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Database: UniProt
Entry: H2LYS0_ORYLA
LinkDB: H2LYS0_ORYLA
Original site: H2LYS0_ORYLA 
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
//
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