ID I3MCJ7_ICTTR Unreviewed; 835 AA.
AC I3MCJ7;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 5 {ECO:0000313|Ensembl:ENSSTOP00000007988.3};
GN Name=ADAMTS5 {ECO:0000313|Ensembl:ENSSTOP00000007988.3};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000007988.3, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000007988.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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; AGTP01083148; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01083149; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01083150; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01083151; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; I3MCJ7; -.
DR STRING; 43179.ENSSTOP00000007988; -.
DR Ensembl; ENSSTOT00000008915.3; ENSSTOP00000007988.3; ENSSTOG00000008876.3.
DR eggNOG; KOG3538; Eukaryota.
DR GeneTree; ENSGT00940000159090; -.
DR HOGENOM; CLU_000660_3_0_1; -.
DR InParanoid; I3MCJ7; -.
DR TreeFam; TF331949; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:InterPro.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0050840; F:extracellular matrix binding; IEA:Ensembl.
DR GO; GO:0008201; F:heparin binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0003180; P:aortic valve morphogenesis; IEA:Ensembl.
DR GO; GO:0042742; P:defense response to bacterium; IEA:Ensembl.
DR GO; GO:0003203; P:endocardial cushion morphogenesis; IEA:Ensembl.
DR GO; GO:0022617; P:extracellular matrix disassembly; IEA:Ensembl.
DR GO; GO:0007520; P:myoblast fusion; IEA:Ensembl.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0003184; P:pulmonary valve morphogenesis; IEA:Ensembl.
DR CDD; cd04273; ZnMc_ADAMTS_like; 1.
DR Gene3D; 2.60.120.830; -; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 2.
DR InterPro; IPR013273; ADAMTS/ADAMTS-like.
DR InterPro; IPR045371; ADAMTS_CR_3.
DR InterPro; IPR010294; ADAMTS_spacer1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR013276; Pept_M12B_ADAM-TS5.
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; 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; PR01860; ADAMTS5.
DR PRINTS; PR01857; ADAMTSFAMILY.
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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR613273-3};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR613273-2, ECO:0000256|PROSITE-
KW ProRule:PRU00276}; Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|PIRSR:PIRSR613273-2, ECO:0000256|PROSITE-
KW ProRule:PRU00276}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..835
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012836246"
FT DOMAIN 267..476
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT REGION 24..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 411
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 270
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 270
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 353
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 353
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 360
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 410
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 414
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 420
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 DISULFID 342..394
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 371..376
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 426..455
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 484..521
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 488..526
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 499..511
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 835 AA; 91916 MW; 3E538EF50CD0D44A CRC64;
MRLGWASLLL CAFRLSLAAA SRAEAPAQDK AQQSPVAAAA AQPRERQGEE ALERVEPLGH
PYPLALQRRS SGLVQNIDQL YSGGGKVGYL IYAGGRRFLL DLERDGSVGT SGFVPIGGGL
SAPRRHRSHC FYRGTVDGSP RSLAVFDLCG GLEGFFAVKH ARYTLKPLLR GPWPEGETGR
VYGDGSARVL HVYTREGFSF EALPPRASCE TPASRPGVHQ RLQLHSSPDR HTALASKLRD
QSALLPMGDP GPQTWWRRRR RSISRARQVE LLLVADASMA RMYGRGLQHY LLTLASIANR
LYSHASIENH IRLVVVKVVV LGDKDKSLEV SKNAATTLKN FCKWQHQHNQ LEDDHEEHYD
AAILFTREDL CGHHSCDTLG MADVGTICSP ERSCAVIEDD GLHAAFTVAH EIGHLLGLSH
DDSKFCEENF GSTEDKRLMS SILTSIDASK PWSKCTSATI TEFLDDGHTS SHGNWGSWGP
WGQCSRSCGG GVQFAYRHCN NPAPRNSGRY CTGKRAIYRS CSVTPCPPNG KSFRHEQCEA
KNGYQSDAKG VKTFVEWVPK YAGVLPADVC KLTCRAKGTG YYVVFSPKVT DGTECRPYSN
SVCVRGKCVR TGCDGIIGSK LQYDKCGVCG GDNSSCTKVI GTFNKKSKGY TDVVRIPEGA
THIKVRQFKA KDQTRFTAYL ALKKKNGEYL INGKYMISTS ETIIDINGTV MNYSGWSQRD
DFLHGMGYSA TKEILIVQIL ATDPTKALDV RYSFFVPKKS TQKVNSVTSH GSNKVGSHLP
QLQWVTGPWL ACSRTCDTGW HTRTVQCQDG NRKLAKGCLL SQRPSAFKQC LLKKC
//
