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
//