ID A0A3B3U3T0_9TELE Unreviewed; 942 AA.
AC A0A3B3U3T0;
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=A disintegrin and metalloproteinase with thrombospondin motifs 15-like {ECO:0000313|Ensembl:ENSPLAP00000007361.1};
OS Poecilia latipinna (sailfin molly).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000007361.1, ECO:0000313|Proteomes:UP000261500};
RN [1] {ECO:0000313|Ensembl:ENSPLAP00000007361.1}
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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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DR AlphaFoldDB; A0A3B3U3T0; -.
DR STRING; 48699.ENSPLAP00000007361; -.
DR Ensembl; ENSPLAT00000004693.1; ENSPLAP00000007361.1; ENSPLAG00000009786.1.
DR GeneTree; ENSGT00940000155801; -.
DR Proteomes; UP000261500; Unplaced.
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; 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; IPR013277; Pept_M12B_ADAM-TS8.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR13723:SF39; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 15; 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; PF01421; Reprolysin; 1.
DR Pfam; PF19030; TSP1_ADAMTS; 2.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01861; ADAMTS8.
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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023049};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR613273-2, ECO:0000256|PROSITE-
KW ProRule:PRU00276}; 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|PIRSR:PIRSR613273-2, ECO:0000256|PROSITE-
KW ProRule:PRU00276}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..942
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017360378"
FT DOMAIN 204..413
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT REGION 794..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 348
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 207
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 207
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 290
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 290
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 297
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 347
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 351
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 357
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="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 411
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 411
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 279..331
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 308..313
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 325..408
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 363..392
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 434..457
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 445..467
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 452..486
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 480..491
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 514..551
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 518..556
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 529..541
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 942 AA; 104614 MW; C648CD10F2FA1645 CRC64;
MFVRTVFLLH FVKFIRCMES EICFPIRLDD DRDDFNNDLD ISVRKRVMKI QAFQQELVID
LQQDSDFIAP SISVQDGFWF SNTDVSTDLR GCFYSGHVNG DRGSYAALSL CKGLNGAFGF
QGWEYFIRPV RNDTRSAQDA HIVRRRPSND LRQNSTSRCA VESDLSPLDA QSLQKYKQTT
DLNNVTETML KKMGRAKRFA SVPRYVETLV AADESMLSFH GDDLKHYLLT LMSVAARLYR
HPSILNSISI TVVKIVIISE EDKGPKVSGN AAMTLRNFCT WQKKMNKHND KHPDYWDTAI
LFTRQDLCGA STCDTLGMAD VGTMCDPKRS CSVIEDDGLP SAFTTAHELG HVFNMPHDNV
KACEDVFGKL QENHMMSPTL IQINRTSPWS PCSAAIITEF LDSGHGDCLL DQPQKTLVLP
DVLPGSSYDL DRQCELAFGE GSKPCPFLQP PCSRLWCTGK SSGHLVCMTR HFPWADGTRC
GDGQVCDRGV CSDRQLQTVK LDGRWGKWGP FGSCSRTCGS GVQLSKRECN NPAPSNGGKY
CQGVRVKYRS CSLNRCPETG GNKAYREEQC ETSGQTFSSN HVAQSVVWVP KYSGVSAKDR
CKLICRANGT GYFYVLSPKV VDGTPCSPDS TGVCVQGKCI KAGCDRVIGS TKKFDKCGIC
GGDNKSCKKV SGLFTKPVHG YNFVVMLPVG AANVDIRQRG YKGMMGDDNY LAVKNSKGHY
LLNGNYIVSA GERDIIVNNS LLRYSGTTGL SETLHAVNPL GEALTVEVLC AGKITPPRIR
YSFYLHRQTK EDKMLKKGER ANSENSVLTK DEMKKDEEDN LKSSYSKMNA PVGKWISAPW
EECSVSCGRG FQRRMVQCLK SDGKPGLDCD SSQRPSATRV CGDPCADWHI GQWSPCSRTC
GKGFKRRPLH CKDQTGLLLP RDLCKGLRKP QELDFCNLSS CQ
//
