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Disintegrin and metalloproteinase domain-containing protein 26A (ADAM 26A) (EC 3.4.24.-) (Testase-3)

 AD26A_MOUSE             Reviewed;         697 AA.
Q9R158; G3X9D0;
31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
03-OCT-2012, sequence version 2.
28-FEB-2018, entry version 138.
RecName: Full=Disintegrin and metalloproteinase domain-containing protein 26A;
Short=ADAM 26A;
EC=3.4.24.-;
AltName: Full=Testase-3;
Flags: Precursor;
Name=Adam26a; Synonyms=Adam26;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Testis;
PubMed=10395895; DOI=10.1016/S0378-1119(99)00208-5;
Zhu G.-Z., Lin Y., Myles D.G., Primakoff P.;
"Identification of four novel ADAMs with potential roles in
spermatogenesis and fertilization.";
Gene 234:227-237(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Sperm surface membrane protein that may be involved in
spermatogenesis and fertilization.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- TISSUE SPECIFICITY: Expressed specifically in testis.
-!- DEVELOPMENTAL STAGE: Adult levels are reached by day 20 after
birth.
-!- DOMAIN: The conserved cysteine present in the cysteine-switch
motif binds the catalytic zinc ion, thus inhibiting the enzyme.
The dissociation of the cysteine from the zinc ion upon the
activation-peptide release activates the enzyme.
-----------------------------------------------------------------------
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EMBL; AF167404; AAD48843.1; -; mRNA.
EMBL; AC131115; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH466554; EDL35532.1; -; Genomic_DNA.
CCDS; CCDS22269.1; -.
RefSeq; NP_034215.2; NM_010085.3.
UniGene; Mm.334510; -.
ProteinModelPortal; Q9R158; -.
SMR; Q9R158; -.
STRING; 10090.ENSMUSP00000058256; -.
MEROPS; M12.229; -.
PaxDb; Q9R158; -.
PRIDE; Q9R158; -.
DNASU; 13525; -.
Ensembl; ENSMUST00000049577; ENSMUSP00000058256; ENSMUSG00000048516.
GeneID; 13525; -.
KEGG; mmu:13525; -.
UCSC; uc009lof.1; mouse.
CTD; 13525; -.
MGI; MGI:105985; Adam26a.
eggNOG; KOG3607; Eukaryota.
eggNOG; ENOG410XX2M; LUCA.
GeneTree; ENSGT00910000144019; -.
HOGENOM; HOG000230883; -.
HOVERGEN; HBG006978; -.
InParanoid; Q9R158; -.
KO; K08613; -.
OMA; VCRKEKN; -.
OrthoDB; EOG091G03BZ; -.
TreeFam; TF314733; -.
PRO; PR:Q9R158; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000048516; -.
Genevisible; Q9R158; MM.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:1990913; C:sperm head plasma membrane; IDA:MGI.
GO; GO:0005178; F:integrin binding; ISS:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
GO; GO:0008237; F:metallopeptidase activity; ISS:MGI.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
CDD; cd04269; ZnMc_adamalysin_II_like; 1.
Gene3D; 3.40.390.10; -; 1.
Gene3D; 4.10.70.10; -; 1.
InterPro; IPR006586; ADAM_Cys-rich.
InterPro; IPR018358; Disintegrin_CS.
InterPro; IPR001762; Disintegrin_dom.
InterPro; IPR036436; Disintegrin_dom_sf.
InterPro; IPR024079; MetalloPept_cat_dom_sf.
InterPro; IPR001590; Peptidase_M12B.
InterPro; IPR002870; Peptidase_M12B_N.
InterPro; IPR034027; Reprolysin_adamalysin.
Pfam; PF08516; ADAM_CR; 1.
Pfam; PF00200; Disintegrin; 1.
Pfam; PF01562; Pep_M12B_propep; 1.
Pfam; PF01421; Reprolysin; 1.
PRINTS; PR00289; DISINTEGRIN.
SMART; SM00608; ACR; 1.
SMART; SM00050; DISIN; 1.
SUPFAM; SSF57552; SSF57552; 1.
PROSITE; PS50215; ADAM_MEPRO; 1.
PROSITE; PS00427; DISINTEGRIN_1; 1.
PROSITE; PS50214; DISINTEGRIN_2; 1.
PROSITE; PS00142; ZINC_PROTEASE; 1.
2: Evidence at transcript level;
Complete proteome; Developmental protein; Differentiation;
Disulfide bond; EGF-like domain; Glycoprotein; Hydrolase; Membrane;
Metal-binding; Metalloprotease; Protease; Reference proteome; Signal;
Spermatogenesis; Transmembrane; Transmembrane helix; Zinc; Zymogen.
SIGNAL 1 22 {ECO:0000255}.
PROPEP 23 187 {ECO:0000250}.
/FTId=PRO_0000029126.
CHAIN 188 697 Disintegrin and metalloproteinase domain-
containing protein 26A.
/FTId=PRO_0000029127.
TOPO_DOM 188 671 Extracellular. {ECO:0000255}.
TRANSMEM 672 692 Helical. {ECO:0000255}.
TOPO_DOM 693 697 Cytoplasmic. {ECO:0000255}.
DOMAIN 195 385 Peptidase M12B. {ECO:0000255|PROSITE-
ProRule:PRU00276}.
DOMAIN 392 478 Disintegrin. {ECO:0000255|PROSITE-
ProRule:PRU00068}.
DOMAIN 616 649 EGF-like.
MOTIF 159 166 Cysteine switch. {ECO:0000250}.
COMPBIAS 479 615 Cys-rich.
ACT_SITE 330 330 {ECO:0000255|PROSITE-ProRule:PRU00276,
ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 161 161 Zinc; in inhibited form. {ECO:0000250}.
METAL 329 329 Zinc; catalytic. {ECO:0000250}.
METAL 333 333 Zinc; catalytic. {ECO:0000250}.
METAL 339 339 Zinc; catalytic. {ECO:0000250}.
CARBOHYD 127 127 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 214 214 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 365 365 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 391 391 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 464 464 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 506 506 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 531 531 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 573 573 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 305 380 {ECO:0000250}.
DISULFID 344 366 {ECO:0000250}.
DISULFID 346 351 {ECO:0000250}.
DISULFID 450 470 {ECO:0000250}.
DISULFID 620 631 {ECO:0000250}.
DISULFID 639 648 {ECO:0000250}.
CONFLICT 48 48 W -> R (in Ref. 1; AAD48843).
{ECO:0000305}.
CONFLICT 446 446 A -> T (in Ref. 1; AAD48843).
{ECO:0000305}.
CONFLICT 452 452 K -> E (in Ref. 1; AAD48843).
{ECO:0000305}.
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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