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Database: UniProt
Entry: G3MY93_BOVIN
LinkDB: G3MY93_BOVIN
Original site: G3MY93_BOVIN 
ID   G3MY93_BOVIN            Unreviewed;       767 AA.
AC   G3MY93;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 2.
DT   27-MAR-2024, entry version 80.
DE   RecName: Full=ADAM metallopeptidase domain 30 {ECO:0008006|Google:ProtNLM};
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 {ECO:0000313|Ensembl:ENSBTAP00000054522.2, ECO:0000313|Proteomes:UP000009136};
RN   [1] {ECO:0000313|Ensembl:ENSBTAP00000054522.2, ECO:0000313|Proteomes:UP000009136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000054522.2,
RC   ECO:0000313|Proteomes:UP000009136};
RA   Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA   Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA   Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT   "ARS-UCD1.2.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSBTAP00000054522.2}
RP   IDENTIFICATION.
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000054522.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   AlphaFoldDB; G3MY93; -.
DR   SMR; G3MY93; -.
DR   STRING; 9913.ENSBTAP00000054522; -.
DR   PaxDb; 9913-ENSBTAP00000054522; -.
DR   Ensembl; ENSBTAT00000063960.2; ENSBTAP00000054522.2; ENSBTAG00000046293.2.
DR   VEuPathDB; HostDB:ENSBTAG00000046293; -.
DR   eggNOG; KOG3607; Eukaryota.
DR   GeneTree; ENSGT00940000162954; -.
DR   HOGENOM; CLU_012714_4_0_1; -.
DR   InParanoid; G3MY93; -.
DR   OMA; FCGLTND; -.
DR   TreeFam; TF314733; -.
DR   Proteomes; UP000009136; Chromosome 3.
DR   Bgee; ENSBTAG00000046293; Expressed in semen and 4 other cell types or tissues.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:1990913; C:sperm head plasma membrane; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; 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:SF148; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 30; 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; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
PE   4: Predicted;
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   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009136};
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}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..767
FT                   /note="ADAM metallopeptidase domain 30"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018631874"
FT   TRANSMEM        683..704
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          202..392
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000259|PROSITE:PS50215"
FT   DOMAIN          398..484
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000259|PROSITE:PS50214"
FT   DOMAIN          628..661
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   REGION          746..767
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        751..767
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         337
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         341
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         347
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   DISULFID        456..476
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT   DISULFID        651..660
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   767 AA;  86454 MW;  B5A0B987AEE4A32B CRC64;
     MRSVRTCLSP GRSLVLAVLL VDSLGKDLHF HPEWGFDSYE ITIPKKLSFR GREQRAARHV
     SYLLKVKGRN RVVHLWPKRF LLPRNLQVFS FTEQGRLLED HPYIPSDCNY MGLVEGNPDS
     QATISTCMGG LRGILKIDAN HYQIEPRKAS SQFEHVVYLL EKEEEFPSDF CGLTNDETVE
     QMAQHENMAR TPDFTESYVH QKYLELALVF DNSRYLYLNS NLTQIINDAI LLTSIADSYF
     QDVRMRIQLL AVEVWTDRDK IRLNFGQLSQ VLGQFVKYRS RDLRVRIPAD WAHLYVHKKF
     KDALAHHWGS VCSMMPSGST SSVLDRNILG PATWTAHVLG HSVGMTHDYE YCQCKGRHSC
     IMGTGRTGFS NCSYAEFYSH VNSGLNCLNN LPGLGYVVKR CGNKIVEENE ECDCGSGEEC
     EEDGCCQPDC KFKEGANCST GLCCHKCQFR PSGYMCRVEE NECDLAEYCN GTSAFCPSDT
     YKQDGTPCKY RSRCVRKGCQ SRTMQCQNIF GADALGAPHQ CYDAVNVIGD QYGNCGILGV
     REYKKCPKER SLCGRLQCIN VETLPDMPDH TILISTHLHK ENLMCWGIGY HLAMVPMGLR
     DLGVINDGTS CGKERVCFNR NCVNSSILNF DCFPEKCNRR GVCNSNRNCH CMYGWAPPLC
     EEVGYGGSID SGPPGPLRKN MPISLQVVIL ILMRLIFLII SVIVKKTPEK IHPEMQETQV
     CSLGQEDTLE KAVAIHTSIL AREISRTEDS GELQSKGSQK SLTRLSD
//
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