Reviewed, UniProtKB/Swiss-Prot Q9BSE5 (SPEB_HUMAN)

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

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	352 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein 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.
Tissue specificity	Highly expressed in liver and kidney. Also found in skeletal muscle, fetal liver, brain, testis, skin and the gastrointestinal tract. Ref.1
Sequence similarities	Belongs to the arginase family. Agmatinase subfamily.

Ontologies

Keywords
Biological process	Putrescine biosynthesis Spermidine biosynthesis
Cellular component	Mitochondrion
Coding sequence diversity	Polymorphism
Domain	Transit peptide
Ligand	Manganese Metal-binding
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	putrescine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW 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 manganese 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	? – 352		Agmatinase, mitochondrial		PRO_0000002089
Sites
	Metal binding	162	1	Manganese 1 By similarity
	Metal binding	185	1	Manganese 1 By similarity
	Metal binding	185	1	Manganese 2 By similarity
	Metal binding	187	1	Manganese 2 By similarity
	Metal binding	189	1	Manganese 1 By similarity
	Metal binding	276	1	Manganese 1 By similarity
	Metal binding	276	1	Manganese 2 By similarity
	Metal binding	278	1	Manganese 2 By similarity
Natural variations
	Natural variant	105	1	G → R: dbSNP rs6429757. Ref.1 Ref.2 Ref.4		VAR_023485
	Natural variant	140	1	R → Q: dbSNP rs11580170. Ref.1		VAR_048332
Experimental info
	Sequence conflict	145	1	Y → C in BAB15633. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9BSE5-1 [UniParc]. Last modified February 20, 2007. Version 2. Checksum: 394738202353314A	FASTA	352	37,660
	10 20 30 40 50 60 MLRLLASGCA RGPGPGVGAR PAAGLFHPGR RQSRQASDAP RNQPPSPEFV ARPVGVCSMM 70 80 90 100 110 120 RLPVQTSPEG LDAAFIGVPL DTGTSNRPGA RFGPRRIREE SVMLGTVNPS TGALPFQSLM 130 140 150 160 170 180 VADLGDVNVN LYNLQDSCRR IQEAYEKIVA AGCIPLTLGG DHTITYPILQ AMAKKHGPVG 190 200 210 220 230 240 LLHVDAHTDT TDKALGEKLY HGAPFRRCVD EGLLDCKRVV QIGIRGSSTT LDPYRYNRSQ 250 260 270 280 290 300 GFRVVLAEDC WMKSLVPLMG EVRQQMGGKP IYISFDIDAL DPAYAPGTGT PEIAGLTPSQ 310 320 330 340 350 ALEIIRGCQG LNVMGCDLVE VSPPYDLSGN TALLAANLLF EMLCALPKVT TV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of human agmatinase. An alternate path for polyamine synthesis induced in liver by hepatitis B virus." Mistry S.K., Burwell T.J., Chambers R.M., Rudolph-Owen L., Spaltmann F., Cook W.J., Morris S.M. Jr. Am. J. Physiol. 282:G375-G381(2002) [PubMed: 11804860] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, VARIANTS ARG-105 AND GLN-140. Tissue: Kidney.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ARG-105.
[3]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ARG-105. Tissue: Ovary.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY057097 mRNA. Translation: AAL24446.1. AK027037 mRNA. Translation: BAB15633.1. AL121992 Genomic DNA. Translation: CAI22366.1. BC005090 mRNA. Translation: AAH05090.1.
IPI	IPI00305360.
RefSeq	NP_079034.3.
UniGene	Hs.567583
3D structure databases
SMR	Q9BSE5. Positions 54-348.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9BSE5.
PTM databases
PhosphoSite	Q9BSE5.
Proteomic databases
PeptideAtlas	Q9BSE5.
PRIDE	Q9BSE5.
Genome annotation databases
Ensembl	ENST00000375826; ENSP00000364986; ENSG00000116771; Homo sapiens. [Genome view]
GeneID	79814.
KEGG	hsa:79814.
NMPDR	fig|9606.3.peg.360.
UCSC	uc001awv.1. human.
Organism-specific databases
CTD	79814.
GeneCards	GC01M015772.
H-InvDB	HIX0000155.
HGNC	HGNC:18407. AGMAT.
HPA	HPA026443.
PharmGKB	PA24619.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG13125.
HOGENOM	HBG391953.
HOVERGEN	Q9BSE5.
InParanoid	Q9BSE5.
OMA	QDSCRLI.
OrthoDB	EOG9RNDVQ.
PhylomeDB	Q9BSE5.
Enzyme and pathway databases
BRENDA	3.5.3.11. 247.
Reactome	REACT_13. Metabolism of amino acids.
Gene expression databases
ArrayExpress	Q9BSE5.
Bgee	Q9BSE5.
CleanEx	HS_AGMAT.
Genevestigator	Q9BSE5.
GermOnline	ENSG00000116771. Homo sapiens.
Family and domain databases
InterPro	IPR005925. Agmatinase. IPR005924. Arginase. IPR006035. Ureohydrolase. IPR020855. Ureohydrolase_Mn_BS. [Graphical view]
Gene3D	G3DSA:3.40.800.10. Ureohydrolase. 1 hit.
PANTHER	PTHR11358. Ureohydrolase. 1 hit.
Pfam	PF00491. Arginase. 1 hit. [Graphical view]
PRINTS	PR00116. ARGINASE.
TIGRFAMs	TIGR01230. agmatinase. 1 hit.
PROSITE	PS01053. ARGINASE_1. 1 hit. PS51409. ARGINASE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	69414.

Entry information

Entry name

SPEB_HUMAN

Accession

Primary (citable) accession number: Q9BSE5
Secondary accession number(s): Q5TDH1, Q9H5J3

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 27, 2002
Last sequence update:	February 20, 2007
Last modified:	February 9, 2010
This is version 80 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.