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Database: UniProt
Entry: Q9R158
LinkDB: Q9R158
Original site: Q9R158 
ID   AD26A_MOUSE             Reviewed;         697 AA.
AC   Q9R158; G3X9D0;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 2.
DT   16-JAN-2019, entry version 142.
DE   RecName: Full=Disintegrin and metalloproteinase domain-containing protein 26A;
DE            Short=ADAM 26A;
DE            EC=3.4.24.-;
DE   AltName: Full=Testase-3;
DE   Flags: Precursor;
GN   Name=Adam26a; Synonyms=Adam26;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RX   PubMed=10395895; DOI=10.1016/S0378-1119(99)00208-5;
RA   Zhu G.-Z., Lin Y., Myles D.G., Primakoff P.;
RT   "Identification of four novel ADAMs with potential roles in
RT   spermatogenesis and fertilization.";
RL   Gene 234:227-237(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Sperm surface membrane protein that may be involved in
CC       spermatogenesis and fertilization.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Expressed specifically in testis.
CC   -!- DEVELOPMENTAL STAGE: Adult levels are reached by day 20 after
CC       birth.
CC   -!- DOMAIN: The conserved cysteine present in the cysteine-switch
CC       motif binds the catalytic zinc ion, thus inhibiting the enzyme.
CC       The dissociation of the cysteine from the zinc ion upon the
CC       activation-peptide release activates the enzyme.
DR   EMBL; AF167404; AAD48843.1; -; mRNA.
DR   EMBL; AC131115; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466554; EDL35532.1; -; Genomic_DNA.
DR   CCDS; CCDS22269.1; -.
DR   RefSeq; NP_034215.2; NM_010085.3.
DR   UniGene; Mm.334510; -.
DR   ProteinModelPortal; Q9R158; -.
DR   SMR; Q9R158; -.
DR   STRING; 10090.ENSMUSP00000058256; -.
DR   MEROPS; M12.229; -.
DR   PaxDb; Q9R158; -.
DR   PRIDE; Q9R158; -.
DR   DNASU; 13525; -.
DR   Ensembl; ENSMUST00000049577; ENSMUSP00000058256; ENSMUSG00000048516.
DR   GeneID; 13525; -.
DR   KEGG; mmu:13525; -.
DR   UCSC; uc009lof.1; mouse.
DR   CTD; 13525; -.
DR   MGI; MGI:105985; Adam26a.
DR   eggNOG; KOG3607; Eukaryota.
DR   eggNOG; ENOG410XX2M; LUCA.
DR   GeneTree; ENSGT00940000162672; -.
DR   HOGENOM; HOG000230883; -.
DR   HOVERGEN; HBG006978; -.
DR   InParanoid; Q9R158; -.
DR   KO; K08613; -.
DR   OMA; HNINEVL; -.
DR   OrthoDB; 162519at2759; -.
DR   TreeFam; TF314733; -.
DR   PRO; PR:Q9R158; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   Bgee; ENSMUSG00000048516; Expressed in 7 organ(s), highest expression level in testis.
DR   Genevisible; Q9R158; MM.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:1990913; C:sperm head plasma membrane; IDA:MGI.
DR   GO; GO:0005178; F:integrin binding; ISS:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008237; F:metallopeptidase activity; ISS:MGI.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
DR   GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR   CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR   Gene3D; 3.40.390.10; -; 1.
DR   Gene3D; 4.10.70.10; -; 1.
DR   InterPro; IPR006586; ADAM_Cys-rich.
DR   InterPro; IPR018358; Disintegrin_CS.
DR   InterPro; IPR001762; Disintegrin_dom.
DR   InterPro; IPR036436; Disintegrin_dom_sf.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   InterPro; IPR002870; Peptidase_M12B_N.
DR   InterPro; IPR034027; Reprolysin_adamalysin.
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; SSF57552; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS00427; DISINTEGRIN_1; 1.
DR   PROSITE; PS50214; DISINTEGRIN_2; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Developmental protein; Differentiation;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Hydrolase; Membrane;
KW   Metal-binding; Metalloprotease; Protease; Reference proteome; Signal;
KW   Spermatogenesis; Transmembrane; Transmembrane helix; Zinc; Zymogen.
