DPYL3_RAT
ID DPYL3_RAT Reviewed; 570 AA.
AC Q62952; Q8K4H3; Q91XM8;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Dihydropyrimidinase-related protein 3;
DE Short=DRP-3;
DE AltName: Full=Collapsin response mediator protein 4;
DE Short=CRMP-4;
DE AltName: Full=TOAD-64/Ulip/CRMP;
DE AltName: Full=TUC-4b;
GN Name=Dpysl3; Synonyms=Crmp4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, ALTERNATIVE SPLICING, AND
RP INTERACTION WITH SYNAPTIC VESICLE PROTEIN 2 AND INTERSECTIN.
RC STRAIN=Sprague-Dawley;
RX PubMed=12684468; DOI=10.1523/jneurosci.23-07-02815.2003;
RA Quinn C.C., Chen E., Kinjo T.G., Kelly G., Bell A.W., Elliott R.C.,
RA McPherson P.S., Hockfield S.;
RT "TUC-4b, a novel TUC family variant, regulates neurite outgrowth and
RT associates with vesicles in the growth cone.";
RL J. Neurosci. 23:2815-2823(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Elliott R.C., Parent J.M., Lowenstein D.H.;
RT "Adult-specific collapsin response mediator protein 4 (CRMP4) transcripts
RT correlate with widespread CRMP4 expression in normal and epileptic adult
RT rats.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-358 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=8815901; DOI=10.1523/jneurosci.16-19-06197.1996;
RA Wang L., Strittmatter S.M.;
RT "A family of rat CRMP genes is differentially expressed in the nervous
RT system.";
RL J. Neurosci. 16:6197-6207(1996).
RN [4]
RP PROTEIN SEQUENCE OF 532-550, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Diao W.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP SUBUNIT.
RX PubMed=9375656; DOI=10.1046/j.1471-4159.1997.69062261.x;
RA Wang L.H., Strittmatter S.M.;
RT "Brain CRMP forms heterotetramers similar to liver dihydropyrimidinase.";
RL J. Neurochem. 69:2261-2269(1997).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=19343716; DOI=10.1002/pmic.200800664;
RA Maurya D.K., Sundaram C.S., Bhargava P.;
RT "Proteome profile of the mature rat olfactory bulb.";
RL Proteomics 9:2593-2599(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-509; THR-514 AND SER-522,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101 (ISOFORM 2), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. {ECO:0000269|PubMed:12684468}.
CC -!- SUBUNIT: Homotetramer, and heterotetramer with CRMP1, DPYSL2, DPYSL4 or
CC DPYSL5 (PubMed:9375656). Interacts with synaptic vesicle protein 2 and
CC SH3A domain of intersectin (PubMed:12684468). Interacts with FLNA (By
CC similarity). {ECO:0000250|UniProtKB:Q14195,
CC ECO:0000269|PubMed:12684468, ECO:0000269|PubMed:9375656}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19343716}. Cell
CC projection, growth cone {ECO:0000269|PubMed:12684468}. Note=Colocalizes
CC with synaptic vesicle protein 2 in the central region of the growth
CC cone. {ECO:0000269|PubMed:12684468}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=TUC-4b;
CC IsoId=Q62952-1; Sequence=Displayed;
CC Name=2; Synonyms=TUC-4a;
CC IsoId=Q62952-2; Sequence=VSP_016557;
CC -!- TISSUE SPECIFICITY: Isoform 2 is expressed in growth cones. Up-
CC regulated in motor neurons during axonal regeneration after sciatic
CC nerve lesion. Overexpression of isoform 2 increased neurite extension
CC and branching. Isoform 1 is expressed throughout neurons and their
CC axons. {ECO:0000269|PubMed:12684468}.
CC -!- DEVELOPMENTAL STAGE: At E17, isoform 2 is expressed in the CNS and PNS.
CC Isoform 2 is expressed at high levels in the dorsal root ganglia,
CC trigeminal ganglia, and throughout the spinal cord with the highest
CC level in the ventral horn. {ECO:0000269|PubMed:12684468}.
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; AF398465; AAM73758.1; -; mRNA.
DR EMBL; AF389425; AAK64497.1; -; mRNA.
DR EMBL; U52104; AAB03282.1; -; mRNA.
DR RefSeq; NP_037066.1; NM_012934.1. [Q62952-1]
DR RefSeq; XP_006254732.1; XM_006254670.3. [Q62952-2]
DR AlphaFoldDB; Q62952; -.
DR SMR; Q62952; -.
DR BioGRID; 247453; 2.
DR IntAct; Q62952; 3.
DR MINT; Q62952; -.
