ID I3MID8_ICTTR Unreviewed; 738 AA.
AC I3MID8;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 76.
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:ENSSTOP00000010773.3};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000010773.3, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000010773.3}
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}.
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; AGTP01091973; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01091974; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01091975; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; I3MID8; -.
DR STRING; 43179.ENSSTOP00000010773; -.
DR Ensembl; ENSSTOT00000012006.3; ENSSTOP00000010773.3; ENSSTOG00000011994.3.
DR eggNOG; KOG3607; Eukaryota.
DR GeneTree; ENSGT00940000161961; -.
DR HOGENOM; CLU_012714_4_3_1; -.
DR InParanoid; I3MID8; -.
DR OrthoDB; 5406290at2759; -.
DR TreeFam; TF314733; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0030534; P:adult behavior; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0008542; P:visual learning; IEA:Ensembl.
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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000005215};
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..738
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein 2"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013220667"
FT TRANSMEM 690..710
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 183..380
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 389..478
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 617..650
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 649..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 336..341
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 450..470
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 640..649
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 738 AA; 82654 MW; 5A1C4895DCD5F789 CRC64;
MLRVLLLLGG LGGLSGYSPR HREHNYERLH VQVTVPVKIR SIKNGGFESH VAYNITIEGK
TYTMNLTQKV FLPHNFKVYG YDGTGIMKPL DKDFQNFCYY QGFVEGYPNS MVMVSACTGL
RGLLQFENAT YGIEPLESSV GFEHVIYQVK YKNETVSLYT EKDIEIKNLP YKIQSIEPQE
MAQYLEMHII VEKHLYDHMG SDTTIVTQKI FQLIGLTNAI FTSFNLTIIL SSLELWVDEN
KMSTAGDANE LLHRFLRWKR SYLVLRPHDV AFLLVYRERT DFVGATFQGK MCERDYGGGV
AMHPKAIGLE SLAIILAQLV SLNMGISYDD VKKCHCPGTI CIMNPEAIHS SGVKIFSNCS
MEDFAHFVSK QKSECLQNHP RLEPSYKQAA VCGNKVVEQG EACDCGTEQE CGANRPVCCE
HSTCALTAGS ECASGPCCSE CKFSKKGHVC RSAANECDLT EYCNGSSQVC QENVFIIDGH
PCSENKWICI GGVCRSGDKQ CEDLFGQGSI FASEDCYNEL NSKTDISGNC GITDDGYKAC
EAKDRKCGKL ICKYGGSHIL QLKDATAIYA NITGDICVSL EYNKGHAEIK NMWVKDGTVC
GTKKVCKEKE CVDNSYLNYD CTPETCNNQG VCNNKRNCHC NADFVPPKCQ EEREGSGGGS
IDSGNHENTA AATERRFIER TYYESRTSRW PFFLVIPFFV ILCVLIGMLV KVHFQRKKWK
SEDYTSDEQL ESETESKE
//
