ID A0A151JXM5_9HYME Unreviewed; 1079 AA.
AC A0A151JXM5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 7 {ECO:0000313|EMBL:KYN39801.1};
GN ORFNames=ALC56_05788 {ECO:0000313|EMBL:KYN39801.1};
OS Trachymyrmex septentrionalis.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Trachymyrmex.
OX NCBI_TaxID=34720 {ECO:0000313|EMBL:KYN39801.1, ECO:0000313|Proteomes:UP000078541};
RN [1] {ECO:0000313|EMBL:KYN39801.1, ECO:0000313|Proteomes:UP000078541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tsep2-gDNA-1 {ECO:0000313|EMBL:KYN39801.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYN39801.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Trachymyrmex septentrionalis WGS genome.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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; KQ981567; KYN39801.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151JXM5; -.
DR STRING; 34720.A0A151JXM5; -.
DR Proteomes; UP000078541; 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; 3.
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; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR13723:SF200; ADAM METALLOPEPTIDASE WITH THROMBOSPONDIN TYPE 1 MOTIF B, ISOFORM B; 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; 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; 5.
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; PS50092; TSP1; 4.
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:KYN39801.1};
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:UP000078541};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR613273-2}.
FT DOMAIN 222..375
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT REGION 153..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 311
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 251
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 251
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 258
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 310
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 314
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 320
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 370
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 373
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 373
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 240..294
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 269..276
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 288..370
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 327..354
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 397..421
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 409..427
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 416..446
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 440..451
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 474..511
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 478..516
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 489..501
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1079 AA; 120957 MW; D4169E3C6F70A830 CRC64;
MQTADFLVCQ VSSFILSGVY TLQEHLHNHE IVIPRKVNHR GDLISENVTH HHHEDGPIVH
YRMAVAGNEY HLELTAVDNF IGRAMVVERR KRDLHVRSPA KSHGSKCHYR GFIKGHRNSR
VALSACDGLA GMLHGDHGEF WLEPVAVSLE EKRGASSADE ATSGDLGAGA RASVYGGPTA
GRPHLVFRRS AERRQRQLEI GATASIDRNA ARMANSIRPR PSSRPLDITV NADKTLYNFC
KWQQKLNPSN DSHPNHHDVA ILVTREDICS RANTPCSTLG VAHVAGMCQP DRSCSVNEDN
GITLAHTITH ELGHNFGMYH DTEKIGCSKR EGDTLHVMTP TFEVDAVGVA WSRCSRRDIT
NFLDQGKGDC LEDEPADNDY AYPDLPPGAM YNAEHQCRLQ FGVREAFVCS PLQEICSKLW
CIVDGSCTTM LHPAAPGTHC GKHMWCQNQE CVPIVDRPRQ IDGGWGEWGL WSECSRTCGA
GVSIVERKCD HPEPAYGGKF CIGERRRYKI CNTQPCPEGT PSFRAVQCSN YDDKEYKGKN
YTWLPYFDQT EPCELYCTDT DESVIVPWGE AALDGTPCNV GTRDMCIAGI CRKVGCDWMV
DSDATEDRCG ICHGDGTQCE TTSGVYDKNE GPGYKEVIII PSGSRNIKIE EVGNSKNYIG
IGVPNSDKYF LNGKRQITLA GEYEVAGTPA LYERDRDREK IRIPGPIKED IAVYLIYRGQ
YRNFGLRYEY TVPKKEPDRA PEYSWVFSDW TLCTVTCGGG TQTSHAVCHE RKSGIVEDLF
CDGIEKPEQK SRECNSNPCP ARWWVGPWQM CPVTCGDGAL RKRSVMCVFS GMGTDRSDLA
LPDRDCDKHM RPEEMEPCPD LPPCGPTSEV PLIVYADNKD MSFYNISLNE QDGITIVDGL
TTEEPEILEF DNVVDENPDN SMYNTKSKWT VSKWSHCSNS KRSRKVTCSV PGDCNPNNKP
PSIEDCYSGK WITGNWGSCN ATCLVKSGVK HRDVQCRDRA SDLLSNDCNL DRRPFDIKRC
YYRRQCANEK NDCKDSVVPS CANYRRMCDV SSIVREKCCA TCTKRRRHVR HNKRHIFTE
//
