ID   DPY3B_XENLA             Reviewed;         571 AA.
AC   Q640K6;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Dihydropyrimidinase-related protein 3-B;
DE            Short=DRP-3-B;
DE   AltName: Full=Collapsin response mediator protein 4 {ECO:0000303|PubMed:17554687};
DE            Short=CRMP-4 {ECO:0000303|PubMed:17554687};
DE            Short=xCRMP4 {ECO:0000303|PubMed:17554687};
GN   Name=dpysl3-b; Synonyms=crmp4 {ECO:0000303|PubMed:17554687};
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] {ECO:0000312|EMBL:AAH82618.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart {ECO:0000312|EMBL:AAH82618.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305}
RP   TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX   PubMed=17554687; DOI=10.1387/ijdb.062235js;
RA   Souopgui J., Klisch T.J., Pieler T., Henningfeld K.A.;
RT   "Expression and regulation of Xenopus CRMP-4 in the developing nervous
RT   system.";
RL   Int. J. Dev. Biol. 51:339-343(2007).
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   -!- TISSUE SPECIFICITY: Expressed in the prospective neuroectoderm at the
CC       end of gastrulation. During open neural plate stages, expressed broadly
CC       throughout the anterior neural plate and in the three bilateral stripes
CC       of the posterior neural plate where primary neurons arise. At tadpole
CC       stages, expression is maintained throughout the central nervous system
CC       and in the eye retina. {ECO:0000269|PubMed:17554687}.
CC   -!- DEVELOPMENTAL STAGE: Expressed zygotically from the end of
CC       gastrulation. Expression increases during neurula stages and is
CC       maintained at a constant level throughout tailbud stages and later
CC       development. {ECO:0000269|PubMed:17554687}.
CC   -!- INDUCTION: By the neuronal determination factor neurog2/X-ngngr-1.
CC       Repressed by Notch signaling. {ECO:0000269|PubMed:17554687}.
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; BC082618; AAH82618.1; -; mRNA.
DR   RefSeq; NP_001087967.1; NM_001094498.1.
DR   AlphaFoldDB; Q640K6; -.
DR   SMR; Q640K6; -.
DR   DNASU; 494650; -.
DR   GeneID; 494650; -.
DR   KEGG; xla:494650; -.
DR   CTD; 494650; -.
DR   Xenbase; XB-GENE-6255615; dpysl3.L.
DR   OrthoDB; 719800at2759; -.
DR   Proteomes; UP000186698; Chromosome 3L.
DR   Bgee; 494650; Expressed in heart and 16 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-B"
FT                   /id="PRO_0000382236"
FT   REGION          502..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;  62022 MW;  58BBCEA68A06C9FC CRC64;
     MSYQGKKNIP RITSDRLLIK GGRIVNDDQS FYADIYMEDG LIKQIGDNLI VPGGVKTIEA
     NGKMVIPGGI DVHTHLQMPY RGMTTVDDFF QGTKAALAGG TTMIVDHVIP EPEASLTEAL
     EKWREWADGK TCCDYSLHVD ITHWSDSVKQ EVETLVKQKG VNSFMVYMAY KDMYQMSNTE
     LYEIFTFLGG LGAIAQVHAE NGDIIAQEQN RMLELGITGP EGHVLSRPEE LEAEAVFRAI
     TIASQTNCPL YVTKVMSKSS VDLISQARKK GYVVFGEPIT ASLGTDGTHY WSKNWAKAAA
     FVTSPPLSPD PTTPDYINSL LASGDLQVTG SAHATFSTAQ KAIGKDNFTL IPEGTNGIEE
     RMSVIWDKSV ATGKMDENQF VAVTSTNAAK IFNLYPRKGR IAVGSDSDLV IWDPDAVKIV
     SAKSHHSAAE YNIFEGMELR GAPLVVICQG KIMMEDGTLH ATQGTGRFIP CSPFPDYVYK
     RIKARTKMAE LHAVPRGMYD GPVHDLASTP KAGTPAGSTK GSPTKQTAPV RNLHHSGFSL
     IGNQADESGV RSASRRIVAP PGGRSNITSL S