DPYL2_BOVIN
ID DPYL2_BOVIN Reviewed; 572 AA.
AC O02675; Q29RI7;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Dihydropyrimidinase-related protein 2;
DE Short=DRP-2;
DE AltName: Full=Neural-specific protein NSP60;
GN Name=DPYSL2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Kamata T.K.;
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 548-565, AND PHOSPHORYLATION AT THR-555.
RX PubMed=10818093; DOI=10.1074/jbc.m001032200;
RA Arimura N., Inagaki N., Chihara K., Menager C., Nakamura N., Amano M.,
RA Iwamatsu A., Goshima Y., Kaibuchi K.;
RT "Phosphorylation of collapsin response mediator protein-2 by Rho-kinase.
RT Evidence for two separate signaling pathways for growth cone collapse.";
RL J. Biol. Chem. 275:23973-23980(2000).
RN [4]
RP INTERACTION WITH MICALL1.
RX PubMed=20801876; DOI=10.1074/jbc.c110.166066;
RA Rahajeng J., Giridharan S.S., Naslavsky N., Caplan S.;
RT "Collapsin response mediator protein-2 (Crmp2) regulates trafficking by
RT linking endocytic regulatory proteins to dynein motors.";
RL J. Biol. Chem. 285:31918-31922(2010).
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. May play a role in
CC endocytosis (By similarity). {ECO:0000250}.
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. Interacts with HTR4. Interacts with CLN6. Interacts with
CC MICALL1. {ECO:0000269|PubMed:20801876}.
CC -!- INTERACTION:
CC O02675; Q8N3F8: MICALL1; Xeno; NbExp=2; IntAct=EBI-8783505, EBI-1056885;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cytoplasm,
CC cytoskeleton {ECO:0000250}. Membrane {ECO:0000250}. Note=Tightly but
CC non-covalently associated with membranes. {ECO:0000250}.
CC -!- PTM: Phosphorylation at Thr-514 by GSK3B abolishes tubulin-binding
CC leading to destabilization of microtubule assembly in axons and
CC neurodegeneration. Phosphorylation by DYRK2 at Ser-522 is required for
CC subsequent phosphorylation by GSK3B (By similarity). {ECO:0000250}.
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; U83278; AAB80618.1; -; Genomic_DNA.
DR EMBL; BC114153; AAI14154.1; -; mRNA.
DR RefSeq; NP_001069468.1; NM_001076000.1.
DR RefSeq; XP_005210344.1; XM_005210287.2.
DR AlphaFoldDB; O02675; -.
DR SMR; O02675; -.
DR IntAct; O02675; 1.
DR STRING; 9913.ENSBTAP00000024448; -.
DR MEROPS; M38.975; -.
DR iPTMnet; O02675; -.
DR PaxDb; O02675; -.
DR PeptideAtlas; O02675; -.
DR PRIDE; O02675; -.
DR Ensembl; ENSBTAT00000024448; ENSBTAP00000024448; ENSBTAG00000018373.
DR GeneID; 533746; -.
DR KEGG; bta:533746; -.
DR CTD; 1808; -.
DR VEuPathDB; HostDB:ENSBTAG00000018373; -.
DR VGNC; VGNC:28195; DPYSL2.
DR eggNOG; KOG2584; Eukaryota.
DR GeneTree; ENSGT01030000234527; -.
DR HOGENOM; CLU_015572_2_2_1; -.
DR InParanoid; O02675; -.
DR OMA; FTHRENF; -.
DR OrthoDB; 719800at2759; -.
DR TreeFam; TF314706; -.
DR Proteomes; UP000009136; Chromosome 8.
DR Bgee; ENSBTAG00000018373; Expressed in prefrontal cortex and 105 other tissues.
DR ExpressionAtlas; O02675; baseline and differential.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; 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:0006897; P:endocytosis; 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 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Developmental protein; Differentiation;
KW Direct protein sequencing; Membrane; Methylation; Neurogenesis;
KW Phosphoprotein; Reference proteome; S-nitrosylation.
FT CHAIN 1..572
FT /note="Dihydropyrimidinase-related protein 2"
FT /id="PRO_0000165912"
FT REGION 512..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 32
FT /note="Phosphotyrosine; by FYN"
FT /evidence="ECO:0000250|UniProtKB:Q16555"
FT MOD_RES 258
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:O08553"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47942"
FT MOD_RES 431
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O08553"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08553"
FT MOD_RES 499
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O08553"
FT MOD_RES 504
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P47942"
FT MOD_RES 507
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08553"
FT MOD_RES 509
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q16555"
FT MOD_RES 512
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O08553"
FT MOD_RES 514
FT /note="Phosphothreonine; by GSK3-beta"
FT /evidence="ECO:0000250|UniProtKB:Q16555"
FT MOD_RES 517
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16555"
FT MOD_RES 518
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16555"
FT MOD_RES 521
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O08553"
FT MOD_RES 522
FT /note="Phosphoserine; by DYRK2"
FT /evidence="ECO:0000250|UniProtKB:Q16555"
FT MOD_RES 537
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08553"
FT MOD_RES 540
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08553"
FT MOD_RES 542
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08553"
FT MOD_RES 555
FT /note="Phosphothreonine; by ROCK2"
FT /evidence="ECO:0000269|PubMed:10818093"
FT MOD_RES 565
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:O08553"
SQ SEQUENCE 572 AA; 62278 MW; 343507ACB9D91BDE CRC64;
MSYQGKKNIP RITSDRLLIK GGKIVNDDQS FYADIYMEDG LIKQIGENLI VPGGVKTIEA
HSRMVIPGGI DVHTRFQMPD QGMTSADDFF QGTKAALAGG TTMIIDHVVP EPGTSLLAAF
DQWREWADSK SCCDYSLHVD ITEWHKGVQE EMEALVKDHG VNSFLVYMAF KDRFQLTDSQ
IYEVLSVIRD IGAIAQVHAE NGDIIAEEQQ RILDLGITGP EGHVLSRPEE VEAEAVNRSI
TIANQTNCPL YITKVMSKSA AEVIAQARKK GTVVYGEPIT ASLGTDGSHY WSKNWAKAAA
FVTSPPLSPD PTTPDFLNSL LSCGDLQVTG SAHCTFNTAQ KAVGKDNFTL IPEGTNGTEE
RMSVIWDKAV VTGKMDENQF VAVTSTNAAK VFNLYPRKGR IAVGSDADLV IWDPDSVKTI
SAKTHNSSLE YNIFEGMECR GSPLVVISQG KIVLEDGTLH VTEGSGRYIP RKPFPDFVYK
RIKARSRLAE LRGVPRGLYD GPVCEVSVTP KTVTPASSAK TSPAKQQAPP VRNLHQSGFS
LSGAQIDDNI PRRTTQRIVA PPGGRANITS LG
