ID H3CXS6_TETNG Unreviewed; 1116 AA.
AC H3CXS6;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif, 10 {ECO:0000313|Ensembl:ENSTNIP00000013061.1};
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000013061.1, ECO:0000313|Proteomes:UP000007303};
RN [1] {ECO:0000313|Proteomes:UP000007303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
RN [2] {ECO:0000313|Ensembl:ENSTNIP00000013061.1}
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 -!- 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 AlphaFoldDB; H3CXS6; -.
DR STRING; 99883.ENSTNIP00000013061; -.
DR Ensembl; ENSTNIT00000013253.1; ENSTNIP00000013061.1; ENSTNIG00000010163.1.
DR GeneTree; ENSGT00940000158404; -.
DR HOGENOM; CLU_000660_1_1_1; -.
DR InParanoid; H3CXS6; -.
DR OMA; TQQCETK; -.
DR TreeFam; TF313537; -.
DR Proteomes; UP000007303; 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: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; 5.
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; IPR010909; PLAC.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR13723:SF26; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 10; 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; PF08686; PLAC; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF19030; TSP1_ADAMTS; 4.
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; 5.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50900; PLAC; 1.
DR PROSITE; PS50092; TSP1; 5.
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 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:UP000007303};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR613273-2}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1116
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003581337"
FT DOMAIN 248..467
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1078..1116
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 58..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 403
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /note="in inhibited form"
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 251
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 342
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 342
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 349
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 402
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 406
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 412
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 462
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 324..386
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 360..367
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 380..462
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 419..446
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 489..511
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 500..518
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 506..541
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 531..546
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 569..606
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 573..611
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 584..596
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1116 AA; 124547 MW; 1D5B18212401ADA8 CRC64;
METLWRTGLV CTVVAIVFAT EVAGGRRDEF VHSQAAFLSG LGQYDIAIPV RVGPHGETLA
AEKPQHHQRR RRSAEDRLPD SVRTSLFYQL STSRNNFLLN LTLQGGLLSR QFRVEYWKRG
RLAWTHPYSP HCHYVGHLND QPHSSKVALS NCNGLQGVIV AGGEEYLIEP LVSPDNQTGA
EKGERAEGRP HVVYKRSSLR HQYKGQSCGV IDEKPMKSAS WWQRTLKRLP ITSGRGQWPL
KRSVSRERYV ETLVVADKMM VGYHGRRDIE QYILAVMNIV AKLFQDSSLG NAVNIVVTRL
ILLMEDQPTL EINHHAGKSL DSFCKWQKTI QHRSSYANAI PDNGIAHHDT AVLITRYDIC
IQKNKPCETL GGLAPVGGMC EPERSCSINE DIGLGTAFTI AHELGHTFGM NHDGMGNACG
PLSQETAKLM ADHITMKTNP FIWSACSRDY ITSFLDSGMG SCLNNVPPKQ EFVYPTTAPG
QVYDADEQCR FQYGVRSRQC KYAEVCSELW CMSKSNRCIT SSIPAAEGTI CQTNTIEKGW
CYKRMCVAYG TRPEGVDGGW GLWSAWGECS RTCGGGVSSS IRHCDSPRPT IGGKYCLGER
KRFRSCNIDE CPAGSRDFRE IQCSDFDGVP FRGKFYTWKP YRGVGGVKPC SLNCLAEGYN
FYTERAPAVV DGTPCRDDSV DVCVNGECKH VGCDRVLGSD VREDRCRMCG GDGSGCVSVE
GLFNHSLPEG GYEEVVRIPK GSVFIHIQEL NISLNYLVLK SKGDQFFING NLSIDTPRRF
NVAGTTFYYR RPPDGPETLE ALGPTNMSLI IMVLVREENP GVHYRFNPPL NRDPLAGFAW
HFTSWSRCSA LCAGGVQTQQ VVCMKHSDRT VAHNHFCDKK SRPKEKRRPC NTEPCSPSWW
TGEWSECSRS CNGGLRTRQV LCKRRLSVTE EKVLDDSACS PLRPALTEPC NNRSCPPEWL
ALDWSECTPS CGPGYRHRVV LCKSGESGDT LPESKCPKHS RPTSRVRCNL KRCPPPQWVT
GPWGECSAKC GLGQEMRAVQ CLTHTGQLSN ECLEHQRPAS MQQCKSKCDL SLSVNADNSE
ECKDVNTVAY CPLVLRFKFC SRPYFRQMCC KTCQGH
//
