ADAM2_MACFA
ID ADAM2_MACFA Reviewed; 735 AA.
AC Q28478; Q28472; Q4R6R6;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 111.
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; ORFNames=QtsA-17331;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RX PubMed=7741716; DOI=10.1042/bj3070843;
RA Perry A.C.F., Gichuhi P.M., Jones R., Hall L.;
RT "Cloning and analysis of monkey fertilin reveals novel alpha subunit
RT isoforms.";
RL Biochem. J. 307:843-850(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8720115;
RX DOI=10.1002/(sici)1098-2795(199601)43:1<70::aid-mrd9>3.0.co;2-r;
RA Ramarao C.S., Myles D.G., White J.M., Primakoff P.;
RT "Initial evaluation of fertilin as an immunocontraceptive antigen and
RT molecular cloning of the cynomolgus monkey fertilin beta subunit.";
RL Mol. Reprod. Dev. 43:70-75(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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 (FDE) 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. {ECO:0000250}.
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DR EMBL; X77653; CAA54733.1; -; mRNA.
DR EMBL; U33959; AAB52699.1; -; mRNA.
DR EMBL; AB169114; BAE01208.1; -; mRNA.
DR PIR; G02937; G02937.
DR RefSeq; NP_001270782.1; NM_001283853.1.
DR AlphaFoldDB; Q28478; -.
DR SMR; Q28478; -.
DR STRING; 9541.XP_005563199.1; -.
DR MEROPS; M12.950; -.
DR GeneID; 102125672; -.
DR CTD; 2515; -.
DR eggNOG; KOG3607; Eukaryota.
DR OrthoDB; 162519at2759; -.
DR Proteomes; UP000233100; Unplaced.
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:0006508; P:proteolysis; IEA:InterPro.
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; Disulfide bond; EGF-like domain; Glycoprotein; Membrane;
KW Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT PROPEP 17..174
FT /evidence="ECO:0000250"
FT /id="PRO_0000029044"
FT CHAIN 175..735
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein 2"
FT /id="PRO_0000029045"
FT TOPO_DOM 17..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 178..375
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 384..473
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DOMAIN 612..645
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT MOD_RES 729
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60718"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 459
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 566
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 287..370
FT /evidence="ECO:0000250"
FT DISULFID 329..354
FT /evidence="ECO:0000250"
FT DISULFID 331..336
FT /evidence="ECO:0000250"
FT DISULFID 445..465
FT /evidence="ECO:0000250"
FT DISULFID 616..627
FT /evidence="ECO:0000250"
FT DISULFID 621..633
FT /evidence="ECO:0000250"
FT DISULFID 635..644
FT /evidence="ECO:0000250"
FT CONFLICT 65
FT /note="F -> S (in Ref. 3; BAE01208)"
FT /evidence="ECO:0000305"
FT CONFLICT 121
FT /note="E -> G (in Ref. 3; BAE01208)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="L -> P (in Ref. 3; BAE01208)"
FT /evidence="ECO:0000305"
FT CONFLICT 681
FT /note="H -> Y (in Ref. 3; BAE01208)"
FT /evidence="ECO:0000305"
FT CONFLICT 723
FT /note="T -> S (in Ref. 1; CAA54733)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 735 AA; 82372 MW; BE84BE1158C60B53 CRC64;
MWRVLFLLSG LGGLWMDSNF DSLPVQITVP EKIRSIIKEE IESQVSYKIV IEGKPYTANL
MQKNFLSHNF RVYSYNGTGI MKPLDQDFQN FCHYQGYIEG YPKSVAMVST CTGLRGLLQF
ENVSYGIEPL ESSVGFEHVI YQVKHKKADV SLYNEKDIES RDLSFKLQSI EPQKDFAKYI
EMHVVVEKQL YNHMGSGTTV VTQKIFQLIG LTNAIFVSLN ITVILSSLEL WIDENKIATT
GDAKELLHTF LRWKRSYLVL RPHDVAFLLV YREKSNYVGA TFQGKMCDAN YAGGVLLHPR
TISLESLAVI LAQLLSLSMG IPYDDINQCQ CSAAVCIMNP EAIHFSGVKI FSNCSIEDFA
HFISKQKSQC LHNQPRLDPF FKQQAVCGNA KLEAGEECDC GTQQNCFLLG AKCCDTATCR
FKAGSNCAEG PCCENCLFMS QERVCRPSFD ECDLPEYCNG TSASCPENHF IQTGHPCGPN
QWVCIDGVCM NGDKQCMDTF GGEAEFGPTE CYSYLNSKTD VSGNCGIGDS GYTQCEADNL
QCGKLICKYA GEFLLQIPRA TIIYANISGH LCVAVEFASD HEDSHKMWIK DGTSCGSNKV
CKNQRCVSSS YLGYDCTTDK CNHRGVCNNK KHCHCSASYL PPDCSVQSDT SPGGSIDSGN
FPLVAVPARL PERRHMENVY HSKPMRWPLF LFIPFFIIFC VLIAIMVKVH FQRKKWRTED
YSTDEQPESE SEPKG
