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Disintegrin and metalloproteinase domain-containing protein 7 (ADAM 7) (Epididymal apical protein I) (EAP I)

 ADAM7_RAT               Reviewed;         789 AA.
Q63180;
31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
23-MAY-2018, entry version 111.
RecName: Full=Disintegrin and metalloproteinase domain-containing protein 7;
Short=ADAM 7;
AltName: Full=Epididymal apical protein I;
Short=EAP I;
Flags: Precursor;
Name=Adam7; Synonyms=Eapi;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 26-38.
TISSUE=Epididymis;
PubMed=1417724; DOI=10.1042/bj2860671;
Perry A.C.F., Jones R., Barker P.J., Hall L.;
"A mammalian epididymal protein with remarkable sequence similarity to
snake venom haemorrhagic peptides.";
Biochem. J. 286:671-675(1992).
-!- FUNCTION: May play an important role in male reproduction
including sperm maturation and gonadotrope function. This is a non
catalytic metalloprotease-like protein (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- TISSUE SPECIFICITY: Expressed specifically in the caput region of
the epididymis.
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EMBL; X66140; CAA46930.1; -; mRNA.
PIR; S28259; S28259.
RefSeq; NP_064697.1; NM_020301.1.
UniGene; Rn.10357; -.
ProteinModelPortal; Q63180; -.
SMR; Q63180; -.
STRING; 10116.ENSRNOP00000019209; -.
MEROPS; M12.956; -.
PaxDb; Q63180; -.
PRIDE; Q63180; -.
GeneID; 29641; -.
KEGG; rno:29641; -.
UCSC; RGD:62032; rat.
CTD; 8756; -.
RGD; 62032; Adam7.
eggNOG; KOG3607; Eukaryota.
eggNOG; ENOG410XX2M; LUCA.
HOGENOM; HOG000230883; -.
HOVERGEN; HBG006978; -.
InParanoid; Q63180; -.
KO; K16071; -.
PhylomeDB; Q63180; -.
PRO; PR:Q63180; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0045177; C:apical part of cell; IDA:RGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
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.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Disulfide bond;
Glycoprotein; Membrane; Reference proteome; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 25 {ECO:0000269|PubMed:1417724}.
PROPEP 26 176 {ECO:0000255}.
/FTId=PRO_0000029058.
CHAIN 177 789 Disintegrin and metalloproteinase domain-
containing protein 7.
/FTId=PRO_0000029059.
TOPO_DOM 177 668 Extracellular. {ECO:0000255}.
TRANSMEM 669 689 Helical. {ECO:0000255}.
TOPO_DOM 690 789 Cytoplasmic. {ECO:0000255}.
DOMAIN 199 393 Peptidase M12B. {ECO:0000255|PROSITE-
ProRule:PRU00276}.
DOMAIN 401 487 Disintegrin. {ECO:0000255|PROSITE-
ProRule:PRU00068}.
COMPBIAS 488 668 Cys-rich.
CARBOHYD 84 84 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 167 167 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 174 174 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 583 583 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 628 628 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 664 664 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 310 388 {ECO:0000250}.
DISULFID 350 372 {ECO:0000250}.
DISULFID 352 357 {ECO:0000250}.
DISULFID 459 479 {ECO:0000250}.
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


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