AMZ1_MOUSE
ID AMZ1_MOUSE Reviewed; 502 AA.
AC Q8BVF9; Q811F9; Q8BMM5;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Archaemetzincin-1;
DE EC=3.4.-.- {ECO:0000250|UniProtKB:Q8TXW1};
DE AltName: Full=Archeobacterial metalloproteinase-like protein 1;
GN Name=Amz1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP RETRACTED PAPER.
RC STRAIN=C57BL/6J;
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].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Cerebellum, and Pituitary;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 226-502.
RC STRAIN=FVB/N; TISSUE=Kidney;
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).
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 -!- SIMILARITY: Belongs to the peptidase M54 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC27003.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ879912; CAI53757.1; -; mRNA.
DR EMBL; AK030521; BAC27003.1; ALT_INIT; mRNA.
DR EMBL; AK078332; BAC37222.1; -; mRNA.
DR EMBL; AK170176; BAE41617.1; -; mRNA.
DR EMBL; BC046428; AAH46428.1; -; mRNA.
DR CCDS; CCDS19824.1; -.
DR RefSeq; NP_775581.1; NM_173405.2.
DR AlphaFoldDB; Q8BVF9; -.
DR STRING; 10090.ENSMUSP00000113911; -.
DR MEROPS; M54.003; -.
DR PhosphoSitePlus; Q8BVF9; -.
DR MaxQB; Q8BVF9; -.
DR PaxDb; Q8BVF9; -.
DR PRIDE; Q8BVF9; -.
DR ProteomicsDB; 282087; -.
DR Antibodypedia; 11135; 54 antibodies from 18 providers.
DR DNASU; 231842; -.
DR Ensembl; ENSMUST00000060918; ENSMUSP00000053110; ENSMUSG00000050022.
DR Ensembl; ENSMUST00000120630; ENSMUSP00000113911; ENSMUSG00000050022.
DR GeneID; 231842; -.
DR KEGG; mmu:231842; -.
DR UCSC; uc009aif.1; mouse.
DR CTD; 155185; -.
DR MGI; MGI:2442258; Amz1.
DR VEuPathDB; HostDB:ENSMUSG00000050022; -.
DR eggNOG; ENOG502QV2Q; Eukaryota.
DR GeneTree; ENSGT00530000063996; -.
DR HOGENOM; CLU_029710_0_0_1; -.
DR InParanoid; Q8BVF9; -.
DR OMA; IEEHGRW; -.
DR OrthoDB; 1092305at2759; -.
DR PhylomeDB; Q8BVF9; -.
DR TreeFam; TF328603; -.
DR BioGRID-ORCS; 231842; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Amz1; mouse.
DR PRO; PR:Q8BVF9; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8BVF9; protein.
DR Bgee; ENSMUSG00000050022; Expressed in ectoplacental cone and 99 other tissues.
DR ExpressionAtlas; Q8BVF9; baseline and differential.
DR Genevisible; Q8BVF9; MM.
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 PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW Zinc.
FT CHAIN 1..502
FT /note="Archaemetzincin-1"
FT /id="PRO_0000159615"
FT REGION 336..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 263
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 262
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 266
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 273
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TXW1"
FT BINDING 278
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TXW1"
FT BINDING 297
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TXW1"
FT BINDING 300
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TXW1"
SQ SEQUENCE 502 AA; 55284 MW; ED401AA7DDCD0050 CRC64;
MVQCKPPQEF SFGPRALKDA LISCDLALKQ MYTSAFSPSE RLFLSEAYNP NRTLFSTLLI
HSAYDWLLSR PEAPEDFETF HASLQLRKQS LARKHIYLQP IDLSEGLAGC PLLDHLRSCA
EAFFLGLRVK CLPSVAAASI NCCSRPSRDT DGLQLHTDGI LSFLKNNKPG DALCVLGLTL
ADLYPHDAWT FTFGRFLPGH EVGVCSFARF SGEFLQAGSS VPDSALLEAA AAGGPETLPR
ERGRTLCFSA LGMVQCCKVT CHELCHLLGL GSCRWLRCLL QGALSLDEVL RRPLDLCPIC
LRKLHHLLGF RLLERYKRLH AWTRVMVEIW SGQEAGEPSV SEDTLPFSAD SGMGCESDTE
PVTSPSEPVT PDGWSHPFPD GPEPVSEDGL GSLMASEVSL TLGGPVDAME EYGQWLTACI
QTLEREGAEE ELLQVDAAVD ALSRWEMFTG QLPVTKQHVP CGKDNVGLRR VLGDKFSSLR
RRLSSRRFAK ASSSHCRWGA EN