ID   DPYL4_RAT               Reviewed;         564 AA.
AC   Q62951;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 147.
DE   RecName: Full=Dihydropyrimidinase-related protein 4;
DE            Short=DRP-4;
DE   AltName: Full=Collapsin response mediator protein 3;
DE            Short=CRMP-3;
DE   AltName: Full=UNC33-like phosphoprotein 4;
DE            Short=ULIP-4;
DE   Flags: Fragment;
GN   Name=Dpysl4; Synonyms=Crmp3, Ulip4;
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].
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   [2]
RP   PROTEIN SEQUENCE OF 36-48; 119-149; 166-181; 263-285; 338-353; 367-382;
RP   416-432 AND 489-511, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Diao W., Kang S.U.;
RL   Submitted (JUL-2007) to UniProtKB.
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 with CRMP1, DPYSL2, DPYSL3 or
CC       DPYSL5. Interacts with PLEXA1 (By similarity). Interacts with FLNA (By
CC       similarity). {ECO:0000250|UniProtKB:O14531,
CC       ECO:0000250|UniProtKB:O35098}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Expressed transiently in developing spinal cord
CC       and selectively in the postnatal cerebellum.
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U52103; AAB03281.1; -; mRNA.
DR   RefSeq; NP_037065.1; NM_012933.1.
DR   AlphaFoldDB; Q62951; -.
DR   SMR; Q62951; -.
DR   BioGRID; 247452; 2.
DR   IntAct; Q62951; 2.
DR   MINT; Q62951; -.
DR   STRING; 10116.ENSRNOP00000029334; -.
DR   MEROPS; M38.977; -.
DR   iPTMnet; Q62951; -.
DR   PhosphoSitePlus; Q62951; -.
DR   jPOST; Q62951; -.
DR   PaxDb; Q62951; -.
DR   PRIDE; Q62951; -.
DR   GeneID; 25417; -.
DR   KEGG; rno:25417; -.
DR   UCSC; RGD:2409; rat.
DR   CTD; 10570; -.
DR   RGD; 2409; Dpysl4.
DR   eggNOG; KOG2584; Eukaryota.
DR   InParanoid; Q62951; -.
DR   OrthoDB; 719800at2759; -.
DR   PhylomeDB; Q62951; -.
DR   Reactome; R-RNO-399956; CRMPs in Sema3A signaling.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0051219; F:phosphoprotein binding; ISO:RGD.
DR   GO; GO:0070997; P:neuron death; IEA:InterPro.
DR   GO; GO:0048666; P:neuron development; IEP:RGD.
DR   GO; GO:0097485; P:neuron projection guidance; IEA:InterPro.
DR   CDD; cd01314; D-HYD; 1.
DR   Gene3D; 2.30.40.10; -; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR030612; DRP4.
DR   InterPro; IPR011778; Hydantoinase/dihydroPyrase.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   PANTHER; PTHR11647:SF55; PTHR11647:SF55; 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   Cytoplasm; Direct protein sequencing; Phosphoprotein; Reference proteome.
FT   CHAIN           <1..564
FT                   /note="Dihydropyrimidinase-related protein 4"
FT                   /id="PRO_0000165923"
FT   MOD_RES         529
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O35098"
FT   MOD_RES         536
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O35098"
FT   NON_TER         1
SQ   SEQUENCE   564 AA;  61086 MW;  42050891CC1436D2 CRC64;
     IPRITSDRLL IKGGKIVNDD QSFHADLYVE DGLIKQIGEN LIVPGGIKTI DAHGLMVLPG
     GVDVHTRLQM PVLGMTPADD FCQGTKAALA GGTTMILDHV FPDAGVSLLA AYEQWRERAD
     SAACCDYSLH VDIPRWHEST KEELEALVRD KGVNSFLVFM AYKDRCQCTD GQIYEIFSLI
     RDLGAVAQVH AENGDIVEEE QKRLLEQGIT GPEGHVLSHP EEVEAEAVYR AVTIAKQANC
     PLYITKVMSK GAADMVAQAK RRGVVVFGEP ITASLGTDGS HYWSKNWAKA AAFVTSPPIN
     PDPTTADHLT SLLSSGDLQV TGSAHCTFTT AQKAVGKDNF TLIPEGINGI EERMSVVWEK
     CVASGKMDEN EFVAVTSTNA AKIFNFYPRK GRVAVGSDAD LVIWNPRATK VISAKSHNLN
     VEYNIFEGVE CRGMPTVVIS QGRVVLEDGN LLVTPGAGRF IPRKTFPDFV YKRIKARNRL
     AEIHGVPRGL YDGPVHEVML PAKPGSGTQA RASCPGKISV PPVRNLHQSG FSLSGSQADD
     HIARRTAQKI MAPPGGRSNI TSLS