GenomeNet

Database: UniProt
Entry: P70505
LinkDB: P70505
Original site: P70505 
ID   ADAM1_RAT               Reviewed;         789 AA.
AC   P70505;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   16-JAN-2019, entry version 121.
DE   RecName: Full=Disintegrin and metalloproteinase domain-containing protein 1;
DE            Short=ADAM 1;
DE            EC=3.4.24.-;
DE   AltName: Full=Fertilin subunit alpha;
DE   Flags: Precursor;
GN   Name=Adam1; Synonyms=Adam1a, Ftna;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000312|EMBL:CAA69908.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC   STRAIN=Sprague-Dawley; TISSUE=Testis;
RX   PubMed=9358007; DOI=10.1093/molehr/3.9.801;
RA   McLaughlin E.A., Frayne J., Barker H.L., Jury J.A., Jones R.,
RA   Ford W.C.L., Hall L.;
RT   "Cloning and sequence analysis of rat fertilin alpha and beta
RT   - developmental expression, processing and immunolocalization.";
RL   Mol. Hum. Reprod. 3:801-809(1997).
CC   -!- FUNCTION: May be involved in sperm-egg fusion.
CC   -!- SUBUNIT: Heterodimer with ADAM2/fertilin subunit beta.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: In the testis, expressed at all stages of
CC       development. {ECO:0000269|PubMed:9358007}.
DR   EMBL; Y08616; CAA69908.1; -; mRNA.
DR   RefSeq; NP_064463.1; NM_020078.1.
DR   UniGene; Rn.42919; -.
DR   ProteinModelPortal; P70505; -.
DR   SMR; P70505; -.
DR   MEROPS; M12.202; -.
DR   PhosphoSitePlus; P70505; -.
DR   PRIDE; P70505; -.
DR   GeneID; 56777; -.
DR   KEGG; rno:56777; -.
DR   UCSC; RGD:621467; rat.
DR   CTD; 8759; -.
DR   RGD; 621467; Adam1a.
DR   HOVERGEN; HBG006978; -.
DR   InParanoid; P70505; -.
DR   KO; K08607; -.
DR   OrthoDB; 162519at2759; -.
DR   PhylomeDB; P70505; -.
DR   BRENDA; 3.4.24.B8; 5301.
DR   PRO; PR:P70505; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
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; NAS:UniProtKB.
DR   GO; GO:0008584; P:male gonad development; IEP:RGD.
DR   GO; GO:0006508; P:proteolysis; NAS:UniProtKB.
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; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
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; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Hydrolase; Membrane; Metal-binding; Metalloprotease; Protease;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix; Zinc.
FT   SIGNAL        1     68       {ECO:0000255}.
FT   PROPEP       69      ?       {ECO:0000255}.
FT                                /FTId=PRO_0000029036.
FT   CHAIN         ?    789       Disintegrin and metalloproteinase domain-
FT                                containing protein 1.
FT                                /FTId=PRO_0000029037.
FT   TOPO_DOM      ?    742       Extracellular. {ECO:0000255}.
FT   TRANSMEM    743    763       Helical. {ECO:0000255}.
FT   TOPO_DOM    764    789       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      238    432       Peptidase M12B. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00276}.
FT   DOMAIN      441    525       Disintegrin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00068}.
FT   DOMAIN      666    700       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   COMPBIAS    526    660       Cys-rich.
FT   ACT_SITE    374    374       {ECO:0000255|PROSITE-ProRule:PRU00276,
FT                                ECO:0000255|PROSITE-ProRule:PRU10095}.
FT   METAL       373    373       Zinc; catalytic. {ECO:0000250}.
FT   METAL       377    377       Zinc; catalytic. {ECO:0000250}.
FT   METAL       383    383       Zinc; catalytic. {ECO:0000250}.
FT   CARBOHYD    259    259       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    410    410       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    633    633       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    720    720       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    348    427       {ECO:0000250}.
FT   DISULFID    388    411       {ECO:0000250}.
FT   DISULFID    390    396       {ECO:0000250}.
FT   DISULFID    497    517       {ECO:0000250}.
FT   DISULFID    670    682       {ECO:0000255}.
FT   DISULFID    676    688       {ECO:0000255}.
FT   DISULFID    690    699       {ECO:0000255}.
SQ   SEQUENCE   789 AA;  86140 MW;  840A43110A4CDEE1 CRC64;
     MSVAASASRS ASTLCSPQIQ QGALKEAKVP PHIWAARHWN LGLRLVPGHA SVRAGILVLL
     IFLPSTLCDL GSVYDSSYET VIPERLPGQG SDDPGGKVSY VLLMQGQKQL LHLEVKGHYS
     ERNFPVYSYH HGILGQEVPL LSQACHYEGH IEGVPGSFVS VSICSGLRGV LIKEETAYGI
     EPLLFSTDFE HILYTMAHQP VVLCNVTPTD SLGDSSQRQG SSKTDELLAL SDLWSHAKYV
     EMFVVVNHQR FQMWGSDVNT TVQAVVDIIA LANSFTRGIN TEVVLVGLEI WTEGDPIEVP
     VDLQATLRNF NLWRQEKLMG RVRHDVAHLI VGHRPGANEG QAFLDGACSG GFAAAVEAFH
     HEDVLLFAAL MAHELGHNLG IRHDRPGCTC GPKHLCLMHE TISKTSGFSN CSSDHFLRFL
     HDHRGACLLD RPWHQSHKRR DAHCGNGVVE ESEECDCGNA CDSHPCCEPT CTLKVGAQCS
     EGLCCYKCTF KKKGTLCRPA EDVCDLPEYC NGITGECPAN SYMQDGTQCD RIYYCSGGLC
     KNPDKQCARI YGYPARSAPE ECYISVNTKA NRFGNCGHPT SANLKYEACS NEDIFCGKLV
     CTDVRYLPQV KPLHSLLQIP YGDDWCWSMD AYNVTDIPDY GDVQGGTYCA PKKVCMESIC
     TGHATLQYDC HPQEMCHGNG VCNNFKHCHC DAGFSPPDCS SGGNGGSVDS GPVGKPADRN
     LSLFGVGESP DSRMEDEEIN LKVVVLVVPI FLIVLLCCLM LIAYLWSEVQ EAVSPGSSST
     TSSSESESD
//
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