DPYL5_MOUSE
ID DPYL5_MOUSE Reviewed; 564 AA.
AC Q9EQF6;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Dihydropyrimidinase-related protein 5;
DE Short=DRP-5;
DE AltName: Full=Collapsin response mediator protein 5;
DE Short=CRMP-5;
GN Name=Dpysl5; Synonyms=Crmp5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP SUBUNIT.
RC STRAIN=Swiss Webster / NIH; TISSUE=Embryo;
RX PubMed=10956643; DOI=10.1074/jbc.m003277200;
RA Fukada M., Watakabe I., Yuasa-Kawada J., Kawachi H., Kuroiwa A.,
RA Matsuda Y., Noda M.;
RT "Molecular characterization of CRMP5, a novel member of the collapsin
RT response mediator protein family.";
RL J. Biol. Chem. 275:37957-37965(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP INTERACTION WITH SEPTIN4, AND SUBCELLULAR LOCATION.
RX PubMed=12581152; DOI=10.1046/j.1365-2443.2003.00617.x;
RA Takahashi S., Inatome R., Yamamura H., Yanagi S.;
RT "Isolation and expression of a novel mitochondrial septin that interacts
RT with CRMP/CRAM in the developing neurones.";
RL Genes Cells 8:81-93(2003).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-509; THR-514; SER-532 AND
RP SER-538, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Liver, Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-559, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Involved in the negative regulation of dendrite outgrowth.
CC {ECO:0000250|UniProtKB:Q9BPU6}.
CC -!- SUBUNIT: Homotetramer, and heterotetramer with other DPYS-like
CC proteins. Interacts with DPYSL2, DPYSL3 and DPYSL4. Interacts with
CC SEPTIN4 isoform 4. Interacts with MAP2 and TUBB3 (By similarity).
CC {ECO:0000250|UniProtKB:Q9BPU6, ECO:0000269|PubMed:10956643,
CC ECO:0000269|PubMed:12581152}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Translocates into
CC the mitochondria upon interaction with SEPTIN4 isoform 4.
CC {ECO:0000269|PubMed:12581152}.
CC -!- TISSUE SPECIFICITY: Detected in brain. {ECO:0000269|PubMed:10956643}.
CC -!- DEVELOPMENTAL STAGE: Detected in whole embryos after 11 days of
CC development. Detected in embryonic head. Highly expressed in newborns
CC and up to 7 days after birth. Expression is decreased after 14 days.
CC {ECO:0000269|PubMed:10956643}.
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; AF249295; AAG37998.1; -; mRNA.
DR EMBL; BC065054; AAH65054.1; -; mRNA.
DR CCDS; CCDS39047.1; -.
DR RefSeq; NP_075534.1; NM_023047.2.
DR RefSeq; XP_006504108.1; XM_006504045.1.
DR AlphaFoldDB; Q9EQF6; -.
DR SMR; Q9EQF6; -.
DR BioGRID; 211143; 7.
DR IntAct; Q9EQF6; 3.
DR MINT; Q9EQF6; -.
DR STRING; 10090.ENSMUSP00000085400; -.
DR MEROPS; M38.978; -.
DR iPTMnet; Q9EQF6; -.
DR PhosphoSitePlus; Q9EQF6; -.
DR SwissPalm; Q9EQF6; -.
DR MaxQB; Q9EQF6; -.
DR PaxDb; Q9EQF6; -.
DR PeptideAtlas; Q9EQF6; -.
DR PRIDE; Q9EQF6; -.
DR ProteomicsDB; 277400; -.
DR Antibodypedia; 28026; 240 antibodies from 28 providers.
DR DNASU; 65254; -.
DR Ensembl; ENSMUST00000088081; ENSMUSP00000085400; ENSMUSG00000029168.
DR Ensembl; ENSMUST00000114729; ENSMUSP00000110377; ENSMUSG00000029168.
DR GeneID; 65254; -.
DR KEGG; mmu:65254; -.
DR UCSC; uc008wvw.1; mouse.
DR CTD; 56896; -.
DR MGI; MGI:1929772; Dpysl5.
DR VEuPathDB; HostDB:ENSMUSG00000029168; -.
DR eggNOG; KOG2584; Eukaryota.
DR GeneTree; ENSGT01030000234527; -.
DR HOGENOM; CLU_015572_2_2_1; -.
DR InParanoid; Q9EQF6; -.
DR OMA; THAHFRD; -.
DR OrthoDB; 719800at2759; -.
DR PhylomeDB; Q9EQF6; -.
DR TreeFam; TF314706; -.
DR Reactome; R-MMU-399956; CRMPs in Sema3A signaling.
DR BioGRID-ORCS; 65254; 6 hits in 72 CRISPR screens.
DR ChiTaRS; Dpysl5; mouse.
DR PRO; PR:Q9EQF6; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9EQF6; protein.
DR Bgee; ENSMUSG00000029168; Expressed in cortical plate and 128 other tissues.
DR ExpressionAtlas; Q9EQF6; baseline and differential.
DR Genevisible; Q9EQF6; MM.
DR GO; GO:0005737; C:cytoplasm; IPI:MGI.
DR GO; GO:0030425; C:dendrite; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
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; TAS:MGI.
DR GO; GO:0050774; P:negative regulation of dendrite morphogenesis; ISO:MGI.
DR CDD; cd01314; D-HYD; 1.
DR Gene3D; 2.30.40.10; -; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR030626; DRP5.
DR InterPro; IPR011778; Hydantoinase/dihydroPyrase.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11647:SF58; PTHR11647:SF58; 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; Methylation; Phosphoprotein; Reference proteome.
FT CHAIN 1..564
FT /note="Dihydropyrimidinase-related protein 5"
FT /id="PRO_0000165925"
FT MOD_RES 509
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 514
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 532
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 538
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 559
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
SQ SEQUENCE 564 AA; 61516 MW; CA93790FC8F9CD98 CRC64;
MLANSASVRI LIKGGKVVND DCTHEADVYI ESGIIQQVGR ELMIPGGAKV IDATGKLVIP
GGIDTSTHFH QTFMNATCVD DFYHGTKAAL VGGTTMIIGH VLPDKETSLV EAYEKCRALA
DPKVCCDYAL HVGITWWAPK VKAEMETLVR EKGVNSFQMF MTYKDLYMLR DSELYQVFHA
CRDIGAIPRV HAENGELVAE GAKEALDLGI TGPEGIEISH PEELEAEATH RVITIANRTH
CPIYLVNVSS ISAGDVIAAA KMQGKVVLAE TTNAHATLTG LHYYHQDWSH AAAYVTVPPL
RLDTNTSTYL MSLLANDTLN IVASDHRPFT TKQKAMGKED FTKIPHGVSG VQDRMSVVWE
RGVVGGKMDE NRFVAVTSSN AAKILNLYPR KGRIIPGADA DVVVWDPEAT KTISASTQVQ
GGDFNLYENM RCHGVPLVTI SRGRVVYENG VFMCAEGTGK FCPLRSFPDI VYKKLVQREK
TLKVRGVDRT PYLGDVAIVV HPGKKEMGTP LADTPTRPVT RHGGMRDLHE SSFSLSGSQI
DDHVPKRASA RILAPPGGRS SGIW
