ID   ADAM2_MOUSE             Reviewed;         735 AA.
AC   Q60718; Q60814; Q9D4G3; Q9QWJ0;
DT   01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2003, sequence version 2.
DT   27-SEP-2017, entry version 144.
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RX   PubMed=7593287;
RA   Evans J.P., Schultz R.M., Kopf G.S.;
RT   "Mouse sperm-egg plasma membrane interactions: analysis of roles of
RT   egg integrins and the mouse sperm homologue of PH-30 (fertilin)
RT   beta.";
RL   J. Cell Sci. 108:3267-3278(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Gupta S.K., Alves K., Palladino L.O., Mark G.E., Hollis G.F.;
RL   Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 17-735.
RC   TISSUE=Testis;
RX   PubMed=7750654; DOI=10.1006/dbio.1995.1152;
RA   Wolfsberg T.G., Straight P.D., Gerena R.L., Huovila A.-P.,
RA   Primakoff P., Myles D.G., White J.M.;
RT   "ADAM, a widely distributed and developmentally regulated gene family
RT   encoding membrane proteins with a disintegrin and metalloprotease
RT   domain.";
RL   Dev. Biol. 169:378-383(1995).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-729, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
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 (QDE) 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.
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DR   EMBL; U16242; AAA90980.1; -; mRNA.
DR   EMBL; U38806; AAD04207.1; -; mRNA.
DR   EMBL; AK016550; BAB30298.1; -; mRNA.
DR   EMBL; U22057; AAA74921.1; -; mRNA.
DR   CCDS; CCDS36959.1; -.
DR   RefSeq; NP_033748.2; NM_009618.3.
DR   UniGene; Mm.422850; -.
DR   ProteinModelPortal; Q60718; -.
DR   SMR; Q60718; -.
DR   CORUM; Q60718; -.
DR   STRING; 10090.ENSMUSP00000022618; -.
DR   MEROPS; M12.950; -.
DR   iPTMnet; Q60718; -.
DR   PhosphoSitePlus; Q60718; -.
DR   PaxDb; Q60718; -.
DR   PRIDE; Q60718; -.
DR   DNASU; 11495; -.
DR   Ensembl; ENSMUST00000022618; ENSMUSP00000022618; ENSMUSG00000022039.
DR   GeneID; 11495; -.
DR   KEGG; mmu:11495; -.
DR   UCSC; uc007uju.1; mouse.
DR   CTD; 2515; -.
DR   MGI; MGI:1340894; Adam2.
DR   eggNOG; KOG3607; Eukaryota.
DR   eggNOG; ENOG410XX2M; LUCA.
DR   GeneTree; ENSGT00880000137877; -.
DR   HOGENOM; HOG000230883; -.
DR   HOVERGEN; HBG103628; -.
DR   InParanoid; Q60718; -.
DR   KO; K06833; -.
DR   OMA; CGKLICK; -.
DR   OrthoDB; EOG091G02F0; -.
DR   PhylomeDB; Q60718; -.
DR   TreeFam; TF314733; -.
DR   Reactome; R-MMU-1300644; Interaction With The Zona Pellucida.
DR   PRO; PR:Q60718; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   Bgee; ENSMUSG00000022039; -.
DR   CleanEx; MM_ADAM2; -.
DR   Genevisible; Q60718; MM.
DR   GO; GO:0009986; C:cell surface; IDA:MGI.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0030534; P:adult behavior; IMP:MGI.
DR   GO; GO:0007155; P:cell adhesion; IGI:MGI.
DR   GO; GO:0007338; P:single fertilization; IEA:InterPro.
DR   GO; GO:0008542; P:visual learning; IMP:MGI.
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; IPR000742; EGF-like_dom.
DR   InterPro; IPR024079; MetalloPept_cat_dom.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   InterPro; IPR002870; Peptidase_M12B_N.
DR   InterPro; IPR034027; Reprolysin_adamalysin.
DR   PANTHER; PTHR11905:SF203; PTHR11905:SF203; 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_0000029046.
FT   CHAIN       181    735       Disintegrin and metalloproteinase domain-
FT                                containing protein 2.
FT                                /FTId=PRO_0000029047.
FT   TOPO_DOM     19    686       Extracellular. {ECO:0000255}.
