GenomeNet

Database: UniProt
Entry: Q99965
LinkDB: Q99965
Original site: Q99965 
ID   ADAM2_HUMAN             Reviewed;         735 AA.
AC   Q99965; P78326; Q9UQQ8;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2003, sequence version 2.
DT   13-FEB-2019, entry version 166.
DE   RecName: Full=Disintegrin and metalloproteinase domain-containing protein 2;
DE            Short=ADAM 2;
DE   AltName: Full=Cancer/testis antigen 15;
DE            Short=CT15;
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   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Testis;
RX   PubMed=9041139;
RX   DOI=10.1002/(SICI)1098-2795(199703)46:3<363::AID-MRD15>3.0.CO;2-#;
RA   Vidaeus C.M., von Kap-Herr C., Golden W.L., Eddy R.L., Shows T.B.,
RA   Herr J.C.;
RT   "Human fertilin beta: identification, characterization, and
RT   chromosomal mapping of an ADAM gene family member.";
RL   Mol. Reprod. Dev. 46:363-369(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Testis;
RX   PubMed=8702389; DOI=10.1006/bbrc.1996.1027;
RA   Gupta S.K., Alves K., Palladino L.O., Mark G.E., Hollis G.F.;
RT   "Molecular cloning of the human fertilin beta subunit.";
RL   Biochem. Biophys. Res. Commun. 224:318-326(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Testis;
RX   PubMed=9070941; DOI=10.1006/geno.1996.4531;
RA   Burkin H.R., Burkin D.J., Davey P.M., Griffin D.K., Affara N.A.;
RT   "Mapping, sequence, and expression analysis of the human fertilin beta
RT   gene (FTNB).";
RL   Genomics 40:190-192(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Testis;
RA   Hall L., Frayne J.;
RT   "Nucleotide sequence of the human fertilin beta transcript.";
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q99965-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q99965-2; Sequence=VSP_005471;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Expressed specifically in spermatogenic cells
CC       in the seminiferous cells. Not detected in fetal tissues.
CC   -!- DOMAIN: A tripeptide motif (FEE) within disintegrin-like domain
CC       could be involved in the binding to egg integrin receptor and thus
CC       could mediate sperm/egg binding.
CC   -!- PTM: The prodomain and the metalloprotease domain are cleaved
CC       during the epididymal maturation of the spermatozoa.
CC   -!- MISCELLANEOUS: In mammals, exists as a heterodimer composed of an
CC       alpha and beta subunits. In human, fertilin subunit alpha is a
CC       pseudogene.
DR   EMBL; U52370; AAC51110.1; -; mRNA.
DR   EMBL; U38805; AAD04206.1; -; mRNA.
DR   EMBL; X99374; CAA67753.1; -; mRNA.
DR   EMBL; AJ133005; CAB40813.1; -; mRNA.
DR   EMBL; BC034957; AAH34957.1; -; mRNA.
DR   CCDS; CCDS34884.1; -. [Q99965-1]
DR   CCDS; CCDS64882.1; -. [Q99965-2]
DR   PIR; JC4861; JC4861.
DR   RefSeq; NP_001265042.1; NM_001278113.1. [Q99965-2]
DR   RefSeq; NP_001265043.1; NM_001278114.1.
DR   RefSeq; NP_001455.3; NM_001464.4. [Q99965-1]
DR   UniGene; Hs.177959; -.
DR   ProteinModelPortal; Q99965; -.
DR   SMR; Q99965; -.
DR   BioGrid; 108791; 10.
DR   STRING; 9606.ENSP00000265708; -.
DR   MEROPS; M12.950; -.
DR   iPTMnet; Q99965; -.
DR   PhosphoSitePlus; Q99965; -.
DR   BioMuta; ADAM2; -.
DR   DMDM; 28202251; -.
DR   REPRODUCTION-2DPAGE; Q99965; -.
DR   PaxDb; Q99965; -.
DR   PeptideAtlas; Q99965; -.
DR   PRIDE; Q99965; -.
DR   ProteomicsDB; 78551; -.
