ID   DPYL3_XENTR             Reviewed;         571 AA.
AC   Q6GL72;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Dihydropyrimidinase-related protein 3 {ECO:0000250|UniProtKB:Q62952};
DE            Short=DRP-3 {ECO:0000250|UniProtKB:Q62952};
DE   AltName: Full=Dihydropyrimidinase-like 3 {ECO:0000312|EMBL:AAH74633.1};
GN   Name=dpysl3 {ECO:0000312|EMBL:AAH74633.1}; ORFNames=TNeu084b06.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1] {ECO:0000312|EMBL:CAJ82805.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Neurula {ECO:0000312|EMBL:CAJ82805.1};
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000312|EMBL:CAJ82805.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Tail bud {ECO:0000312|EMBL:AAH74633.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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).
CC       {ECO:0000250|UniProtKB:Q62952}.
CC   -!- SUBUNIT: Homotetramer and heterotetramer.
CC       {ECO:0000250|UniProtKB:Q62952}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q62952}. Cell
CC       projection, growth cone {ECO:0000250|UniProtKB:Q62952}.
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; CR942629; CAJ82805.1; -; mRNA.
DR   EMBL; BC074633; AAH74633.1; -; mRNA.
DR   RefSeq; NP_001005637.1; NM_001005637.1.
DR   AlphaFoldDB; Q6GL72; -.
DR   SMR; Q6GL72; -.
DR   MEROPS; M38.976; -.
DR   PaxDb; Q6GL72; -.
DR   DNASU; 448103; -.
DR   GeneID; 448103; -.
DR   KEGG; xtr:448103; -.
DR   CTD; 1809; -.
DR   Xenbase; XB-GENE-944729; dpysl3.
DR   eggNOG; KOG2584; Eukaryota.
DR   InParanoid; Q6GL72; -.
DR   OrthoDB; 719800at2759; -.
DR   Reactome; R-XTR-399956; CRMPs in Sema3A signaling.
DR   Proteomes; UP000008143; Chromosome 3.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000012718; Expressed in central nervous system and 17 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   GO; GO:0051764; P:actin crosslink formation; IBA:GO_Central.
DR   GO; GO:0051017; P:actin filament bundle assembly; IEA:InterPro.
DR   GO; GO:0051491; P:positive regulation of filopodium assembly; IEA:InterPro.
DR   GO; GO:0030334; P:regulation of cell migration; IEA:InterPro.
DR   GO; GO:0010975; P:regulation of neuron projection development; IEA:InterPro.
DR   GO; GO:0048678; P:response to axon injury; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Cell projection; Cytoplasm; Reference proteome.
FT   CHAIN           1..571
FT                   /note="Dihydropyrimidinase-related protein 3"
FT                   /id="PRO_0000382237"
FT   REGION          509..571
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        512..550
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   571 AA;  62003 MW;  B90C987F07B59FA9 CRC64;
     MSYQGKKNIP RITSDRLLIK GGRIVNDDQS FYADIYMEDG LIKQIGDNLI VPGGVKTIEA
     NGKMVIPGGI DVHTHLQMPY RGMTTVDDFF QGTKAALAGG TTMIVDHVIP EPEASLTEAF
     EKWREWADGK TCCDYSLHVD ITHWNDSVKQ EVEALVKQKG VNSFMVYMAY KDLYQMSNTE
     LYEVFTFLGG LGAIAQVHAE NGDIIAQEQN RMLELGITGP EGHVLSRPEE LEAEAVFRAI
     TIASQTNCPL YVTKVMSKSS VDLISQARKK GYVVFGEPIT ASLGTDGTHY WSKNWAKAAA
     FVTSPPLSPD PTTPDYINSL LASGDLQVTG SAHATFSTAQ KAIGKDNFTL IPEGTNGIEE
     RMSVIWDKAV ATGKMDENQF VAVTSTNAAK IFNLYPRKGR IAVGSDSDLV IWDPDAVKIV
     SAKSHHSAAE YNIFEGMELR GAPLVVICQG KIMMEDGTLH VTQGTGRFIP CSPFPDYVYK
     RIKARTKMAE LHAVPRGMYD GPVYDLASTP KAGTPAGSTK GSPTKQTAPV RNLHHSGFSL
     AGNQGDESGV RSASRRIVAP PGGRSNITSL S