GenomeNet

Database: UniProt
Entry: Q28478
LinkDB: Q28478
Original site: Q28478 
ID   ADAM2_MACFA             Reviewed;         735 AA.
AC   Q28478; Q28472; Q4R6R6;
DT   01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   10-APR-2019, entry version 100.
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; ORFNames=QtsA-17331;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RX   PubMed=7741716; DOI=10.1042/bj3070843;
RA   Perry A.C.F., Gichuhi P.M., Jones R., Hall L.;
RT   "Cloning and analysis of monkey fertilin reveals novel alpha subunit
RT   isoforms.";
RL   Biochem. J. 307:843-850(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8720115;
RX   DOI=10.1002/(SICI)1098-2795(199601)43:1<70::AID-MRD9>3.0.CO;2-R;
RA   Ramarao C.S., Myles D.G., White J.M., Primakoff P.;
RT   "Initial evaluation of fertilin as an immunocontraceptive antigen and
RT   molecular cloning of the cynomolgus monkey fertilin beta subunit.";
RL   Mol. Reprod. Dev. 43:70-75(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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 (FDE) 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; X77653; CAA54733.1; -; mRNA.
DR   EMBL; U33959; AAB52699.1; -; mRNA.
DR   EMBL; AB169114; BAE01208.1; -; mRNA.
DR   PIR; G02937; G02937.
DR   RefSeq; NP_001270782.1; NM_001283853.1.
DR   UniGene; Mfa.3947; -.
DR   ProteinModelPortal; Q28478; -.
DR   SMR; Q28478; -.
DR   STRING; 9541.XP_005563199.1; -.
DR   MEROPS; M12.950; -.
DR   PRIDE; Q28478; -.
DR   GeneID; 102125672; -.
DR   KEGG; mcf:102125672; -.
DR   CTD; 2515; -.
DR   HOVERGEN; HBG103628; -.
DR   KO; K06833; -.
DR   OrthoDB; 162519at2759; -.
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; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Membrane; Phosphoprotein; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     16       {ECO:0000255}.
FT   PROPEP       17    174       {ECO:0000250}.
FT                                /FTId=PRO_0000029044.
FT   CHAIN       175    735       Disintegrin and metalloproteinase domain-
FT                                containing protein 2.
FT                                /FTId=PRO_0000029045.
FT   TOPO_DOM     17    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. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   COMPBIAS    476    606       Cys-rich.
FT   MOD_RES     729    729       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q60718}.
FT   CARBOHYD     76     76       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
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   CONFLICT     65     65       F -> S (in Ref. 3; BAE01208).
FT                                {ECO:0000305}.
FT   CONFLICT    121    121       E -> G (in Ref. 3; BAE01208).
FT                                {ECO:0000305}.
FT   CONFLICT    225    225       L -> P (in Ref. 3; BAE01208).
FT                                {ECO:0000305}.
FT   CONFLICT    681    681       H -> Y (in Ref. 3; BAE01208).
FT                                {ECO:0000305}.
FT   CONFLICT    723    723       T -> S (in Ref. 1; CAA54733).
FT                                {ECO:0000305}.
SQ   SEQUENCE   735 AA;  82372 MW;  BE84BE1158C60B53 CRC64;
     MWRVLFLLSG LGGLWMDSNF DSLPVQITVP EKIRSIIKEE IESQVSYKIV IEGKPYTANL
     MQKNFLSHNF RVYSYNGTGI MKPLDQDFQN FCHYQGYIEG YPKSVAMVST CTGLRGLLQF
     ENVSYGIEPL ESSVGFEHVI YQVKHKKADV SLYNEKDIES RDLSFKLQSI EPQKDFAKYI
     EMHVVVEKQL YNHMGSGTTV VTQKIFQLIG LTNAIFVSLN ITVILSSLEL WIDENKIATT
     GDAKELLHTF LRWKRSYLVL RPHDVAFLLV YREKSNYVGA TFQGKMCDAN YAGGVLLHPR
     TISLESLAVI LAQLLSLSMG IPYDDINQCQ CSAAVCIMNP EAIHFSGVKI FSNCSIEDFA
     HFISKQKSQC LHNQPRLDPF FKQQAVCGNA KLEAGEECDC GTQQNCFLLG AKCCDTATCR
     FKAGSNCAEG PCCENCLFMS QERVCRPSFD ECDLPEYCNG TSASCPENHF IQTGHPCGPN
     QWVCIDGVCM NGDKQCMDTF GGEAEFGPTE CYSYLNSKTD VSGNCGIGDS GYTQCEADNL
     QCGKLICKYA GEFLLQIPRA TIIYANISGH LCVAVEFASD HEDSHKMWIK DGTSCGSNKV
     CKNQRCVSSS YLGYDCTTDK CNHRGVCNNK KHCHCSASYL PPDCSVQSDT SPGGSIDSGN
     FPLVAVPARL PERRHMENVY HSKPMRWPLF LFIPFFIIFC VLIAIMVKVH FQRKKWRTED
     YSTDEQPESE SEPKG
//
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