GenomeNet

Database: UniProt
Entry: Q63202
LinkDB: Q63202
Original site: Q63202 
ID   ADAM2_RAT               Reviewed;         737 AA.
AC   Q63202;
DT   01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2003, sequence version 2.
DT   16-JAN-2019, entry version 132.
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   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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
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).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-731, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
RA   Lundby C., Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14
RT   different rat organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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   -!- DOMAIN: A tripeptide motif (NQE) 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 prodomain and the metalloprotease domain are cleaved
CC       during the epididymal maturation of the spermatozoa.
CC       {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA68127.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; X99794; CAA68127.1; ALT_INIT; mRNA.
DR   RefSeq; NP_064462.1; NM_020077.1.
DR   UniGene; Rn.42917; -.
DR   ProteinModelPortal; Q63202; -.
DR   STRING; 10116.ENSRNOP00000061122; -.
DR   MEROPS; M12.950; -.
DR   iPTMnet; Q63202; -.
DR   PhosphoSitePlus; Q63202; -.
DR   PaxDb; Q63202; -.
DR   PRIDE; Q63202; -.
DR   GeneID; 56806; -.
DR   KEGG; rno:56806; -.
DR   UCSC; RGD:69299; rat.
DR   CTD; 2515; -.
DR   RGD; 69299; Adam2.
DR   eggNOG; KOG3607; Eukaryota.
DR   eggNOG; ENOG410XX2M; LUCA.
DR   HOGENOM; HOG000230883; -.
DR   HOVERGEN; HBG103628; -.
DR   InParanoid; Q63202; -.
DR   KO; K06833; -.
DR   OrthoDB; 162519at2759; -.
DR   PhylomeDB; Q63202; -.
DR   PRO; PR:Q63202; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0001669; C:acrosomal vesicle; IDA:RGD.
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:0008584; P:male gonad development; IEP:RGD.
DR   GO; GO:0007338; P:single fertilization; IEA:InterPro.
DR   GO; GO:0007283; P:spermatogenesis; IEP:RGD.
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   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   1: Evidence at protein 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     18       {ECO:0000255}.
FT   PROPEP       19    180       {ECO:0000250}.
FT                                /FTId=PRO_0000029050.
FT   CHAIN       181    737       Disintegrin and metalloproteinase domain-
FT                                containing protein 2.
FT                                /FTId=PRO_0000029051.
FT   TOPO_DOM     19    688       Extracellular. {ECO:0000255}.
FT   TRANSMEM    689    709       Helical. {ECO:0000255}.
FT   TOPO_DOM    710    737       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      184    381       Peptidase M12B. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00276}.
FT   DOMAIN      389    478       Disintegrin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00068}.
FT   DOMAIN      617    650       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   COMPBIAS    482    616       Cys-rich.
FT   MOD_RES     731    731       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   CARBOHYD    128    128       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    226    226       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    359    359       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    464    464       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    491    491       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    571    571       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    293    376       {ECO:0000250}.
FT   DISULFID    335    360       {ECO:0000250}.
FT   DISULFID    337    342       {ECO:0000250}.
FT   DISULFID    450    470       {ECO:0000250}.
FT   DISULFID    621    632       {ECO:0000250}.
FT   DISULFID    626    638       {ECO:0000250}.
FT   DISULFID    640    649       {ECO:0000250}.
SQ   SEQUENCE   737 AA;  82311 MW;  647E92A90D7CC1D1 CRC64;
     MWLLLLLLSG LSRLGGLSEP QTEGTREKLH VQVTVPEKIR SITSEGYETQ VTYSLKIEGK
     TYILNLMQKA FLPPNFRVYS YDSTGIMRPL EQKFQNICYF QGYIEGYPNS MVIVSTCTGL
     RGVLQFGNVS YGIEPLESSS GFEHVIYQVE PKKGDTLLYA EKDMDLRDPQ YKIRSIKPQR
     TVSHYLEIHI VVEKQMFEHI GADTAVVTQK IFQLIGLTNA IFAPFNLTVI LSSLEFWMDE
     NKISTTGDAN KLLYRFLKWK QSYLVLRPHD MAFLLVYRDT TDYVGATYQG KMCDKNYAGG
     VALHPKAVTL ESLAIILVQL LSLSMGVAYD DVNTCQCGVP ICVMNPEALH SSGVRSFSNC
     SMEDFSKFIV SQSSHCLQNQ PHLQPSYKMA VCGNGELEEG EVCDCGQEGC DDKPPPCCNP
     TTCQLSEGST CSTGSCCDAS CNLKAKGELC RPANQECDVT EYCNGTSEVC EEDFFVQDGH
     PCAEQKWICI NGTCQSGAQQ CRDLFGTDAD YGTKECYSEL NSKSDISGSC GITPTGYKDC
     APNDRMCGKL ICIYQSEDIL KMRSAIVIYA NISGQICISL EYPPGHKESK KMCVRDGTVC
     GSGKVCLNQE CVEDTFLNYD CTPEKCNHHG VCNNKKHCHC EPTYLPPDCK NTEDTWPGGS
     VDSGNQQRAE SIPARSYVAS AYRSKSARWP FFLIIPFYVV ILVLIGMLVK VYSQRKKWRM
     DDFSSEEQFE SESESKD
//
DBGET integrated database retrieval system