ID   DPYL3_HUMAN             Reviewed;         570 AA.
AC   Q14195; Q93012;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-JAN-2012, entry version 110.
DE   RecName: Full=Dihydropyrimidinase-related protein 3;
DE            Short=DRP-3;
DE   AltName: Full=Collapsin response mediator protein 4;
DE            Short=CRMP-4;
DE   AltName: Full=Unc-33-like phosphoprotein 1;
DE            Short=ULIP-1;
GN   Name=DPYSL3; Synonyms=CRMP4, DRP3, ULIP, ULIP1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=97128821; PubMed=8973361; DOI=10.1016/S0378-1119(96)00445-3;
RA   Hamajima N., Matsuda K., Sakata S., Tamaki N., Sasaki M., Nonaka M.;
RT   "A novel gene family defined by human dihydropyrimidinase and three
RT   related proteins with differential tissue distribution.";
RL   Gene 180:157-163(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=97277371; PubMed=9115293; DOI=10.1074/jbc.272.18.12195;
RA   Gaetano C., Matsuo T., Thiele C.J.;
RT   "Identification and characterization of a retinoic acid-regulated
RT   human homologue of the unc-33-like phosphoprotein gene (hUlip) from
RT   neuroblastoma cells.";
RL   J. Biol. Chem. 272:12195-12201(1997).
RN   [3]
RP   PROTEIN SEQUENCE OF 24-56; 82-122; 131-157; 239-254; 259-268; 346-368;
RP   375-397; 401-418; 424-440; 452-480; 488-511 AND 532-550, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA   Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL   Submitted (DEC-2008) to UniProtKB.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-522 AND SER-551, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [5]
RP   PHOSPHORYLATION AT SER-522 BY DYRK2, AND PHOSPHORYLATION AT THR-509;
RP   THR-514 AND SER-518 BY GSK3.
RX   PubMed=16611631; DOI=10.1074/jbc.M513344200;
RA   Cole A.R., Causeret F., Yadirgi G., Hastie C.J., McLauchlan H.,
RA   McManus E.J., Hernandez F., Eickholt B.J., Nikolic M., Sutherland C.;
RT   "Distinct priming kinases contribute to differential regulation of
RT   collapsin response mediator proteins by glycogen synthase kinase-3 in
RT   vivo.";
RL   J. Biol. Chem. 281:16591-16598(2006).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
CC   -!- FUNCTION: Necessary for signaling by class 3 semaphorins and
CC       subsequent remodeling of the cytoskeleton. Plays a role in axon
CC       guidance, neuronal growth cone collapse and cell migration (By
CC       similarity).
CC   -!- SUBUNIT: Homotetramer, and heterotetramer with CRMP1, DPYSL2,
CC       DPYSL4 or DPYSL5 (By similarity). Interacts with synaptic vesicle
CC       protein 2 and SH3A domain of intersectin (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell projection,
CC       growth cone (By similarity). Note=Colocalizes with synaptic
CC       vesicle protein 2 in the central region of the growth cone (By
CC       similarity).
CC   -!- TISSUE SPECIFICITY: Mainly expressed in heart and skeletal muscle.
CC       Also strongly expressed in fetal brain and spinal cord.
CC   -!- PTM: Phosphorylation on Ser-522 by DYRK2 promotes subsequent
CC       phosphorylation on Thr-509, Thr-514 and Ser-518 by GSK3.
CC   -!- SIMILARITY: Belongs to the DHOase family.
CC       Hydantoinase/dihydropyrimidinase subfamily.
CC   -!- CAUTION: Lacks most of the conserved residues that are essential
CC       for binding the metal cofactor and hence for dihydropyrimidinase
CC       activity. Its enzyme activity is therefore unsure.
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DR   EMBL; D78014; BAA11192.1; -; mRNA.
DR   EMBL; Y07818; CAA69153.1; -; mRNA.
DR   IPI; IPI00872788; -.
DR   PIR; JC5318; JC5318.
DR   RefSeq; NP_001184223.1; NM_001197294.1.
DR   RefSeq; NP_001378.1; NM_001387.2.
DR   UniGene; Hs.519659; -.
DR   ProteinModelPortal; Q14195; -.
DR   SMR; Q14195; 14-490.
DR   IntAct; Q14195; 1.
DR   STRING; Q14195; -.
DR   MEROPS; M38.976; -.
DR   PhosphoSite; Q14195; -.
DR   DMDM; 3122050; -.
DR   REPRODUCTION-2DPAGE; Q14195; -.
DR   UCD-2DPAGE; Q14195; -.
DR   PRIDE; Q14195; -.
DR   Ensembl; ENST00000398514; ENSP00000381526; ENSG00000113657.
DR   GeneID; 1809; -.
DR   KEGG; hsa:1809; -.
DR   UCSC; uc003lon.1; human.
DR   CTD; 1809; -.
DR   GeneCards; GC05M146750; -.
DR   H-InvDB; HIX0024842; -.
DR   HGNC; HGNC:3015; DPYSL3.
DR   HPA; HPA010948; -.
DR   MIM; 601168; gene.
DR   neXtProt; NX_Q14195; -.
DR   PharmGKB; PA27473; -.
DR   eggNOG; prNOG04131; -.
DR   HOVERGEN; HBG000806; -.
DR   OrthoDB; EOG48PMJT; -.
DR   PhylomeDB; Q14195; -.
DR   Reactome; REACT_111045; Developmental Biology.
DR   NextBio; 7373; -.
DR   ArrayExpress; Q14195; -.
DR   Bgee; Q14195; -.
DR   CleanEx; HS_DPYSL3; -.
DR   Genevestigator; Q14195; -.
DR   GermOnline; ENSG00000113657; Homo sapiens.
DR   GO; GO:0044297; C:cell body; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0031941; C:filamentous actin; ISS:UniProtKB.
DR   GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR   GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR   GO; GO:0035374; F:chondroitin sulfate binding; ISS:UniProtKB.
DR   GO; GO:0016812; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides; IEA:InterPro.
DR   GO; GO:0017124; F:SH3 domain binding; ISS:UniProtKB.
DR   GO; GO:0051764; P:actin crosslink formation; ISS:UniProtKB.
DR   GO; GO:0051017; P:actin filament bundle assembly; ISS:UniProtKB.
DR   GO; GO:0007411; P:axon guidance; TAS:Reactome.
DR   GO; GO:0071345; P:cellular response to cytokine stimulus; ISS:UniProtKB.
DR   GO; GO:0030336; P:negative regulation of cell migration; ISS:UniProtKB.
DR   GO; GO:0010977; P:negative regulation of neuron projection development; ISS:UniProtKB.
DR   GO; GO:0051491; P:positive regulation of filopodium assembly; ISS:UniProtKB.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
DR   GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR   GO; GO:0006208; P:pyrimidine base catabolic process; IEA:InterPro.
DR   GO; GO:0048678; P:response to axon injury; ISS:UniProtKB.
DR   InterPro; IPR006680; Amidohydro_1.
DR   InterPro; IPR011778; Hydantoinase/dihydroPyrase.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; Metalo_hydrolase; 1.
DR   TIGRFAMs; TIGR02033; D-hydantoinase; 1.
PE   1: Evidence at protein level;
KW   Cell projection; Complete proteome; Cytoplasm;
KW   Direct protein sequencing; Phosphoprotein; Polymorphism;
KW   Reference proteome.
FT   CHAIN         1    570       Dihydropyrimidinase-related protein 3.
FT                                /FTId=PRO_0000165917.
FT   MOD_RES     499    499       Phosphotyrosine (By similarity).
FT   MOD_RES     509    509       Phosphothreonine; by GSK3.
FT   MOD_RES     514    514       Phosphothreonine; by GSK3.
FT   MOD_RES     518    518       Phosphoserine; by GSK3.
FT   MOD_RES     522    522       Phosphoserine; by DYRK2.
FT   MOD_RES     541    541       Phosphoserine (By similarity).
FT   MOD_RES     551    551       Phosphoserine.
FT   VARIANT     442    442       A -> S (in dbSNP:rs2304044).
FT                                /FTId=VAR_020485.
FT   CONFLICT     49     49       L -> V (in Ref. 2; CAA69153).
FT   CONFLICT    142    142       T -> A (in Ref. 2; CAA69153).
SQ   SEQUENCE   570 AA;  61963 MW;  9D6AFE86CBB33AD5 CRC64;
     MSYQGKKNIP RITSDRLLIK GGRIVNDDQS FYADIYMEDG LIKQIGDNLI VPGGVKTIEA
     NGKMVIPGGI DVHTHFQMPY KGMTTVDDFF QGTKAALAGG TTMIIDHVVP EPESSLTEAY
     EKWREWADGK SCCDYALHVD ITHWNDSVKQ EVQNLIKDKG VNSFMVYMAY KDLYQVSNTE
     LYEIFTCLGE LGAIAQVHAE NGDIIAQEQT RMLEMGITGP EGHVLSRPEE LEAEAVFRAI
     TIASQTNCPL YVTKVMSKSA ADLISQARKK GNVVFGEPIT ASLGIDGTHY WSKNWAKAAA
     FVTSPPLSPD PTTPDYINSL LASGDLQLSG SAHCTFSTAQ KAIGKDNFTA IPEGTNGVEE
     RMSVIWDKAV ATGKMDENQF VAVTSTNAAK IFNLYPRKGR ISVGSDSDLV IWDPDAVKIV
     SAKNHQSAAE YNIFEGMELR GAPLVVICQG KIMLEDGNLH VTQGAGRFIP CSPFSDYVYK
     RIKARRKMAD LHAVPRGMYD GPVFDLTTTP KGGTPAGSAR GSPTRPNPPV RNLHQSGFSL
     SGTQVDEGVR SASKRIVAPP GGRSNITSLS
//