AMZ1_RAT
ID AMZ1_RAT Reviewed; 501 AA.
AC Q400C9; B1H214;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP RETRACTED PAPER.
RC STRAIN=Wistar;
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] {ECO:0000312|EMBL:EDL89721.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000312|EMBL:EDL89721.1};
RX PubMed=15632090; DOI=10.1101/gr.2889405;
RA Florea L., Di Francesco V., Miller J., Turner R., Yao A., Harris M.,
RA Walenz B., Mobarry C., Merkulov G.V., Charlab R., Dew I., Deng Z.,
RA Istrail S., Li P., Sutton G.;
RT "Gene and alternative splicing annotation with AIR.";
RL Genome Res. 15:54-66(2005).
RN [4] {ECO:0000312|EMBL:AAI60815.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen {ECO:0000312|EMBL:AAI60815.1};
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}.
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DR EMBL; AJ879913; CAI53758.1; -; mRNA.
DR EMBL; CH474012; EDL89721.1; -; Genomic_DNA.
DR EMBL; BC160815; AAI60815.1; -; mRNA.
DR RefSeq; NP_001040557.1; NM_001047092.1.
DR RefSeq; XP_006248992.1; XM_006248930.3.
DR RefSeq; XP_006248993.1; XM_006248931.3.
DR RefSeq; XP_006248994.1; XM_006248932.3.
DR RefSeq; XP_006248995.1; XM_006248933.3.
DR AlphaFoldDB; Q400C9; -.
DR STRING; 10116.ENSRNOP00000037159; -.
DR MEROPS; M54.003; -.
DR PaxDb; Q400C9; -.
DR Ensembl; ENSRNOT00000039726; ENSRNOP00000037159; ENSRNOG00000024264.
DR GeneID; 304317; -.
DR KEGG; rno:304317; -.
DR UCSC; RGD:1311314; rat.
DR CTD; 155185; -.
DR RGD; 1311314; Amz1.
DR eggNOG; ENOG502QV2Q; Eukaryota.
DR GeneTree; ENSGT00530000063996; -.
DR HOGENOM; CLU_029710_0_0_1; -.
DR InParanoid; Q400C9; -.
DR OMA; IEEHGRW; -.
DR OrthoDB; 1092305at2759; -.
DR PhylomeDB; Q400C9; -.
DR TreeFam; TF328603; -.
DR PRO; PR:Q400C9; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Proteomes; UP000234681; Chromosome 12.
DR Bgee; ENSRNOG00000024264; Expressed in spleen and 17 other tissues.
DR ExpressionAtlas; Q400C9; 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; -; 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..501
FT /note="Archaemetzincin-1"
FT /id="PRO_0000159616"
FT REGION 349..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 262
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 261
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="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q8TXW1"
FT BINDING 272
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TXW1"
FT BINDING 277
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TXW1"
FT BINDING 296
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TXW1"
FT BINDING 299
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TXW1"
SQ SEQUENCE 501 AA; 55323 MW; A95870427395BAAE CRC64;
MVQCRPPQEF SFGPRALKDA LISCDLALKQ LYTSAFSPSE RLFLSEAYNP HRTLFSTLLI
HSAFDWLLSR PEAPEDFETF HASLQLRKQS LARKHIYLQP IDLSEGLAGC PLLDHLRSCA
EAFFLGLRVK CLPSVASASI NCCSRPARDT DGLQLHTDGI LSFLKNNKPG DALCVLGLTL
ADLYPHDAWT FTFGRFLPGH EVGVCSFARF SGEFLQAGSS IPDSALLEAA AGGPETLPQE
GGQTLCYSAL GMVQCCKVTC HELCHLLGLG SCRWLRCLLQ GVLSLDEALR RPLDLCPICL
RKLHHLLGFR LLERYKRLHT WTRVMLEMWS GQEAGEPSVS EDTLPFSADS GMGCESDTEP
VTSPSEPVTP DAWSHTFPDG PEPVSEEGLS SLAASEVLLK LGGPVDALEE YRQWLDACIQ
ALEREVAEEE LVQVDAAVDA LGRWEMFTGQ LPVTKQYMPC VKDNVGLRRV LGDKFSSLRR
RLSSRRLAKA SSSQCHWGAE N
