ID H2LYS0_ORYLA Unreviewed; 1184 AA.
AC H2LYS0;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 24-JAN-2024, entry version 73.
DE SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 14 {ECO:0000313|Ensembl:ENSORLP00000011290.2};
GN Name=LOC101172200 {ECO:0000313|Ensembl:ENSORLP00000011290.2};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000011290.2, ECO:0000313|Proteomes:UP000001038};
RN [1] {ECO:0000313|Ensembl:ENSORLP00000011290.2, ECO:0000313|Proteomes:UP000001038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000011290.2,
RC ECO:0000313|Proteomes:UP000001038};
RX PubMed=17554307; DOI=10.1038/nature05846;
RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT "The medaka draft genome and insights into vertebrate genome evolution.";
RL Nature 447:714-719(2007).
RN [2] {ECO:0000313|Ensembl:ENSORLP00000011290.2}
RP IDENTIFICATION.
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000011290.2};
RG Ensembl;
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}.
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DR AlphaFoldDB; H2LYS0; -.
DR STRING; 8090.ENSORLP00000011290; -.
DR Ensembl; ENSORLT00000011291.2; ENSORLP00000011290.2; ENSORLG00000009003.2.
DR eggNOG; KOG3538; Eukaryota.
DR GeneTree; ENSGT00940000158426; -.
DR HOGENOM; CLU_000660_4_1_1; -.
DR InParanoid; H2LYS0; -.
DR TreeFam; TF313537; -.
DR Proteomes; UP000001038; Chromosome 19.
DR Bgee; ENSORLG00000009003; Expressed in sexually immature organism and 4 other cell types or tissues.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
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; 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:SF24; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 14; 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:UP000001038};
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..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1184
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017294057"
FT DOMAIN 249..453
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1048..1086
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 54..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1097..1184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1148..1162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1165..1184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 392
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 252
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 252
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 344
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="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 395
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 401
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 448
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 451
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 451
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 326..375
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 369..448
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 408..434
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 475..500
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 486..509
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 495..528
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 522..533
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 557..594
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 561..599
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 572..584
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1184 AA; 132446 MW; BEA0D2DFB76CBD03 CRC64;
MNRFYLSIFL TWACECFSHF VPSEKVSGKL REYGLIVPFS TDSHGRYISH VVSAGSGSKS
SDAASSLGSI SSSSRRRRRV ARGAPEMPSA TSPAAQHLFF NVTVFGKELH LRLKANRRLV
APGAFVEWQE DFKEKSKEHI SGDCVFTGDV TDMPEASVAI SNCDGLAGLI RTDKGEFFIE
PLEKGQQDVE SKGRVHVVYR RSAIKAGQQK SDFHNEDVGI ADLPAALDLV EHKLSESERK
RRHAKKDDYN IEVLLAVDDS VVRFHGKEHV QNYVLTLMNI VDEIYHDESL GTNINIVLVR
MIMVGYRQSI SLIERGNPSR SLEQVCRWAN TQQRHNPDHA EYHDHAIFLT RQDFGPAGMQ
GYAPVTGMCH PLRSCTLNHE DGFSSAFVVA HETGHVLGME HDGQGNRCAD ETSMGSIMAP
LVQAAFHRYH WSRCSKQELN RYIHSYDCLL DDPFEHKWPK LPELPGINYS MDEQCRFDFG
VGYKMCTAFR TYDPCKQLWC SHPDNQYFCK TKKGPPVDGT DCAPGKWCFK GHCIWRSSQE
PQGHDGSWSS WSKFGSCSRT CGGGIRSRSR QCNNPPPAYG GRDCPGSAFD YQMCNTEECA
GAYEDFRAQQ CIQRSNKYHK NMKHTWLPYE DPDDSRKCEL SCISKETEEI VFMNQVVHDG
TRCSYSDPYS VCARGECLHV GCDKEVGSYK EEDKCGVCEG DNSHCRTVKL TLTKTPKKNG
MLKMFDIPIG ARHIVIEENE TSSHIIAVKN QVSGNFILNE KSEDAKLKTF IKNGLQWEYS
SDGDRETLKT SGPLHDGIVV LVIPMEEEVK ISLTYKYIIH EDLLPLITNN NVLLSELDTY
EWALKSWSQC SKPCGGGIQY TKYGCRRKSD GRLVHRNFCE SSKKPKPIRK RCNMLECSQP
KWVMEDWSPC SKSCGKLGYQ TRVVQCMQAL HNGTSRPIHS KHCPTNRPET RRVCNHTACP
AQWRTGAWSQ CSVSCGEGIQ QRQVVCKTSD NTVGECEGEK PETVLICKLS PCPGLPLSSP
SSQMTENATM NGEAVYQMVP KNPVDKMSNE PCLGDKSIFC QMEVLARYCS IPGYYKLCCE
SCSRKEGLPT NALDLHKPEV FPTQNPSKTA DAAARTSPPT DAALLQTPAD VSDREPPLPP
GPPLPTADAS GGQNSTLSPD AVRSRRDNLG SERDSGHRTL SARK
//