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A2AS89

- SPEB_MOUSE

UniProt

A2AS89 - SPEB_MOUSE

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Protein

Agmatinase, mitochondrial

Gene

Agmat

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

Agmatine + H2O = putrescine + urea.

Cofactori

Manganese.PROSITE-ProRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi168 – 1681Manganese 1PROSITE-ProRule annotation
Metal bindingi193 – 1931Manganese 2PROSITE-ProRule annotation
Metal bindingi284 – 2841Manganese 2PROSITE-ProRule annotation

GO - Molecular functioni

  1. agmatinase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. putrescine biosynthetic process from arginine Source: UniProtKB-UniPathway
  2. spermidine biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Putrescine biosynthesis, Spermidine biosynthesis

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00534; UER00287.

Names & Taxonomyi

Protein namesi
Recommended name:
Agmatinase, mitochondrial (EC:3.5.3.11)
Alternative name(s):
Agmatine ureohydrolase
Short name:
AUH
Gene namesi
Name:Agmat
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:1923236. Agmat.

Subcellular locationi

Mitochondrion By similarity

GO - Cellular componenti

  1. extracellular vesicular exosome Source: Ensembl
  2. mitochondrion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3636MitochondrionSequence AnalysisAdd
BLAST
Chaini37 – 358322Agmatinase, mitochondrialPRO_0000320072Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei199 – 1991N6-acetyllysine1 Publication
Modified residuei223 – 2231N6-acetyllysine; alternate1 Publication
Modified residuei223 – 2231N6-succinyllysine; alternate1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiA2AS89.
PaxDbiA2AS89.
PRIDEiA2AS89.

PTM databases

PhosphoSiteiA2AS89.

Expressioni

Tissue specificityi

Detected only in liver.1 Publication

Gene expression databases

BgeeiA2AS89.
CleanExiMM_AGMAT.
ExpressionAtlasiA2AS89. baseline and differential.
GenevestigatoriA2AS89.

Structurei

3D structure databases

ProteinModelPortaliA2AS89.
SMRiA2AS89. Positions 61-355.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the arginase family. Agmatinase subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0010.
GeneTreeiENSGT00530000063082.
HOGENOMiHOG000204320.
HOVERGENiHBG023165.
InParanoidiA2AS89.
KOiK01480.
OMAiERETHGT.
OrthoDBiEOG7M98GH.
PhylomeDBiA2AS89.
TreeFamiTF328612.

Family and domain databases

Gene3Di3.40.800.10. 1 hit.
InterProiIPR005925. Agmatinase-rel.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
[Graphical view]
PANTHERiPTHR11358. PTHR11358. 1 hit.
PfamiPF00491. Arginase. 1 hit.
[Graphical view]
PIRSFiPIRSF036979. Arginase. 1 hit.
PRINTSiPR00116. ARGINASE.
TIGRFAMsiTIGR01230. agmatinase. 1 hit.
PROSITEiPS51409. ARGINASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

A2AS89-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLRLLRSSWA RGLGSGVATW RPSAGLFRPG CPGIRQASGA SDTPHHQSPS
60 70 80 90 100
SESPVQPVGV GVCSMMRLPL QSSPEGLDAA FIGVPLDTGT SNRPGARFGP
110 120 130 140 150
CRIREESLML GAVNPSTGAL PFQSLRVADL GNVNVNLYNL QDSCLLIREA
160 170 180 190 200
YQNVLAAGCI PLTLGGDQTI TYPILQAVAK EHGPVGLVHV GAHTNTTDKP
210 220 230 240 250
REEKVYHRTP FRRSVDEGLL DSKRVVQIGI RGSSRTLDPY RYSRSQGFRV
260 270 280 290 300
VLAEDCWMKS LVPLMAEVRQ QMGGKPLYIS FAIDALDPAY APGTGTPEIA
310 320 330 340 350
GLTPSQALEI IRGCQGLNVV GCDLVEVSPP YDLSGNTALL AANLLFEMLC

ALPKVTTV
Length:358
Mass (Da):38,255
Last modified:February 20, 2007 - v1
Checksum:iC98ED338165794B0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti145 – 1451L → R in AAI15694. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL928577 Genomic DNA. Translation: CAM23129.1.
BC115693 mRNA. Translation: AAI15694.1.
CCDSiCCDS38941.1.
RefSeqiNP_001074877.1. NM_001081408.1.
UniGeneiMm.30032.

Genome annotation databases

EnsembliENSMUST00000038161; ENSMUSP00000040853; ENSMUSG00000040706.
GeneIDi75986.
KEGGimmu:75986.
UCSCiuc008vpe.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL928577 Genomic DNA. Translation: CAM23129.1 .
BC115693 mRNA. Translation: AAI15694.1 .
CCDSi CCDS38941.1.
RefSeqi NP_001074877.1. NM_001081408.1.
UniGenei Mm.30032.

3D structure databases

ProteinModelPortali A2AS89.
SMRi A2AS89. Positions 61-355.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei A2AS89.

Proteomic databases

MaxQBi A2AS89.
PaxDbi A2AS89.
PRIDEi A2AS89.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000038161 ; ENSMUSP00000040853 ; ENSMUSG00000040706 .
GeneIDi 75986.
KEGGi mmu:75986.
UCSCi uc008vpe.1. mouse.

Organism-specific databases

CTDi 79814.
MGIi MGI:1923236. Agmat.

Phylogenomic databases

eggNOGi COG0010.
GeneTreei ENSGT00530000063082.
HOGENOMi HOG000204320.
HOVERGENi HBG023165.
InParanoidi A2AS89.
KOi K01480.
OMAi ERETHGT.
OrthoDBi EOG7M98GH.
PhylomeDBi A2AS89.
TreeFami TF328612.

Enzyme and pathway databases

UniPathwayi UPA00534 ; UER00287 .

Miscellaneous databases

NextBioi 344385.
PROi A2AS89.
SOURCEi Search...

Gene expression databases

Bgeei A2AS89.
CleanExi MM_AGMAT.
ExpressionAtlasi A2AS89. baseline and differential.
Genevestigatori A2AS89.

Family and domain databases

Gene3Di 3.40.800.10. 1 hit.
InterProi IPR005925. Agmatinase-rel.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
[Graphical view ]
PANTHERi PTHR11358. PTHR11358. 1 hit.
Pfami PF00491. Arginase. 1 hit.
[Graphical view ]
PIRSFi PIRSF036979. Arginase. 1 hit.
PRINTSi PR00116. ARGINASE.
TIGRFAMsi TIGR01230. agmatinase. 1 hit.
PROSITEi PS51409. ARGINASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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. 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.

Entry informationi

Entry nameiSPEB_MOUSE
AccessioniPrimary (citable) accession number: A2AS89
Secondary accession number(s): Q14BN7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: February 20, 2007
Last modified: October 29, 2014
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

May have little or no activity due to the lack of several residues essential for manganese binding and catalytic activity.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3