Q14195 (DPYL3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dihydropyrimidinase-related protein 3
Short name=DRP-3

Alternative name(s):
Collapsin response mediator protein 4
Short name=CRMP-4
Unc-33-like phosphoprotein 1
Short name=ULIP-1

Gene names

Name:	DPYSL3
Synonyms:	CRMP4, DRP3, ULIP, ULIP1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	570 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, neuronal growth cone collapse and cell migration By similarity.
Subunit structure	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 expressed in heart and skeletal muscle. Also strongly expressed in fetal brain and spinal cord.
Post-translational modification	Phosphorylation on Ser-522 by DYRK2 promotes subsequent phosphorylation on Thr-509, Thr-514 and Ser-518 by GSK3.
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	Cell projection Cytoplasm
Coding sequence diversity	Polymorphism
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	actin crosslink formation Inferred from sequence or structural similarity. Source: UniProtKB actin filament bundle assembly Inferred from sequence or structural similarity. Source: UniProtKB axon guidance Traceable author statement. Source: Reactome cellular response to cytokine stimulus Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of cell migration Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of neuron projection development Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of filopodium assembly Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of neuron projection development Inferred from sequence or structural similarity. Source: UniProtKB protein homooligomerization Inferred from sequence or structural similarity. Source: UniProtKB pyrimidine base catabolic process Inferred from electronic annotation. Source: InterPro response to axon injury Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	cell body Inferred from sequence or structural similarity. Source: UniProtKB cytosol Inferred from sequence or structural similarity. Source: UniProtKB extracellular space Inferred from sequence or structural similarity. Source: UniProtKB filamentous actin Inferred from sequence or structural similarity. Source: UniProtKB growth cone Inferred from sequence or structural similarity. Source: UniProtKB lamellipodium Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	SH3 domain binding Inferred from sequence or structural similarity. Source: UniProtKB chondroitin sulfate binding Inferred from sequence or structural similarity. Source: UniProtKB 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 – 570	570	Dihydropyrimidinase-related protein 3		PRO_0000165917
Amino acid modifications
	Modified residue	499	1	Phosphotyrosine By similarity
	Modified residue	509	1	Phosphothreonine; by GSK3 Ref.5
	Modified residue	514	1	Phosphothreonine; by GSK3 Ref.5
	Modified residue	518	1	Phosphoserine; by GSK3 Ref.5
	Modified residue	522	1	Phosphoserine; by DYRK2 Ref.4 Ref.5
	Modified residue	541	1	Phosphoserine By similarity
	Modified residue	551	1	Phosphoserine Ref.4
Natural variations
	Natural variant	442	1	A → S. Corresponds to variant rs2304044 [ dbSNP | Ensembl ].		VAR_020485
Experimental info
	Sequence conflict	49	1	L → V in CAA69153. Ref.2
	Sequence conflict	142	1	T → A in CAA69153. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q14195 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 9D6AFE86CBB33AD5	FASTA	570	61,963
	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

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: 8973361] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[2]	"Identification and characterization of a retinoic acid-regulated human homologue of the unc-33-like phosphoprotein gene (hUlip) from neuroblastoma cells." Gaetano C., Matsuo T., Thiele C.J. J. Biol. Chem. 272:12195-12201(1997) [PubMed: 9115293] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[3]	Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: 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, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[4]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-522 AND SER-551, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[5]	"Distinct priming kinases contribute to differential regulation of collapsin response mediator proteins by glycogen synthase kinase-3 in vivo." Cole A.R., Causeret F., Yadirgi G., Hastie C.J., McLauchlan H., McManus E.J., Hernandez F., Eickholt B.J., Nikolic M., Sutherland C. J. Biol. Chem. 281:16591-16598(2006) [PubMed: 16611631] [Abstract] Cited for: PHOSPHORYLATION AT SER-522 BY DYRK2, PHOSPHORYLATION AT THR-509; THR-514 AND SER-518 BY GSK3.
[6]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D78014 mRNA. Translation: BAA11192.1. Y07818 mRNA. Translation: CAA69153.1.
IPI	IPI00872788.
PIR	JC5318.
RefSeq	NP_001184223.1. NM_001197294.1. NP_001378.1. NM_001387.2.
UniGene	Hs.519659.
3D structure databases
ProteinModelPortal	Q14195.
SMR	Q14195. Positions 14-490.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q14195. 1 interaction.
STRING	Q14195.
Protein family/group databases
MEROPS	M38.976.
PTM databases
PhosphoSite	Q14195.
Polymorphism databases
DMDM	3122050.
2D gel databases
REPRODUCTION-2DPAGE	Q14195.
UCD-2DPAGE	Q14195.
Proteomic databases
PRIDE	Q14195.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000398514; ENSP00000381526; ENSG00000113657.
GeneID	1809.
KEGG	hsa:1809.
UCSC	uc003lon.1. human.
Organism-specific databases
CTD	1809.
GeneCards	GC05M146750.
H-InvDB	HIX0024842.
HGNC	HGNC:3015. DPYSL3.
HPA	HPA010948.
MIM	601168. gene.
neXtProt	NX_Q14195.
PharmGKB	PA27473.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG04131.
HOVERGEN	HBG000806.
OrthoDB	EOG48PMJT.
PhylomeDB	Q14195.
Enzyme and pathway databases
Reactome	REACT_111045. Developmental Biology.
Gene expression databases
ArrayExpress	Q14195.
Bgee	Q14195.
CleanEx	HS_DPYSL3.
Genevestigator	Q14195.
GermOnline	ENSG00000113657. 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
NextBio	7373.
SOURCE	Search...

Entry information

Entry name

DPYL3_HUMAN

Accession

Primary (citable) accession number: Q14195
Secondary accession number(s): Q93012

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	November 1, 1996
Last modified:	January 25, 2012
This is version 110 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.