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DPYL2_PONAB
ID   DPYL2_PONAB             Reviewed;         572 AA.
AC   Q5R9Y6;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=Dihydropyrimidinase-related protein 2;
DE            Short=DRP-2;
GN   Name=DPYSL2;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
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 by DYRK2 at Ser-522 is required for subsequent
CC       phosphorylation by GSK3B. Phosphorylation at Thr-514 by GSK3B abolishes
CC       tubulin-binding leading to destabilization of microtubule assembly in
CC       axons and neurodegeneration (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; CR859244; CAH91424.1; -; mRNA.
DR   RefSeq; NP_001125834.1; NM_001132362.1.
DR   AlphaFoldDB; Q5R9Y6; -.
DR   SMR; Q5R9Y6; -.
DR   STRING; 9601.ENSPPYP00000020686; -.
DR   MEROPS; M38.975; -.
DR   Ensembl; ENSPPYT00000021515; ENSPPYP00000020686; ENSPPYG00000018458.
DR   GeneID; 100172763; -.
DR   KEGG; pon:100172763; -.
DR   CTD; 1808; -.
DR   eggNOG; KOG2584; Eukaryota.
DR   GeneTree; ENSGT01030000234527; -.
DR   HOGENOM; CLU_015572_2_2_1; -.
DR   InParanoid; Q5R9Y6; -.
DR   OMA; FTHRENF; -.
DR   OrthoDB; 719800at2759; -.
DR   TreeFam; TF314706; -.
DR   Proteomes; UP000001595; Chromosome 8.
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   2: Evidence at transcript level;
KW   Cytoplasm; Cytoskeleton; Developmental protein; Differentiation; Membrane;
KW   Methylation; Neurogenesis; Phosphoprotein; Reference proteome;
KW   S-nitrosylation.
FT   CHAIN           1..572
FT                   /note="Dihydropyrimidinase-related protein 2"
FT                   /id="PRO_0000284994"
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:0000250|UniProtKB:O02675"
FT   MOD_RES         565
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:O08553"
SQ   SEQUENCE   572 AA;  62294 MW;  5CDB6CF7F5C308AD CRC64;
     MSYQGKKNIP RITSDRLLIK GGKIVNDDQS FYADIYMEDG LIKQIGENLI VPGGVKTIEA
     HSRMVIPGGI DVHTRFQMPD QGMTSADDFF QGTKAALAGG TTMIIDHVVP EPGTSLLAAF
     DQWREWADSK SCCDYSLHVD ISEWHKGIQE EMEALVKDHG VNSFLVYMAF KDRFQLTDCQ
     IYEVLSVIRD IGAIAQVHAE NGDIIAEEQQ RILDLGITGP EGHVLSRPEE VEAEAVNRAI
     TIANQTNCPL YITKVMSKSS 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
 
 
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