ID G5B0Q1_HETGA Unreviewed; 1283 AA.
AC G5B0Q1;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 9 {ECO:0000313|EMBL:EHB02865.1};
GN ORFNames=GW7_00190 {ECO:0000313|EMBL:EHB02865.1};
OS Heterocephalus glaber (Naked mole rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Heterocephalus.
OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB02865.1, ECO:0000313|Proteomes:UP000006813};
RN [1] {ECO:0000313|EMBL:EHB02865.1, ECO:0000313|Proteomes:UP000006813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993625; DOI=10.1038/nature10533;
RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT "Genome sequencing reveals insights into physiology and longevity of the
RT naked mole rat.";
RL Nature 479:223-227(2011).
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; JH167826; EHB02865.1; -; Genomic_DNA.
DR STRING; 10181.G5B0Q1; -.
DR MEROPS; M12.021; -.
DR eggNOG; KOG3538; Eukaryota.
DR InParanoid; G5B0Q1; -.
DR Proteomes; UP000006813; 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; 8.
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:SF33; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 9; 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; 8.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 10.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 8.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50092; TSP1; 9.
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 Hydrolase {ECO:0000256|ARBA:ARBA00023049};
KW Integrin {ECO:0000313|EMBL:EHB02865.1};
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:UP000006813};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Zinc {ECO:0000256|PIRSR:PIRSR613273-2, ECO:0000256|PROSITE-
KW ProRule:PRU00276}.
FT DOMAIN 84..290
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 50..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 947..976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..35
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 226
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 87
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 87
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 174
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 225
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 229
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 235
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 285
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 159..209
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 185..191
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 203..285
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 241..269
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 312..334
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 323..343
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 329..366
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 356..371
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 394..431
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 398..436
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 409..421
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1283 AA; 141926 MW; 1D6C445E8C666BE6 CRC64;
MYKLHVAPKP VSVVTDTGHR SSRRKNRRKG SRRKWGATIH PAGDVAALHS GSAAEPPAAL
GNRTDGLRDR GTRRRTKRFL SYPRFVEVMV VADNKMLLYH GANLQHYVLT LMAIVASIYK
DPSIGNLINI VIVNLVVIHD EQEGPPISFN AQTTLKNFCQ WQHSKNYPGG IQHDTAVLIT
RQDICRAHDK CDTLGLAELG TICDPYRSCS ISEDSGLSTA FTIAHELGHV FNMPHDDSNK
CREEGVKNTQ HVMAPTLTVD TNPWIWSKCS RKYITEFLDT GYGECLLNEP ESRPYSLPSQ
LPGLFYSVNK QCEFIFGPGA ELCPYMVQCR RLWCNVKRKD QSCQTQHTPW ADGTECEPGK
ASAQHCKFGF CVPKEMEGPA VDGSWGSWSP YGTCSRTCGG GIKTAIRECD QPEPRHGGKY
CVGRRMKFKS CSLEPCLKQK QDFRDEQCAH FDGKHFNING LLPTVRWVPK YSGILMKDRC
KLFCRVAGST AYYQLRDRVV DGTPCGQDTN DICVQGLCRQ AGCDHVLNSK ARRDKCGVCG
GDNSSCRTVA GTFNAVHYGY NTVVRIPAGA TSIDVRQHSF SGKSEDDNYL ALSSSKGEFL
LNGDFVVTMS KKEIRIGKAM IEYSGSDNIV ERINSTDRID QELVLQVLSV GKLYNPDVRY
SFNVPIEGRL QQFYWNSRGP WQACSKPCQG VRRRKPVCTR ESDQLPVSDQ RCDRLPQPEP
ITEACGTDCD LRWHVGGRSE CSAQCGLGYR TLDVYCARYS RLDGKTEKVD DSFCSSHPKP
NNQEKCSGEC NTGGWRYSAW TECSKSCDGG SQRRRAICVN SQNDVLDDNK CTHQEKVTTQ
RCNEFPCPQW QSGDWSECLV TCGKGHRHRQ VWCQFGEDRV SDKICDPQAK PASMQPCQQS
ECASWQAGPW GQCSVTCGQG YQLRAVKCVL GTYMAVVDDS GCSAGTRPTD TQDCEVSPCQ
PPPVAPEARS PHGGRRTQWR FGSWTSCSAT CGKGTRMRYV SCRGEDGSVA DESACASLPR
PEAREGCSVT PCGQWKASDW SACSVTCGQG RATRQVVCVN YSDHVVGQSE CDLDYIPETD
QDCSMAPCPR WGPDRGWAAS HPFQNEDFRP RGAGPSRTHV LSGNQWRTGP WGACSSTCAG
GSQRRVVVCQ DENGYPARDC VERIKPDEQR ACEAGPCPQW VSGSWGECTK PCGGGVRTRL
VVCQRASGQR FPDLSCDVLE KPPDREQCGA HTCPDGTWSA GPWSSMVTQE SCGGHSDVTE
HVCLIPDRVP GSSFLLARLT DSD
//
