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   24-JAN-2024, entry version 162.
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.ENSP00000464635; -.
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; 9606-ENSP00000352976; -.
DR   PeptideAtlas; Q86W34; -.
DR   ProteomicsDB; 1468; -.
DR   ProteomicsDB; 70111; -. [Q86W34-4]
DR   Pumba; Q86W34; -.
DR   Antibodypedia; 19248; 82 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   AGR; HGNC:28041; -.
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; CQWLSCV; -.
DR   OrthoDB; 2719238at2759; -.
DR   PhylomeDB; Q86W34; -.
DR   TreeFam; TF328603; -.
DR   PathwayCommons; Q86W34; -.
DR   SignaLink; Q86W34; -.
DR   BioGRID-ORCS; 51321; 11 hits in 1150 CRISPR screens.
DR   ChiTaRS; AMZ2; human.
DR   GenomeRNAi; 51321; -.
DR   Pharos; Q86W34; Tbio.
DR   PRO; PR:Q86W34; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; Q86W34; Protein.
DR   Bgee; ENSG00000196704; Expressed in sperm and 202 other cell types or tissues.
DR   ExpressionAtlas; Q86W34; baseline and differential.
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; Collagenase (Catalytic Domain); 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR012962; Pept_M54_archaemetzincn.
DR   PANTHER; PTHR32205:SF5; ARCHAEMETZINCIN-2; 1.
DR   PANTHER; PTHR32205; ARCHAEMETZINCIN-2-RELATED; 1.
DR   Pfam; PF07998; Peptidase_M54; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
DR   Genevisible; Q86W34; HS.
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
//