ID S7Q093_MYOBR Unreviewed; 652 AA.
AC S7Q093;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 5 {ECO:0000313|EMBL:EPQ16683.1};
GN ORFNames=D623_10008279 {ECO:0000313|EMBL:EPQ16683.1};
OS Myotis brandtii (Brandt's bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ16683.1, ECO:0000313|Proteomes:UP000052978};
RN [1] {ECO:0000313|Proteomes:UP000052978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23962925; DOI=10.1038/ncomms3212;
RA Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y.,
RA Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., Hee Yim S.,
RA Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., Chen G., Kulakova O.I.,
RA Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., Sunyaev S.R., Zhang G.,
RA Krogh A., Wang J., Gladyshev V.N.;
RT "Genome analysis reveals insights into physiology and longevity of the
RT Brandt's bat Myotis brandtii.";
RL Nat. Commun. 4:2212-2212(2013).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR613273-2};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR613273-2};
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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DR EMBL; KE164280; EPQ16683.1; -; Genomic_DNA.
DR RefSeq; XP_005880711.2; XM_005880649.2.
DR AlphaFoldDB; S7Q093; -.
DR MEROPS; M12.225; -.
DR GeneID; 102254159; -.
DR KEGG; myb:102254159; -.
DR CTD; 11096; -.
DR eggNOG; KOG3538; Eukaryota.
DR OrthoDB; 2910701at2759; -.
DR Proteomes; UP000052978; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:InterPro.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04273; ZnMc_ADAMTS_like; 1.
DR Gene3D; 2.60.120.830; -; 1.
DR Gene3D; 3.40.1620.60; -; 2.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 2.
DR InterPro; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR013273; ADAMTS/ADAMTS-like.
DR InterPro; IPR041645; ADAMTS_CR_2.
DR InterPro; IPR045371; ADAMTS_CR_3.
DR InterPro; IPR010294; ADAMTS_spacer1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR13723:SF37; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 5; 1.
DR PANTHER; PTHR13723; ADAMTS A DISINTEGRIN AND METALLOPROTEASE WITH THROMBOSPONDIN MOTIFS PROTEASE; 1.
DR Pfam; PF17771; ADAMTS_CR_2; 1.
DR Pfam; PF19236; ADAMTS_CR_3; 1.
DR Pfam; PF05986; ADAMTS_spacer1; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF19030; TSP1_ADAMTS; 1.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00209; TSP1; 2.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 2.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50092; TSP1; 2.
PE 4: Predicted;
KW Calcium {ECO:0000256|PIRSR:PIRSR613273-2};
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR613273-3};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023049};
KW Integrin {ECO:0000313|EMBL:EPQ16683.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR613273-2, ECO:0000256|PROSITE-
KW ProRule:PRU00276}; Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000052978};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Zinc {ECO:0000256|PIRSR:PIRSR613273-2, ECO:0000256|PROSITE-
KW ProRule:PRU00276}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 9..198
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT ACT_SITE 133
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 82
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 193
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 196
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 196
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 64..116
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 93..98
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 110..193
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 148..177
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 219..241
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 230..251
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 236..270
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 264..275
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 301..338
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 305..343
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 316..328
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 652 AA; 71740 MW; 8223999FA124AEC9 CRC64;
MARLYGRGLQ HYLLTLASIA NRLYSHASIE NHIRLAVVKV VVLGDKDKSL EVSKNAATTL
KNFCKWQHQH NQLGDDHEEH YDAAILFTRQ DLCGHHSCDT LGMADVGTIC SPERSCAVIE
DDGLHAAFTV AHEIGHLLGL SHDDSKFCEE NFGSTEDKRL MSSILTSIDA SKPWSKCASA
TITEFLDDGH GNCLLDLPRK QILGPEELPG QTYDATQQCN LTFGPEYSVC PGMDVCARLW
CAVVRQGQMV CLTKKLPAVE GTPCGKGRIC LQGKCVDKTK KKYYSTSSHG NWGSWGSWGQ
CSRSCGGGVQ FAYRHCNNPA PRNSGRYCTG KRAIYRSCSV MPCPANGKSF RHEQCEAKNG
YQSDAKGVKT FVEWVPKYAG VLPGDVCKLT CRAKGTGYYV VFSPKVTDGT ECRPYSNSVC
VRGKCVRTGC DGIIGSKLQY DKCGVCGGDN SSCTKIIGTF NKKSKGYTDV VRIPEGATHI
KVRQFKAKDQ TRFTAYLALK KKNGEYLING KYMISTSETI VDLNGTVMNY SGWSHRDDFL
HGMGYAATKE ILIVQILATD PTKALDVRYS FFVPKKSTLK GNSVTNHGSN KVGSHAPQLQ
WVTGPWLACS RSCDTGWHTR TVQCQDGNRK LAKGCLLSQR PSAFKQCLLK KC
//
