SPEB_MOUSE
ID SPEB_MOUSE Reviewed; 358 AA.
AC A2AS89; Q14BN7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Agmatinase, mitochondrial;
DE EC=3.5.3.11 {ECO:0000250|UniProtKB:Q9BSE5};
DE AltName: Full=Agmatine ureohydrolase;
DE Short=AUH;
DE Flags: Precursor;
GN Name=Agmat;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
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 [3]
RP TISSUE SPECIFICITY.
RX PubMed=11914032; DOI=10.1006/mgme.2001.3277;
RA Iyer R.K., Kim H.K., Tsoa R.W., Grody W.W., Cederbaum S.D.;
RT "Cloning and characterization of human agmatinase.";
RL Mol. Genet. Metab. 75:209-218(2002).
RN [4]
RP POTENTIAL LACK OF CATALYTIC ACTIVITY.
RX PubMed=15028567; DOI=10.1196/annals.1304.003;
RA Morris S.M. Jr.;
RT "Vertebrate agmatinases: what role do they play in agmatine catabolism?";
RL Ann. N. Y. Acad. Sci. 1009:30-33(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
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).
RN [6]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-223, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-199 AND LYS-223, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=agmatine + H2O = putrescine + urea; Xref=Rhea:RHEA:13929,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:58145,
CC ChEBI:CHEBI:326268; EC=3.5.3.11;
CC Evidence={ECO:0000250|UniProtKB:Q9BSE5};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00742};
CC -!- PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis via
CC agmatine pathway; putrescine from agmatine: step 1/1.
CC {ECO:0000250|UniProtKB:Q9BSE5}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected only in liver.
CC {ECO:0000269|PubMed:11914032}.
CC -!- SIMILARITY: Belongs to the arginase family. Agmatinase subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00742}.
CC -!- CAUTION: May have little or no activity due to the lack of several
CC residues essential for manganese binding and catalytic activity.
CC {ECO:0000305|PubMed:15028567}.
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DR EMBL; AL928577; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC115693; AAI15694.1; -; mRNA.
DR CCDS; CCDS38941.1; -.
DR RefSeq; NP_001074877.1; NM_001081408.1.
DR AlphaFoldDB; A2AS89; -.
DR SMR; A2AS89; -.
DR STRING; 10090.ENSMUSP00000040853; -.
DR iPTMnet; A2AS89; -.
DR PhosphoSitePlus; A2AS89; -.
DR SwissPalm; A2AS89; -.
DR jPOST; A2AS89; -.
DR MaxQB; A2AS89; -.
DR PaxDb; A2AS89; -.
DR PeptideAtlas; A2AS89; -.
DR PRIDE; A2AS89; -.
DR ProteomicsDB; 261568; -.
DR Antibodypedia; 14379; 93 antibodies from 20 providers.
DR Ensembl; ENSMUST00000038161; ENSMUSP00000040853; ENSMUSG00000040706.
DR GeneID; 75986; -.
DR KEGG; mmu:75986; -.
DR UCSC; uc008vpe.1; mouse.
DR CTD; 79814; -.
DR MGI; MGI:1923236; Agmat.
DR VEuPathDB; HostDB:ENSMUSG00000040706; -.
DR eggNOG; KOG2964; Eukaryota.
DR GeneTree; ENSGT00950000183195; -.
DR HOGENOM; CLU_039478_0_0_1; -.
DR InParanoid; A2AS89; -.
DR OMA; YELTTIM; -.
DR OrthoDB; 921352at2759; -.
DR PhylomeDB; A2AS89; -.
DR TreeFam; TF328612; -.
DR Reactome; R-MMU-351143; Agmatine biosynthesis.
DR UniPathway; UPA00534; UER00287.
DR BioGRID-ORCS; 75986; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Agmat; mouse.
DR PRO; PR:A2AS89; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; A2AS89; protein.
DR Bgee; ENSMUSG00000040706; Expressed in left lobe of liver and 94 other tissues.
DR Genevisible; A2AS89; MM.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0008783; F:agmatinase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0033389; P:putrescine biosynthetic process from arginine, using agmatinase; IBA:GO_Central.
DR GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR005925; Agmatinase-rel.
DR InterPro; IPR006035; Ureohydrolase.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR11358; PTHR11358; 1.
DR Pfam; PF00491; Arginase; 1.
DR PIRSF; PIRSF036979; Arginase; 1.
DR PRINTS; PR00116; ARGINASE.
DR SUPFAM; SSF52768; SSF52768; 1.
DR TIGRFAMs; TIGR01230; agmatinase; 1.
DR PROSITE; PS51409; ARGINASE_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Hydrolase; Manganese; Metal-binding; Mitochondrion;
KW Putrescine biosynthesis; Reference proteome; Spermidine biosynthesis;
KW Transit peptide.
FT TRANSIT 1..36
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 37..358
FT /note="Agmatinase, mitochondrial"
FT /id="PRO_0000320072"
FT REGION 31..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 168
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 193
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 284
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT MOD_RES 199
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 223
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 223
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 145
FT /note="L -> R (in Ref. 2; AAI15694)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 358 AA; 38255 MW; C98ED338165794B0 CRC64;
MLRLLRSSWA RGLGSGVATW RPSAGLFRPG CPGIRQASGA SDTPHHQSPS SESPVQPVGV
GVCSMMRLPL QSSPEGLDAA FIGVPLDTGT SNRPGARFGP CRIREESLML GAVNPSTGAL
PFQSLRVADL GNVNVNLYNL QDSCLLIREA YQNVLAAGCI PLTLGGDQTI TYPILQAVAK
EHGPVGLVHV GAHTNTTDKP REEKVYHRTP FRRSVDEGLL DSKRVVQIGI RGSSRTLDPY
RYSRSQGFRV VLAEDCWMKS LVPLMAEVRQ QMGGKPLYIS FAIDALDPAY APGTGTPEIA
GLTPSQALEI IRGCQGLNVV GCDLVEVSPP YDLSGNTALL AANLLFEMLC ALPKVTTV
