ID Q4W7T6_ORYLA Unreviewed; 220 AA.
AC Q4W7T6; H2LU60;
DT 05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE RecName: Full=Metalloproteinase inhibitor 2 {ECO:0000256|ARBA:ARBA00013520};
DE AltName: Full=Tissue inhibitor of metalloproteinases 2 {ECO:0000256|ARBA:ARBA00030102};
GN Name=timp-2b {ECO:0000313|EMBL:BAD99515.1};
GN Synonyms=timp2b {ECO:0000313|Ensembl:ENSORLP00000009634.2};
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|EMBL:BAD99515.1};
RN [1] {ECO:0000313|EMBL:BAD99515.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15941829; DOI=10.1073/pnas.0502423102;
RA Ogiwara K., Takano N., Shinohara M., Murakami M., Takahashi T.;
RT "Gelatinase A and membrane-type matrix metalloproteinases 1 and 2 are
RT responsible for follicle rupture during ovulation in the medaka.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:8442-8447(2005).
RN [2] {ECO:0000313|Ensembl:ENSORLP00000009634.2, ECO:0000313|Proteomes:UP000001038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000009634.2,
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 [3] {ECO:0000313|Ensembl:ENSORLP00000009634.2}
RP IDENTIFICATION.
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000009634.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the protease inhibitor I35 (TIMP) family.
CC {ECO:0000256|ARBA:ARBA00011027}.
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DR EMBL; AB193468; BAD99515.1; -; mRNA.
DR RefSeq; NP_001188455.1; NM_001201526.2.
DR STRING; 8090.ENSORLP00000009634; -.
DR MEROPS; I35.002; -.
DR Ensembl; ENSORLT00000009635.2; ENSORLP00000009634.2; ENSORLG00000007689.2.
DR GeneID; 100529200; -.
DR KEGG; ola:100529200; -.
DR CTD; 406650; -.
DR eggNOG; KOG4745; Eukaryota.
DR GeneTree; ENSGT00940000158348; -.
DR HOGENOM; CLU_084029_0_0_1; -.
DR OMA; ITRCTSI; -.
DR OrthoDB; 5403389at2759; -.
DR TreeFam; TF317409; -.
DR Proteomes; UP000001038; Chromosome 8.
DR Bgee; ENSORLG00000007689; Expressed in heart and 14 other cell types or tissues.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IBA:GO_Central.
DR GO; GO:0002020; F:protease binding; IBA:GO_Central.
DR GO; GO:0051045; P:negative regulation of membrane protein ectodomain proteolysis; IBA:GO_Central.
DR GO; GO:0034097; P:response to cytokine; IBA:GO_Central.
DR GO; GO:0009725; P:response to hormone; IBA:GO_Central.
DR CDD; cd03585; NTR_TIMP; 1.
DR Gene3D; 2.40.50.120; -; 1.
DR Gene3D; 3.90.370.10; Tissue inhibitor of metalloproteinase-1. Chain B, domain 1; 1.
DR InterPro; IPR001134; Netrin_domain.
DR InterPro; IPR001820; TIMP.
DR InterPro; IPR008993; TIMP-like_OB-fold.
DR InterPro; IPR027465; TIMP_C.
DR InterPro; IPR030490; TIMP_CS.
DR PANTHER; PTHR11844; METALLOPROTEASE INHIBITOR; 1.
DR PANTHER; PTHR11844:SF24; METALLOPROTEINASE INHIBITOR 2; 1.
DR Pfam; PF00965; TIMP; 1.
DR SMART; SM00206; NTR; 1.
DR SUPFAM; SSF50242; TIMP-like; 1.
DR PROSITE; PS50189; NTR; 1.
DR PROSITE; PS00288; TIMP; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR601820-3};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR601820-1};
KW Metalloenzyme inhibitor {ECO:0000256|ARBA:ARBA00023215};
KW Metalloprotease inhibitor {ECO:0000256|ARBA:ARBA00022608};
KW Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW Reference proteome {ECO:0000313|Proteomes:UP000001038};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR601820-1}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..220
FT /note="Metalloproteinase inhibitor 2"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041158861"
FT DOMAIN 27..152
FT /note="NTR"
FT /evidence="ECO:0000259|PROSITE:PS50189"
FT BINDING 27
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared with metalloproteinase partner"
FT /evidence="ECO:0000256|PIRSR:PIRSR601820-1"
FT SITE 40
FT /note="Involved in metalloproteinase-binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR601820-2"
FT SITE 67
FT /note="Involved in metalloproteinase-binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR601820-2"
FT DISULFID 27..98
FT /evidence="ECO:0000256|PIRSR:PIRSR601820-3"
FT DISULFID 29..127
FT /evidence="ECO:0000256|PIRSR:PIRSR601820-3"
FT DISULFID 39..152
FT /evidence="ECO:0000256|PIRSR:PIRSR601820-3"
FT DISULFID 154..201
FT /evidence="ECO:0000256|PIRSR:PIRSR601820-3"
FT DISULFID 159..164
FT /evidence="ECO:0000256|PIRSR:PIRSR601820-3"
FT DISULFID 172..193
FT /evidence="ECO:0000256|PIRSR:PIRSR601820-3"
SQ SEQUENCE 220 AA; 24712 MW; B519E4A2692B32E3 CRC64;
MTWMNNSCLV TLAVLLLWRV EEIAEACSCS PAHPQQAVCN SDVVIRAKLV GRQEVDAGND
IYGNTIKRIK YDVKQIKMFK GPSHDIDAVY TAPSSSLCGV SMDTTGKKEY LITGKLETDG
TMHVTLCDFI DQWDAMTATQ KKNLIQRYES SCDCKITHCT SIPCVLSSPT ECLWTDWVIE
KTVKGEQAKH YACIKRNDDS CAWYRGSTPP RKEFLDIEDP
//