ADAM1_RAT
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 03-AUG-2022, entry version 131.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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., Ford W.C.L.,
RA 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}.
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DR EMBL; Y08616; CAA69908.1; -; mRNA.
DR RefSeq; NP_064463.1; NM_020078.1.
DR AlphaFoldDB; P70505; -.
DR SMR; P70505; -.
DR MEROPS; M12.203; -.
DR GlyGen; P70505; 4 sites.
DR PhosphoSitePlus; P70505; -.
DR GeneID; 56777; -.
DR KEGG; rno:56777; -.
DR UCSC; RGD:621467; rat.
DR CTD; 8759; -.
DR RGD; 621467; Adam1a.
DR InParanoid; P70505; -.
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:0045121; C:membrane raft; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:0007339; P:binding of sperm to zona pellucida; ISO:RGD.
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; 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 Disulfide bond; EGF-like domain; Glycoprotein; Hydrolase; Membrane;
KW Metal-binding; Metalloprotease; Protease; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Zinc.
FT SIGNAL 1..68
FT /evidence="ECO:0000255"
FT PROPEP 69..?
FT /evidence="ECO:0000255"
FT /id="PRO_0000029036"
FT CHAIN ?..789
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein 1"
FT /id="PRO_0000029037"
FT TOPO_DOM ?..742
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 743..763
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 764..789
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 238..432
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 441..525
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DOMAIN 666..700
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT ACT_SITE 374
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 373
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 377
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 383
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 633
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 720
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 348..427
FT /evidence="ECO:0000250"
FT DISULFID 388..411
FT /evidence="ECO:0000250"
FT DISULFID 390..396
FT /evidence="ECO:0000250"
FT DISULFID 497..517
FT /evidence="ECO:0000250"
FT DISULFID 670..682
FT /evidence="ECO:0000255"
FT DISULFID 676..688
FT /evidence="ECO:0000255"
FT DISULFID 690..699
FT /evidence="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
