ADAM7_MACFA
ID ADAM7_MACFA Reviewed; 776 AA.
AC Q28475;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 98.
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 Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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. Not detectable in the testis.
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DR EMBL; X66139; CAA46929.1; -; mRNA.
DR PIR; S28258; S28258.
DR AlphaFoldDB; Q28475; -.
DR SMR; Q28475; -.
DR STRING; 9541.XP_005562913.1; -.
DR MEROPS; M12.956; -.
DR eggNOG; KOG3607; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
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_0000029054"
FT CHAIN 177..776
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein 7"
FT /id="PRO_0000029055"
FT TOPO_DOM 26..669
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 670..690
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 691..776
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 199..394
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 402..488
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT REGION 757..776
FT /note="Disordered"
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 584
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 629
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 665
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 310..389
FT /evidence="ECO:0000250"
FT DISULFID 350..373
FT /evidence="ECO:0000250"
FT DISULFID 352..357
FT /evidence="ECO:0000250"
FT DISULFID 460..480
FT /evidence="ECO:0000250"
SQ SEQUENCE 776 AA; 88362 MW; 0208E8C9A8A28C10 CRC64;
MLPGCIFLMI LLILQVKEKV ILGVEGQQLV YPKKLPLMQK RDIGHTHDDD IEETYEEELM
YEIKLNRKTL VLHLLRSREF LGSNYSETFY SMKGEAFTRH LQIMDHCFYQ GSIVHEYDSA
ASISTCNGLR GFFRVNDQRY LIEPVKYSDE GEHLVFKYNP RVPYVANYSC TELNFTRKTV
PGDTESEGDP KMKAIHNEKY IELFIVADDT VYRRNSHPHN KLRNRIWGMV NFVNMIYKTL
NIHVTLVGIE IWTHEDKIEL HSNIETTLLR FSSWQERILK TRKDFDHVVL LSGKWIYTHV
QGISYPAGMC LPYYSTSIIK DLLPDTNIIA NRMAHQLGHN LGMQHDEFPC TCPSGKCVMD
SDGSIPALKF SKCSQNQYHQ YLKDYKPTCM LNIPFPCNFD DFQFCGNKKL DEGEECDCGP
PQECTNPCCD AHTCVLKPGF TCAEGECCES CQIKKAGSIC RPAEDECDFP EMCTGHSPAC
PKDQFRVNGF PCKNSEGYCF MGKCPTRRDQ CSELFDDEAT ESHDICYKMN TKGNKFGYCK
NKENRFLPCE EKDVRCGKIY CTGGELSYLL GEDKTYHLKD PQQNATVKCK TIFLYHDSTD
IGLVASGTKC GDGMVCNNGE CLNMEKVYNS TNCPSQCHEN PMDDHGLQCH CEEGQAPVAW
EETLNVTNVA ILIVVLVLVI VGIGVLILLI RYQKCIKLKQ VQSPPIETLG VENKGYFGDE
QQMRTEPILP EIHFLNQRTP ESLESLPTSF SSPHYITLKP ASKDSRGIAD PNQSAK
