DPYL3_MOUSE
ID DPYL3_MOUSE Reviewed; 570 AA.
AC Q62188;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Dihydropyrimidinase-related protein 3;
DE Short=DRP-3;
DE AltName: Full=Unc-33-like phosphoprotein 1;
DE Short=ULIP-1;
GN Name=Dpysl3; Synonyms=Drp3, Ulip;
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].
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=8551352; DOI=10.1523/jneurosci.16-02-00688.1996;
RA Byk T., Dobransky T., Cifuentes-Diaz C., Sobel A.;
RT "Identification and molecular characterization of Unc-33-like
RT phosphoprotein (Ulip), a putative mammalian homolog of the axonal guidance-
RT associated unc-33 gene product.";
RL J. Neurosci. 16:688-701(1996).
RN [2]
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 [3]
RP PROTEIN SEQUENCE OF 468-480.
RC TISSUE=Brain;
RA Lubec G., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [4]
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 [5]
RP INTERACTION WITH 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).
RN [6]
RP IDENTIFICATION BY 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-431, AND IDENTIFICATION BY
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-514; SER-518 AND SER-522, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259; TYR-499; THR-509;
RP THR-514; SER-518; SER-536; SER-539; SER-541 AND THR-543, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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).
CC -!- FUNCTION: Necessary for signaling by class 3 semaphorins and subsequent
CC remodeling of the cytoskeleton. Plays a role in axon guidance, neuronal
CC growth cone collapse and cell migration (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotetramer, and heterotetramer with CRMP1, DPYSL2, DPYSL4 or
CC DPYSL5. Interacts with synaptic vesicle protein 2 and SH3A domain of
CC intersectin (By similarity). Interacts with FLNA (By similarity).
CC {ECO:0000250|UniProtKB:Q14195, ECO:0000250|UniProtKB:Q62952}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell projection, growth
CC cone {ECO:0000250}. Note=Colocalizes with synaptic vesicle protein 2 in
CC the central region of the growth cone. {ECO:0000250}.
CC -!- PTM: Phosphorylation on Ser-522 by DYRK2 promotes subsequent
CC phosphorylation on Thr-509, Thr-514 and Ser-518 by GSK3. {ECO:0000250}.
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; X87817; CAA61082.1; -; mRNA.
DR EMBL; BC023003; AAH23003.1; -; mRNA.
DR CCDS; CCDS37801.1; -.
DR PIR; S55525; S55525.
DR RefSeq; NP_033494.1; NM_009468.5.
DR AlphaFoldDB; Q62188; -.
DR SMR; Q62188; -.
DR BioGRID; 204437; 13.
DR IntAct; Q62188; 3.
DR MINT; Q62188; -.
DR STRING; 10090.ENSMUSP00000025379; -.
DR MEROPS; M38.976; -.
DR iPTMnet; Q62188; -.
DR PhosphoSitePlus; Q62188; -.
DR SwissPalm; Q62188; -.
DR REPRODUCTION-2DPAGE; IPI00122349; -.
DR REPRODUCTION-2DPAGE; Q62188; -.
DR jPOST; Q62188; -.
DR MaxQB; Q62188; -.
DR PaxDb; Q62188; -.
DR PeptideAtlas; Q62188; -.
DR PRIDE; Q62188; -.
DR ProteomicsDB; 279483; -.
DR Antibodypedia; 1526; 306 antibodies from 29 providers.
DR DNASU; 22240; -.
DR Ensembl; ENSMUST00000025379; ENSMUSP00000025379; ENSMUSG00000024501.
DR GeneID; 22240; -.
DR KEGG; mmu:22240; -.
DR UCSC; uc008euh.3; mouse.
DR CTD; 1809; -.
DR MGI; MGI:1349762; Dpysl3.
DR VEuPathDB; HostDB:ENSMUSG00000024501; -.
DR eggNOG; KOG2584; Eukaryota.
DR GeneTree; ENSGT01030000234527; -.
DR InParanoid; Q62188; -.
DR OMA; RNFVCSP; -.
DR PhylomeDB; Q62188; -.
DR TreeFam; TF314706; -.
DR Reactome; R-MMU-399956; CRMPs in Sema3A signaling.
DR BioGRID-ORCS; 22240; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Dpysl3; mouse.
DR PRO; PR:Q62188; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q62188; protein.
DR Bgee; ENSMUSG00000024501; Expressed in superior cervical ganglion and 262 other tissues.
DR ExpressionAtlas; Q62188; baseline and differential.
DR Genevisible; Q62188; MM.
DR GO; GO:0044297; C:cell body; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0070382; C:exocytic vesicle; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0031941; C:filamentous actin; ISS:UniProtKB.
DR GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0035374; F:chondroitin sulfate binding; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0051219; F:phosphoprotein binding; IPI:BHF-UCL.
DR GO; GO:0017124; F:SH3 domain binding; ISS:UniProtKB.
DR GO; GO:0051764; P:actin crosslink formation; ISS:UniProtKB.
DR GO; GO:0051017; P:actin filament bundle assembly; ISS:UniProtKB.
DR GO; GO:0071345; P:cellular response to cytokine stimulus; ISS:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IDA:MGI.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; ISS:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:0048678; P:response to axon injury; ISS:UniProtKB.
DR CDD; cd01314; D-HYD; 1.
DR Gene3D; 2.30.40.10; -; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR030628; DRP3.
DR InterPro; IPR011778; Hydantoinase/dihydroPyrase.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11647:SF57; PTHR11647:SF57; 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 Cell projection; Cytoplasm; Direct protein sequencing; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..570
FT /note="Dihydropyrimidinase-related protein 3"
FT /id="PRO_0000165918"
FT REGION 506..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 431
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 499
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 509
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 514
FT /note="Phosphothreonine; by GSK3"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 518
FT /note="Phosphoserine; by GSK3"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 522
FT /note="Phosphoserine; by DYRK2"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 536
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 539
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 541
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 543
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 570 AA; 61936 MW; 14C339BF90015D96 CRC64;
MSYQGKKNIP RITSDRLLIK GGRIVNDDQS FYADIYMEDG LIKQIGDNLI VPGGVKTIEA
NGKMVIPGGI DVHTHFQMPY KGMTTVDDFF QGTKAALAGG TTMIIDHVVP EPESSLTEAY
EKWREWADGK SCCDYALHVD ITHWNDSVKQ EVQSLSKEKG VNSFMVYMAY KDLYQVSNTE
LYEIFTCLGE LGAIAQVHAE NGDIIAQEQA RMLEMGITGP EGHVLSRPEE LEAEAVFRAI
TVASQTNCPL YVTKVMSKSA ADLISQARKK GNVVFGEPIT ASLGIDGTHY WSKNWAKAAA
FVTSPPLSPD PTTPDYINSL LASGDLQLSG SAHCTFSTAQ KAIGKDNFTA IPEGTNGVEE
RMSVIWDKAV ATGKMDENQF VAVTSTNAAK IFNLYPRKGR IAVGSDSDLV IWDPDALKIV
SAKNHQSVAE YNIFEGMELR GAPLVVICQG KIMLEDGNLH VTQGAGRFIP CSPFSDYVYK
RIKARRKMAD LHAVPRGMYD GPVFDLTTTP KGGTPAGSTR GSPTRPNPPV RNLHQSGFSL
SGTQVDEGVR SASKRIVAPP GGRSNITSLS