DR STRING; 10116.ENSRNOP00000025880; -.
DR MEROPS; M38.976; -.
DR iPTMnet; Q62952; -.
DR PhosphoSitePlus; Q62952; -.
DR World-2DPAGE; 0004:Q62952; -.
DR jPOST; Q62952; -.
DR PaxDb; Q62952; -.
DR PRIDE; Q62952; -.
DR Ensembl; ENSRNOT00000025880; ENSRNOP00000025880; ENSRNOG00000018992. [Q62952-2]
DR Ensembl; ENSRNOT00000087876; ENSRNOP00000070679; ENSRNOG00000018992. [Q62952-1]
DR GeneID; 25418; -.
DR KEGG; rno:25418; -.
DR UCSC; RGD:2410; rat. [Q62952-1]
DR CTD; 1809; -.
DR RGD; 2410; Dpysl3.
DR eggNOG; KOG2584; Eukaryota.
DR GeneTree; ENSGT01030000234527; -.
DR InParanoid; Q62952; -.
DR OMA; RNFVCSP; -.
DR OrthoDB; 719800at2759; -.
DR PhylomeDB; Q62952; -.
DR TreeFam; TF314706; -.
DR Reactome; R-RNO-399956; CRMPs in Sema3A signaling.
DR PRO; PR:Q62952; -.
DR Proteomes; UP000002494; Chromosome 18.
DR Bgee; ENSRNOG00000018992; Expressed in testis and 19 other tissues.
DR Genevisible; Q62952; RN.
DR GO; GO:0044297; C:cell body; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0031941; C:filamentous actin; IDA:UniProtKB.
DR GO; GO:0030426; C:growth cone; IDA:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0035374; F:chondroitin sulfate binding; IDA:RGD.
DR GO; GO:0031005; F:filamin binding; ISO:RGD.
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; IPI:UniProtKB.
DR GO; GO:0051219; F:phosphoprotein binding; ISO:RGD.
DR GO; GO:0017124; F:SH3 domain binding; IDA:RGD.
DR GO; GO:0051764; P:actin crosslink formation; IDA:UniProtKB.
DR GO; GO:0051017; P:actin filament bundle assembly; IDA:UniProtKB.
DR GO; GO:0071345; P:cellular response to cytokine stimulus; IEP:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; IMP:UniProtKB.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IMP:UniProtKB.
DR GO; GO:0007399; P:nervous system development; ISO:RGD.
DR GO; GO:0048666; P:neuron development; IEP:RGD.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; IDA:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IDA:RGD.
DR GO; GO:0048678; P:response to axon injury; IEP: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 Alternative splicing; Cell projection; Cytoplasm;
KW Direct protein sequencing; Phosphoprotein; Reference proteome.
FT CHAIN 1..570
FT /note="Dihydropyrimidinase-related protein 3"
FT /id="PRO_0000165919"
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:0000250|UniProtKB:Q14195"
FT MOD_RES 431
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q62188"
FT MOD_RES 499
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q62188"
FT MOD_RES 509
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 514
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 518
FT /note="Phosphoserine; by GSK3"
FT /evidence="ECO:0000250|UniProtKB:Q14195"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 536
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62188"
FT MOD_RES 539
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62188"
FT MOD_RES 541
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62188"
FT MOD_RES 543
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q62188"
FT VAR_SEQ 1..13
FT /note="MSYQGKKNIPRIT -> MASGRRGWDSSHEDDLPVYLARPGTTDQVPRQKYG
FT GMFCNVEGAFESKTLDFDALSVGQRGAKTPRSSQGSGRGAGNRPGVEGDTRRGPGREES
FT REPVPESPKPAGVEIRSATGKEVLQNLGPKDK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12684468"
FT /id="VSP_016557"
FT MOD_RES Q62952-2:101
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 570 AA; 61967 MW; 4EF1981CDE9A8708 CRC64;
MSYQGKKNIP RITSDRLLIK GGRIVNDDQS FYADIYMEDG LIKQIGDNLI VPGGVKTIEA
NGKMVMPGGI DVHTHFQMPY KGMTTVDDFF QGTKAALAGG TTMIIDHVVP EPESSLTEAY
EKWREWADGK SCCDYALHVD ITHWNDSVKQ EVQNLSKEKG 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 IWDPDAVKIV
SAKNHQSVAE YNIFEGMELR GAPLVVICQG KIMLEDGNLH VTQGAGRFIP CSPFSDYVYK
RIKARRKMAD LHAVPRGMYD GPVFDLTTTP KGGTPAGSTR GSPTRPNPPV RNLHQSGFSL
SGTQVDEGVR SASKRIVAPP GGRSNITSLS
