ID   DPY3A_XENLA             Reviewed;         571 AA.
AC   O13022; Q7ZWQ8;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 2.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Dihydropyrimidinase-related protein 3-A;
DE            Short=DRP-3-A;
DE   AltName: Full=Neural-specific protein 1;
GN   Name=dpysl3-a; Synonyms=dpysl3, nsp1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RA   Engel E.R., Lepperdinger G., Richter K.;
RL   Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Tail bud;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (FEB-2003) 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). {ECO:0000250}.
CC   -!- SUBUNIT: Homotetramer and heterotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell projection, growth
CC       cone {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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA73509.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; Y13069; CAA73509.1; ALT_FRAME; mRNA.
DR   EMBL; BC046836; AAH46836.1; -; mRNA.
DR   RefSeq; NP_001080111.1; NM_001086642.1.
DR   AlphaFoldDB; O13022; -.
DR   SMR; O13022; -.
DR   MEROPS; M38.976; -.
DR   DNASU; 379803; -.
DR   GeneID; 379803; -.
DR   KEGG; xla:379803; -.
DR   CTD; 379803; -.
DR   Xenbase; XB-GENE-944735; dpysl3.S.
DR   Proteomes; UP000186698; Chromosome 3S.
DR   Bgee; 379803; Expressed in brain 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: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-A"
FT                   /id="PRO_0000165920"
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"
FT   CONFLICT        241
FT                   /note="T -> I (in Ref. 1; CAA73509)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        470
FT                   /note="H -> P (in Ref. 1; CAA73509)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   571 AA;  62129 MW;  1A1AB9B71EFB79AA CRC64;
     MSYQGKKNIP RITSERLLIK GGRIVNDDQS FYADIYMEDG LIKQIGDNLI VPGGVKTIEA
     NGKMVIPGGI DVHTHLQMPY RGMTTVDDFL QGTKAALAGG TTMIVDHVIP EPEASLTEAF
     EKWREWADGK TCCDYSLHVD ITHWSDSVKQ EVETLVKQKG VNSFMVYMAY KDLYQMSNTE
     LYEIFTFLGS LGAIAQVHAE NGDIIAQEQN RMLELGITGP EGHVLSRPEE LEAEAVFRAI
     TIASQTNCPL YVTKVMSKSS VDLISQARKK GYVVFGEPIT ASLGTDGTHY WSKNWAKAAA
     FVTSPPLSPD PTTPDYINSL LASGDLQVTG SAHATFSTAQ KAIGKDNFTL IPEGTNGIEE
     RMSVIWDKSV ATGKMDENQF VSVTSTNAAK IFNLYPRKGR IAVGSDSDLV IWDPDAVKIV
     SAKSHHSAAE YNIFEGMELR GAPLVVICQG KIMMEDGTLH VTQGTGRFIH CSPFPDYVYK
     RIKARTKMAE LHGVPRGMYD GPVYDLASTP KAGTPAGSTK GSPTKQTPPV RNLHHSAFSL
     AGNQGDESGV RSASRRIVAP PGGRSNITSL S