AMZ2_RAT
ID AMZ2_RAT Reviewed; 359 AA.
AC Q400C7; Q5U2S2;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Archaemetzincin-2;
DE EC=3.4.-.- {ECO:0000250|UniProtKB:Q8TXW1};
DE AltName: Full=Archeobacterial metalloproteinase-like protein 2;
GN Name=Amz2;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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 -!- CAUTION: The protein has been described as presenting a second isoform
CC with a missign Lys in position 309 (PubMed:15972818). However, the
CC paper has been retracted. {ECO:0000269|PubMed:15972818,
CC ECO:0000305|PubMed:30808005}.
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DR EMBL; AJ879915; CAI53760.1; -; mRNA.
DR EMBL; BC085886; AAH85886.1; -; mRNA.
DR AlphaFoldDB; Q400C7; -.
DR SMR; Q400C7; -.
DR BioGRID; 262101; 1.
DR IntAct; Q400C7; 4.
DR STRING; 10116.ENSRNOP00000000263; -.
DR MEROPS; M54.002; -.
DR PaxDb; Q400C7; -.
DR GeneID; 360650; -.
DR CTD; 51321; -.
DR RGD; 1304846; Amz2.
DR VEuPathDB; HostDB:ENSRNOG00000000246; -.
DR eggNOG; ENOG502QVTZ; Eukaryota.
DR HOGENOM; CLU_029710_2_1_1; -.
DR InParanoid; Q400C7; -.
DR OMA; QCVMQGS; -.
DR OrthoDB; 1092305at2759; -.
DR PhylomeDB; Q400C7; -.
DR PRO; PR:Q400C7; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000000246; Expressed in testis and 19 other tissues.
DR Genevisible; Q400C7; RN.
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 Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW Zinc.
FT CHAIN 1..359
FT /note="Archaemetzincin-2"
FT /id="PRO_0000159621"
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"
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"
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"
FT BINDING 265
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 270
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 289
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 292
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 359 AA; 41379 MW; 91F10D6D24FC2F2A CRC64;
MQVLRHSEHT LKTALLSKNP DLVSQYEKLD AGEQRLMNEA FQPRNNLFEP ITLHSQSDWI
SSHPEAPQDF EQFFSDRYRK APCPKKHIIY IQPIGFLGNT RVISEEYIKW LKGYCEAFFY
GLKVKFLEPV SVSATKCSFR VNENTQNLQI HTGHILAFLK RNKPEDAFCI VGITMIDLYP
RDSWNFVFGQ ASLSSGVGIF SFARYGKDFY TSKYEGSVKV PQRTVSSDYS IFDNYYIPEI
TSVLLLRSCK TLTHEIGHIL GLRHCQWLAC LMQGSNHLEE SDRRPLNVCP ICLRKLQSAI
GFNIVERYKA LVKWIDDESC GESGATPKSS SEHVYLPKPV EAFKDWREWI LRCIAVLEK
