ADAM2_CAVPO
ID ADAM2_CAVPO Reviewed; 735 AA.
AC Q60411;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 116.
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 Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RX PubMed=8248170; DOI=10.1073/pnas.90.22.10783;
RA Wolfsberg T.G., Bazan J.F., Blobel C.P., Myles D.G., Primakoff P.,
RA White J.M.;
RT "The precursor region of a protein active in sperm-egg fusion contains a
RT metalloprotease and a disintegrin domain: structural, functional, and
RT evolutionary implications.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:10783-10787(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 383-735.
RC TISSUE=Testis;
RX PubMed=1552944; DOI=10.1038/356248a0;
RA Blobel C.P., Wolfsberg T.G., Turck C.W., Myles D.G., Primakoff P.,
RA White J.M.;
RT "A potential fusion peptide and an integrin ligand domain in a protein
RT active in sperm-egg fusion.";
RL Nature 356:248-252(1992).
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 -!- DEVELOPMENTAL STAGE: Expression begins during meiotic prophase.
CC -!- DOMAIN: A tripeptide motif (TDE) 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}.
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; Z11720; CAA77784.1; -; mRNA.
DR PIR; S23403; S23403.
DR RefSeq; NP_001166381.1; NM_001172910.1.
DR AlphaFoldDB; Q60411; -.
DR SMR; Q60411; -.
DR STRING; 10141.ENSCPOP00000017917; -.
DR MEROPS; M12.950; -.
DR GeneID; 100135471; -.
DR KEGG; cpoc:100135471; -.
DR CTD; 2515; -.
DR eggNOG; KOG3607; Eukaryota.
DR InParanoid; Q60411; -.
DR OrthoDB; 162519at2759; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
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..15
FT /evidence="ECO:0000255"
FT PROPEP 16..176
FT /evidence="ECO:0000250"
FT /id="PRO_0000029040"
FT CHAIN 177..735
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein 2"
FT /id="PRO_0000029041"
FT TOPO_DOM 16..680
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 681..701
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 702..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..470
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DOMAIN 610..643
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 716..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 723
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60718"
FT CARBOHYD 55
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 288
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 456
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 564
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 442..455
FT /evidence="ECO:0000255"
FT DISULFID 614..625
FT /evidence="ECO:0000250"
FT DISULFID 619..631
FT /evidence="ECO:0000250"
FT DISULFID 633..642
FT /evidence="ECO:0000250"
SQ SEQUENCE 735 AA; 81905 MW; 7535FC39F44FB645 CRC64;
MLCLLLLLCG LASLGGPLKK YVENSGMQIT VPEKIRSVKR GSVESEVSYK IVIENTTYIV
NLVRKMFLPH DFQVYSYDSA GIMKPFEDYS QNFCYYQGHI EGFPTSLASI STCAGLRGLL
QFETVSYGIE PLKSSIGFEH VIYPVKHDNE KSQYLKKSIN VKNVVYKIKS IKSSVRTHYI
EMHIIVEKNL YKHMGGNTAT VTEKIFQLVG LMNAFFSTLN LTVILASLEL WIDENKIPTT
GDVNELLHAF QKWKKSYLVL RPHDVAFLLV YRESPSYIGA IFQGMICNTS YGGGIALHSK
TITLDSFGVI LVQLLSVSMG IAYDNADLCR CRGAICLMSP EAVFSSGMKM FSNCSVKAFK
LFTSSQVSQC LQNQPYLEPV YRSNPVCGNN RVEQGEDCDC GSQEECQDTC CDAATCRLKS
TSRCAQGPCC NQCEFKTKGE VCRESTDECD LPEYCNGSSG ACQEDLYVIN GHRCANEEWI
CMNGRCLSGK AQVQETFGTE MEMGSVDCFE QLNTKNDITG NCGILSPGNY KACGASNWKC
GKLICSYDKS EILRNKEGMT IYANISGHIC VSIEYPPGHA KSALMWVRDG TVCGPSEVCR
QQQCVSSSYL GYDCTPATCS DHGVCNNKRH CHCNPTYVPP NCETQDSTKP GGSVDSGNLR
YEPIPETYFV EGAYHTKSRK WPFFLIIPFF VIFSVLVATV VKVYYQKKKW KTEDYANDEN
IESESEPKSS KVSSK
