A2AS89 (SPEB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Agmatinase, mitochondrial
EC=3.5.3.11

Alternative name(s):
Agmatine ureohydrolase
Short name=AUH

Gene names

Name:

Agmat

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	358 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Catalytic activity	Agmatine + H2O = putrescine + urea.
Cofactor	Manganese Potential.
Pathway	Amine and polyamine biosynthesis; putrescine biosynthesis via agmatine pathway; putrescine from agmatine: step 1/1.
Subcellular location	Mitochondrion By similarity.
Sequence similarities	Belongs to the arginase family. Agmatinase subfamily.

Ontologies

Keywords
Biological process	Putrescine biosynthesis Spermidine biosynthesis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Manganese Metal-binding
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	putrescine biosynthetic process from arginine Inferred from electronic annotation. Source: UniProtKB-UniPathway spermidine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	agmatinase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Mitochondrion Potential
	Chain	? – 358		Agmatinase, mitochondrial		PRO_0000320072
Sites
	Metal binding	168	1	Manganese 1 By similarity
	Metal binding	193	1	Manganese 2 By similarity
	Metal binding	284	1	Manganese 2 By similarity
Experimental info
	Sequence conflict	145	1	L → R in AAI15694. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	A2AS89 [UniParc]. Last modified February 20, 2007. Version 1. Checksum: C98ED338165794B0	FASTA	358	38,255
	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

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. , 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].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL928577 Genomic DNA. Translation: CAM23129.1. BC115693 mRNA. Translation: AAI15694.1.
IPI	IPI00110843.
RefSeq	NP_001074877.1. NM_001081408.1.
UniGene	Mm.30032.
3D structure databases
ProteinModelPortal	A2AS89.
SMR	A2AS89. Positions 61-355.
ModBase	Search...
PTM databases
PhosphoSite	A2AS89.
Proteomic databases
PaxDb	A2AS89.
PRIDE	A2AS89.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000038161; ENSMUSP00000040853; ENSMUSG00000040706.
GeneID	75986.
KEGG	mmu:75986.
UCSC	uc008vpe.1. mouse.
Organism-specific databases
CTD	79814.
MGI	MGI:1923236. Agmat.
Phylogenomic databases
eggNOG	COG0010.
GeneTree	ENSGT00530000063082.
HOGENOM	HOG000204320.
HOVERGEN	HBG023165.
InParanoid	A2AS89.
KO	K01480.
OMA	PFDNTSS.
OrthoDB	EOG43R3MX.
Enzyme and pathway databases
UniPathway	UPA00534; UER00287.
Gene expression databases
ArrayExpress	A2AS89.
Bgee	A2AS89.
CleanEx	MM_AGMAT.
Genevestigator	A2AS89.
Family and domain databases
Gene3D	3.40.800.10. 1 hit.
InterPro	IPR005925. Agmatinase-rel. IPR006035. Ureohydrolase. IPR023696. Ureohydrolase_domain. [Graphical view]
PANTHER	PTHR11358. PTHR11358. 1 hit.
Pfam	PF00491. Arginase. 1 hit. [Graphical view]
PIRSF	PIRSF036979. Arginase. 1 hit.
PRINTS	PR00116. ARGINASE.
TIGRFAMs	TIGR01230. agmatinase. 1 hit.
PROSITE	PS01053. ARGINASE_1. False negative. PS51409. ARGINASE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	344385.
SOURCE	Search...

Entry information

Entry name

SPEB_MOUSE

Accession

Primary (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 3, 2013
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program