ID L5MDT0_MYODS Unreviewed; 1042 AA.
AC L5MDT0;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 8 {ECO:0000313|EMBL:ELK36784.1};
GN ORFNames=MDA_GLEAN10021254 {ECO:0000313|EMBL:ELK36784.1};
OS Myotis davidii (David's myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK36784.1, ECO:0000313|Proteomes:UP000010556};
RN [1] {ECO:0000313|Proteomes:UP000010556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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; KB101169; ELK36784.1; -; Genomic_DNA.
DR AlphaFoldDB; L5MDT0; -.
DR MEROPS; M12.208; -.
DR eggNOG; KOG3607; Eukaryota.
DR Proteomes; UP000010556; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; 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:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
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; IPR013111; EGF_extracell.
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:SF20; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 8; 1.
DR Pfam; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF07974; EGF_2; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Integrin {ECO:0000313|EMBL:ELK36784.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Reference proteome {ECO:0000313|Proteomes:UP000010556};
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..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1042
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003971121"
FT TRANSMEM 659..682
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 198..398
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 406..492
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 614..646
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 714..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 989..1016
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 726..746
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..766
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 333
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 332
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 336
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 342
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 464..484
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 618..628
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 636..645
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1042 AA; 112078 MW; 017907D971A1F73F CRC64;
MLHLGLWLLG VWWLQVAAPS PPLSHVEQYE VVRPQRLPGP RARRALPSSV GLYPESVSYV
LGAPGNTFTL HLRKNRDLVG SGYTETYTAA NGSQVTEQLQ RQDHCFYQGH VEGHPLSAAS
LSTCDGLRGF FQAGSAVHLI EPLDGSGEEG QHALYKAQHL QQKAGTCGVS NTSLESMLGP
RTLAAFRPRN RPLSRKTRFV ELYVVTDSRE FQKLGSREAV RRRVLEVVNH VDKLYQELKF
RVVLVGLDIW NHGDKIQVSS DASVTLDNFL TWRAQNLVGR HPHDNVQLIT GIDFAGSTVG
LAKVSAMCSQ NSGAVNQDHS PNPIGVACTL AHEMGHNLGM DHDENVQGCY CPESRTRGGC
VMAGSIGSTF PTLFSQCSQD DLETFVEKPR ITCIANAPDP DRLVGGPVCG NGFVEQGEQC
DCGYPQDCRD RCCNTTTCQL AEGAECAHGA CCHECRVKPA GKLCRPGKDA CDLDEYCDGQ
RPSCPEDAFQ ENGTPCPGGY CYNGACPTRA QRCQDLWGPG TQPARETCYS FNVLPGCQSN
ARLGAERAGC ETLFCEGGQK PPERASCTFT YSSAICQALN LDGGSGFERV LEGTRCGNER
VCWKGLCQDF HVYRSRNCSA QCNGHGVCNH KGQCHCQPGW APPHCTELLA ELRVASRSLL
MGVVVPVVLL VTLALTVLGV VVHRKAGSRI RGRNVAPKTA MGLSNPLFQK RGFGPEKGMA
PAPTTHSPEP VTTMSANHSG PLPRPTASAV TPTRPPPAPP ATMSSPLFPV PMYTQQSPAQ
LRPAPPTKPL PEQKPRQVIK PTSVPPVPPV KPKAGGANPG TTENFTINLG LLGVSHQEDS
TEGDIRKVVA NTPGAIEPIL CALKEKVVDA VREDPPGAGL LVGAFVPQPL KSLQDPGVSG
ADADGLWLGL ATTPHAGSTQ TPDVCGKRAA ASRQACGALE FTHLQGRAGV LSSPVPSGVK
TLQSQRAEKT GHYACRGRDP AGGPREHLNT GVQQLLEEKE QALAILQETV QVLQMKVIRL
EHLVELKDRR ISELTRRGIE PQ
//
