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Database: UniProt
Entry: Q7M763_MOUSE
LinkDB: Q7M763_MOUSE
Original site: Q7M763_MOUSE 
ID   Q7M763_MOUSE            Unreviewed;       760 AA.
AC   Q7M763;
DT   15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2003, sequence version 1.
DT   27-MAR-2024, entry version 173.
DE   SubName: Full=A disintegrin and metallopeptidase domain 20 {ECO:0000313|Ensembl:ENSMUSP00000057794.8};
DE   SubName: Full=Testase-8 {ECO:0000313|EMBL:CAD66451.1};
GN   Name=Adam20 {ECO:0000313|Ensembl:ENSMUSP00000057794.8,
GN   ECO:0000313|MGI:MGI:2152342};
GN   Synonyms=4930529F22Rik {ECO:0000313|MGI:MGI:2152342}, Adam38
GN   {ECO:0000313|EMBL:CAD66451.1};
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 {ECO:0000313|EMBL:CAD66451.1};
RN   [1] {ECO:0000313|EMBL:BAE21514.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE21514.1};
RC   TISSUE=Testis {ECO:0000313|EMBL:BAE21514.1};
RX   PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2] {ECO:0000313|EMBL:BAE21514.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE21514.1};
RC   TISSUE=Testis {ECO:0000313|EMBL:BAE21514.1};
RX   PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to prepare
RT   full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [3] {ECO:0000313|EMBL:BAE21514.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE21514.1};
RC   TISSUE=Testis {ECO:0000313|EMBL:BAE21514.1};
RX   PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., Sumi N.,
RA   Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., Yamamoto R.,
RA   Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., Fujiwake S.,
RA   Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., Yoneda Y.,
RA   Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., Okazaki Y.,
RA   Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format sequencing
RT   pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [4] {ECO:0000313|EMBL:BAE21514.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE21514.1};
RC   TISSUE=Testis {ECO:0000313|EMBL:BAE21514.1};
RX   PubMed=11217851; DOI=10.1038/35055500;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [5] {ECO:0000313|EMBL:BAE21514.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE21514.1};
RC   TISSUE=Testis {ECO:0000313|EMBL:BAE21514.1};
RX   PubMed=12466851; DOI=10.1038/nature01266;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [6] {ECO:0000313|EMBL:CAD66451.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:CAD66451.1};
RX   PubMed=12838346; DOI=10.1038/nrg1111;
RA   Puente X.S., Sanchez L.M., Overall C.M., Lopez-Otin C.;
RT   "Human and mouse proteases: a comparative genomic approach.";
RL   Nat. Rev. Genet. 4:544-558(2003).
RN   [7] {ECO:0000313|EMBL:BAE21514.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE21514.1};
RC   TISSUE=Testis {ECO:0000313|EMBL:BAE21514.1};
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K., Hori F.,
RA   Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S., Kawai J., Kojima M.,
RA   Konno H., Murata M., Nakamura M., Ninomiya N., Nishiyori H., Nomura K.,
RA   Ohno M., Sakazume N., Sano H., Sasaki D., Shibata K., Shiraki T.,
RA   Tagami M., Tagami Y., Waki K., Watahiki A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [8] {ECO:0000313|EMBL:BAE21514.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE21514.1};
RC   TISSUE=Testis {ECO:0000313|EMBL:BAE21514.1};
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [9] {ECO:0000313|EMBL:BAE21514.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE21514.1};
RC   TISSUE=Testis {ECO:0000313|EMBL:BAE21514.1};
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [10] {ECO:0000313|Ensembl:ENSMUSP00000057794.8, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000057794.8,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [11] {ECO:0000313|Ensembl:ENSMUSP00000057794.8}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000057794.8};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   EMBL; AK133113; BAE21514.1; -; mRNA.
DR   EMBL; BN000119; CAD66451.1; -; Genomic_DNA.
DR   RefSeq; NP_001009548.1; NM_001009548.2.
DR   RefSeq; XP_006509516.1; XM_006509453.1.
DR   STRING; 10090.ENSMUSP00000057794; -.
DR   MEROPS; M12.251; -.
DR   PaxDb; 10090-ENSMUSP00000057794; -.
DR   ProteomicsDB; 332710; -.
DR   DNASU; 384806; -.
DR   Ensembl; ENSMUST00000056331.8; ENSMUSP00000057794.8; ENSMUSG00000046282.8.
DR   GeneID; 384806; -.
