ADAM2_RABIT
ID ADAM2_RABIT Reviewed; 751 AA.
AC Q28660;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 122.
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8914066;
RX DOI=10.1002/(sici)1098-2795(199610)45:2<107::aid-mrd1>3.0.co;2-x;
RA Hardy C.M., Holland M.K.;
RT "Cloning and expression of recombinant rabbit fertilin.";
RL Mol. Reprod. Dev. 45:107-116(1996).
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 (VGE) 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; U46070; AAA93321.1; -; mRNA.
DR RefSeq; NP_001076146.1; NM_001082677.1.
DR AlphaFoldDB; Q28660; -.
DR SMR; Q28660; -.
DR MEROPS; M12.950; -.
DR PRIDE; Q28660; -.
DR GeneID; 100009397; -.
DR KEGG; ocu:100009397; -.
DR CTD; 2515; -.
DR InParanoid; Q28660; -.
DR OrthoDB; 162519at2759; -.
DR Proteomes; UP000001811; 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..173
FT /evidence="ECO:0000250"
FT /id="PRO_0000029049"
FT CHAIN 174..751
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein 2"
FT /id="PRO_0000029048"
FT TOPO_DOM 17..702
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 703..723
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 724..751
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 177..374
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 612..645
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT MOD_RES 745
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60718"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 434
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 559
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 566
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 643
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 286..369
FT /evidence="ECO:0000250"
FT DISULFID 328..353
FT /evidence="ECO:0000250"
FT DISULFID 330..335
FT /evidence="ECO:0000250"
FT DISULFID 444..464
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"
SQ SEQUENCE 751 AA; 83617 MW; 824C6FBFC4A9FCE1 CRC64;
MLRVLFLLCG LSGLRTKENS ERLHVQVTVP EKMRSVTSEG FETEVVYNIV IEGKTYTLNL
MQKLFLPRDF RVYGYDSTGI MKDLEQQFQN FCYYQGFVEG YPNSMVIVST CTGLRGLLQF
ENVTYGIEPL ESSIGFEHVI YQVKNKNESI SLYAEKEVEF RDLPYKVQSV QPREFSQYIE
MHVVVEKNLY KHMGSDTAVV SQKIFQLIGL TNAVFTSFNI TIILSSLELW IDENKISTTG
DANELLYRFL KWKKSYLVLR PHDVAFLLVY REIAKYVGAT FQGKMCDINY SGGVALHPKT
ISLESLAIIL AQLLSLSMGI AYDDINKCKC PGSVCIMNPE AIHSSGVKIF SNCSIEDFSR
FISKQKSQCL QNLPRLEPFY KQDAVCGNSI VEAGEMCDCG TAEECGRAVP ICCNSATCRL
EVGSQCAEGE CCENCTFKER GQSCRPPVGE CDLFEYCNGT SALCPDDIVI QNGHPCGENQ
WICVDGSCIS PPEQCKSIFG EEVEGGTPEC YEELNAMADI ILGICGITHD GYKKCESGNR
KCGKLMCKHT TENIIDIKNA TIIYANVSGS ICLSLEYKPD HLDAAKMWVP NGAVCGSNKI
CRDKACVETT YVNLGCTLQN CNNQGICNSL QHCHCNPTFL PPNCSAVDER WAGGSVDSGN
FQGGGVPGIG GLTSVGTPPF IPGVPGVRRY MEDVYQTAKP TRWPFFLLIP FFIILGALIA
ILVKVQFQRK KWKTEDYTSD EQFESDSELK E
