ADAM2_HUMAN
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 03-AUG-2022, entry version 183.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 chromosomal
RT 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 gene
RT (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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Sperm surface membrane protein that may be involved in sperm-
CC egg plasma membrane adhesion and fusion during fertilization. Could
CC have a direct role in sperm-zona binding or migration of sperm from the
CC uterus into the oviduct. Interactions with egg membrane could be
CC mediated via binding between its disintegrin-like domain to one or more
CC integrins receptors on the egg. This is a non catalytic
CC metalloprotease-like protein.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane 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 -!- TISSUE SPECIFICITY: Expressed specifically in spermatogenic cells in
CC the seminiferous cells. Not detected in fetal tissues.
CC -!- DOMAIN: A tripeptide motif (FEE) within disintegrin-like domain could
CC be involved in the binding to egg integrin receptor and thus could
CC mediate sperm/egg binding.
CC -!- PTM: The prodomain and the metalloprotease domain are cleaved during
CC the epididymal maturation of the spermatozoa.
CC -!- MISCELLANEOUS: In mammals, exists as a heterodimer composed of an alpha
CC and beta subunits. In human, fertilin subunit alpha is a pseudogene.
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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 AlphaFoldDB; Q99965; -.
DR SMR; Q99965; -.
DR BioGRID; 108791; 11.
DR IntAct; Q99965; 7.
DR STRING; 9606.ENSP00000265708; -.
DR MEROPS; M12.950; -.
DR GlyGen; Q99965; 5 sites.
DR iPTMnet; Q99965; -.
DR PhosphoSitePlus; Q99965; -.
DR BioMuta; ADAM2; -.
DR DMDM; 28202251; -.
DR REPRODUCTION-2DPAGE; Q99965; -.
DR MassIVE; Q99965; -.
DR PaxDb; Q99965; -.
DR PeptideAtlas; Q99965; -.
DR PRIDE; Q99965; -.
DR ProteomicsDB; 78551; -. [Q99965-1]
DR ProteomicsDB; 78552; -. [Q99965-2]
DR Antibodypedia; 11200; 212 antibodies from 31 providers.
DR DNASU; 2515; -.
DR Ensembl; ENST00000265708.9; ENSP00000265708.4; ENSG00000104755.16. [Q99965-1]
DR Ensembl; ENST00000347580.8; ENSP00000343854.4; ENSG00000104755.16. [Q99965-2]
DR Ensembl; ENST00000613160.4; ENSP00000484999.1; ENSG00000276286.4. [Q99965-2]
DR Ensembl; ENST00000620181.4; ENSP00000482337.1; ENSG00000276286.4. [Q99965-1]
DR GeneID; 2515; -.
DR KEGG; hsa:2515; -.
DR MANE-Select; ENST00000265708.9; ENSP00000265708.4; NM_001464.5; NP_001455.3.
DR UCSC; uc003xnj.5; human. [Q99965-1]
DR CTD; 2515; -.
DR DisGeNET; 2515; -.
DR GeneCards; ADAM2; -.
DR HGNC; HGNC:198; ADAM2.
DR HPA; ENSG00000104755; Tissue enriched (testis).
DR MIM; 601533; gene.
DR neXtProt; NX_Q99965; -.
DR OpenTargets; ENSG00000104755; -.
DR PharmGKB; PA24515; -.
DR VEuPathDB; HostDB:ENSG00000104755; -.
DR eggNOG; KOG3607; Eukaryota.
DR GeneTree; ENSGT00940000161961; -.
DR InParanoid; Q99965; -.
DR OMA; FCYYQGH; -.
DR OrthoDB; 162519at2759; -.
DR PhylomeDB; Q99965; -.
DR TreeFam; TF314733; -.
DR PathwayCommons; Q99965; -.
DR Reactome; R-HSA-2534343; Interaction With Cumulus Cells And The Zona Pellucida.
DR SignaLink; Q99965; -.
DR BioGRID-ORCS; 2515; 19 hits in 1066 CRISPR screens.
DR ChiTaRS; ADAM2; human.
DR GeneWiki; ADAM2; -.
DR GenomeRNAi; 2515; -.
DR Pharos; Q99965; Tbio.
DR PRO; PR:Q99965; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q99965; protein.
DR Bgee; ENSG00000104755; Expressed in testis and 26 other tissues.
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; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
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:0006508; P:proteolysis; IEA:InterPro.
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; Disulfide bond; EGF-like domain;
KW Glycoprotein; Membrane; Phosphoprotein; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT PROPEP 17..174
FT /id="PRO_0000029042"
FT CHAIN 175..735
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein 2"
FT /id="PRO_0000029043"
FT TOPO_DOM 175..686
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 687..707
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 708..735
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 178..375
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 384..473
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DOMAIN 612..645
FT /note="EGF-like"
FT MOD_RES 729
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60718"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 459
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 566
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 287..370
FT /evidence="ECO:0000250"
FT DISULFID 329..354
FT /evidence="ECO:0000250"
FT DISULFID 331..336
FT /evidence="ECO:0000250"
FT DISULFID 445..465
FT /evidence="ECO:0000250"
FT DISULFID 616..627
FT /evidence="ECO:0000250"
FT DISULFID 621..633
FT /evidence="ECO:0000250"
FT DISULFID 635..644
FT /evidence="ECO:0000250"
FT VAR_SEQ 172..190
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_005471"
FT VARIANT 10
FT /note="G -> W (in dbSNP:rs34800519)"
FT /id="VAR_035217"
FT CONFLICT 3
FT /note="Missing (in Ref. 2; AAD04206)"
FT /evidence="ECO:0000305"
FT CONFLICT 21
FT /note="D -> H (in Ref. 3; CAA67753)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="E -> D (in Ref. 3; CAA67753)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="V -> G (in Ref. 3; CAA67753)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="V -> A (in Ref. 2; AAD04206)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="D -> H (in Ref. 1; AAC51110)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="I -> T (in Ref. 1; AAC51110)"
FT /evidence="ECO:0000305"
FT CONFLICT 388
FT /note="G -> S (in Ref. 3; CAA67753)"
FT /evidence="ECO:0000305"
FT CONFLICT 396..398
FT /note="EEC -> DEF (in Ref. 3; CAA67753)"
FT /evidence="ECO:0000305"
FT CONFLICT 501
FT /note="G -> S (in Ref. 3; CAA67753)"
FT /evidence="ECO:0000305"
FT CONFLICT 529
FT /note="D -> Y (in Ref. 3; CAA67753)"
FT /evidence="ECO:0000305"
FT CONFLICT 579
FT /note="S -> G (in Ref. 3; CAA67753)"
FT /evidence="ECO:0000305"
FT CONFLICT 588
FT /note="W -> L (in Ref. 3; CAA67753)"
FT /evidence="ECO:0000305"
FT CONFLICT 603
FT /note="N -> D (in Ref. 3; CAA67753)"
FT /evidence="ECO:0000305"
FT CONFLICT 629..630
FT /note="NK -> KQ (in Ref. 3; CAA67753)"
FT /evidence="ECO:0000305"
FT CONFLICT 638
FT /note="S -> F (in Ref. 3; CAA67753)"
FT /evidence="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
