AD26A_MOUSE
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 03-AUG-2022, entry version 157.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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 spermatogenesis
RT 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., 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 [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 protein.
CC -!- TISSUE SPECIFICITY: Expressed specifically in testis.
CC -!- DEVELOPMENTAL STAGE: Adult levels are reached by day 20 after birth.
CC -!- DOMAIN: The conserved cysteine present in the cysteine-switch motif
CC binds the catalytic zinc ion, thus inhibiting the enzyme. The
CC dissociation of the cysteine from the zinc ion upon the activation-
CC peptide release activates the enzyme.
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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 AlphaFoldDB; Q9R158; -.
DR SMR; Q9R158; -.
DR BioGRID; 199332; 8.
DR STRING; 10090.ENSMUSP00000058256; -.
DR MEROPS; M12.229; -.
DR GlyGen; Q9R158; 8 sites.
DR PaxDb; Q9R158; -.
DR PRIDE; Q9R158; -.
DR ProteomicsDB; 281935; -.
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 VEuPathDB; HostDB:ENSMUSG00000048516; -.
DR eggNOG; KOG3607; Eukaryota.
DR GeneTree; ENSGT00940000162672; -.
DR HOGENOM; CLU_012714_4_0_1; -.
DR InParanoid; Q9R158; -.
DR OMA; DVGCLFA; -.
DR OrthoDB; 162519at2759; -.
DR PhylomeDB; Q9R158; -.
DR TreeFam; TF314733; -.
DR BioGRID-ORCS; 13525; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q9R158; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9R158; protein.
DR Bgee; ENSMUSG00000048516; Expressed in spermatid and 13 other tissues.
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:0005886; C:plasma membrane; IBA:GO_Central.
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:0008584; P:male gonad development; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; 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 Developmental protein; Differentiation; Disulfide bond; EGF-like domain;
KW Glycoprotein; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Signal; Spermatogenesis; Transmembrane;
KW Transmembrane helix; Zinc; Zymogen.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..187
FT /evidence="ECO:0000250"
FT /id="PRO_0000029126"
FT CHAIN 188..697
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein 26A"
FT /id="PRO_0000029127"
FT TOPO_DOM 188..671
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 672..692
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 693..697
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 195..385
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 392..478
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DOMAIN 616..649
FT /note="EGF-like"
FT MOTIF 159..166
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT ACT_SITE 330
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /note="in inhibited form"
FT /evidence="ECO:0000250"
FT BINDING 329
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 333
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 339
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 506
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 531
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 573
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 305..380
FT /evidence="ECO:0000250"
FT DISULFID 344..366
FT /evidence="ECO:0000250"
FT DISULFID 346..351
FT /evidence="ECO:0000250"
FT DISULFID 450..470
FT /evidence="ECO:0000250"
FT DISULFID 620..631
FT /evidence="ECO:0000250"
FT DISULFID 639..648
FT /evidence="ECO:0000250"
FT CONFLICT 48
FT /note="W -> R (in Ref. 1; AAD48843)"
FT /evidence="ECO:0000305"
FT CONFLICT 446
FT /note="A -> T (in Ref. 1; AAD48843)"
FT /evidence="ECO:0000305"
FT CONFLICT 452
FT /note="K -> E (in Ref. 1; AAD48843)"
FT /evidence="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
