ID A0A3B4G3L9_9CICH Unreviewed; 284 AA.
AC A0A3B4G3L9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Metalloproteinase inhibitor 3 {ECO:0000256|ARBA:ARBA00013517};
DE AltName: Full=Tissue inhibitor of metalloproteinases 3 {ECO:0000256|ARBA:ARBA00030101};
GN Name=TIMP3 {ECO:0000313|Ensembl:ENSPNYP00000016338.1};
OS Pundamilia nyererei.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000016338.1, ECO:0000313|Proteomes:UP000261460};
RN [1] {ECO:0000313|Ensembl:ENSPNYP00000016338.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- SIMILARITY: Belongs to the protease inhibitor I35 (TIMP) family.
CC {ECO:0000256|ARBA:ARBA00011027}.
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DR AlphaFoldDB; A0A3B4G3L9; -.
DR STRING; 303518.ENSPNYP00000016338; -.
DR Ensembl; ENSPNYT00000016746.1; ENSPNYP00000016338.1; ENSPNYG00000012365.1.
DR GeneTree; ENSGT00940000159601; -.
DR Proteomes; UP000261460; Unplaced.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IEA:UniProtKB-KW.
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 PANTHER; PTHR11844; METALLOPROTEASE INHIBITOR; 1.
DR PANTHER; PTHR11844:SF22; METALLOPROTEINASE INHIBITOR 3; 1.
DR Pfam; PF00965; TIMP; 1.
DR SMART; SM00206; NTR; 1.
DR SUPFAM; SSF50242; TIMP-like; 1.
DR PROSITE; PS50189; NTR; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR601820-3};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Metal-binding {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 Secreted {ECO:0000256|ARBA:ARBA00022530};
KW Zinc {ECO:0000256|PIRSR:PIRSR601820-1}.
FT DOMAIN 97..216
FT /note="NTR"
FT /evidence="ECO:0000259|PROSITE:PS50189"
FT BINDING 97
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 DISULFID 97..164
FT /evidence="ECO:0000256|PIRSR:PIRSR601820-3"
FT DISULFID 99..191
FT /evidence="ECO:0000256|PIRSR:PIRSR601820-3"
FT DISULFID 109..216
FT /evidence="ECO:0000256|PIRSR:PIRSR601820-3"
FT DISULFID 218..265
FT /evidence="ECO:0000256|PIRSR:PIRSR601820-3"
FT DISULFID 223..228
FT /evidence="ECO:0000256|PIRSR:PIRSR601820-3"
FT DISULFID 236..257
FT /evidence="ECO:0000256|PIRSR:PIRSR601820-3"
SQ SEQUENCE 284 AA; 32424 MW; 9F2E104B53D2A1EC CRC64;
MCACAPPRDQ GETLEQREAS CDRRAALQTW TVLAEPATST DYLLKQQPAC GGDSADLVGQ
FYSREGVRKF GEMHSVYLVS LLFIFSTLHV NQLTEGCSCA LTHPQDAFCN SDIVIRAKVV
GKKLLRDGPF GTMRYTVKQM KMYKGFEKVQ HVQHIYTDAS ESLCGVKFDI NKYQYLITGR
VYDGKVYTGL CNLNERWERL SLAQKKGINH RYQLGCNCRI KPCHYLPCFV TSKNECLWTD
MLSHFGYPGY QSRHYACIQQ KEGYCSWYRG MTTRDKTTIN ATDP
//
