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Q86W34 (AMZ2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Archaemetzincin-2

EC=3.4.-.-
Alternative name(s):
Archeobacterial metalloproteinase-like protein 2
Gene names
Name:AMZ2
ORF Names:BM-014
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length360 AA.
Sequence statusComplete.
Protein existenceEvidence 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

Cofactor

Binds 2 zinc ions per subunit. One is catalytic, whereas the other seems to have a structural role By similarity.

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. Down-regulated in testis from patients with maturation arrest (MA) or Sertoli cell-only syndrome (SCOS). Ref.1 Ref.7

Sequence similarities

Belongs to the peptidase M54 family.

Biophysicochemical properties

pH dependence:

Optimum pH is 7.0. Ref.1

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 diversityAlternative splicing
Polymorphism
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Molecular_functionmetallopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q86W34-4)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q86W34-5)

The sequence of this isoform differs from the canonical sequence as follows:
     96-153: Missing.
Note: Gene prediction based on EST data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 360360Archaemetzincin-2
PRO_0000159617

Sites

Active site2551Proton acceptor By similarity
Metal binding2541Zinc 1; catalytic; via tele nitrogen By similarity
Metal binding2581Zinc 1; catalytic; via tele nitrogen By similarity
Metal binding2641Zinc 1; catalytic; via tele nitrogen By similarity
Metal binding2651Zinc 2 By similarity
Metal binding2701Zinc 2 By similarity
Metal binding2891Zinc 2 By similarity
Metal binding2921Zinc 2 By similarity

Natural variations

Alternative sequence96 – 15358Missing in isoform 2.
VSP_047263
Natural variant301N → D. Ref.1 Ref.2 Ref.3 Ref.4 Ref.6
Corresponds to variant rs3213690 [ dbSNP | Ensembl ].
VAR_024850
Natural variant1461H → Q.
Corresponds to variant rs3207194 [ dbSNP | Ensembl ].
VAR_047343

Experimental info

Sequence conflict41I → V in AAF64270. Ref.2
Sequence conflict61H → Y in AAF64270. Ref.2
Sequence conflict131T → I in AAF64270. Ref.2
Sequence conflict151L → V in AAF64270. Ref.2
Sequence conflict291L → V in AAF64270. Ref.2
Sequence conflict51 – 522IT → CI in AAF64270. Ref.2
Sequence conflict761D → H in AAF64270. Ref.2
Sequence conflict811T → I in AAF64270. Ref.2
Sequence conflict851N → D in AAF64270. Ref.2
Sequence conflict921Q → R in AAF64270. Ref.2
Sequence conflict991N → S in AAF64270. Ref.2
Sequence conflict1211G → R in AAF64270. Ref.2
Sequence conflict2071S → G in AAF64270. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 11, 2011. Version 2.
Checksum: D74E7F7CE7873CBF

FASTA36041,263
        10         20         30         40         50         60 
MQIIRHSEQT LKTALISKNP VLVSQYEKLN 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 

« Hide

Isoform 2 [UniParc].

Checksum: 2AE9FB8B77CC8293
Show »

FASTA30234,595

References

« Hide '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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, TISSUE SPECIFICITY, VARIANT ASP-30.
[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. expand/collapse author list , Gu J., Chen S.-J., Chen Z.
Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ASP-30.
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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ASP-30.
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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ASP-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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ASP-30.
Tissue: Bone marrow and Lung.
[7]"Identification of ten novel genes involved in human spermatogenesis by microarray analysis of testicular tissue."
Lin Y.H., Lin Y.M., Teng Y.N., Hsieh T.Y., Lin Y.S., Kuo P.L.
Fertil. Steril. 86:1650-1658(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS11674.1. [Q86W34-4]
CCDS32714.1. [Q86W34-5]
RefSeqNP_001028741.1. NM_001033569.1. [Q86W34-4]
NP_001028742.1. NM_001033570.1. [Q86W34-4]
NP_001028743.1. NM_001033571.1. [Q86W34-4]
NP_001028744.1. NM_001033572.1. [Q86W34-4]
NP_001028746.1. NM_001033574.1. [Q86W34-5]
NP_001275983.1. NM_001289054.1. [Q86W34-4]
NP_001275985.1. NM_001289056.1. [Q86W34-4]
NP_057711.3. NM_016627.4. [Q86W34-4]
XP_005257490.1. XM_005257433.2. [Q86W34-4]
XP_005257492.1. XM_005257435.2. [Q86W34-4]
XP_005257493.1. XM_005257436.1. [Q86W34-4]
XP_005257494.1. XM_005257437.1. [Q86W34-4]
UniGeneHs.293560.

3D structure databases

ProteinModelPortalQ86W34.
SMRQ86W34. Positions 144-297.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119472. 2 interactions.

Protein family/group databases

MEROPSM54.002.

PTM databases

PhosphoSiteQ86W34.

Polymorphism databases

DMDM317373321.

Proteomic databases

MaxQBQ86W34.
PaxDbQ86W34.
PRIDEQ86W34.

Protocols and materials databases

DNASU51321.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000359783; ENSP00000352831; ENSG00000196704. [Q86W34-5]
ENST00000359904; ENSP00000352976; ENSG00000196704. [Q86W34-4]
ENST00000392720; ENSP00000376481; ENSG00000196704. [Q86W34-4]
ENST00000573646; ENSP00000458752; ENSG00000262747. [Q86W34-4]
ENST00000574972; ENSP00000458372; ENSG00000262747. [Q86W34-5]
ENST00000575682; ENSP00000461778; ENSG00000262747. [Q86W34-4]
ENST00000577866; ENSP00000464133; ENSG00000196704. [Q86W34-4]
ENST00000577985; ENSP00000464635; ENSG00000196704. [Q86W34-4]
ENST00000580753; ENSP00000463012; ENSG00000196704. [Q86W34-4]
ENST00000582462; ENSP00000463297; ENSG00000262747. [Q86W34-4]
ENST00000583572; ENSP00000462911; ENSG00000262747. [Q86W34-4]
ENST00000584964; ENSP00000462793; ENSG00000262747. [Q86W34-4]
GeneID51321.
KEGGhsa:51321.
UCSCuc002jgr.1. human. [Q86W34-4]

Organism-specific databases

CTD51321.
GeneCardsGC17P066244.
HGNCHGNC:28041. AMZ2.
HPAHPA023299.
HPA052406.
MIM615169. gene.
neXtProtNX_Q86W34.
PharmGKBPA162376414.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1913.
HOGENOMHOG000293350.
HOVERGENHBG080165.
InParanoidQ86W34.
KOK06974.
OMAKLQCAIG.
OrthoDBEOG7WX08V.
PhylomeDBQ86W34.
TreeFamTF328603.

Gene expression databases

ArrayExpressQ86W34.
BgeeQ86W34.
CleanExHS_AMZ2.
GenevestigatorQ86W34.

Family and domain databases

Gene3D3.40.390.10. 1 hit.
InterProIPR024079. MetalloPept_cat_dom.
IPR012962. Pept_M54_archaemetzincn.
[Graphical view]
PfamPF07998. Peptidase_M54. 1 hit.
[Graphical view]
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAMZ2. human.
GenomeRNAi51321.
NextBio54701.
PROQ86W34.
SOURCESearch...

Entry information

Entry nameAMZ2_HUMAN
AccessionPrimary (citable) accession number: Q86W34
Secondary accession number(s): A6NLD9 expand/collapse secondary AC list , B3KR44, Q5XKF1, Q9NZE2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: January 11, 2011
Last modified: July 9, 2014
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM