AMZ2_HUMAN
ID AMZ2_HUMAN Reviewed; 360 AA.
AC Q86W34; A6NLD9; B3KR44; Q5XKF1; Q9NZE2;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Archaemetzincin-2;
DE EC=3.4.-.- {ECO:0000250|UniProtKB:Q8TXW1};
DE AltName: Full=Archeobacterial metalloproteinase-like protein 2;
GN Name=AMZ2; ORFNames=BM-014;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP RETRACTED PAPER.
RX PubMed=15972818; DOI=10.1074/jbc.m504533200;
RA Diaz-Perales A., Quesada V., Peinado J.R., Ugalde A.P., Alvarez J.,
RA Suarez M.F., Gomis-Rueth X., Lopez-Otin C.;
RT "Identification and characterization of human archaemetzincin-1 and - 2,
RT two novel members of a family of metalloproteases widely distributed in
RT Archaea.";
RL J. Biol. Chem. 280:30367-30375(2005).
RN [2]
RP RETRACTION NOTICE OF PUBMED:15972818.
RX PubMed=30808005; DOI=10.1074/jbc.w118.007328;
RA Diaz-Perales A., Quesada V., Peinado J.R., Ugalde A.P., Alvarez J.,
RA Suarez M.F., Gomis-Rueth F.X., Lopez-Otin C.;
RL J. Biol. Chem. 294:1434-1434(2019).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ASP-30.
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ASP-30.
RC TISSUE=Amygdala, and Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ASP-30.
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ASP-30.
RC TISSUE=Bone marrow, and Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=17074343; DOI=10.1016/j.fertnstert.2006.04.039;
RA Lin Y.H., Lin Y.M., Teng Y.N., Hsieh T.Y., Lin Y.S., Kuo P.L.;
RT "Identification of ten novel genes involved in human spermatogenesis by
RT microarray analysis of testicular tissue.";
RL Fertil. Steril. 86:1650-1658(2006).
CC -!- FUNCTION: Probable zinc metalloprotease.
CC {ECO:0000250|UniProtKB:Q8TXW1}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q8TXW1};
CC Note=Binds 2 Zn(2+) ions per subunit. One is catalytic, whereas the
CC other seems to have a structural role. {ECO:0000250|UniProtKB:Q8TXW1};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q86W34-4; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86W34-5; Sequence=VSP_047263;
CC -!- TISSUE SPECIFICITY: Down-regulated in testis from patients with
CC maturation arrest (MA) or Sertoli cell-only syndrome (SCOS).
CC {ECO:0000269|PubMed:17074343}.
CC -!- SIMILARITY: Belongs to the peptidase M54 family. {ECO:0000305}.
CC -!- CAUTION: An article reported the identification and characterization of
CC this protein as zinc metalloprotease in different tissues; however,
CC this paper was later retracted. {ECO:0000269|PubMed:15972818,
CC ECO:0000305|PubMed:30808005}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF64270.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=AAF64270.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ635358; CAG25750.1; -; mRNA.
DR EMBL; AF208856; AAF64270.1; ALT_SEQ; mRNA.
DR EMBL; AK126146; BAC86462.1; -; mRNA.
DR EMBL; AK090981; BAG52256.1; -; mRNA.
DR EMBL; AC005332; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471099; EAW89050.1; -; Genomic_DNA.
DR EMBL; BC050709; AAH50709.1; -; mRNA.
DR EMBL; BC056271; AAH56271.1; -; mRNA.
DR CCDS; CCDS11674.1; -. [Q86W34-4]
DR CCDS; CCDS32714.1; -. [Q86W34-5]
DR RefSeq; NP_001028741.1; NM_001033569.1. [Q86W34-4]
DR RefSeq; NP_001028742.1; NM_001033570.1. [Q86W34-4]
DR RefSeq; NP_001028743.1; NM_001033571.1. [Q86W34-4]
DR RefSeq; NP_001028744.1; NM_001033572.1. [Q86W34-4]
DR RefSeq; NP_001028746.1; NM_001033574.1. [Q86W34-5]
DR RefSeq; NP_001275983.1; NM_001289054.1. [Q86W34-4]
DR RefSeq; NP_001275985.1; NM_001289056.1. [Q86W34-4]
DR RefSeq; NP_001333400.1; NM_001346471.1. [Q86W34-4]
DR RefSeq; NP_001333401.1; NM_001346472.1. [Q86W34-4]
DR RefSeq; NP_001333402.1; NM_001346473.1. [Q86W34-4]
DR RefSeq; NP_001333403.1; NM_001346474.1. [Q86W34-4]
DR RefSeq; NP_001333404.1; NM_001346475.1. [Q86W34-4]
DR RefSeq; NP_001333405.1; NM_001346476.1. [Q86W34-4]
DR RefSeq; NP_001333406.1; NM_001346477.1. [Q86W34-4]
DR RefSeq; NP_001333407.1; NM_001346478.1. [Q86W34-4]
DR RefSeq; NP_001333408.1; NM_001346479.1. [Q86W34-4]
DR RefSeq; NP_001333409.1; NM_001346480.1. [Q86W34-5]
DR RefSeq; NP_057711.3; NM_016627.4. [Q86W34-4]
DR AlphaFoldDB; Q86W34; -.
DR SMR; Q86W34; -.
DR BioGRID; 119472; 40.
DR IntAct; Q86W34; 13.
DR STRING; 9606.ENSP00000352976; -.
DR MEROPS; M54.002; -.
DR iPTMnet; Q86W34; -.
DR PhosphoSitePlus; Q86W34; -.
DR BioMuta; AMZ2; -.
DR DMDM; 317373321; -.
DR EPD; Q86W34; -.
DR jPOST; Q86W34; -.
DR MassIVE; Q86W34; -.
DR MaxQB; Q86W34; -.
DR PaxDb; Q86W34; -.
DR PeptideAtlas; Q86W34; -.
DR PRIDE; Q86W34; -.
DR ProteomicsDB; 1468; -.
DR ProteomicsDB; 70111; -. [Q86W34-4]
DR Antibodypedia; 19248; 75 antibodies from 20 providers.
DR DNASU; 51321; -.
DR Ensembl; ENST00000359783.8; ENSP00000352831.4; ENSG00000196704.14. [Q86W34-5]
DR Ensembl; ENST00000359904.8; ENSP00000352976.3; ENSG00000196704.14. [Q86W34-4]
DR Ensembl; ENST00000392720.6; ENSP00000376481.2; ENSG00000196704.14. [Q86W34-4]
DR Ensembl; ENST00000577866.5; ENSP00000464133.1; ENSG00000196704.14. [Q86W34-4]
DR Ensembl; ENST00000577985.5; ENSP00000464635.1; ENSG00000196704.14. [Q86W34-4]
DR Ensembl; ENST00000580753.5; ENSP00000463012.1; ENSG00000196704.14. [Q86W34-4]
DR Ensembl; ENST00000612294.4; ENSP00000483162.1; ENSG00000196704.14. [Q86W34-4]
DR Ensembl; ENST00000674770.2; ENSP00000501934.1; ENSG00000196704.14. [Q86W34-4]
DR GeneID; 51321; -.
DR KEGG; hsa:51321; -.
DR MANE-Select; ENST00000359904.8; ENSP00000352976.3; NM_016627.5; NP_057711.3.
DR UCSC; uc002jgs.2; human. [Q86W34-4]
DR CTD; 51321; -.
DR GeneCards; AMZ2; -.
DR HGNC; HGNC:28041; AMZ2.
DR HPA; ENSG00000196704; Low tissue specificity.
DR MIM; 615169; gene.
DR neXtProt; NX_Q86W34; -.
DR OpenTargets; ENSG00000196704; -.
DR PharmGKB; PA162376414; -.
DR VEuPathDB; HostDB:ENSG00000196704; -.
DR eggNOG; ENOG502QVTZ; Eukaryota.
DR GeneTree; ENSGT00530000063996; -.
DR HOGENOM; CLU_029710_2_1_1; -.
DR InParanoid; Q86W34; -.
DR OMA; QCVMQGS; -.
DR OrthoDB; 1092305at2759; -.
DR PhylomeDB; Q86W34; -.
DR TreeFam; TF328603; -.
DR PathwayCommons; Q86W34; -.
DR SignaLink; Q86W34; -.
DR BioGRID-ORCS; 51321; 11 hits in 1072 CRISPR screens.
DR ChiTaRS; AMZ2; human.
DR GenomeRNAi; 51321; -.
DR Pharos; Q86W34; Tdark.
DR PRO; PR:Q86W34; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q86W34; protein.
DR Bgee; ENSG00000196704; Expressed in sperm and 200 other tissues.
DR ExpressionAtlas; Q86W34; baseline and differential.
DR Genevisible; Q86W34; HS.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd11375; Peptidase_M54; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR012962; Pept_M54_archaemetzincn.
DR Pfam; PF07998; Peptidase_M54; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Zinc.
FT CHAIN 1..360
FT /note="Archaemetzincin-2"
FT /id="PRO_0000159617"
FT ACT_SITE 255
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 254
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q8TXW1"
FT BINDING 258
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q8TXW1"
FT BINDING 264
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q8TXW1"
FT BINDING 265
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TXW1"
FT BINDING 270
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TXW1"
FT BINDING 289
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TXW1"
FT BINDING 292
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TXW1"
FT VAR_SEQ 96..153
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_047263"
FT VARIANT 30
FT /note="N -> D (in dbSNP:rs3213690)"
FT /evidence="ECO:0000269|PubMed:11042152,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:16625196"
FT /id="VAR_024850"
FT VARIANT 146
FT /note="H -> Q (in dbSNP:rs3207194)"
FT /id="VAR_047343"
FT CONFLICT 4
FT /note="I -> V (in Ref. 3; AAF64270)"
FT /evidence="ECO:0000305"
FT CONFLICT 6
FT /note="H -> Y (in Ref. 3; AAF64270)"
FT /evidence="ECO:0000305"
FT CONFLICT 13
FT /note="T -> I (in Ref. 3; AAF64270)"
FT /evidence="ECO:0000305"
FT CONFLICT 15
FT /note="L -> V (in Ref. 3; AAF64270)"
FT /evidence="ECO:0000305"
FT CONFLICT 29
FT /note="L -> V (in Ref. 3; AAF64270)"
FT /evidence="ECO:0000305"
FT CONFLICT 51..52
FT /note="IT -> CI (in Ref. 3; AAF64270)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="D -> H (in Ref. 3; AAF64270)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="T -> I (in Ref. 3; AAF64270)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="N -> D (in Ref. 3; AAF64270)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="Q -> R (in Ref. 3; AAF64270)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="N -> S (in Ref. 3; AAF64270)"
FT /evidence="ECO:0000305"
FT CONFLICT 121
FT /note="G -> R (in Ref. 3; AAF64270)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="S -> G (in Ref. 3; AAF64270)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 360 AA; 41263 MW; D74E7F7CE7873CBF CRC64;
MQIIRHSEQT LKTALISKNP VLVSQYEKLN AGEQRLMNEA FQPASDLFGP ITLHSPSDWI
TSHPEAPQDF EQFFSDPYRK TPSPNKRSIY IQSIGSLGNT RIISEEYIKW LTGYCKAYFY
GLRVKLLEPV PVSVTRCSFR VNENTHNLQI HAGDILKFLK KKKPEDAFCV VGITMIDLYP
RDSWNFVFGQ ASLTDGVGIF SFARYGSDFY SMHYKGKVKK LKKTSSSDYS IFDNYYIPEI
TSVLLLRSCK TLTHEIGHIF GLRHCQWLAC LMQGSNHLEE ADRRPLNLCP ICLHKLQCAV
GFSIVERYKA LVRWIDDESS DTPGATPEHS HEDNGNLPKP VEAFKEWKEW IIKCLAVLQK
