ADAM2_RAT
ID ADAM2_RAT Reviewed; 737 AA.
AC Q63202;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2003, sequence version 2.
DT 03-AUG-2022, entry version 142.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Testis;
RX PubMed=9358007; DOI=10.1093/molehr/3.9.801;
RA McLaughlin E.A., Frayne J., Barker H.L., Jury J.A., Jones R., Ford W.C.L.,
RA Hall L.;
RT "Cloning and sequence analysis of rat fertilin alpha and beta
RT - developmental expression, processing and immunolocalization.";
RL Mol. Hum. Reprod. 3:801-809(1997).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-731, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- DOMAIN: A tripeptide motif (NQE) 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 prodomain and the metalloprotease domain are cleaved during
CC the epididymal maturation of the spermatozoa. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA68127.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X99794; CAA68127.1; ALT_INIT; mRNA.
DR RefSeq; NP_064462.1; NM_020077.1.
DR AlphaFoldDB; Q63202; -.
DR SMR; Q63202; -.
DR STRING; 10116.ENSRNOP00000061122; -.
DR MEROPS; M12.950; -.
DR GlyGen; Q63202; 6 sites.
DR iPTMnet; Q63202; -.
DR PhosphoSitePlus; Q63202; -.
DR PaxDb; Q63202; -.
DR GeneID; 56806; -.
DR KEGG; rno:56806; -.
DR UCSC; RGD:69299; rat.
DR CTD; 2515; -.
DR RGD; 69299; Adam2.
DR eggNOG; KOG3607; Eukaryota.
DR InParanoid; Q63202; -.
DR OrthoDB; 162519at2759; -.
DR PhylomeDB; Q63202; -.
DR PRO; PR:Q63202; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0001669; C:acrosomal vesicle; IDA:RGD.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0030534; P:adult behavior; ISO:RGD.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; ISO:RGD.
DR GO; GO:0008584; P:male gonad development; IEP:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0007283; P:spermatogenesis; IEP:RGD.
DR GO; GO:0008542; P:visual learning; ISO:RGD.
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_0000029050"
FT CHAIN 181..737
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein 2"
FT /id="PRO_0000029051"
FT TOPO_DOM 19..688
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 689..709
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 710..737
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..478
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DOMAIN 617..650
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT MOD_RES 731
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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 359
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 491
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 571
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 450..470
FT /evidence="ECO:0000250"
FT DISULFID 621..632
FT /evidence="ECO:0000250"
FT DISULFID 626..638
FT /evidence="ECO:0000250"
FT DISULFID 640..649
FT /evidence="ECO:0000250"
SQ SEQUENCE 737 AA; 82311 MW; 647E92A90D7CC1D1 CRC64;
MWLLLLLLSG LSRLGGLSEP QTEGTREKLH VQVTVPEKIR SITSEGYETQ VTYSLKIEGK
TYILNLMQKA FLPPNFRVYS YDSTGIMRPL EQKFQNICYF QGYIEGYPNS MVIVSTCTGL
RGVLQFGNVS YGIEPLESSS GFEHVIYQVE PKKGDTLLYA EKDMDLRDPQ YKIRSIKPQR
TVSHYLEIHI VVEKQMFEHI GADTAVVTQK IFQLIGLTNA IFAPFNLTVI LSSLEFWMDE
NKISTTGDAN KLLYRFLKWK QSYLVLRPHD MAFLLVYRDT TDYVGATYQG KMCDKNYAGG
VALHPKAVTL ESLAIILVQL LSLSMGVAYD DVNTCQCGVP ICVMNPEALH SSGVRSFSNC
SMEDFSKFIV SQSSHCLQNQ PHLQPSYKMA VCGNGELEEG EVCDCGQEGC DDKPPPCCNP
TTCQLSEGST CSTGSCCDAS CNLKAKGELC RPANQECDVT EYCNGTSEVC EEDFFVQDGH
PCAEQKWICI NGTCQSGAQQ CRDLFGTDAD YGTKECYSEL NSKSDISGSC GITPTGYKDC
APNDRMCGKL ICIYQSEDIL KMRSAIVIYA NISGQICISL EYPPGHKESK KMCVRDGTVC
GSGKVCLNQE CVEDTFLNYD CTPEKCNHHG VCNNKKHCHC EPTYLPPDCK NTEDTWPGGS
VDSGNQQRAE SIPARSYVAS AYRSKSARWP FFLIIPFYVV ILVLIGMLVK VYSQRKKWRM
DDFSSEEQFE SESESKD
