DPYL3_DANRE
ID DPYL3_DANRE Reviewed; 567 AA.
AC Q52PJ5;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Dihydropyrimidinase-related protein 3 {ECO:0000250|UniProtKB:Q62952};
DE Short=DRP-3 {ECO:0000250|UniProtKB:Q62952};
DE AltName: Full=Collapsin response mediator protein 4 {ECO:0000312|EMBL:AAX86825.1};
DE Short=CRMP-4 {ECO:0000303|PubMed:15922676};
GN Name=dpysl3 {ECO:0000312|ZFIN:ZDB-GENE-050720-2};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAX86825.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain {ECO:0000269|PubMed:15922676};
RX PubMed=15922676; DOI=10.1016/j.modgep.2005.03.009;
RA Schweitzer J., Becker C.G., Schachner M., Becker T.;
RT "Expression of collapsin response mediator proteins in the nervous system
RT of embryonic zebrafish.";
RL Gene Expr. Patterns 5:809-816(2005).
RN [2] {ECO:0000312|EMBL:AAI62272.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2008) 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 -!- TISSUE SPECIFICITY: At 16 hours post-fertilization, expressed in the
CC presumptive nucleus of the medial longitudinal fascicle, the
CC presumptive trigeminal ganglion and the spinal cord. Expression in the
CC spinal cord is strongest towards the rostral, more mature, spinal cord,
CC and weaker towards the caudal spinal cord. At 24 hours post-
CC fertilization, expressed in the olfactory placode, in the telencephalon
CC and diencephalon but not in the proliferating ventricular zone.
CC Expressed in the epiphysis, the nucleus of the medial longitudinal
CC fascicle and in the area close to the nucleus of the posterior
CC commissure. Expression in the hindbrain is restricted to reticulospinal
CC neurons. In the cranial ganglia, expressed in the trigeminal,
CC acoustic/anterior lateral line and posterior lateral line ganglion. In
CC the spinal cord, expressed in the large dorsally-located Rohon-Beard
CC neurons. {ECO:0000269|PubMed:15922676}.
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; AY987373; AAX86825.1; -; mRNA.
DR EMBL; BC162272; AAI62272.1; -; mRNA.
DR EMBL; BC162579; AAI62579.1; -; mRNA.
DR RefSeq; NP_001018348.1; NM_001020512.1.
DR AlphaFoldDB; Q52PJ5; -.
DR SMR; Q52PJ5; -.
DR STRING; 7955.ENSDARP00000108688; -.
DR MEROPS; M38.976; -.
DR PaxDb; Q52PJ5; -.
DR PRIDE; Q52PJ5; -.
DR Ensembl; ENSDART00000065097; ENSDARP00000065096; ENSDARG00000002587.
DR GeneID; 553166; -.
DR KEGG; dre:553166; -.
DR CTD; 1809; -.
DR ZFIN; ZDB-GENE-050720-2; dpysl3.
DR eggNOG; KOG2584; Eukaryota.
DR GeneTree; ENSGT01030000234527; -.
DR HOGENOM; CLU_015572_2_2_1; -.
DR InParanoid; Q52PJ5; -.
DR OMA; RNFVCSP; -.
DR OrthoDB; 719800at2759; -.
DR PhylomeDB; Q52PJ5; -.
DR TreeFam; TF314706; -.
DR Reactome; R-DRE-399956; CRMPs in Sema3A signaling.
DR PRO; PR:Q52PJ5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 21.
DR Bgee; ENSDARG00000002587; Expressed in brain and 52 other tissues.
DR ExpressionAtlas; Q52PJ5; baseline and differential.
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:0007411; P:axon guidance; IMP:ZFIN.
DR GO; GO:0007409; P:axonogenesis; IGI:ZFIN.
DR GO; GO:0048936; P:peripheral nervous system neuron axonogenesis; IMP:ZFIN.
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; 1.
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..567
FT /note="Dihydropyrimidinase-related protein 3"
FT /id="PRO_0000382468"
FT REGION 505..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..537
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 567 AA; 61544 MW; 882A172CC09D34D4 CRC64;
MSYQGKKNIP KITSERLLIK GGRIVNDDQS FYADIYMEDG VIKQIGDNLI VPGGVKTIEA
NGKMVIPGGI DIHTHLQMPF RGTTTADDFT QGTKAALAGG TTMIVDHVIP EPGCSLLEAF
DRWSKWADEK ACCDYSLHVD ITHWNDSVKQ EVETLIKEKG VNSFQVYMAF KDLYQMSNTE
LYEVFTFLGE HGGIAQVHAE NGEIIAEEQA RMLEMGITGP EGHVLSRPEE LEAEAVFRAV
TIASQTNCPL YVTRVMSKSA ADIISQARKK GNVVFGEPIT ASLGTDGTHY WSKNWAKAAS
FVTSPPLSPD PTTPDYLNTL LASGDLSVVG SAHCTFSVAQ KAIGKDDFTQ IPEGVNGAEE
RMSIIWDKAV VTGKMDENMF VAVTSTNAAK ILNLYPRKGR IAVGSDSDLV IWDTDAVRTI
TAKTHHSAAE YNVFEGMELR GAPMLVVCQG KIVLEDGNLH ATSGTGRFIP CSPFPDFAYK
RVKARKQLAI LKAVPRGMYD GPVSEFSPMS RGGTPSASTR TSPTKVPVRN LHQSGFTLSG
PEEAPIRPAG RRIVVPPGGR SNITSLS
