ID A0A3B3SFK0_9TELE Unreviewed; 935 AA.
AC A0A3B3SFK0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 1 {ECO:0000313|Ensembl:ENSPKIP00000029522.1};
GN Name=ADAMTS1 {ECO:0000313|Ensembl:ENSPKIP00000029522.1};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000029522.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000029522.1}
RP IDENTIFICATION.
RG Ensembl;
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}.
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DR AlphaFoldDB; A0A3B3SFK0; -.
DR STRING; 1676925.ENSPKIP00000029522; -.
DR Ensembl; ENSPKIT00000010319.1; ENSPKIP00000029522.1; ENSPKIG00000010736.1.
DR GeneTree; ENSGT00940000156815; -.
DR OrthoDB; 2910701at2759; -.
DR Proteomes; UP000261540; Unplaced.
DR GO; GO:0031012; C: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; -; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 3.
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; IPR013274; Pept_M12B_ADAM-TS1.
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:SF40; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 1; 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; 2.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01858; ADAMTS1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00209; TSP1; 3.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 3.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50092; TSP1; 3.
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 Repeat {ECO:0000256|ARBA:ARBA00022737};
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..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..935
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017434563"
FT DOMAIN 223..432
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT REGION 173..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 367
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 183
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 226
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 226
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 309
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 309
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 316
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 366
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 370
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 376
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 427
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 430
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 430
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 298..350
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 327..332
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 344..427
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 382..411
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 453..476
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 464..487
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 471..506
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 500..511
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 537..574
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 541..579
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 552..564
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 935 AA; 102875 MW; CA647B2038450D71 CRC64;
MRSFLCISLG WLAALYVSTA HGAWMESAVV PVRLYPAQAK DETVQPRTHS NEEREKVGER
RIYQLDAFGK RIVLDLETDQ TFLATGFVFQ MIGQPESPDP ETQRVSDSRA MAGCFFSGQV
NGETDSAAAL NVCHGLKGGF YADGEECFIQ PDSDTDSGVS DSSLHILRCK SRKPHAEDGG
SKCGVNEEEE RQPLRKEKGV IADPAAPDHK AHHRSRRFVS TPRYVELLLV ADKLMADFHG
ARLKPYLLTI MAVAARLYRH PSIHNSITLA VVKVLVVNDE QHGPNVSRNA ALTLRDFCKW
QRQHNPPSDR HPEHYDTAVL FTKQDLCGPH SCETLGMADV GTACDPERSC SIVEDDGLQT
AFFVAHELGH VLNMLHDDAK QCTSINDPTL PPLMMSSTLY NLNHQQPWSP CSALRITSFL
DNGHGDCLLD KPQKAELLPK ALPGSIYDVD QQCRLMFGEE SQHCPDANTT CAALWCTVNN
AGGLLVCQTK SFPWADGTPC GKDRWCLAGE CLHKSKATEF QTPVNGGWGI WGPWGDCSRT
CGGGVQYSFR DCDNPTPKNG GKYCEGKRIQ YRSCNTEPCP DTNGLSFREE QCLAHNDISS
SMSFGTSGGV EWVPKYAGVS PKDRCKLICR AKGTGYFFIL KPKVADGTPC SPDSTSVCVQ
GQCVKAGCDL VIGSNRRFDK CGVCGGDGST CKKVSRSLKF ASPGYQDVVV IPAGATHVDI
KQHGHHQDSS YLALRRQDGT YLLNGDYKLT TLETDIFLRG ALLRYSGASA TLERIRSFGP
LPEPLTVVVL SVGDSPRPRI KLTFFAPRPV GRRPSINAIQ ETGSAEWVMR DWGQCSLTCG
GGLQQRNVDC LDSRGRPSSE CPVELRPPIS RPCPPHPCPI WQLGMWSPCS KTCGQSFRKR
TLHCMSHSGR LLGYESCDPK ARPRPLLEMC RQRPC
//
