ADAM7_MOUSE
ID ADAM7_MOUSE Reviewed; 789 AA.
AC O35227; F8VQC6;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Disintegrin and metalloproteinase domain-containing protein 7;
DE Short=ADAM 7;
DE Flags: Precursor;
GN Name=Adam7;
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 STRAIN=C57BL/6J; TISSUE=Epididymis;
RX PubMed=9322939; DOI=10.1210/endo.138.10.5468;
RA Cornwall G.A., Hsia N.;
RT "ADAM7, a member of the ADAM (A Disintegrin And Metalloprotease) gene
RT family is specifically expressed in the mouse anterior pituitary and
RT epididymis.";
RL Endocrinology 138:4262-4272(1997).
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).
CC -!- FUNCTION: May play an important role in male reproduction including
CC sperm maturation and gonadotrope function. This is a non catalytic
CC metalloprotease-like protein.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in the apical region of the proximal
CC caput epididymal epithelium and in the anterior pituitary,
CC specifically, in the gonadotrophes.
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DR EMBL; AF013107; AAC53368.1; -; mRNA.
DR EMBL; AC154706; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS27234.1; -.
DR RefSeq; NP_031428.2; NM_007402.2.
DR AlphaFoldDB; O35227; -.
DR SMR; O35227; -.
DR BioGRID; 197971; 9.
DR STRING; 10090.ENSMUSP00000022640; -.
DR MEROPS; M12.956; -.
DR GlyGen; O35227; 6 sites.
DR PhosphoSitePlus; O35227; -.
DR PaxDb; O35227; -.
DR PRIDE; O35227; -.
DR ProteomicsDB; 281937; -.
DR Antibodypedia; 22842; 86 antibodies from 21 providers.
DR DNASU; 11500; -.
DR Ensembl; ENSMUST00000022640; ENSMUSP00000022640; ENSMUSG00000022056.
DR GeneID; 11500; -.
DR KEGG; mmu:11500; -.
DR UCSC; uc007ulr.1; mouse.
DR CTD; 8756; -.
DR MGI; MGI:107247; Adam7.
DR VEuPathDB; HostDB:ENSMUSG00000022056; -.
DR eggNOG; KOG3607; Eukaryota.
DR GeneTree; ENSGT00940000161406; -.
DR HOGENOM; CLU_012714_6_0_1; -.
DR InParanoid; O35227; -.
DR OMA; NYSCAEL; -.
DR OrthoDB; 162519at2759; -.
DR PhylomeDB; O35227; -.
DR TreeFam; TF314733; -.
DR BioGRID-ORCS; 11500; 1 hit in 72 CRISPR screens.
DR PRO; PR:O35227; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; O35227; protein.
DR Bgee; ENSMUSG00000022056; Expressed in animal zygote and 20 other tissues.
DR Genevisible; O35227; MM.
DR GO; GO:0045177; C:apical part of cell; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0004175; F:endopeptidase activity; IDA:MGI.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
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.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PROPEP 24..176
FT /evidence="ECO:0000250"
FT /id="PRO_0000419681"
FT CHAIN 177..789
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein 7"
FT /id="PRO_0000029056"
FT TOPO_DOM 24..667
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 668..689
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 690..789
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 199..393
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 401..487
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT REGION 764..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..783
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 583
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 628
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 664
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 310..388
FT /evidence="ECO:0000250"
FT DISULFID 350..372
FT /evidence="ECO:0000250"
FT DISULFID 352..357
FT /evidence="ECO:0000250"
FT DISULFID 459..479
FT /evidence="ECO:0000250"
FT CONFLICT 2..3
FT /note="LT -> FP (in Ref. 1; AAC53368)"
FT /evidence="ECO:0000305"
FT CONFLICT 8
FT /note="W -> L (in Ref. 1; AAC53368)"
FT /evidence="ECO:0000305"
FT CONFLICT 28
FT /note="E -> Q (in Ref. 1; AAC53368)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="V -> M (in Ref. 1; AAC53368)"
FT /evidence="ECO:0000305"
FT CONFLICT 224..225
FT /note="KR -> NG (in Ref. 1; AAC53368)"
FT /evidence="ECO:0000305"
FT CONFLICT 253
FT /note="S -> L (in Ref. 1; AAC53368)"
FT /evidence="ECO:0000305"
FT CONFLICT 397
FT /note="E -> K (in Ref. 1; AAC53368)"
FT /evidence="ECO:0000305"
FT CONFLICT 414
FT /note="E -> K (in Ref. 1; AAC53368)"
FT /evidence="ECO:0000305"
FT CONFLICT 495
FT /note="E -> K (in Ref. 1; AAC53368)"
FT /evidence="ECO:0000305"
FT CONFLICT 572..574
FT /note="DKA -> NKT (in Ref. 1; AAC53368)"
FT /evidence="ECO:0000305"
FT CONFLICT 679
FT /note="Missing (in Ref. 1; AAC53368)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 789 AA; 89188 MW; 9C14BAE5D589AF76 CRC64;
MLTTGIFWMT VLISHIQERG IVGVEGQELV HPKKLPLLHK RDLERIHDSD IPEEYEEELL
YEIKLGKKTL ILHLLKAREF LSSNYSETYY NVKREVFTKH PQILDHCFYQ GSIIHEFDSA
ASISTCNGLR GFFRVNDQRY LIEPVKYSDD GEHLVYKYNV KAPYATNHSC VGLNFTKKSA
LIDVENIEEH NAEDHHKEKF IELFVVADEY VYRRNNKPQN KLRKRIWGMV NFVNMIYKTL
NIHVTLAGFE IWSAGDKIEI VSNLESTLLH FSTWQETVLK KRKDFDHVIL LSGKWLYTSM
QGIAYPGGIC QILRSCSVVK DLLPDVNIIG NRMAHQLGHS LGMQHDGFPC TCPLGKCVMG
DGSIPAIKFS KCSQTQYQQF LQDQKPACIL NNPFPEEFND YPFCGNKKVD EGEECDCGPV
QECTNPCCDA HKCVLKPGFT CVEGECCESC QMKKEGAVCR LAKNECDISE VCTGYSPECP
KDEFQANGFP CRNGEGYCFM GLCPTRNEQC SELFIGGAEE SHSLCYRMNK KGNRFGYCKN
KGNTFVPCEE KDLKCGKIYC SGGRPSSRLG EDKAYNLKNV KQNVTIKCRT MFLHHNSRDM
GLVNSGTKCG DGMVCSNGEC IEMEKAYNST ICSSPCDEND VDDNEPECQC EEGSIITEWG
EALNLTSVSI MVIVLVMVII GVGLVILLIR YQKCIKMKQV QSSPREIRGV ENKGYFPEEH
QTRSEPILTD IHPLHTTAES LERVPSSFSS PHYITLKSVS KDSRGIADPK QTDNVNLNLD
TQSGCERLG
