ID   DPYL2_CHICK             Reviewed;         572 AA.
AC   Q90635;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Dihydropyrimidinase-related protein 2;
DE            Short=DRP-2;
DE   AltName: Full=Collapsin response mediator protein CRMP-62;
GN   Name=DPYSL2;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Spinal ganglion;
RX   PubMed=7637782; DOI=10.1038/376509a0;
RA   Goshima Y., Nakamura F., Strittmatter P., Strittmatter S.M.;
RT   "Collapsin-induced growth cone collapse mediated by an intracellular
RT   protein related to UNC-33.";
RL   Nature 376:509-514(1995).
CC   -!- FUNCTION: Plays a role in neuronal development and polarity, as well as
CC       in axon growth and guidance, neuronal growth cone collapse and cell
CC       migration. Necessary for signaling by class 3 semaphorins and
CC       subsequent remodeling of the cytoskeleton (By similarity).
CC       {ECO:0000250, ECO:0000269|PubMed:7637782}.
CC   -!- SUBUNIT: Homotetramer, and heterotetramer with CRMP1, DPYSL3, DPYSL4 or
CC       DPYSL5. Interacts through its C-terminus with the C-terminus of
CC       CYFIP1/SRA1 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7637782}.
CC   -!- TISSUE SPECIFICITY: Detected in the developing chick nervous system.
CC       {ECO:0000269|PubMed:7637782}.
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; U17277; AAA93200.1; -; mRNA.
DR   PIR; S58889; S58889.
DR   RefSeq; XP_015152784.1; XM_015297298.1.
DR   AlphaFoldDB; Q90635; -.
DR   SMR; Q90635; -.
DR   IntAct; Q90635; 1.
DR   STRING; 9031.ENSGALP00000030864; -.
DR   MEROPS; M38.975; -.
DR   iPTMnet; Q90635; -.
DR   PaxDb; Q90635; -.
DR   PRIDE; Q90635; -.
DR   Ensembl; ENSGALT00000000305; ENSGALP00000000304; ENSGALG00000000227.
DR   GeneID; 395155; -.
DR   CTD; 1808; -.
DR   VEuPathDB; HostDB:geneid_395155; -.
DR   eggNOG; KOG2584; Eukaryota.
DR   GeneTree; ENSGT01030000234527; -.
DR   HOGENOM; CLU_015572_2_2_1; -.
DR   InParanoid; Q90635; -.
DR   Reactome; R-GGA-437239; Recycling pathway of L1.
DR   PRO; PR:Q90635; -.
DR   Proteomes; UP000000539; Chromosome 22.
DR   Bgee; ENSGALG00000000227; Expressed in cerebellum and 12 other tissues.
DR   ExpressionAtlas; Q90635; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   GO; GO:0007411; P:axon guidance; IEA:InterPro.
DR   GO; GO:0007420; P:brain development; IEA:InterPro.
DR   GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0030516; P:regulation of axon extension; IEA:InterPro.
DR   GO; GO:0045664; P:regulation of neuron differentiation; IEA:InterPro.
DR   CDD; cd01314; D-HYD; 1.
DR   Gene3D; 2.30.40.10; -; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR030615; DRP2.
DR   InterPro; IPR011778; Hydantoinase/dihydroPyrase.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   PANTHER; PTHR11647:SF56; PTHR11647:SF56; 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   Cytoplasm; Developmental protein; Differentiation; Neurogenesis;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..572
FT                   /note="Dihydropyrimidinase-related protein 2"
FT                   /id="PRO_0000165916"
FT   REGION          512..537
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         509
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         518
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         522
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   572 AA;  62331 MW;  85DB9E3DD5E54D8D CRC64;
     MSYQGKKNIP RITSDRLLIK GGKIVNDDQS FYADIYMEDG LIKQIGENLI VPGGVKTIEA
     HGRMVIPGGI DVHTRFQMPE QGMTSADDFF QGTKAALAGG TTMIIDHVVP EPGTSLLTAF
     DQWREWADSK SCCDYSLHVD ITEWHKGVQE EMEALVKDHG VNSFLVYMAF KDRFQLSDSQ
     IYEVLSVIRD IGATAQVHAE NGDIIAEEQQ RILELGITGP EGHVLSRPEE VEAEAVNRAI
     TIANQTNCPL YITKVMSKSA AEVIAQARKK GTVVYGEPIT ASLGTDGSHY WSKNWAKAAA
     FVTSPPLSPD PTTPDFLNSL LSCGDLQVTG SAHCTFNTAQ KAVGKDNFTL IPEGTNGTEE
     RMSIIWDKAV VTGKMDENQF VAVTSTNAAK IFNLYPRKGR IAVGSDADLV IWDPDSVKTI
     SAKTHNISLE YNIFEGMECR GSPLVVISQG KIVLEDGNLH VTEGSGRYIP RKPFPDFVYK
     RIKARSRLAE LRGVPRGLYD GPVCEVSVTP KTVTPASSAK TSPAKQQAPP VRNLHQSGFS
     LSGAQIDDNI PRRTTQRIVA PPGGRANITS LG