ID G5BY91_HETGA Unreviewed; 406 AA.
AC G5BY91;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Disintegrin and metalloproteinase domain-containing protein 2 {ECO:0000256|ARBA:ARBA00020159};
DE AltName: Full=Fertilin subunit beta {ECO:0000256|ARBA:ARBA00030994};
DE AltName: Full=PH-30 {ECO:0000256|ARBA:ARBA00032022};
DE AltName: Full=PH30-beta {ECO:0000256|ARBA:ARBA00031933};
GN ORFNames=GW7_07617 {ECO:0000313|EMBL:EHB14252.1};
OS Heterocephalus glaber (Naked mole rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Heterocephalus.
OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB14252.1, ECO:0000313|Proteomes:UP000006813};
RN [1] {ECO:0000313|EMBL:EHB14252.1, ECO:0000313|Proteomes:UP000006813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993625; DOI=10.1038/nature10533;
RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT "Genome sequencing reveals insights into physiology and longevity of the
RT naked mole rat.";
RL Nature 479:223-227(2011).
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. {ECO:0000256|ARBA:ARBA00025231}.
CC -!- SUBUNIT: Heterodimer with ADAM1/fertilin subunit alpha.
CC {ECO:0000256|ARBA:ARBA00011609}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; JH172442; EHB14252.1; -; Genomic_DNA.
DR AlphaFoldDB; G5BY91; -.
DR STRING; 10181.G5BY91; -.
DR eggNOG; KOG3607; Eukaryota.
DR InParanoid; G5BY91; -.
DR Proteomes; UP000006813; Unassembled WGS sequence.
DR GO; GO:0016020; C: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:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 4.10.70.10; Disintegrin domain; 1.
DR InterPro; IPR006586; ADAM_Cys-rich.
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 PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR PANTHER; PTHR11905:SF108; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 2; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; Blood coagulation inhibitor (disintegrin); 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
PE 4: Predicted;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Integrin {ECO:0000313|EMBL:EHB14252.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000006813};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..406
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein 2"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013379620"
FT TRANSMEM 344..368
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 63..168
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 283..316
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 124..129
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 306..315
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 406 AA; 45622 MW; A1759EF3C76E2B98 CRC64;
MLSVLLLLSG LRALGEPLTN GEYEDSSFEL PAAAVCPGSA SLYPTPGKLP PLGPRSWGHH
VASFCRPSTS PPSSEFFQYI ELHLIVEKDL HPKSMNLDSF AVILVQLLSL SMGITYDDVN
RCHCPGAVCV MNPEAIHSGG VKIFSDCSMN DFARFTSKPM SQCLQNQPRL QTAYQGTTCG
NKIVEAGETC DCGTEEFKSS EEICRNRVDE CDLPEFCNGS SADCQEDLFI LNGHPCGENK
WICMNGKCVS GKTQCEAAFG EGIYDHLIFY VCRNKECVAD SFLGYDCTPA TCNNNGVCNN
KKACQCYPGY LPPDCSIKIP VYGAQFDPER HYIKGVYQTK PKNWPFLLII PFLIIFSVLI
AIVVKVYFQR KKWRTEDYIS EEYVDFVFKF YYFYNFWYNN LLIASW
//
