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A2AS89 (SPEB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Agmatinase, mitochondrial

EC=3.5.3.11
Alternative name(s):
Agmatine ureohydrolase
Short name=AUH
Gene names
Name:Agmat
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length358 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Agmatine + H2O = putrescine + urea. Ref.4

Cofactor

Manganese Potential.

Pathway

Amine and polyamine biosynthesis; putrescine biosynthesis via agmatine pathway; putrescine from agmatine: step 1/1.

Subcellular location

Mitochondrion By similarity.

Tissue specificity

Detected only in liver. Ref.3

Sequence similarities

Belongs to the arginase family. Agmatinase subfamily.

Caution

May have little or no activity due to the lack of several residues essential for manganese binding and catalytic activity (Ref.4).

Ontologies

Keywords
   Biological processPutrescine biosynthesis
Spermidine biosynthesis
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandManganese
Metal-binding
   Molecular functionHydrolase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processputrescine biosynthetic process from arginine

Inferred from electronic annotation. Source: UniProtKB-UniPathway

spermidine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionagmatinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3636Mitochondrion Potential
Chain37 – 358322Agmatinase, mitochondrial
PRO_0000320072

Sites

Metal binding1681Manganese 1 By similarity
Metal binding1931Manganese 2 By similarity
Metal binding2841Manganese 2 By similarity

Amino acid modifications

Modified residue1991N6-acetyllysine Ref.6
Modified residue2231N6-acetyllysine; alternate Ref.6
Modified residue2231N6-succinyllysine; alternate Ref.5

Experimental info

Sequence conflict1451L → R in AAI15694. Ref.2

Sequences

Sequence LengthMass (Da)Tools
A2AS89 [UniParc].

Last modified February 20, 2007. Version 1.
Checksum: C98ED338165794B0

FASTA35838,255
        10         20         30         40         50         60 
MLRLLRSSWA RGLGSGVATW RPSAGLFRPG CPGIRQASGA SDTPHHQSPS SESPVQPVGV 

        70         80         90        100        110        120 
GVCSMMRLPL QSSPEGLDAA FIGVPLDTGT SNRPGARFGP CRIREESLML GAVNPSTGAL 

       130        140        150        160        170        180 
PFQSLRVADL GNVNVNLYNL QDSCLLIREA YQNVLAAGCI PLTLGGDQTI TYPILQAVAK 

       190        200        210        220        230        240 
EHGPVGLVHV GAHTNTTDKP REEKVYHRTP FRRSVDEGLL DSKRVVQIGI RGSSRTLDPY 

       250        260        270        280        290        300 
RYSRSQGFRV VLAEDCWMKS LVPLMAEVRQ QMGGKPLYIS FAIDALDPAY APGTGTPEIA 

       310        320        330        340        350 
GLTPSQALEI IRGCQGLNVV GCDLVEVSPP YDLSGNTALL AANLLFEMLC ALPKVTTV 

« Hide

References

« Hide 'large scale' references
[1]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"Cloning and characterization of human agmatinase."
Iyer R.K., Kim H.K., Tsoa R.W., Grody W.W., Cederbaum S.D.
Mol. Genet. Metab. 75:209-218(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[4]"Vertebrate agmatinases: what role do they play in agmatine catabolism?"
Morris S.M. Jr.
Ann. N. Y. Acad. Sci. 1009:30-33(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: POTENTIAL LACK OF CATALYTIC ACTIVITY.
[5]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-223, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[6]"Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-199 AND LYS-223, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL928577 Genomic DNA. Translation: CAM23129.1.
BC115693 mRNA. Translation: AAI15694.1.
RefSeqNP_001074877.1. NM_001081408.1.
UniGeneMm.30032.

3D structure databases

ProteinModelPortalA2AS89.
SMRA2AS89. Positions 61-355.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteA2AS89.

Proteomic databases

PaxDbA2AS89.
PRIDEA2AS89.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000038161; ENSMUSP00000040853; ENSMUSG00000040706.
GeneID75986.
KEGGmmu:75986.
UCSCuc008vpe.1. mouse.

Organism-specific databases

CTD79814.
MGIMGI:1923236. Agmat.

Phylogenomic databases

eggNOGCOG0010.
GeneTreeENSGT00530000063082.
HOGENOMHOG000204320.
HOVERGENHBG023165.
InParanoidA2AS89.
KOK01480.
OMAKPDYSLY.
OrthoDBEOG7M98GH.
PhylomeDBA2AS89.
TreeFamTF328612.

Enzyme and pathway databases

UniPathwayUPA00534; UER00287.

Gene expression databases

ArrayExpressA2AS89.
BgeeA2AS89.
CleanExMM_AGMAT.
GenevestigatorA2AS89.

Family and domain databases

Gene3D3.40.800.10. 1 hit.
InterProIPR005925. Agmatinase-rel.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
[Graphical view]
PANTHERPTHR11358. PTHR11358. 1 hit.
PfamPF00491. Arginase. 1 hit.
[Graphical view]
PIRSFPIRSF036979. Arginase. 1 hit.
PRINTSPR00116. ARGINASE.
TIGRFAMsTIGR01230. agmatinase. 1 hit.
PROSITEPS51409. ARGINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio344385.
PROA2AS89.
SOURCESearch...

Entry information

Entry nameSPEB_MOUSE
AccessionPrimary (citable) accession number: A2AS89
Secondary accession number(s): Q14BN7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: February 20, 2007
Last modified: April 16, 2014
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot