ID A0A8P0SDL0_CANLF Unreviewed; 934 AA. AC A0A8P0SDL0; DT 28-JUN-2023, integrated into UniProtKB/TrEMBL. DT 28-JUN-2023, sequence version 1. DT 08-NOV-2023, entry version 3. DE SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 5 {ECO:0000313|Ensembl:ENSCAFP00000012608.5}; GN Name=ADAMTS5 {ECO:0000313|Ensembl:ENSCAFP00000012608.5, GN ECO:0000313|VGNC:VGNC:37601}; OS Canis lupus familiaris (Dog) (Canis familiaris). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis. OX NCBI_TaxID=9615 {ECO:0000313|Ensembl:ENSCAFP00000012608.5, ECO:0000313|Proteomes:UP000002254}; RN [1] {ECO:0000313|Ensembl:ENSCAFP00000012608.5, ECO:0000313|Proteomes:UP000002254} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000012608.5}; RX PubMed=16341006; DOI=10.1038/nature04338; RG Broad Sequencing Platform; RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B., RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E., RA Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F., RA Smith D.R., deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W., RA Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S., RA Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A., RA Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P., RA Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A., RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P., RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P., RA Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B., RA Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A., RA Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M., RA Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., RA Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., RA Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S., RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C., RA Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G., RA Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N., RA Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A., RA Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A., RA Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M., RA Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., RA LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A., RA Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S., RA Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., RA Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., RA Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N., RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S., RA Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M., RA Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F., RA Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T., RA Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C., RA Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C., RA Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D., RA Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H., RA Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J., RA Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J., RA Zembek L., Zimmer A., Lander E.S.; RT "Genome sequence, comparative analysis and haplotype structure of the RT domestic dog."; RL Nature 438:803-819(2005). RN [2] {ECO:0000313|Ensembl:ENSCAFP00000012608.5} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR Ensembl; ENSCAFT00000013627.5; ENSCAFP00000012608.5; ENSCAFG00000024758.5. DR VGNC; VGNC:37601; ADAMTS5. DR Proteomes; UP000002254; Chromosome 31. DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:InterPro. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; 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; -; 2. DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1. DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 2. 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; IPR013276; Pept_M12B_ADAM-TS5. 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:SF37; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 5; 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; 1. DR Pfam; PF00090; TSP_1; 1. DR PRINTS; PR01860; ADAMTS5. DR PRINTS; PR01857; ADAMTSFAMILY. DR SMART; SM00608; ACR; 1. DR SMART; SM00209; TSP1; 2. DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1. DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 2. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS50092; TSP1; 2. 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, ECO:0000256|PIRSR:PIRSR613276- KW 4}; 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 Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR613273-2}; KW Zymogen {ECO:0000256|ARBA:ARBA00023145}. FT SIGNAL 1..20 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 21..934 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5039933770" FT DOMAIN 271..480 FT /note="Peptidase M12B" FT /evidence="ECO:0000259|PROSITE:PS50215" FT REGION 20..71 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 207..259 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 213..252 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 415 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1, FT ECO:0000256|PROSITE-ProRule:PRU00276" FT BINDING 274 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2" FT BINDING 274 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2" FT BINDING 357 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2" FT BINDING 357 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2" FT BINDING 364 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2" FT BINDING 414 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 418 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 424 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 475 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2" FT BINDING 478 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2" FT BINDING 478 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2" FT CARBOHYD 502 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000256|PIRSR:PIRSR613276-4" FT CARBOHYD 732 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000256|PIRSR:PIRSR613276-4" FT DISULFID 346..398 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" FT DISULFID 375..380 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" FT DISULFID 392..475 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" FT DISULFID 430..459 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" FT DISULFID 501..523 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" FT DISULFID 512..533 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" FT DISULFID 518..552 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" FT DISULFID 546..557 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" FT DISULFID 583..620 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" FT DISULFID 587..625 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" FT DISULFID 598..610 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" SQ SEQUENCE 934 AA; 101775 MW; 3209D009F8AFEB92 CRC64; MLLGWASLLL GALRLPPVAA GPAAAPAQDK AGQPWAAAAA AQPRRRQGEE AREPAEPPGH PHPLAPQRRS SGLVQNVDQI YAGGGKVGYL VYAGGRRFLL DLERDGSVGA AGSAPAGRGP GAPRRHRDHC FYRGTVDGSP RSLAVLDLCG GLDGFFAVRH ARYTLKPLLR GPWAGAGAGA EAERVYGDGS PRILHVYTRE GFSFEALPPR TSCETPASPP GPRERPPAHS SPDPRWSPAP PFPAPPAASP DGGPGPQTWW RRRRRSISRA RQVELLLVAD ASMARMYGRG LQHYLLTLAS IANRLYSHAS IENHIRLAVV KVVVLGDKDK SLEVSKNAAT TLKNFCKWQH QHNQLGDDHE EHYDAAILFT REDLCGHHSC DTLGMADVGT ICSPERSCAV IEDDGLHAAF TVAHEIGHLL GLSHDDSKFC EENFGSTEDK RLMSSILTSI DASKPWSKCT SATITEFLDD GHGNCLLDLP RKQILGPEEL PGQTYDATQQ CNLTFGPEYS VCPGMDVCAR LWCAVVRQGQ MVCLTKKLPA VEGTPCGKGR ICLQGKCVDK TKKKYYSTSS HGNWGSWGSW GQCSRSCGGG VQFAYRHCNN PAPRNNGRYC TGKRAIYRSC NVTPCPPNGK SFRHEQCEAK NGYQSDAKGV KTFVEWVPKY AGVLLGDVCK LTCRAKGTGY YVVFSPKVTD GTECRPYSNS VCVRGKCVRT GCDGIIGSKL QYDKCAVCGG DNSSCTKVVG TFNKKSKGYT DVVRIPEGAT HIKVRQFKAK DQTRFTAYLA LKKKNGEYLI NGKYMISTSE TIIDINGTVM NYSGWSHRDD FLHGMGYSAT KEILIVQILA TDPTKALDVR YSFFVPKKST QKVNSVTSHA SNKVGSHTPQ LQWVTGPWLA CSRTCDTGWH TRTVQCQDAN RKLAKGCLLS QRPSAFKQCL LKKC //