ID G5B1A1_HETGA Unreviewed; 1543 AA.
AC G5B1A1;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 14 {ECO:0000313|EMBL:EHB03062.1};
GN ORFNames=GW7_10650 {ECO:0000313|EMBL:EHB03062.1};
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:EHB03062.1, ECO:0000313|Proteomes:UP000006813};
RN [1] {ECO:0000313|EMBL:EHB03062.1, 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 -!- 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}.
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DR EMBL; JH167923; EHB03062.1; -; Genomic_DNA.
DR STRING; 10181.G5B1A1; -.
DR eggNOG; KOG3538; Eukaryota.
DR InParanoid; G5B1A1; -.
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; -; 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; IPR045762; ADNP_Znf.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR010909; PLAC.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR13723:SF24; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 14; 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; PF19627; ADNP_N; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF19030; TSP1_ADAMTS; 3.
DR Pfam; PF00090; TSP_1; 1.
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:ARBA00022801};
KW Integrin {ECO:0000313|EMBL:EHB03062.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR613273-2};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000006813};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR613273-2}.
FT DOMAIN 618..787
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1386..1424
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 173..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1428..1543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1428..1446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1485..1502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 726
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 681
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 725
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 729
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 735
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 782
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 785
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 785
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 663..709
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 703..782
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 742..768
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 809..834
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 820..843
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 829..862
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 856..867
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 891..928
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 895..933
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 906..918
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1543 AA; 170076 MW; 773894243BBEA8F3 CRC64;
MDYSNRGFQL DLDANGNLLF PHLHFVTILP REKLGEHEVY LAILAGIHSK SLVPVYIKVR
PQPETVSNNP SKQKLTCPFC FGTFVTADAY ELHLKERHHV MPTVHTMLRS PAFKCIHCCG
VYTGNMTLAA IAVHLLHGRS APKDSSSDLQ VQPGFTESSD LVLVNGEVIP DSTFPTKRKL
PDGHLGTEDQ RGGEESPLVV NSEAAPEPRL SGKLSDYAVT VPCSTDFQGR FLSHVVSGSA
EASAGSVVVD RTPIPPLHSR HLRVARSPLS PDRGTLPPGE AQRYFLYFNV TVFGKELHLR
LRPNRRLVVP GASVEWQEDF QELLRHPLQQ ECVYTGGVTG XXXXXXXXXX XXXXXXXXXX
XXXXMPGAAV AISNCDGLAG LIRTDSTDYF IEPLERGQQQ KEAGGRTHVV YRREAIQWDR
AEPHHDLHNE AFGLGDLPNL LGLVGDQLGD TERKRRHAKP SSYSIEVLLA VDDSVVRFHG
REHVQNYLLT LMNIAVVMNL GEGRCSNRRQ IRRLSILFHS KTVETRPANV AYEGVWNTAT
VNLRREEHLR QMKGSVCLRY AGHCVLLSEG PELWSQGSVL HIAVISLDLK KVIAANPLPS
TSPILSTFRS SSDQGRHVDE IYHDESLGAH MNIALVRLIM VGYRQSLSLI ERGNPARSLE
QVCRWAHSQQ RQDPDHAEHH DHVVFLTRQN FGPSGYAPVT GMCHPLRSCA LNHEDGFSSA
FVVAHETGHV LGMEHDGQGN GCADETSLGS VMAPLVQAAF HRFHWSRCSK LELSRYLPSY
DCLLDDPFEP AWPQPPELPG IDYSMDEQCR FDFGTGYQTC LAFRTFEPCK QLWCSHPDNP
YFCKTKKGPP LDGTECEPGK WCFKGHCIWK SPEQTYGQDG GWSSWSKFGS CSRSCGGGVQ
SRSRSCDNPP PAYGGRPCSG PLFEYQICNR EDCPGPYEDF RAQQCAKRNS YYIHQNAKHS
WVPYEPDDDT QKCELICQSV DTGEVVYMNQ VVHDGTRCSY RDPYSVCARG QCVPIGCDKE
VGSMKADDKC GVCGGDNSHC RTVKGTLGKA SKQAAALKLV QIPAGARHIQ IETLEKAPHR
IAVKNQVTGS FILNPKGKEA LSRTFTALGL EWEHEVKDAK DSLKTSGPLP EAIAVLVLPP
AEGSPRGSLA YKYVIHEDLL PLIGSNNVLL EETDTYEWAL KSWAPCTKAC GGGIQFTKYG
CRRRRDHHMV QQHLCDPRKR PKPIRRRCNQ HPCPQPGWVT AEWAACSRSC GKLGGQTRGV
QCLLPLSNGT RKALPAKACP GARPEARRPC LRIPCPAQWR MGAWSQCSAT CGAGVQQRQV
VCRTTANSLR QCEGDKPDTS QVCSLPACEG NLQNSTATAE IQELVTLEGQ QVSESGTLPP
MNKRSPTEPC VGDRSIFCQM EVLDLHCAIP GYHRLCCVSC SKKASGPNAS LSSTPTFPTP
GSHLAQPKAT PNIMEPTMEP EGADDHQHGR PTQLPGPPDT RSSVPQPYLV PQTLSPRVFG
GTSPATPQAP PWGWTPAAVT ASEDQGRPRE ESRHRGPAFP PPP
//
