ID A0A3Q3ADJ9_KRYMA Unreviewed; 915 AA.
AC A0A3Q3ADJ9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 15 {ECO:0000313|Ensembl:ENSKMAP00000009279.1};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000009279.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000009279.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; A0A3Q3ADJ9; -.
DR Ensembl; ENSKMAT00000009415.1; ENSKMAP00000009279.1; ENSKMAG00000006923.1.
DR GeneTree; ENSGT00940000155801; -.
DR Proteomes; UP000264800; Unplaced.
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; -; 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; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000264800};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Zinc {ECO:0000256|PIRSR:PIRSR613273-2, ECO:0000256|PROSITE-
KW ProRule:PRU00276}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 184..393
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 328
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 187
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 187
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 270
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 270
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 277
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 327
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 331
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 337
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 388
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 391
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 391
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 259..311
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 288..293
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 305..388
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 343..372
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 414..436
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 425..446
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 431..465
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 459..470
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 494..531
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 498..536
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 509..521
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 915 AA; 100688 MW; FDE3465C7A5EDA37 CRC64;
MCMEGGRRSG GDSPEREKHR QEERVDETVF KLSAFRQDFY LHLTPDSSFL AVGSIPEEES
SDLRRCFYSG TVNADPDSFA ALSLCRGLQG CFSYKGMEYF ITQSSGEAEA ASESGSLLER
THAIRRRSRA AQPGANTTSR CGVPPDTNFS FPLDKYKHLN TIGGLTDAVL KSLGRSKRFV
SVPRFVEVLV VADESMATFH GDDLKHYLLT LMAVAARLYK HPSILNSISI VVVGFMVIND
ADMGPKVSSN AALSLRNFCS WQKKLNKPSD KHPEYWDTAI LFTKQDLCGA TTCDTLGMAD
VGTVCDPKRS CSVIEDDGLP SAFTTAHELG HVFSMPHDNV KACEKVFGKL KDNHMMSPTL
IQINRSQPWS VCSAAIITEF LDRGYGDCLL DQPQMQLSLH DSLPGSSYSL HRQCELAFGP
GSKPCPYMQP CLKLWCTGKA HGQLVCQTRH FPWADGTSCG NGKVCYRSAC VDMNSTVHIK
VDGRWGKWGA FGDCSRSCGG GVQLAGRQCN NPVPENGGKY CYGLRIKYRS CNLNPCPEKG
KSFREEQCEA FNGINLNTNR LGSTVAWVPK YSGISSKDKC KLICRANGTG YFYVLAPKVV
DGTPCSPDTS AVCVQGKCIK AGCDGKLDSN KKFDKCGVCG GDNHGCKKVS GMFTKPVNGY
NFVVTLPVGA ANIDIRQRGY RGMISDENYL AVKDRHGKYL LNGNYVVSAA ERDMLVKGSL
LRYSGTSTSV ETLQAITPLQ EPLTVEVLSV GKMTPPRVCY SFYTLKESKE EKTLWKEKKS
HKMQNSVLVD GKNTKIKKES MVKGPVSHWV TRGWEACTVT CGNGSQRRLV QCQSMEGHPT
VDCDNSQKPV AVRACGDPCP IWDVGTWSNC SKSCGRGFKR RLVRCMTENG LILPREHCSG
KIKPQELDLC NWKPC
//