FT   TRANSMEM    687    707       Helical. {ECO:0000255}.
FT   TOPO_DOM    708    735       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      184    381       Peptidase M12B. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00276}.
FT   DOMAIN      389    476       Disintegrin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00068}.
FT   DOMAIN      615    648       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   COMPBIAS    480    611       Cys-rich.
FT   MOD_RES     729    729       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   CARBOHYD    128    128       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    226    226       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    279    279       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    359    359       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    463    463       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    489    489       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    569    569       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    585    585       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    449    469       {ECO:0000250}.
FT   DISULFID    619    630       {ECO:0000250}.
FT   DISULFID    624    636       {ECO:0000250}.
FT   DISULFID    638    647       {ECO:0000250}.
FT   CONFLICT      2      2       W -> R (in Ref. 2; AAD04207).
FT                                {ECO:0000305}.
FT   CONFLICT     17     20       LSQS -> IRHE (in Ref. 4; AAA74921).
FT                                {ECO:0000305}.
FT   CONFLICT     24     25       GT -> A (in Ref. 4; AAA74921).
FT                                {ECO:0000305}.
FT   CONFLICT    113    113       I -> M (in Ref. 1; AAA90980).
FT                                {ECO:0000305}.
FT   CONFLICT    234    242       LEFWMDENK -> WNFGWMKQ (in Ref. 4;
FT                                AAA74921). {ECO:0000305}.
FT   CONFLICT    246    247       TG -> QA (in Ref. 4; AAA74921).
FT                                {ECO:0000305}.
FT   CONFLICT    286    286       A -> L (in Ref. 4; AAA74921).
FT                                {ECO:0000305}.
FT   CONFLICT    331    332       DV -> RRL (in Ref. 4; AAA74921).
FT                                {ECO:0000305}.
FT   CONFLICT    382    382       R -> T (in Ref. 2; AAD04207).
FT                                {ECO:0000305}.
FT   CONFLICT    658    658       S -> T (in Ref. 4; AAA74921).
FT                                {ECO:0000305}.
FT   CONFLICT    679    679       A -> R (in Ref. 2; AAD04207).
FT                                {ECO:0000305}.
FT   CONFLICT    712    712       Q -> P (in Ref. 1; AAA90980).
FT                                {ECO:0000305}.
SQ   SEQUENCE   735 AA;  82375 MW;  75EC8529CF5B8E2B CRC64;
     MWLILLLLSG LSELGGLSQS QTEGTREKLH VQVTVPEKIR SVTSNGYETQ VTYNLKIEGK
     TYTLDLMQKP FLPPNFRVYS YDNAGIMRSL EQKFQNICYF QGYIEGYPNS MVIVSTCTGL
     RGFLQFGNVS YGIEPLESSS GFEHVIYQVE PEKGGALLYA EKDIDLRDSQ YKIRSIKPQR
     IVSHYLEIHI VVEKQMFEHI GADTAIVTQK IFQLIGLANA IFAPFNLTVI LSSLEFWMDE
     NKILTTGDAN KLLYRFLKWK QSYLVLRPHD MAFLLVYRNT TDYVGATYQG KMCDKNYAGG
     VALHPKAVTL ESLAIILVQL LSLSMGLAYD DVNKCQCGVP VCVMNPEAPH SSGVRAFSNC
     SMEDFSKFIT SQSSHCLQNQ PRLQPSYKMA VCGNGEVEED EICDCGKKGC AEMPPPCCNP
     DTCKLSDGSE CSSGICCNSC KLKRKGEVCR LAQDECDVTE YCNGTSEVCE DFFVQNGHPC
     DNRKWICING TCQSGEQQCQ DLFGIDAGFG SSECFWELNS KSDISGSCGI SAGGYKECPP
     NDRMCGKIIC KYQSENILKL RSATVIYANI SGHVCVSLEY PQGHNESQKM WVRDGTVCGS
     NKVCQNQKCV ADTFLGYDCN LEKCNHHGVC NNKKNCHCDP TYLPPDCKRM KDSYPGGSID
     SGNKERAEPI PVRPYIASAY RSKSPRWPFF LIIPFYVVIL VLIGMLVKVY SQRMKWRMDD
     FSSEEQFESE SESKD
//