AMZ2_MOUSE
ID AMZ2_MOUSE Reviewed; 359 AA.
AC Q400C8; Q8BVM5; Q8K3B9; Q9D121;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
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 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] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Testis;
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] (ISOFORM 1).
RC STRAIN=129; TISSUE=Mammary tumor;
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 [5]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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=Q400C8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q400C8-2; Sequence=VSP_016984, VSP_016985;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in testis.
CC {ECO:0000269|PubMed:17074343}.
CC -!- DEVELOPMENTAL STAGE: Expression in testis begins at about postnatal day
CC 10 (P10), with adult level of expression reached at P20.
CC {ECO:0000269|PubMed:17074343}.
CC -!- SIMILARITY: Belongs to the peptidase M54 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH25087.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB23148.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC35928.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC36674.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ879914; CAI53759.1; -; mRNA.
DR EMBL; AK004062; BAB23148.1; ALT_FRAME; mRNA.
DR EMBL; AK075748; BAC35928.1; ALT_INIT; mRNA.
DR EMBL; AK077195; BAC36674.1; ALT_INIT; mRNA.
DR EMBL; BC025087; AAH25087.1; ALT_INIT; mRNA.
DR RefSeq; NP_001239122.1; NM_001252193.1.
DR RefSeq; NP_079551.3; NM_025275.4.
DR AlphaFoldDB; Q400C8; -.
DR SMR; Q400C8; -.
DR BioGRID; 199513; 3.
DR STRING; 10090.ENSMUSP00000099350; -.
DR MEROPS; M54.002; -.
DR iPTMnet; Q400C8; -.
DR PhosphoSitePlus; Q400C8; -.
DR EPD; Q400C8; -.
DR MaxQB; Q400C8; -.
DR PaxDb; Q400C8; -.
DR PRIDE; Q400C8; -.
DR ProteomicsDB; 296352; -. [Q400C8-1]
DR ProteomicsDB; 296353; -. [Q400C8-2]
DR Antibodypedia; 19248; 75 antibodies from 20 providers.
DR DNASU; 13929; -.
DR Ensembl; ENSMUST00000103061; ENSMUSP00000099350; ENSMUSG00000020610. [Q400C8-1]
DR GeneID; 13929; -.
DR KEGG; mmu:13929; -.
DR CTD; 51321; -.
DR MGI; MGI:104837; Amz2.
DR VEuPathDB; HostDB:ENSMUSG00000020610; -.
DR eggNOG; ENOG502QVTZ; Eukaryota.
DR GeneTree; ENSGT00530000063996; -.
DR InParanoid; Q400C8; -.
DR OMA; QCVMQGS; -.
DR OrthoDB; 1092305at2759; -.
DR BioGRID-ORCS; 13929; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Amz2; mouse.
DR PRO; PR:Q400C8; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q400C8; protein.
DR Bgee; ENSMUSG00000020610; Expressed in seminiferous tubule of testis and 261 other tissues.
DR ExpressionAtlas; Q400C8; 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 Pfam; PF07998; Peptidase_M54; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Zinc.
FT CHAIN 1..359
FT /note="Archaemetzincin-2"
FT /id="PRO_0000159619"
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"
FT VAR_SEQ 310..321
FT /note="ALVKWIDDESCN -> MNEERLQQQLQI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016984"
FT VAR_SEQ 322..359
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016985"
SQ SEQUENCE 359 AA; 41341 MW; 909A226405DBDF4B CRC64;
MQVLRHSEHT LKTALLSKNP VLVSQYEKLD AGEQRLMNEA FQPRSNLFEP ITVHSQSDWI
SSHPEAPQDF EQFFSDRYRK APCPKKHIIY IQSIGSLGNT RVISEEYIKW LKGYCEAFFY
GLKVKFLEPV SVSETKCSFR VNEHTQNLQI HTGHILAFLK KNKPEDAFCI VGITMIDLYP
RDSWNFVFGQ ASLSSGVGIF SFARYGKDFY TSKYEGNVTS LQLTSPTDYS IFDNYYIPEI
TSVLLLRSCK TLTHEIGHIL GLRHCQWLAC LMQGSNHLEE SDRRPLNVCP ICLRKLQSAI
GFNIVERYRA LVKWIDDESC NESGATPKSS SEHAHLPKPV EAFKDWREWL MRCIALLEK
