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Database: UniProt
Entry: F6TYF6_MONDO
LinkDB: F6TYF6_MONDO
Original site: F6TYF6_MONDO 
ID   F6TYF6_MONDO            Unreviewed;      1128 AA.
AC   F6TYF6;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 3.
DT   24-JAN-2024, entry version 76.
DE   SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 17 {ECO:0000313|Ensembl:ENSMODP00000015905.4};
GN   Name=ADAMTS17 {ECO:0000313|Ensembl:ENSMODP00000015905.4};
OS   Monodelphis domestica (Gray short-tailed opossum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Didelphimorphia; Didelphidae; Monodelphis.
OX   NCBI_TaxID=13616 {ECO:0000313|Ensembl:ENSMODP00000015905.4, ECO:0000313|Proteomes:UP000002280};
RN   [1] {ECO:0000313|Ensembl:ENSMODP00000015905.4, ECO:0000313|Proteomes:UP000002280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17495919; DOI=10.1038/nature05805;
RA   Mikkelsen T.S., Wakefield M.J., Aken B., Amemiya C.T., Chang J.L., Duke S.,
RA   Garber M., Gentles A.J., Goodstadt L., Heger A., Jurka J., Kamal M.,
RA   Mauceli E., Searle S.M., Sharpe T., Baker M.L., Batzer M.A., Benos P.V.,
RA   Belov K., Clamp M., Cook A., Cuff J., Das R., Davidow L., Deakin J.E.,
RA   Fazzari M.J., Glass J.L., Grabherr M., Greally J.M., Gu W., Hore T.A.,
RA   Huttley G.A., Kleber M., Jirtle R.L., Koina E., Lee J.T., Mahony S.,
RA   Marra M.A., Miller R.D., Nicholls R.D., Oda M., Papenfuss A.T., Parra Z.E.,
RA   Pollock D.D., Ray D.A., Schein J.E., Speed T.P., Thompson K.,
RA   VandeBerg J.L., Wade C.M., Walker J.A., Waters P.D., Webber C.,
RA   Weidman J.R., Xie X., Zody M.C., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA   Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA   Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA   Bayul T., Berlin A., Bessette D., Bloom T., Bloom T., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA   D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA   Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA   Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA   Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA   Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA   Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA   Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA   Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA   Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA   Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA   Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA   Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA   Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA   Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA   Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA   Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA   Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA   Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA   Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA   Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA   Chin C., Gnerre S., MacCallum I., Graves J.A., Ponting C.P., Breen M.,
RA   Samollow P.B., Lander E.S., Lindblad-Toh K.;
RT   "Genome of the marsupial Monodelphis domestica reveals innovation in non-
RT   coding sequences.";
RL   Nature 447:167-177(2007).
RN   [2] {ECO:0000313|Ensembl:ENSMODP00000015905.4}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-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   RefSeq; XP_001372991.2; XM_001372954.3.
DR   AlphaFoldDB; F6TYF6; -.
DR   STRING; 13616.ENSMODP00000015905; -.
DR   MEROPS; M12.027; -.
DR   Ensembl; ENSMODT00000016198.4; ENSMODP00000015905.4; ENSMODG00000012713.4.
DR   GeneID; 100020525; -.
DR   KEGG; mdo:100020525; -.
DR   CTD; 170691; -.
DR   eggNOG; KOG3538; Eukaryota.
DR   GeneTree; ENSGT00940000158773; -.
DR   HOGENOM; CLU_000660_8_0_1; -.
DR   InParanoid; F6TYF6; -.
DR   OMA; TCVMAKA; -.
DR   OrthoDB; 2910701at2759; -.
DR   TreeFam; TF313537; -.
DR   Proteomes; UP000002280; Chromosome 1.
DR   Bgee; ENSMODG00000012713; Expressed in skeleton of lower jaw and 11 other cell types or tissues.
DR   GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
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; IPR006586; ADAM_Cys-rich.
