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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
 
 
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