ID L5LE80_MYODS Unreviewed; 962 AA.
AC L5LE80;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 17 {ECO:0000313|EMBL:ELK24191.1};
DE Flags: Fragment;
GN ORFNames=MDA_GLEAN10019496 {ECO:0000313|EMBL:ELK24191.1};
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:ELK24191.1, 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 -!- 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 -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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; KB112968; ELK24191.1; -; Genomic_DNA.
DR AlphaFoldDB; L5LE80; -.
DR MEROPS; M12.027; -.
DR eggNOG; KOG3538; Eukaryota.
DR Proteomes; UP000010556; 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; -; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 4.
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; IPR010909; PLAC.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR13723:SF151; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 17; 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; 4.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 4.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 4.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50900; PLAC; 1.
DR PROSITE; PS50092; TSP1; 4.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|PIRSR:PIRSR613273-2};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR613273-3};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023049};
KW Integrin {ECO:0000313|EMBL:ELK24191.1};
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:UP000010556};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Zinc {ECO:0000256|PIRSR:PIRSR613273-2, ECO:0000256|PROSITE-
KW ProRule:PRU00276}.
FT DOMAIN 88..308
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 908..947
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT ACT_SITE 246
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 91
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 91
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
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 245
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 249
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 255
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 303
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 164..229
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 204..211
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 223..303
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 262..287
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 332..356
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 343..364
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ELK24191.1"
SQ SEQUENCE 962 AA; 105985 MW; 6FBC3F4EAAC0A1F3 CRC64;
CFFSGQVGLI QLGQEQVLLQ PLNSSRGPHG GREHLLRRKW SLAPSPSAQA QAPGPLCQVL
TEKKKPGKGG PSLDWRERRS AIRLTNEHTV ETLVVADADM VQYHGAEAAQ RFILTVMNMV
YNMFQHQTLG IKVNIQVTKL VLLRQRPAKL SIGHHGERSL ESFCHWQNEE YGGARYLGNN
QVPGGKDDTP PVDAAVFVTR TDFCVHKDEP CDTVGIAYLG GVCSAKRKCV LAEDNGLNLA
FTIAHELGHN LGMNHDDDHA SCAGRSHIMS GEWVKGRNPS DLSWSSCSRD DLENFLKSKV
STCLLVTDPR SQHAVRLPHK LPGMHYSANE QCQILFGTNA TFCRNMEHLM CAGLWCLVEG
DASCKTKLDP PLDGTECGAD KVPTPANPRG QPPSLGHWAL PGPGGAHCLG ASVEHAVCEN
PPCPKGLPSF RDQQCQTHDR LSSKKKGLLT AVVVDDKPCE LYCSPLGKES PLLVADRVLD
GTPCGPYETD LCVHGRCQKI GCDGIIGSAA KEDRCGVCSG DGKTCRVVKG DFSHSRGTGY
IEAAVIPAGA RRIRVVEDKP AHSFLALKDS SRRSINSDWK IELPGEFQIA GTTVRYVRRG
LWEKISAKGP TKIPLHLMVL LFHDQNYGIH YEYTIPVNAT AENQSEPEKP HDSLFIWTHS
GWEGCSVQCG GGERRTIVSC TRIVNKTTTL VNDSECPAAS RPEPQVRRCN SHPCQARWVA
GPWSPCSATC EKGVQQREVT CVHQLPNGTH VTTRPLYCQG ARPAPVQSCE GQDCLSIWEA
SEWSQCSASC GHGTQKRTVT CTNSQGKCDA STRPRAEEAC EDYSGCYAWR TGDWSKCSST
CGKGLQSRVV QCMHKVTGRH GNECPTLSKP AAYRQCHQEV CNDKINVNNS QEAPSLVLSE
PWRGRPALTY KCTRDQWTVY CRVIREKNLC QDMRWYQRCC QTCRDFYANK MRRPLPPPSP
SS
//