DR   ProteomicsDB; 78552; -. [Q99965-2]
DR   DNASU; 2515; -.
DR   Ensembl; ENST00000265708; ENSP00000265708; ENSG00000104755. [Q99965-1]
DR   Ensembl; ENST00000347580; ENSP00000343854; ENSG00000104755. [Q99965-2]
DR   Ensembl; ENST00000613160; ENSP00000484999; ENSG00000276286. [Q99965-2]
DR   Ensembl; ENST00000620181; ENSP00000482337; ENSG00000276286. [Q99965-1]
DR   GeneID; 2515; -.
DR   KEGG; hsa:2515; -.
DR   UCSC; uc003xnj.5; human. [Q99965-1]
DR   CTD; 2515; -.
DR   DisGeNET; 2515; -.
DR   EuPathDB; HostDB:ENSG00000104755.14; -.
DR   GeneCards; ADAM2; -.
DR   H-InvDB; HIX0025571; -.
DR   HGNC; HGNC:198; ADAM2.
DR   HPA; CAB022390; -.
DR   HPA; HPA024621; -.
DR   HPA; HPA026581; -.
DR   MIM; 601533; gene.
DR   neXtProt; NX_Q99965; -.
DR   OpenTargets; ENSG00000104755; -.
DR   PharmGKB; PA24515; -.
DR   eggNOG; KOG3607; Eukaryota.
DR   eggNOG; ENOG410XX2M; LUCA.
DR   GeneTree; ENSGT00940000161961; -.
DR   HOGENOM; HOG000230883; -.
DR   HOVERGEN; HBG103628; -.
DR   InParanoid; Q99965; -.
DR   KO; K06833; -.
DR   OMA; WPFFLLI; -.
DR   OrthoDB; 162519at2759; -.
DR   PhylomeDB; Q99965; -.
DR   TreeFam; TF314733; -.
DR   Reactome; R-HSA-1300644; Interaction With The Zona Pellucida.
DR   ChiTaRS; ADAM2; human.
DR   GeneWiki; ADAM2; -.
DR   GenomeRNAi; 2515; -.
DR   PRO; PR:Q99965; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   Bgee; ENSG00000104755; Expressed in 28 organ(s), highest expression level in testis.
DR   ExpressionAtlas; Q99965; baseline and differential.
DR   Genevisible; Q99965; HS.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR   GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR   GO; GO:0005178; F:integrin binding; TAS:ProtInc.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008237; F:metallopeptidase activity; TAS:ProtInc.
DR   GO; GO:0030534; P:adult behavior; IEA:Ensembl.
DR   GO; GO:0007339; P:binding of sperm to zona pellucida; TAS:Reactome.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0007342; P:fusion of sperm to egg plasma membrane involved in single fertilization; TAS:ProtInc.
DR   GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0008542; P:visual learning; IEA:Ensembl.
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; 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.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell adhesion; Complete proteome;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Membrane;
KW   Phosphoprotein; Polymorphism; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     16       {ECO:0000255}.
FT   PROPEP       17    174
FT                                /FTId=PRO_0000029042.
FT   CHAIN       175    735       Disintegrin and metalloproteinase domain-
FT                                containing protein 2.
FT                                /FTId=PRO_0000029043.
FT   TOPO_DOM    175    686       Extracellular. {ECO:0000255}.
FT   TRANSMEM    687    707       Helical. {ECO:0000255}.
FT   TOPO_DOM    708    735       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      178    375       Peptidase M12B. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00276}.
FT   DOMAIN      384    473       Disintegrin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00068}.
FT   DOMAIN      612    645       EGF-like.
FT   COMPBIAS    477    606       Cys-rich.
FT   MOD_RES     729    729       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    459    459       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    566    566       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    445    465       {ECO:0000250}.
FT   DISULFID    616    627       {ECO:0000250}.
FT   DISULFID    621    633       {ECO:0000250}.
FT   DISULFID    635    644       {ECO:0000250}.
FT   VAR_SEQ     172    190       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_005471.
