ADAM7_RAT
ID ADAM7_RAT Reviewed; 789 AA.
AC Q63180;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Disintegrin and metalloproteinase domain-containing protein 7;
DE Short=ADAM 7;
DE AltName: Full=Epididymal apical protein I;
DE Short=EAP I;
DE Flags: Precursor;
GN Name=Adam7; Synonyms=Eapi;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 26-38.
RC TISSUE=Epididymis;
RX PubMed=1417724; DOI=10.1042/bj2860671;
RA Perry A.C.F., Jones R., Barker P.J., Hall L.;
RT "A mammalian epididymal protein with remarkable sequence similarity to
RT snake venom haemorrhagic peptides.";
RL Biochem. J. 286:671-675(1992).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed specifically in the caput region of the
CC epididymis.
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DR EMBL; X66140; CAA46930.1; -; mRNA.
DR PIR; S28259; S28259.
DR RefSeq; NP_064697.1; NM_020301.1.
DR AlphaFoldDB; Q63180; -.
DR SMR; Q63180; -.
DR STRING; 10116.ENSRNOP00000019209; -.
DR MEROPS; M12.956; -.
DR GlyGen; Q63180; 6 sites.
DR PaxDb; Q63180; -.
DR GeneID; 29641; -.
DR KEGG; rno:29641; -.
DR UCSC; RGD:62032; rat.
DR CTD; 8756; -.
DR RGD; 62032; Adam7.
DR eggNOG; KOG3607; Eukaryota.
DR InParanoid; Q63180; -.
DR OrthoDB; 162519at2759; -.
DR PhylomeDB; Q63180; -.
DR PRO; PR:Q63180; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0045177; C:apical part of cell; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0004175; F:endopeptidase activity; ISO:RGD.
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 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:1417724"
FT PROPEP 26..176
FT /evidence="ECO:0000255"
FT /id="PRO_0000029058"
FT CHAIN 177..789
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein 7"
FT /id="PRO_0000029059"
FT TOPO_DOM 177..668
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 669..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 762..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..789
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"
SQ SEQUENCE 789 AA; 89362 MW; EF11E7F1C5EF0779 CRC64;
MFPTGIFLMS VLISQMQGRG IVGVEGQELV HPKKLSLLQK RDLERIHDSD TPEEYEEELL
YEIKLGRKTL TLHLLKAREF LALNYSETYY NIKREMVTRH PQILDHCFYQ GSIIHEFDSA
ASISTCNGLR GFFRVNDQRY LIEPVKYSDE GDHLVFKYNV KAPYATNYSC EGLNFTKKST
LIDAKIIEEH KVEDYHKEKF IELFVVADEF VYRRNSKPQN KLRKRIWGMV NFVNMIYKAL
NIRVTLTGME IWSAGDEIEI VSNLESTLLH FSTWQETVLK KRKDFDHVIL LSGKWLYTSM
QGIAYPGGIC QTLRSCSVVK DLLPDVNIIG NRMAHQLGHS LGMRHDDFPC TCPLGKCVMG
AGSIPAIKFS KCSQTQYQQF LKNQKPACIL NNPLPEEFND YPFCGNKKVD EGEECDCGPV
QECTNPCCDA HKCVLKPGFT CVEGECCESC QMKKEGVICR PAKNECDISE VCTGYSPECP
KDESQANGFP CKNGEGYCFM GLCPTRDDQC AELFSGGAEE SHSLCYRMNQ KGNRFGYCKN
KDNTFVPCEE KDLKCGKIYC TGGRRSAHLG EDKTYNLKNV KQNISIKCKT MFLYHNSRDM
GLVNSGTKCG EGMVCSNGEC IEMEKAYNST ICSSLCDEND VDDNEPDCQC EEGPIITEWG
EALNLTSVSI MVVVLVMVII GVGLVILLIR YQKCIKMKQV QSSSREIRGI ENKVYFPDEH
QTRSEPIFTD IYPLHNTAES LERVPSTFSS PHYITLKSVS KDPRGIADPK QNDNMNLNLD
SQSDCTRLG
