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   24-JAN-2024, entry version 179.
DE   RecName: Full=Disintegrin and metalloproteinase domain-containing protein 2 {ECO:0000312|MGI:MGI:1340894};
DE            Short=ADAM 2;
DE   AltName: Full=Fertilin subunit beta {ECO:0000312|MGI:MGI:1340894};
DE   AltName: Full=PH-30;
DE            Short=PH30;
DE   AltName: Full=PH30-beta {ECO:0000312|MGI:MGI:1340894};
DE   Flags: Precursor;
GN   Name=Adam2 {ECO:0000312|MGI:MGI:1340894};
GN   Synonyms=Ftnb {ECO:0000312|MGI:MGI:1340894};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Testis;
RX   PubMed=7593287; DOI=10.1242/jcs.108.10.3267;
RA   Evans J.P., Schultz R.M., Kopf G.S.;
RT   "Mouse sperm-egg plasma membrane interactions: analysis of roles of egg
RT   integrins and the mouse sperm homologue of PH-30 (fertilin) 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., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., 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., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., 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., Primakoff P.,
RA   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 domain.";
RL   Dev. Biol. 169:378-383(1995).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-729, AND IDENTIFICATION BY
RP   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 expression.";
RL   Cell 143:1174-1189(2010).
RN   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=20945367; DOI=10.1002/jcp.22444;
RA   Han C., Park I., Lee B., Jin S., Choi H., Kwon J.T., Kwon Y.I., Kim D.H.,
RA   Park Z.Y., Cho C.;
RT   "Identification of heat shock protein 5, calnexin and integral membrane
RT   protein 2B as Adam7-interacting membrane proteins in mouse sperm.";
RL   J. Cell. Physiol. 226:1186-1195(2011).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer with ADAM1/fertilin subunit alpha.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed in the testis and testicular sperm (at
CC       protein level). {ECO:0000269|PubMed:20945367,
CC       ECO:0000269|PubMed:7593287}.
CC   -!- DOMAIN: A tripeptide motif (QDE) within disintegrin-like domain could
CC       be involved in the binding to egg integrin receptor and thus could
CC       mediate sperm/egg binding. {ECO:0000250}.
CC   -!- PTM: The signal and the metalloprotease domain are cleaved during the
CC       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   AlphaFoldDB; Q60718; -.
DR   SMR; Q60718; -.
DR   BioGRID; 197966; 9.
DR   CORUM; Q60718; -.
DR   IntAct; Q60718; 1.
DR   MINT; Q60718; -.
DR   STRING; 10090.ENSMUSP00000022618; -.
DR   MEROPS; M12.950; -.
DR   GlyCosmos; Q60718; 8 sites, No reported glycans.
DR   GlyGen; Q60718; 8 sites.
DR   iPTMnet; Q60718; -.
DR   PhosphoSitePlus; Q60718; -.
DR   PaxDb; 10090-ENSMUSP00000022618; -.
DR   ProteomicsDB; 285614; -.
DR   Antibodypedia; 11200; 241 antibodies from 31 providers.
DR   DNASU; 11495; -.
DR   Ensembl; ENSMUST00000022618.6; ENSMUSP00000022618.6; ENSMUSG00000022039.7.
DR   GeneID; 11495; -.
DR   KEGG; mmu:11495; -.
DR   UCSC; uc007uju.1; mouse.
DR   AGR; MGI:1340894; -.
DR   CTD; 2515; -.
DR   MGI; MGI:1340894; Adam2.
DR   VEuPathDB; HostDB:ENSMUSG00000022039; -.
DR   eggNOG; KOG3607; Eukaryota.
DR   GeneTree; ENSGT00940000161961; -.
DR   HOGENOM; CLU_012714_4_1_1; -.
DR   InParanoid; Q60718; -.
DR   OMA; FCYYQGH; -.
DR   OrthoDB; 5406290at2759; -.
DR   PhylomeDB; Q60718; -.
DR   TreeFam; TF314733; -.
DR   Reactome; R-MMU-2534343; Interaction With Cumulus Cells And The Zona Pellucida.
DR   BioGRID-ORCS; 11495; 6 hits in 77 CRISPR screens.
DR   ChiTaRS; Adam2; mouse.
DR   PRO; PR:Q60718; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   RNAct; Q60718; Protein.
DR   Bgee; ENSMUSG00000022039; Expressed in spermatocyte and 9 other cell types or tissues.
DR   GO; GO:0001669; C:acrosomal vesicle; ISO:MGI.
DR   GO; GO:0009986; C:cell surface; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR   GO; GO:0030534; P:adult behavior; IMP:MGI.
DR   GO; GO:0007339; P:binding of sperm to zona pellucida; IBA:GO_Central.
DR   GO; GO:0007155; P:cell adhesion; IGI:MGI.
DR   GO; GO:0008584; P:male gonad development; IBA:GO_Central.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   GO; GO:0008542; P:visual learning; IMP:MGI.
DR   CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 4.10.70.10; Disintegrin domain; 1.
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; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR   PANTHER; PTHR11905:SF108; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 2; 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; Blood coagulation inhibitor (disintegrin); 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 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.
DR   Genevisible; Q60718; MM.
PE   1: Evidence at protein level;
KW   Cell adhesion; Disulfide bond; EGF-like domain; Glycoprotein; Membrane;
KW   Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..180
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000029046"
FT   CHAIN           181..735
FT                   /note="Disintegrin and metalloproteinase domain-containing
FT                   protein 2"
FT                   /id="PRO_0000029047"
FT   TOPO_DOM        19..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          184..381
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   DOMAIN          389..476
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DOMAIN          615..648
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   MOD_RES         729
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CARBOHYD        128
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        226
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        279
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        359
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        463
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        489
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        569
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        585
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        293..376
FT                   /evidence="ECO:0000250"
FT   DISULFID        335..360
FT                   /evidence="ECO:0000250"
FT   DISULFID        337..342
FT                   /evidence="ECO:0000250"
FT   DISULFID        449..469
FT                   /evidence="ECO:0000250"
FT   DISULFID        619..630
FT                   /evidence="ECO:0000250"
FT   DISULFID        624..636
FT                   /evidence="ECO:0000250"
FT   DISULFID        638..647
FT                   /evidence="ECO:0000250"
FT   CONFLICT        2
FT                   /note="W -> R (in Ref. 2; AAD04207)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        17..20
FT                   /note="LSQS -> IRHE (in Ref. 4; AAA74921)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        24..25
FT                   /note="GT -> A (in Ref. 4; AAA74921)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        113
FT                   /note="I -> M (in Ref. 1; AAA90980)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        234..242
FT                   /note="LEFWMDENK -> WNFGWMKQ (in Ref. 4; AAA74921)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        246..247
FT                   /note="TG -> QA (in Ref. 4; AAA74921)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        286
FT                   /note="A -> L (in Ref. 4; AAA74921)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        331..332
FT                   /note="DV -> RRL (in Ref. 4; AAA74921)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        382
FT                   /note="R -> T (in Ref. 2; AAD04207)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        658
FT                   /note="S -> T (in Ref. 4; AAA74921)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        679
FT                   /note="A -> R (in Ref. 2; AAD04207)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        712
FT                   /note="Q -> P (in Ref. 1; AAA90980)"
FT                   /evidence="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
//