ID H2QW23_PANTR Unreviewed; 735 AA.
AC H2QW23;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 75.
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 Name=ADAM2 {ECO:0000313|Ensembl:ENSPTRP00000034565.3,
GN ECO:0000313|VGNC:VGNC:11931};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000034565.3, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000034565.3, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000034565.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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; AACZ04065564; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_519722.3; XM_519722.5.
DR MEROPS; M12.950; -.
DR PaxDb; 9598-ENSPTRP00000034565; -.
DR Ensembl; ENSPTRT00000037400.3; ENSPTRP00000034565.3; ENSPTRG00000020185.6.
DR Ensembl; ENSPTRT00000077454.1; ENSPTRP00000063381.1; ENSPTRG00000020185.6.
DR GeneID; 464133; -.
DR KEGG; ptr:464133; -.
DR CTD; 2515; -.
DR VGNC; VGNC:11931; ADAM2.
DR eggNOG; KOG3607; Eukaryota.
DR GeneTree; ENSGT00940000161961; -.
DR HOGENOM; CLU_012714_4_3_1; -.
DR OMA; FCYYQGH; -.
DR OrthoDB; 5406290at2759; -.
DR TreeFam; TF314733; -.
DR Proteomes; UP000002277; Chromosome 8.
DR Bgee; ENSPTRG00000020185; Expressed in testis.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0008584; P:male gonad development; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd04269; ZnMc_adamalysin_II_like; 1.
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; 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; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR PANTHER; PTHR11905:SF108; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 2; 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; Blood coagulation inhibitor (disintegrin); 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 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 4: Predicted;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002277};
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..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..735
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein 2"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014304809"
FT TRANSMEM 687..707
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 178..375
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 384..473
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 612..645
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 331..336
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 445..465
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 635..644
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 735 AA; 82382 MW; 8D52EB9FFB307C5F CRC64;
MWRVLFLLSG LGGLRMDSNF DSLPVQITVP EKIRSIIKEG IESQASYKIV IEGKPYTVNL
MQKNFLPHNF RVYSYSGTGI MKPLDQDFQN FCHYQGYIEG YPKSVVMVST CTGLRGLLQF
ENVSYGIKPL ESSVGFEHVI YQVKHKKADV SLYNEKDTES RDLSFKLQSV EPQQDFAKYI
EMHVIVEKQL YNHMGSDTTV VAQKIFQLIG LTNAIFVSFN ITIILSSLEL WIDENKIATT
GEANELLHTF LRWKTSYLVL RPHDVAFLLV YREKSNYVGA TFQGKMCDAN YAGGVVLHPR
IISLESLAVI LAQLLSLSMG ITYDDINKCQ CSGAVCIMNP EAIHFSGVKI FSNCSIEDFA
HFISKQKSQC LHNQPRLDPF FKKQAVCGNA KLEAGEECDC GTEQDCALIG ETCCDIATCR
FKAGSNCAEG PCCENCLFMS KGRMCRPSFE ECDLPEYCNG SSASCPENHY VQTGHPCGLN
QWICINGVCM SGDKQCTDTF GKEVEFGPSE CYSHLNSKTD VSGNCGISDS GYTQCEADNL
QCGKLICKYV GKFLLQIPRA TIIYANISGH LCIAVEFASD HADSQKMWIK DGTSCGSNKV
CRNQRCVSSS YLGYDCTTDK CSNRGVCNNK KHCHCSASYL PPDCSVQSDL WPGGSIDSGN
FPPVAIPARL HERRYIENIY HSKPMRWPFF LFIPFFIIFC VLIAITVKVH FQRKKWRTED
YSSDEQPESE SEPKG
//
