DDAH2_MOUSE
ID DDAH2_MOUSE Reviewed; 285 AA.
AC Q99LD8;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=N(G),N(G)-dimethylarginine dimethylaminohydrolase 2;
DE Short=DDAH-2;
DE Short=Dimethylarginine dimethylaminohydrolase 2;
DE EC=3.5.3.18;
DE AltName: Full=DDAHII;
DE AltName: Full=Dimethylargininase-2;
GN Name=Ddah2;
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 [LARGE SCALE MRNA].
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 [2]
RP PROTEIN SEQUENCE OF 183-194, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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).
CC -!- FUNCTION: Hydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-
CC monomethyl-L-arginine (MMA) which act as inhibitors of NOS. Has
CC therefore a role in the regulation of nitric oxide generation (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(omega),N(omega)-dimethyl-L-arginine = dimethylamine +
CC L-citrulline; Xref=Rhea:RHEA:17305, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57743, ChEBI:CHEBI:58040, ChEBI:CHEBI:58326; EC=3.5.3.18;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Mitochondrion
CC {ECO:0000250}. Note=Translocates from cytosol to mitochondrion upon IL-
CC 1beta stimulation in chondrocytes. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DDAH family. {ECO:0000305}.
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DR EMBL; BC003328; AAH03328.1; -; mRNA.
DR CCDS; CCDS50082.1; -.
DR RefSeq; NP_001177378.1; NM_001190449.1.
DR RefSeq; XP_006524675.1; XM_006524612.3.
DR AlphaFoldDB; Q99LD8; -.
DR SMR; Q99LD8; -.
DR BioGRID; 206177; 4.
DR STRING; 10090.ENSMUSP00000007255; -.
DR iPTMnet; Q99LD8; -.
DR PhosphoSitePlus; Q99LD8; -.
DR REPRODUCTION-2DPAGE; IPI00336881; -.
DR UCD-2DPAGE; Q99LD8; -.
DR EPD; Q99LD8; -.
DR jPOST; Q99LD8; -.
DR MaxQB; Q99LD8; -.
DR PaxDb; Q99LD8; -.
DR PeptideAtlas; Q99LD8; -.
DR PRIDE; Q99LD8; -.
DR ProteomicsDB; 279609; -.
DR Antibodypedia; 27580; 277 antibodies from 34 providers.
DR DNASU; 51793; -.
DR Ensembl; ENSMUST00000007255; ENSMUSP00000007255; ENSMUSG00000007039.
DR GeneID; 51793; -.
DR KEGG; mmu:51793; -.
DR UCSC; uc008cfi.2; mouse.
DR CTD; 23564; -.
DR MGI; MGI:1859016; Ddah2.
DR VEuPathDB; HostDB:ENSMUSG00000007039; -.
DR eggNOG; ENOG502QW4J; Eukaryota.
DR GeneTree; ENSGT00940000160769; -.
DR InParanoid; Q99LD8; -.
DR OMA; CPYGRFT; -.
DR OrthoDB; 1469762at2759; -.
DR PhylomeDB; Q99LD8; -.
DR TreeFam; TF314737; -.
DR BRENDA; 3.5.3.18; 3474.
DR Reactome; R-MMU-203615; eNOS activation.
DR BioGRID-ORCS; 51793; 5 hits in 72 CRISPR screens.
DR PRO; PR:Q99LD8; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q99LD8; protein.
DR Bgee; ENSMUSG00000007039; Expressed in ventricular zone and 229 other tissues.
DR ExpressionAtlas; Q99LD8; baseline and differential.
DR Genevisible; Q99LD8; MM.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0016597; F:amino acid binding; ISO:MGI.
DR GO; GO:0016403; F:dimethylargininase activity; ISS:UniProtKB.
DR GO; GO:0006527; P:arginine catabolic process; ISA:MGI.
DR GO; GO:0006525; P:arginine metabolic process; ISO:MGI.
DR GO; GO:0000052; P:citrulline metabolic process; ISS:UniProtKB.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IBA:GO_Central.
DR InterPro; IPR033199; DDAH.
DR InterPro; IPR033202; DDAH2.
DR PANTHER; PTHR12737; PTHR12737; 1.
DR PANTHER; PTHR12737:SF16; PTHR12737:SF16; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Hydrolase; Mitochondrion;
KW Reference proteome.
FT CHAIN 1..285
FT /note="N(G),N(G)-dimethylarginine dimethylaminohydrolase 2"
FT /id="PRO_0000171122"
FT ACT_SITE 171
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 276
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
SQ SEQUENCE 285 AA; 29646 MW; 3795D0BA2D314EE5 CRC64;
MGTPGEGLGR CSHALIRGVP ESLASGEGAG AGLPALDLAK AQREHGVLGG KLRQRLGLQL
LELPPEESLP LGPLLGDTAV IQGDTALITR PWSPARRPEV DGVRKALQDL GLRIVEMGDE
NATLDGTDVL FTGREFFVGL SKWTNHRGAE IVADTFRDFA VSTVPVSGSS HLRGLCGMGG
PRTVVAGSSE AAQKAVRAMA ALTDHPYASL TLPDDAASDC LFLRPGLPGA TPFLLHRGGG
DLPNSQEALQ KLSDVTLVPV SCSELEKAGA GLSSLCLVLS TRPHC