DR   KEGG; mmu:384806; -.
DR   UCSC; uc012gcp.1; mouse.
DR   AGR; MGI:2152342; -.
DR   CTD; 8748; -.
DR   MGI; MGI:2152342; Adam20.
DR   VEuPathDB; HostDB:ENSMUSG00000046282; -.
DR   eggNOG; KOG3607; Eukaryota.
DR   GeneTree; ENSGT00940000161067; -.
DR   HOGENOM; CLU_012714_4_0_1; -.
DR   OMA; YNTNCAV; -.
DR   OrthoDB; 5406290at2759; -.
DR   TreeFam; TF314733; -.
DR   BioGRID-ORCS; 384806; 1 hit in 76 CRISPR screens.
DR   Proteomes; UP000000589; Chromosome 8.
DR   Bgee; ENSMUSG00000046282; Expressed in spermatid and 3 other cell types or tissues.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:1990913; C:sperm head plasma membrane; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR   GO; GO:0008584; P:male gonad development; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 4.10.70.10; Disintegrin domain; 1.
DR   InterPro; IPR006586; ADAM_Cys-rich.
DR   InterPro; IPR001762; Disintegrin_dom.
DR   InterPro; IPR036436; Disintegrin_dom_sf.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   InterPro; IPR002870; Peptidase_M12B_N.
DR   InterPro; IPR034027; Reprolysin_adamalysin.
DR   PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR   PANTHER; PTHR11905:SF232; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 20; 1.
DR   Pfam; PF08516; ADAM_CR; 1.
DR   Pfam; PF00200; Disintegrin; 1.
DR   Pfam; PF01562; Pep_M12B_propep; 1.
DR   Pfam; PF01421; Reprolysin; 1.
DR   PRINTS; PR00289; DISINTEGRIN.
DR   SMART; SM00608; ACR; 1.
DR   SMART; SM00050; DISIN; 1.
DR   SUPFAM; SSF57552; Blood coagulation inhibitor (disintegrin); 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS50214; DISINTEGRIN_2; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW   Proteomics identification {ECO:0007829|EPD:Q7M763};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT   TRANSMEM        702..722
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          221..398
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000259|PROSITE:PS50215"
FT   DOMAIN          420..506
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000259|PROSITE:PS50214"
FT   DOMAIN          644..677
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   REGION          733..760
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        736..750
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        356
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         355
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         359
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         365
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   DISULFID        478..498
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT   DISULFID        667..676
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   760 AA;  86147 MW;  BA9602AF7222CDC9 CRC64;
     MQTTQRASSF AAAEDNIAMD KAVVYTRIPH LYVWLEILNI LSSRPLTGYA QHTSLPEVVI
     PLRVTGNRPM WAMGWLTYSL HFGGQKHFIH IKAKKFLVSR LFSVFTYTKQ GALHKDQPYV
     QNDCYYHGHM DGDPESMVAI TTCYGGFQGI LQINGTVYEI KPKNLSSTFE HLVHKMDSEE
     TELLPMRCAL TEEIAKQMKR QQNENPTLMQ NHYEEWWTHR SFLDLALVVD CERIRYHNNN
     KSHVLVEVFL IISLINKIYF ALDIEVVLIG LELWNEGNLV PVDRMQILLE EFCVWKTLSL
     NIRIPNDIAH LFVNHSFGKF LGLAYVGTVC LPSHNCGVDR LLGPNLFQFA HIIAHEIGHN
     LGMEHDSSSC TCGGINYCLM SSTYSFNPEF SNCSYSNFWT TYATTNCLRK EKMSIGNLQI
     QFCGNGVVDD GEQCDCGDRH MCERDQCCNS RCALNDGAAC AFGLCCLYCQ IMPAGTVCRE
     EVNECDLPEW CNGHSHKCPN DVYLLDGSPC RDGGYCYEKR CNNRDEQCKQ IFGKEARSAD
     HSCYRELNTQ GDRFGNCGMI RDAYLRCHDS DILCGRVQCE NVTRIPFLRD HSTVHWTHLN
     GVTCWGTDYH FGMTIPDIGI VKDGTDCGPE HVCINKKCVS KPIWLEQCSS KTCTMKGVCN
     NLHHCHCNRG WDPPHCLESG FGGSVDSGPP PGEEESQQHM DLVLITPILS IVSLVFLLPW
     LLNRYIRTSS KFEEPTVSTS KEEEESHVAS NESEAQQVET
//
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