ADAM2_MOUSE
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 03-AUG-2022, entry version 171.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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).
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 specifically in testis.
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 GlyGen; Q60718; 8 sites.
DR iPTMnet; Q60718; -.
DR PhosphoSitePlus; Q60718; -.
DR PaxDb; Q60718; -.
DR PRIDE; Q60718; -.
DR ProteomicsDB; 285614; -.
DR Antibodypedia; 11200; 212 antibodies from 31 providers.
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 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; 162519at2759; -.
DR PhylomeDB; Q60718; -.
DR TreeFam; TF314733; -.
DR Reactome; R-MMU-2534343; Interaction With Cumulus Cells And The Zona Pellucida.
DR BioGRID-ORCS; 11495; 5 hits in 72 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 tissues.
DR Genevisible; Q60718; MM.
DR GO; GO:0001669; C:acrosomal vesicle; ISO:MGI.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
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:0010628; P:positive regulation of gene expression; IMP:MGI.
DR GO; GO:0006508; P:proteolysis; 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; 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 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; 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
