210        220        230        240 
LYEIFTCLGE LGAIAQVHAE NGDIIAQEQT RMLEMGITGP EGHVLSRPEE LEAEAVFRAI 

       250        260        270        280        290        300 
TIASQTNCPL YVTKVMSKSA ADLISQARKK GNVVFGEPIT ASLGIDGTHY WSKNWAKAAA 

       310        320        330        340        350        360 
FVTSPPLSPD PTTPDYINSL LASGDLQLSG SAHCTFSTAQ KAIGKDNFTA IPEGTNGVEE 

       370        380        390        400        410        420 
RMSVIWDKAV ATGKMDENQF VAVTSTNAAK IFNLYPRKGR ISVGSDSDLV IWDPDAVKIV 

       430        440        450        460        470        480 
SAKNHQSAAE YNIFEGMELR GAPLVVICQG KIMLEDGNLH VTQGAGRFIP CSPFSDYVYK 

       490        500        510        520        530        540 
RIKARRKMAD LHAVPRGMYD GPVFDLTTTP KGGTPAGSAR GSPTRPNPPV RNLHQSGFSL 

       550        560        570 
SGTQVDEGVR SASKRIVAPP GGRSNITSLS

Q14195 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools