Reviewed, UniProtKB/Swiss-Prot Q86W34 (AMZ2_HUMAN)

Names and origin

Protein names

Recommended name:
    Archaemetzincin-2
    EC=3.-.-.-
Alternative name(s):
    Archeobacterial metalloproteinase-like protein 2

Gene names

Name:	AMZ2
ORF Names:	BM-014

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	360 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Zinc metalloprotease. Exhibits activity against angiotensin-3 in vitro. Does not hydrolyze either neurogranin or angiotensin-2. Ref.1
Enzyme regulation	Inhibited by the general metalloprotease inhibitors o-phenanthroline and batimastat. Also significantly inhibited by amastatin, which is an inhibitor of aminopeptidases. Not inhibited by 4-(2-aminoethyl)-benzenesulfonyl fluoride, E-64, and TIMPS (tissue inhibitors of metalloproteinases), which are inhibitors of serine, cysteine, and matrix metalloproteases, respectively. Ref.1
Tissue specificity	Predominantly expressed in heart and testis. Also expressed at lower levels in kidney, liver, pancreas, lung, brain and placenta. Expressed in fetal tissues such as kidney, liver, lung and brain. Ref.1
Sequence similarities	Belongs to the peptidase M54 family.
Biophysicochemical properties	pH dependence: Optimum pH is 7.0.
Sequence caution	The sequence AAF64270.1 differs from that shown. Reason: Erroneous termination at position 98. Translated as Gly. The sequence AAF64270.1 differs from that shown. Reason: Frameshift at position 55.

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
Technical term	Complete proteome
Gene Ontology (GO)
Molecular function	metallopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW zinc 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
	Chain	1 – 360	360	Archaemetzincin-2		PRO_0000159617
Sites
	Active site	255	1	By similarity
	Metal binding	254	1	Zinc; catalytic By similarity
	Metal binding	258	1	Zinc; catalytic By similarity
	Metal binding	265	1	Zinc; catalytic Potential
Natural variations
	Natural variant	30	1	D → N: dbSNP rs3213690. Ref.4		VAR_024850
	Natural variant	146	1	H → Q: dbSNP rs3207194.		VAR_047343
Experimental info
	Sequence conflict	4	1	I → V in AAF64270. Ref.2
	Sequence conflict	6	1	H → Y in AAF64270. Ref.2
	Sequence conflict	13	1	T → I in AAF64270. Ref.2
	Sequence conflict	15	1	L → V in AAF64270. Ref.2
	Sequence conflict	29	1	L → V in AAF64270. Ref.2
	Sequence conflict	51 – 52	2	IT → CI in AAF64270. Ref.2
	Sequence conflict	76	1	D → H in AAF64270. Ref.2
	Sequence conflict	81	1	T → I in AAF64270. Ref.2
	Sequence conflict	85	1	N → D in AAF64270. Ref.2
	Sequence conflict	92	1	Q → R in AAF64270. Ref.2
	Sequence conflict	99	1	N → S in AAF64270. Ref.2
	Sequence conflict	121	1	G → R in AAF64270. Ref.2
	Sequence conflict	207	1	S → G in AAF64270. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q86W34-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: D063B77B852F39DD	FASTA	360	41,264
	10 20 30 40 50 60 MQIIRHSEQT LKTALISKNP VLVSQYEKLD AGEQRLMNEA FQPASDLFGP ITLHSPSDWI 70 80 90 100 110 120 TSHPEAPQDF EQFFSDPYRK TPSPNKRSIY IQSIGSLGNT RIISEEYIKW LTGYCKAYFY 130 140 150 160 170 180 GLRVKLLEPV PVSVTRCSFR VNENTHNLQI HAGDILKFLK KKKPEDAFCV VGITMIDLYP 190 200 210 220 230 240 RDSWNFVFGQ ASLTDGVGIF SFARYGSDFY SMHYKGKVKK LKKTSSSDYS IFDNYYIPEI 250 260 270 280 290 300 TSVLLLRSCK TLTHEIGHIF GLRHCQWLAC LMQGSNHLEE ADRRPLNLCP ICLHKLQCAV 310 320 330 340 350 360 GFSIVERYKA LVRWIDDESS DTPGATPEHS HEDNGNLPKP VEAFKEWKEW IIKCLAVLQK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and characterization of human archaemetzincin-1 and - 2, two novel members of a family of metalloproteases widely distributed in Archaea." Diaz-Perales A., Quesada V., Peinado J.R., Ugalde A.P., Alvarez J., Suarez M.F., Gomis-Rueth X., Lopez-Otin C. J. Biol. Chem. 280:30367-30375(2005) [PubMed: 15972818] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, TISSUE SPECIFICITY.
[2]	"Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells." Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X. , Gu J., Chen S.-J., Chen Z. Genome Res. 10:1546-1560(2000) [PubMed: 11042152] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Umbilical cord blood.
[3]	"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]. Tissue: Amygdala and Thymus.
[4]	"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage." Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C. Nature 440:1045-1049(2006) [PubMed: 16625196] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ASN-30.
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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]. Tissue: Bone marrow and Lung.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ635358 mRNA. Translation: CAG25750.1. AF208856 mRNA. Translation: AAF64270.1. Sequence problems. AK126146 mRNA. Translation: BAC86462.1. AK090981 mRNA. Translation: BAG52256.1. AC005332 Genomic DNA. No translation available. CH471099 Genomic DNA. Translation: EAW89050.1. BC050709 mRNA. Translation: AAH50709.1. BC056271 mRNA. Translation: AAH56271.1.
IPI	IPI00010239.
RefSeq	NP_001028746.1. NP_057711.3.
UniGene	Hs.293560
3D structure databases
ModBase	Search...
Protein family/group databases
MEROPS	M54.002.
Proteomic databases
PRIDE	Q86W34.
Genome annotation databases
Ensembl	ENST00000359904; ENSP00000352976; ENSG00000196704; Homo sapiens. [Genome view] ENST00000392720; ENSP00000376481; ENSG00000196704; Homo sapiens. [Genome view] ENST00000402427; ENSP00000384754; ENSG00000196704; Homo sapiens. [Genome view] ENST00000440663; ENSP00000407874; ENSG00000196704; Homo sapiens. [Genome view] ENST00000445412; ENSP00000408432; ENSG00000196704; Homo sapiens. [Genome view] ENST00000455065; ENSP00000411470; ENSG00000196704; Homo sapiens. [Genome view]
GeneID	51321.
Organism-specific databases
CTD	51321.
GeneCards	GC17P063756.
H-InvDB	HIX0014113.
HGNC	HGNC:28041. AMZ2.
HPA	HPA023299.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q86W34.
HOVERGEN	Q86W34.
Gene expression databases
ArrayExpress	Q86W34.
Bgee	Q86W34.
CleanEx	HS_AMZ2.
Genevestigator	Q86W34.
GermOnline	ENSG00000196704. Homo sapiens.
Family and domain databases
InterPro	IPR012962. Pept_M54_archaemetzncn. [Graphical view]
Pfam	PF07998. Peptidase_M54. 1 hit. [Graphical view]
PROSITE	PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	54701.

Entry information

Entry name

AMZ2_HUMAN

Accession

Primary (citable) accession number: Q86W34
Secondary accession number(s): B3KR44, Q5XKF1, Q9NZE2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 10, 2006
Last sequence update:	June 1, 2003
Last modified:	November 24, 2009
This is version 62 of the entry and version 1 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.