ADAM2_BOVIN
ID ADAM2_BOVIN Reviewed; 745 AA.
AC O77780;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 124.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RX PubMed=9160725; DOI=10.1095/biolreprod56.5.1245;
RA Waters S.I., White J.M.;
RT "Biochemical and molecular characterization of bovine fertilin alpha and
RT beta (ADAM 1 and ADAM 2): a candidate sperm-egg binding/fusion complex.";
RL Biol. Reprod. 56:1245-1254(1997).
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 (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}.
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DR EMBL; AF086808; AAC62753.1; -; mRNA.
DR RefSeq; NP_776653.1; NM_174228.1.
DR AlphaFoldDB; O77780; -.
DR SMR; O77780; -.
DR STRING; 9913.ENSBTAP00000012384; -.
DR MEROPS; M12.950; -.
DR PRIDE; O77780; -.
DR GeneID; 281599; -.
DR KEGG; bta:281599; -.
DR CTD; 2515; -.
DR eggNOG; KOG3607; Eukaryota.
DR InParanoid; O77780; -.
DR OrthoDB; 162519at2759; -.
DR Proteomes; UP000009136; 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_0000029038"
FT CHAIN 175..745
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein 2"
FT /id="PRO_0000029039"
FT TOPO_DOM 17..696
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 697..717
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 718..745
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 178..375
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 383..472
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DOMAIN 611..644
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 654..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 739
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60718"
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 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 558
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 444..457
FT /evidence="ECO:0000255"
FT DISULFID 615..626
FT /evidence="ECO:0000250"
FT DISULFID 620..632
FT /evidence="ECO:0000250"
FT DISULFID 634..643
FT /evidence="ECO:0000250"
SQ SEQUENCE 745 AA; 83150 MW; B5D8DC0168999B00 CRC64;
MLCLLFLLLG LTGLQTDDNS ERLRVQFTVP EKIRSTSSGG VETHVSYIIL IEGKTYTVNL
MQKAFLPHNF RVYGYSGTGS MKPLEHEFQN FCYYQGYIEG YPNSMAIIST CTGLRGLLQF
ENVSYGIEPL EPSIGFEHMV YQIKPRDSSS SVYTEREIEL REKPYKIQNV EPLPDFSQYI
EMHIVVEKDL YNHMGADTTV VIQKIFQLTG LTNAIFTSLN ITVILSSLEL WIDENKIPVT
GDANELLHRF VKWKRSYLVL RPHDMAFLLV YREKSNYIGA TFQGRMCDKH YGGGVALHSS
TISLESLAVI IAQLLSLSMG IPYDDINKCH CPGDVCIMNP AAVHSSGVKL FSNCSVEDFL
RFISKPKSQC LQNQPRLDPT YKSAVCGNGK VEEGEQCDCG NKKACDALPD TCCVADTCRF
QPGSACDTGL CCESCAFIPK GHICRGSTDE CDLHEYCNGS SAACQEDVYV QDGHPCGQNQ
WLCISGICVD GIKQCFDIFG EGTSYAPAEC FQRLNSMNDL SGNCGVTPTG FTPCTSENVR
CGKLLCTYDK REVISVENAS VMYSNINGKI CIGLHYEYGN EDEGMMWVKD GTVCGESKIC
QNKQCVDSSF LNYDCNPEKC NNQGVCNNKK HCHCNPSYLP PNCEHSAPGW EGGSIDSGNF
PPSEPPTGGP AFTDVGTTPL AESRYIENVY RSKPTRWPFF LFIPFFIILC VLIATLVKVY
FQRKKWRTED YTSDEQLESE SEPKD
