ID   DDAH2_RAT               Reviewed;         285 AA.
AC   Q6MG60;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 119.
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   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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15060004; DOI=10.1101/gr.1987704;
RA   Hurt P., Walter L., Sudbrak R., Klages S., Mueller I., Shiina T., Inoko H.,
RA   Lehrach H., Guenther E., Reinhardt R., Himmelbauer H.;
RT   "The genomic sequence and comparative analysis of the rat major
RT   histocompatibility complex.";
RL   Genome Res. 14:631-639(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary, and Thymus;
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   PROTEIN SEQUENCE OF 106-142; 148-173; 183-194 AND 268-285, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
RA   Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U.;
RL   Submitted (JUL-2007) to UniProtKB.
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; BX883045; CAE83986.1; -; Genomic_DNA.
DR   EMBL; BC086443; AAH86443.1; -; mRNA.
DR   EMBL; BC097930; AAH97930.1; -; mRNA.
DR   RefSeq; NP_001159408.1; NM_001165936.1.
DR   RefSeq; NP_997697.1; NM_212532.2.
DR   AlphaFoldDB; Q6MG60; -.
DR   SMR; Q6MG60; -.
DR   BioGRID; 254630; 1.
DR   IntAct; Q6MG60; 1.
DR   STRING; 10116.ENSRNOP00000001118; -.
DR   iPTMnet; Q6MG60; -.
DR   PhosphoSitePlus; Q6MG60; -.
DR   SwissPalm; Q6MG60; -.
DR   jPOST; Q6MG60; -.
DR   PaxDb; Q6MG60; -.
DR   PRIDE; Q6MG60; -.
DR   Ensembl; ENSRNOT00000088251; ENSRNOP00000069121; ENSRNOG00000000842.
DR   GeneID; 294239; -.
DR   KEGG; rno:294239; -.
DR   UCSC; RGD:1302955; rat.
DR   CTD; 23564; -.
DR   RGD; 1302955; Ddah2.
DR   VEuPathDB; HostDB:ENSRNOG00000029682; -.
DR   eggNOG; ENOG502QW4J; Eukaryota.
DR   GeneTree; ENSGT00940000160769; -.
DR   InParanoid; Q6MG60; -.
DR   OMA; CPYGRFT; -.
DR   OrthoDB; 1469762at2759; -.
DR   PhylomeDB; Q6MG60; -.
DR   TreeFam; TF314737; -.
DR   BRENDA; 3.5.3.18; 5301.
DR   Reactome; R-RNO-203615; eNOS activation.
DR   PRO; PR:Q6MG60; -.
DR   Proteomes; UP000002494; Chromosome 20.
DR   Bgee; ENSRNOG00000000842; Expressed in heart and 20 other tissues.
DR   Genevisible; Q6MG60; RN.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0016597; F:amino acid binding; IDA:RGD.
DR   GO; GO:0016403; F:dimethylargininase activity; IDA:RGD.
DR   GO; GO:0006527; P:arginine catabolic process; IEA:InterPro.
DR   GO; GO:0006525; P:arginine metabolic process; IDA:RGD.
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_0000270760"
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;  29688 MW;  C28D60FF20CEAEFF CRC64;
     MGTPGEGLGR CSHALIRGVP ESLASGEGAG AGLPALDLAK AQREHGVLGG KLRQRLGLQL
     LELPPEESLP LGPLLGDTAV IQGDTALITR PWSPARRPEV DGVRKALQDL GLRIVEMGDE
     NATLDGTDVL FTGREFFVGL SKWTNHRGAE IVADTFRDFA VSTVPVSGAS HLRGLCGMGG
     PRTVVAGSSE AAQKAVRAMA ALTDHPYASL TLPDDAASDC LFLRPGLPGT TPFLLHRGGG
     DLPNSQEALQ KLSDVTLVPV SCSELEKVGA GLSSLCLVLS TRPHC