DPYL5_RAT
ID DPYL5_RAT Reviewed; 564 AA.
AC Q9JHU0;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Dihydropyrimidinase-related protein 5;
DE Short=DRP-5;
DE AltName: Full=UNC33-like phosphoprotein 6;
DE Short=ULIP-6;
GN Name=Dpysl5; Synonyms=Ulip6;
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].
RX PubMed=11034345; DOI=10.1016/s0014-5793(00)01952-9;
RA Horiuchi M., El Far O., Betz H.;
RT "Ulip6, a novel unc-33 and dihydropyrimidinase related protein highly
RT expressed in developing rat brain.";
RL FEBS Lett. 480:283-286(2000).
RN [2]
RP PROTEIN SEQUENCE OF 17-40; 171-189; 232-248; 344-354; 384-390 AND 552-559,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
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 (By similarity).
CC Interacts with MAP2 and TUBB3 (By similarity).
CC {ECO:0000250|UniProtKB:Q9BPU6, ECO:0000250|UniProtKB:Q9EQF6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in embryonic and early postnatal
CC brain and spinal cord.
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; AJ131436; CAB95193.1; -; mRNA.
DR RefSeq; NP_075412.1; NM_023023.1.
DR RefSeq; XP_017449839.1; XM_017594350.1.
DR AlphaFoldDB; Q9JHU0; -.
DR SMR; Q9JHU0; -.
DR BioGRID; 249320; 1.
DR STRING; 10116.ENSRNOP00000012274; -.
DR MEROPS; M38.978; -.
DR iPTMnet; Q9JHU0; -.
DR PhosphoSitePlus; Q9JHU0; -.
DR World-2DPAGE; 0004:Q9JHU0; -.
DR jPOST; Q9JHU0; -.
DR PaxDb; Q9JHU0; -.
DR PRIDE; Q9JHU0; -.
DR Ensembl; ENSRNOT00000012273; ENSRNOP00000012274; ENSRNOG00000008996.
DR GeneID; 65208; -.
DR KEGG; rno:65208; -.
DR CTD; 56896; -.
DR RGD; 620467; Dpysl5.
DR eggNOG; KOG2584; Eukaryota.
DR GeneTree; ENSGT01030000234527; -.
DR HOGENOM; CLU_015572_2_2_1; -.
DR InParanoid; Q9JHU0; -.
DR OMA; THAHFRD; -.
DR OrthoDB; 719800at2759; -.
DR PhylomeDB; Q9JHU0; -.
DR TreeFam; TF314706; -.
DR Reactome; R-RNO-399956; CRMPs in Sema3A signaling.
DR PRO; PR:Q9JHU0; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000008996; Expressed in frontal cortex and 12 other tissues.
DR Genevisible; Q9JHU0; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0030425; C:dendrite; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
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:0050774; P:negative regulation of dendrite morphogenesis; IEA:Ensembl.
DR GO; GO:0030182; P:neuron differentiation; IEP:RGD.
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; Direct protein sequencing; Methylation; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..564
FT /note="Dihydropyrimidinase-related protein 5"
FT /id="PRO_0000165926"
FT MOD_RES 509
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9EQF6"
FT MOD_RES 514
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9EQF6"
FT MOD_RES 532
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9EQF6"
FT MOD_RES 538
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9EQF6"
FT MOD_RES 559
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9EQF6"
SQ SEQUENCE 564 AA; 61540 MW; E078B9002F54975E CRC64;
MLANSASVRI LIKGGKVVND DCTHEADVYI ENGIIQQVGR ELMIPGGAKV IDATGKLVIP
GGIDTSTHFH QTFMNATCVD DFYHGTKAAL VGGTTMIIGH VLPDKETSLV EAYEKCRALA
DPKVCCDYAL HVGITWWAPK VKAEMETLVR EKGVNSFQMF MTYKDLYMLR DSELYQVFHA
CRDFGAIPRV 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 PYLGDVAVVV NPGKKEMGTP LADTPTRPVT RHGGMRDLHE SSFSLSGSQI
DDHVPKRASA RILAPPGGRS SGIW
