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Database: UniProt
Entry: O77780
LinkDB: O77780
Original site: O77780 
ID   ADAM2_BOVIN             Reviewed;         745 AA.
AC   O77780;
DT   01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   10-APR-2019, entry version 114.
DE   RecName: Full=Disintegrin and metalloproteinase domain-containing protein 2;
DE            Short=ADAM 2;
DE   AltName: Full=Fertilin subunit beta;
DE   AltName: Full=PH-30;
DE            Short=PH30;
DE   AltName: Full=PH30-beta;
DE   Flags: Precursor;
GN   Name=ADAM2; Synonyms=FTNB;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RX   PubMed=9160725; DOI=10.1095/biolreprod56.5.1245;
RA   Waters S.I., White J.M.;
RT   "Biochemical and molecular characterization of bovine fertilin alpha
RT   and beta (ADAM 1 and ADAM 2): a candidate sperm-egg binding/fusion
RT   complex.";
RL   Biol. Reprod. 56:1245-1254(1997).
CC   -!- FUNCTION: Sperm surface membrane protein that may be involved in
CC       sperm-egg plasma membrane adhesion and fusion during
CC       fertilization. Could have a direct role in sperm-zona binding or
CC       migration of sperm from the uterus into the oviduct. Interactions
CC       with egg membrane could be mediated via binding between its
CC       disintegrin-like domain to one or more integrins receptors on the
CC       egg. This is a non catalytic metalloprotease-like protein (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer with ADAM1/fertilin subunit alpha.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Expressed specifically in testis.
CC   -!- DOMAIN: A tripeptide motif (TDE) within disintegrin-like domain
CC       could be involved in the binding to egg integrin receptor and thus
CC       could mediate sperm/egg binding. {ECO:0000250}.
CC   -!- PTM: The signal and the metalloprotease domain are cleaved during
CC       the epididymal maturation of the spermatozoa. {ECO:0000250}.
DR   EMBL; AF086808; AAC62753.1; -; mRNA.
DR   RefSeq; NP_776653.1; NM_174228.1.
DR   UniGene; Bt.139; -.
DR   ProteinModelPortal; O77780; -.
DR   SMR; O77780; -.
DR   STRING; 9913.ENSBTAP00000012384; -.
DR   MEROPS; M12.950; -.
DR   PRIDE; O77780; -.
DR   GeneID; 281599; -.
DR   KEGG; bta:281599; -.
DR   CTD; 2515; -.
DR   HOGENOM; HOG000230883; -.
DR   HOVERGEN; HBG103628; -.
DR   InParanoid; O77780; -.
DR   KO; K06833; -.
DR   OrthoDB; 162519at2759; -.
DR   Proteomes; UP000009136; 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:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0007338; P:single fertilization; 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; IPR033958; ADAM2.
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   PANTHER; PTHR11905:SF108; PTHR11905:SF108; 1.
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; PS50026; EGF_3; 1.
PE   2: Evidence at transcript level;
KW   Cell adhesion; Complete proteome; Disulfide bond; EGF-like domain;
KW   Glycoprotein; Membrane; Phosphoprotein; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     16       {ECO:0000255}.
FT   PROPEP       17    174       {ECO:0000250}.
FT                                /FTId=PRO_0000029038.
FT   CHAIN       175    745       Disintegrin and metalloproteinase domain-
FT                                containing protein 2.
FT                                /FTId=PRO_0000029039.
FT   TOPO_DOM     17    696       Extracellular. {ECO:0000255}.
FT   TRANSMEM    697    717       Helical. {ECO:0000255}.
FT   TOPO_DOM    718    745       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      178    375       Peptidase M12B. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00276}.
FT   DOMAIN      383    472       Disintegrin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00068}.
FT   DOMAIN      611    644       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   COMPBIAS    148    151       Poly-Ser.
FT   COMPBIAS    475    605       Cys-rich.
FT   MOD_RES     739    739       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q60718}.
FT   CARBOHYD    122    122       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    220    220       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    353    353       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    458    458       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    558    558       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    287    370       {ECO:0000250}.
FT   DISULFID    329    354       {ECO:0000250}.
FT   DISULFID    331    336       {ECO:0000250}.
FT   DISULFID    444    457       {ECO:0000255}.
FT   DISULFID    615    626       {ECO:0000250}.
FT   DISULFID    620    632       {ECO:0000250}.
FT   DISULFID    634    643       {ECO:0000250}.
SQ   SEQUENCE   745 AA;  83150 MW;  B5D8DC0168999B00 CRC64;
     MLCLLFLLLG LTGLQTDDNS ERLRVQFTVP EKIRSTSSGG VETHVSYIIL IEGKTYTVNL
     MQKAFLPHNF RVYGYSGTGS MKPLEHEFQN FCYYQGYIEG YPNSMAIIST CTGLRGLLQF
     ENVSYGIEPL EPSIGFEHMV YQIKPRDSSS SVYTEREIEL REKPYKIQNV EPLPDFSQYI
     EMHIVVEKDL YNHMGADTTV VIQKIFQLTG LTNAIFTSLN ITVILSSLEL WIDENKIPVT
     GDANELLHRF VKWKRSYLVL RPHDMAFLLV YREKSNYIGA TFQGRMCDKH YGGGVALHSS
     TISLESLAVI IAQLLSLSMG IPYDDINKCH CPGDVCIMNP AAVHSSGVKL FSNCSVEDFL
     RFISKPKSQC LQNQPRLDPT YKSAVCGNGK VEEGEQCDCG NKKACDALPD TCCVADTCRF
     QPGSACDTGL CCESCAFIPK GHICRGSTDE CDLHEYCNGS SAACQEDVYV QDGHPCGQNQ
     WLCISGICVD GIKQCFDIFG EGTSYAPAEC FQRLNSMNDL SGNCGVTPTG FTPCTSENVR
     CGKLLCTYDK REVISVENAS VMYSNINGKI CIGLHYEYGN EDEGMMWVKD GTVCGESKIC
     QNKQCVDSSF LNYDCNPEKC NNQGVCNNKK HCHCNPSYLP PNCEHSAPGW EGGSIDSGNF
     PPSEPPTGGP AFTDVGTTPL AESRYIENVY RSKPTRWPFF LFIPFFIILC VLIATLVKVY
     FQRKKWRTED YTSDEQLESE SEPKD
//
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