ID   A0A8M9PJM4_DANRE        Unreviewed;      1192 AA.
AC   A0A8M9PJM4;
DT   03-AUG-2022, integrated into UniProtKB/TrEMBL.
DT   03-AUG-2022, sequence version 1.
DT   08-NOV-2023, entry version 8.
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};
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 (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}.
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   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
//