ID A0A8M9PJM4_DANRE Unreviewed; 1192 AA. AC A0A8M9PJM4; DT 03-AUG-2022, integrated into UniProtKB/TrEMBL. DT 03-AUG-2022, sequence version 1. DT 24-JAN-2024, entry version 9. DE SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 3 isoform X1 {ECO:0000313|RefSeq:XP_021331662.1}; GN Name=adamts3 {ECO:0000313|RefSeq:XP_021331662.1, GN ECO:0000313|ZFIN:ZDB-GENE-110223-1}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Danionidae; Danioninae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|Proteomes:UP000000437, ECO:0000313|RefSeq:XP_021331662.1}; RN [1] {ECO:0000313|Proteomes:UP000000437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23594743; DOI=10.1038/nature12111; RG Genome Reference Consortium Zebrafish; RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J., RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D., RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B., RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J., RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D., RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B., RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P., RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., RA Rogers J., Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the human RT genome."; RL Nature 496:498-503(2013). RN [2] {ECO:0000313|RefSeq:XP_021331662.1} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:XP_021331662.1}; RG RefSeq; RL Submitted (SEP-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 RefSeq; XP_021331662.1; XM_021475987.1. DR ZFIN; ZDB-GENE-110223-1; adamts3. DR Proteomes; UP000000437; Chromosome 5. 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; -; 2. 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; 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:SF158; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 3; 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; 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. 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:UP000000437}; 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..20 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 21..1192 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5035442364" FT DOMAIN 248..452 FT /note="Peptidase M12B" FT /evidence="ECO:0000259|PROSITE:PS50215" FT DOMAIN 1028..1071 FT /note="PLAC" FT /evidence="ECO:0000259|PROSITE:PS50900" FT REGION 1107..1192 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1107..1137 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1175..1192 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 391 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="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 343 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2" FT BINDING 390 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 394 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 400 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 447 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2" FT BINDING 450 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2" FT BINDING 450 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2" FT DISULFID 325..374 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" FT DISULFID 368..447 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" FT DISULFID 407..433 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" FT DISULFID 474..499 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" FT DISULFID 485..508 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" FT DISULFID 494..527 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" FT DISULFID 521..532 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" FT DISULFID 555..592 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" FT DISULFID 559..597 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" FT DISULFID 570..582 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" SQ SEQUENCE 1192 AA; 134921 MW; 1385783A6E35B50B CRC64; MVVLSLRLLI VGVVVSLTSA HLAGEIIDKE DLLKNRLKEY GLITPISTDA EGHFLSHFLS ANHKQRVKRD VLEGSAPAPD RLFFNITVFG KEFHLRLHPN QRLVAPGAMV EWHDDIEIAG NATDNRTHFE RILKRELLKT DCTFIGDITD VPGASVAINN CDGLAGMIRT DSDEYFIEPL EQGTQEHEER GRVHVVYRRS AVLQTPSDIS LDYQPIEPEL DTPRMLDNIA KQVNKTVRRR RHAGDEDYNI EILLGVDDSV VRFHGKEHVQ NYLLTLMNIV NEIYHDESLE VHINVVLVRM IMLGYAKSIS LIERGNPSRS LENVCRWAFV QQKEDPEHSE HHDHAIFLTR QGFGPTGMQG YAPVTGMCHP VRSCTLNHED GFSSAFVVAH ETGHVLGMEH DGQGNRCGDE TAMGSVMAPL VQAAFHRYHW SMCSGQELKR YIHSYDCLLD DPFKHDWPQL PELPGINYSM DEQCRFDFGV GYKICTSFRT FDPCKQLWCS HPDNPYFCKT KKGPPLDGTE CAPGKWCYKG HCMWKNANQV KQDGAWGAWS KYGSCSRSCG MGVRFRTRQC NNPVPSNGGQ DCPGVNYEYQ LCNTDDCPKH FEDFRAQQCQ LRNSHFEYQN AKHHWLPYEH PDANKRCHLY CQSKETGDVA YMKQLVHDGT RCSYKDPYSI CVRGECVKVG CDREIGSNKV EDKCGVCGGD NSHCRTVKGT FTRVPKKAGK TRGAFLLPKG ARNVYLNETA DSRNVMGYLK MFLIPPGARH VIIQEHEASP QILAIKNQAT GHYVLNGKGE DARSRRFIEM GVEWDYLVEE DVETLHTDGP LNDAIVVLII PKDNETRSTL MYKYIIHEDS VPLNNNNVIQ EDTYEWALKS WSQCSRPCAG GFQYTKYGCR KKGDNKMVHR GYCDVNKKPK PIRRMCNLQD CTQPQWITEE WEHCTKTCGS LGYQIRTVRC VQFLHEGTNR SIHSKYCNGE KPEMRRACNR VACPAQWRTG AWSECSVSCG EGVSRRLVTC RIGDQCTGEK PESQKPCRPR PCHDEPCGGD KSIFCQMEVL ARYCSIPGYN KLCCESCSRR SGTFAPLLHE AAETEEELRF GSASQLLETL SAAANGSLKV PQQHQRGSTS QGQFSKQAAT PPPRKHNTEN SKTQKRLKPS TRNLPALSIH SSWSEDGVKD APMQLESFQE SQWPTTSSEV ER //