FT   SIGNAL        1     22       {ECO:0000255}.
FT   PROPEP       23    187       {ECO:0000250}.
FT                                /FTId=PRO_0000029126.
FT   CHAIN       188    697       Disintegrin and metalloproteinase domain-
FT                                containing protein 26A.
FT                                /FTId=PRO_0000029127.
FT   TOPO_DOM    188    671       Extracellular. {ECO:0000255}.
FT   TRANSMEM    672    692       Helical. {ECO:0000255}.
FT   TOPO_DOM    693    697       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      195    385       Peptidase M12B. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00276}.
FT   DOMAIN      392    478       Disintegrin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00068}.
FT   DOMAIN      616    649       EGF-like.
FT   MOTIF       159    166       Cysteine switch. {ECO:0000250}.
FT   COMPBIAS    479    615       Cys-rich.
FT   ACT_SITE    330    330       {ECO:0000255|PROSITE-ProRule:PRU00276,
FT                                ECO:0000255|PROSITE-ProRule:PRU10095}.
FT   METAL       161    161       Zinc; in inhibited form. {ECO:0000250}.
FT   METAL       329    329       Zinc; catalytic. {ECO:0000250}.
FT   METAL       333    333       Zinc; catalytic. {ECO:0000250}.
FT   METAL       339    339       Zinc; catalytic. {ECO:0000250}.
FT   CARBOHYD    127    127       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    214    214       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    365    365       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    391    391       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    464    464       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    506    506       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    531    531       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    573    573       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    305    380       {ECO:0000250}.
FT   DISULFID    344    366       {ECO:0000250}.
FT   DISULFID    346    351       {ECO:0000250}.
FT   DISULFID    450    470       {ECO:0000250}.
FT   DISULFID    620    631       {ECO:0000250}.
FT   DISULFID    639    648       {ECO:0000250}.
FT   CONFLICT     48     48       W -> R (in Ref. 1; AAD48843).
FT                                {ECO:0000305}.
FT   CONFLICT    446    446       A -> T (in Ref. 1; AAD48843).
FT                                {ECO:0000305}.
FT   CONFLICT    452    452       K -> E (in Ref. 1; AAD48843).
FT                                {ECO:0000305}.
SQ   SEQUENCE   697 AA;  78747 MW;  E90B15E1996AB7E7 CRC64;
     MFLKFCLWTM FFFSAWSPIG HAKYSSLLEV VTPLRVTVTR GNNISPGWLS YSLNIGGQRH
     IITMKPKKNL ISRNFLLFTY SDQGDLLEQH HFVQNDCYYH GYVDEDLESP VIVNTCFGSL
     QGTLEINGTS YEIMPKSSTS TFEHLVYKMD SGDSESSPMR CGLSEEETAQ QTKLQESNAP
     TLLQIPYENW WTHHRFIEYF VVLDHKQYVH RNNNITTCIQ DMLQIVNGVN GYYLQIDTDV
     VLTTLEVWNE KNYINVELSI FKVLGDFCTW KQNMFGNRIR HDIIHLLVRQ GYGLYLGLAY
     LADVCTPYNC GVSSVLSDVM SDMAHIVAHE MGHNFGMKHD GIGCTCGLKD CLMAPYKTNS
     PKFSNCSYEE MYSVVTKRSC LYDIPEALVT NLTVCGNKVV EEGEQCDCGN SESCLQDPCC
     SSDCVLKPGA QCAFGLCCKN CQFLKAGTVC RKEKNECDLP EWCNGTSAEC PGDVYKADGI
     PCSGEGYCYK MECHQRDEQC RKIFGNGSRS ADEICYMEMN RQGDRFGNCG NDSSTYRTCQ
     IADVLCGQIQ CENVIQLPQR RNHETVHYTH FSNITCWTMD YHFGITIDDI GAVSDGTAYA
     PDHICVDRKC VSKSVLVSNC SPQLYHMQGI CNNKQHCHCG VTWKPPDCQK RGHGGSIDSG
     PPPLPLSHSK WIVYILIVLD VCIVIIIYLF SFYKLSK
//
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