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   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR13723:SF151; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 17; 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; 4.
DR   Pfam; PF00090; TSP_1; 1.
DR   PRINTS; PR01857; ADAMTSFAMILY.
DR   SMART; SM00608; ACR; 1.
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.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|PIRSR:PIRSR613273-2};
KW   Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
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:UP000002280};
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};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..1128
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5023931253"
FT   DOMAIN          241..461
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000259|PROSITE:PS50215"
FT   DOMAIN          1081..1120
FT                   /note="PLAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50900"
FT   REGION          61..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        399
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         244
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT   BINDING         244
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT   BINDING         346
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT   BINDING         398
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         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         408
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         456
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT   DISULFID        317..382
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        357..364
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        376..456
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3,
FT                   ECO:0000256|PROSITE-ProRule:PRU00276"
FT   DISULFID        415..440
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        485..509
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        496..517
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        504..536
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        530..541
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        564..601
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        568..606
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        579..591
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ   SEQUENCE   1128 AA;  126161 MW;  5CB393735DE7E986 CRC64;
     MFDGSLLPPL LFHLLLLLLF GELDTSAAVG SVTAFELEVV LPQRVRPEDI HLLPLPTADL
     GAGGYGSPRE RRRRQPHTAA STEQSPDSGK RGFLLHLPAF GRDLYLQLRR DLRFLSRGFV
     VEEHGTAGSR IPEAELCFYT GHVLGYNNSF ASVSTCGGLI GYIQIGKEQM LIQPVNNSNG
     SFNGREHLVR RKRSSNSGDH AKSWIPDELC TVITEKKKPK KNKTTSDWRE RRNAIRLTNE
     YTVETLVVAD ADMVRYHGAE AAQRFILTVM NMVYNMFQHH SLGIKVNIQV TKLVLLRNRP
     AKLSIGHHGE RSLESFCHWQ NEEYGGAKYL GNNQVPGGKD DTPPVDAAVF VTRTDFCVHK
     DEPCDTVGIA YLGGVCSAKR KCVLAEDNGL NLAFTIAHEL GHNMGMNHDD DHLSCAGRSH
     IMSGEWVKGR NPSDLSWSSC SRDDLENFLK SKVSMCLLVT DPRSQYAVRL PHKLPGMHYS
     AEEQCQILFG TNATFCKNME HLMCAGLWCL VEGDTSCKTK LDPPLDGTEC GADKWCRAGE
     CVNKTPIPEH VDGDWSTWSP WSMCSRTCGT GARFRQRKCD NPPPGPGGTN CWGASVEHIV
     CENLPCPKGV PSFRDQQCQS HDRYNYKKKG PLTAVIIDDK PCELYCSPLG KESPMLIADR
     VLDGTPCGPY ETDLCVHGRC QKIGCDGIIG SAAKEDRCGI CNGDGKTCKV VKGDFNHTKG
     MGYIEAAVIP AGARRIRVVE DKPAHSFLAL KDSSKKSINN DWKIELPGEF QIAGTTVRYV
     RRGLWEKISA KGPTKIPLHL MVLLFHDQNY GIHYEYTVPV NYTAEIQNEP EKLQDSLYIW
     THSGWEGCSV QCGGGERKTI VSCTKIINKT MTLANDSDCQ HVSRPEPQVR RCNLHPCQSR
     WMTGHWSPCS ATCEKGIQHR EVTCVYQLQN GTYVNTRDFY CLSHKPTTVQ SCEGRDCLSI
     WEASEWSKCS ADCGIGTQRR TVACTNSQGK CDQTTRPKAE EECEDYTGCF EWKTGDWSKC
     SSTCGKGLQS RVVQCMHKIT GRHGNECPIL SKPAAYRQCH QEVCNEKINV NTITSPRLAA
     LTYKCTGDQW TVYCRVIREK NLCQDMRWYQ RCCQTCRDFY ANKMQQKS
//
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