FT   VARIANT      10     10       G -> W (in dbSNP:rs34800519).
FT                                /FTId=VAR_035217.
FT   CONFLICT      3      3       Missing (in Ref. 2; AAD04206).
FT                                {ECO:0000305}.
FT   CONFLICT     21     21       D -> H (in Ref. 3; CAA67753).
FT                                {ECO:0000305}.
FT   CONFLICT     99     99       E -> D (in Ref. 3; CAA67753).
FT                                {ECO:0000305}.
FT   CONFLICT    106    106       V -> G (in Ref. 3; CAA67753).
FT                                {ECO:0000305}.
FT   CONFLICT    170    170       V -> A (in Ref. 2; AAD04206).
FT                                {ECO:0000305}.
FT   CONFLICT    288    288       D -> H (in Ref. 1; AAC51110).
FT                                {ECO:0000305}.
FT   CONFLICT    321    321       I -> T (in Ref. 1; AAC51110).
FT                                {ECO:0000305}.
FT   CONFLICT    388    388       G -> S (in Ref. 3; CAA67753).
FT                                {ECO:0000305}.
FT   CONFLICT    396    398       EEC -> DEF (in Ref. 3; CAA67753).
FT                                {ECO:0000305}.
FT   CONFLICT    501    501       G -> S (in Ref. 3; CAA67753).
FT                                {ECO:0000305}.
FT   CONFLICT    529    529       D -> Y (in Ref. 3; CAA67753).
FT                                {ECO:0000305}.
FT   CONFLICT    579    579       S -> G (in Ref. 3; CAA67753).
FT                                {ECO:0000305}.
FT   CONFLICT    588    588       W -> L (in Ref. 3; CAA67753).
FT                                {ECO:0000305}.
FT   CONFLICT    603    603       N -> D (in Ref. 3; CAA67753).
FT                                {ECO:0000305}.
FT   CONFLICT    629    630       NK -> KQ (in Ref. 3; CAA67753).
FT                                {ECO:0000305}.
FT   CONFLICT    638    638       S -> F (in Ref. 3; CAA67753).
FT                                {ECO:0000305}.
SQ   SEQUENCE   735 AA;  82457 MW;  92867B5340BEE01F CRC64;
     MWRVLFLLSG LGGLRMDSNF DSLPVQITVP EKIRSIIKEG IESQASYKIV IEGKPYTVNL
     MQKNFLPHNF RVYSYSGTGI MKPLDQDFQN FCHYQGYIEG YPKSVVMVST CTGLRGVLQF
     ENVSYGIEPL ESSVGFEHVI YQVKHKKADV SLYNEKDIES RDLSFKLQSV EPQQDFAKYI
     EMHVIVEKQL YNHMGSDTTV VAQKVFQLIG LTNAIFVSFN ITIILSSLEL WIDENKIATT
     GEANELLHTF LRWKTSYLVL RPHDVAFLLV YREKSNYVGA TFQGKMCDAN YAGGVVLHPR
     TISLESLAVI LAQLLSLSMG ITYDDINKCQ CSGAVCIMNP EAIHFSGVKI FSNCSFEDFA
     HFISKQKSQC LHNQPRLDPF FKQQAVCGNA KLEAGEECDC GTEQDCALIG ETCCDIATCR
     FKAGSNCAEG PCCENCLFMS KERMCRPSFE ECDLPEYCNG SSASCPENHY VQTGHPCGLN
     QWICIDGVCM SGDKQCTDTF GKEVEFGPSE CYSHLNSKTD VSGNCGISDS GYTQCEADNL
     QCGKLICKYV GKFLLQIPRA TIIYANISGH LCIAVEFASD HADSQKMWIK DGTSCGSNKV
     CRNQRCVSSS YLGYDCTTDK CNDRGVCNNK KHCHCSASYL PPDCSVQSDL WPGGSIDSGN
     FPPVAIPARL PERRYIENIY HSKPMRWPFF LFIPFFIIFC VLIAIMVKVN FQRKKWRTED
     YSSDEQPESE SEPKG
//
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