GenomeNet

Database: UniProt
Entry: Q60411
LinkDB: Q60411
Original site: Q60411 
ID   ADAM2_CAVPO             Reviewed;         735 AA.
AC   Q60411;
DT   01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JAN-2019, entry version 108.
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   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia;
OC   Hystricomorpha; Caviidae; Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RX   PubMed=8248170; DOI=10.1073/pnas.90.22.10783;
RA   Wolfsberg T.G., Bazan J.F., Blobel C.P., Myles D.G., Primakoff P.,
RA   White J.M.;
RT   "The precursor region of a protein active in sperm-egg fusion contains
RT   a metalloprotease and a disintegrin domain: structural, functional,
RT   and evolutionary implications.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:10783-10787(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 383-735.
RC   TISSUE=Testis;
RX   PubMed=1552944; DOI=10.1038/356248a0;
RA   Blobel C.P., Wolfsberg T.G., Turck C.W., Myles D.G., Primakoff P.,
RA   White J.M.;
RT   "A potential fusion peptide and an integrin ligand domain in a protein
RT   active in sperm-egg fusion.";
RL   Nature 356:248-252(1992).
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   -!- DEVELOPMENTAL STAGE: Expression begins during meiotic prophase.
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; Z11720; CAA77784.1; -; mRNA.
DR   PIR; S23403; S23403.
DR   RefSeq; NP_001166381.1; NM_001172910.1.
DR   ProteinModelPortal; Q60411; -.
DR   STRING; 10141.ENSCPOP00000017917; -.
DR   MEROPS; M12.950; -.
DR   PRIDE; Q60411; -.
DR   GeneID; 100135471; -.
DR   CTD; 2515; -.
DR   eggNOG; KOG3607; Eukaryota.
DR   eggNOG; ENOG410XX2M; LUCA.
DR   HOGENOM; HOG000230883; -.
DR   HOVERGEN; HBG103628; -.
DR   InParanoid; Q60411; -.
DR   OrthoDB; 162519at2759; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
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     15       {ECO:0000255}.
FT   PROPEP       16    176       {ECO:0000250}.
FT                                /FTId=PRO_0000029040.
FT   CHAIN       177    735       Disintegrin and metalloproteinase domain-
FT                                containing protein 2.
FT                                /FTId=PRO_0000029041.
FT   TOPO_DOM     16    680       Extracellular. {ECO:0000255}.
FT   TRANSMEM    681    701       Helical. {ECO:0000255}.
FT   TOPO_DOM    702    735       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      178    375       Peptidase M12B. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00276}.
FT   DOMAIN      384    470       Disintegrin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00068}.
FT   DOMAIN      610    643       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   COMPBIAS    473    609       Cys-rich.
FT   MOD_RES     723    723       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q60718}.
FT   CARBOHYD     55     55       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    220    220       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    288    288       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    353    353       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    456    456       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    564    564       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    442    455       {ECO:0000255}.
FT   DISULFID    614    625       {ECO:0000250}.
FT   DISULFID    619    631       {ECO:0000250}.
FT   DISULFID    633    642       {ECO:0000250}.
SQ   SEQUENCE   735 AA;  81905 MW;  7535FC39F44FB645 CRC64;
     MLCLLLLLCG LASLGGPLKK YVENSGMQIT VPEKIRSVKR GSVESEVSYK IVIENTTYIV
     NLVRKMFLPH DFQVYSYDSA GIMKPFEDYS QNFCYYQGHI EGFPTSLASI STCAGLRGLL
     QFETVSYGIE PLKSSIGFEH VIYPVKHDNE KSQYLKKSIN VKNVVYKIKS IKSSVRTHYI
     EMHIIVEKNL YKHMGGNTAT VTEKIFQLVG LMNAFFSTLN LTVILASLEL WIDENKIPTT
     GDVNELLHAF QKWKKSYLVL RPHDVAFLLV YRESPSYIGA IFQGMICNTS YGGGIALHSK
     TITLDSFGVI LVQLLSVSMG IAYDNADLCR CRGAICLMSP EAVFSSGMKM FSNCSVKAFK
     LFTSSQVSQC LQNQPYLEPV YRSNPVCGNN RVEQGEDCDC GSQEECQDTC CDAATCRLKS
     TSRCAQGPCC NQCEFKTKGE VCRESTDECD LPEYCNGSSG ACQEDLYVIN GHRCANEEWI
     CMNGRCLSGK AQVQETFGTE MEMGSVDCFE QLNTKNDITG NCGILSPGNY KACGASNWKC
     GKLICSYDKS EILRNKEGMT IYANISGHIC VSIEYPPGHA KSALMWVRDG TVCGPSEVCR
     QQQCVSSSYL GYDCTPATCS DHGVCNNKRH CHCNPTYVPP NCETQDSTKP GGSVDSGNLR
     YEPIPETYFV EGAYHTKSRK WPFFLIIPFF VIFSVLVATV VKVYYQKKKW KTEDYANDEN
     IESESEPKSS KVSSK
//
DBGET integrated database retrieval system