Tag | Content |
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CPLM ID | CPLM-022758 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Serine protease HTRA1 |
Protein Synonyms/Alias | High-temperature requirement A serine peptidase 1; Serine protease 11 |
Gene Name | Htra1 |
Gene Synonyms/Alias | Htra; Prss11 |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
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373 | ESHDRQAKGKAVTKK | acetylation | [1] | 375 | HDRQAKGKAVTKKKY | acetylation | [1] |
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Reference | [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV. Cell Rep. 2012 Aug 30;2(2):419-31. [ PMID: 22902405] |
Functional Description | Serine protease with a variety of targets, including extracellular matrix proteins such as fibronectin. HTRA1-generated fibronectin fragments further induce synovial cells to up-regulate MMP1 and MMP3 production. May also degrade proteoglycans, such as aggrecan, decorin and fibromodulin. Through cleavage of proteoglycans, may release soluble FGF-glycosaminoglycan complexes that promote the range and intensity of FGF signals in the extracellular space. Regulates the availability of insulin-like growth factors (IGFs) by cleaving IGF-binding proteins. Inhibits signaling mediated by TGF-beta family members. This activity requires the integrity of the catalytic site, but it is unclear whether it leads to the proteolytic degradation of TGF-beta proteins themselves (PubMed:18551132) or not (PubMed:14973287). By acting on TGF-beta signaling, may regulate many physiological processes, including retinal angiogenesis and neuronal survival and maturation during development. Intracellularly, degrades TSC2, leading to the activation of TSC2 downstream targets. |
Sequence Annotation | DOMAIN 33 100 IGFBP N-terminal. DOMAIN 98 157 Kazal-like. DOMAIN 365 467 PDZ. REGION 204 364 Serine protease. ACT_SITE 220 220 Charge relay system (Potential). ACT_SITE 250 250 Charge relay system (Potential). ACT_SITE 328 328 Charge relay system (Potential). |
Keyword | Complete proteome; Cytoplasm; Growth factor binding; Hydrolase; Protease; Reference proteome; Secreted; Serine protease; Signal. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 480 AA |
Protein Sequence | MQSLRTTLLS LLLLLLAAPS LALPSGTGRS APAATVCPEH CDPTRCAPPP TDCEGGRVRD 60 ACGCCEVCGA LEGAACGLQE GPCGEGLQCV VPFGVPASAT VRRRAQAGLC VCASSEPVCG 120 SDAKTYTNLC QLRAASRRSE KLRQPPVIVL QRGACGQGQE DPNSLRHKYN FIADVVEKIA 180 PAVVHIELYR KLPFSKREVP VASGSGFIVS EDGLIVTNAH VVTNKNRVKV ELKNGATYEA 240 KIKDVDEKAD IALIKIDHQG KLPVLLLGRS SELRPGEFVV AIGSPFSLQN TVTTGIVSTT 300 QRGGKELGLR NSDMDYIQTD AIINYGNSGG PLVNLDGEVI GINTLKVTAG ISFAIPSDKI 360 KKFLTESHDR QAKGKAVTKK KYIGIRMMSL TSSKAKELKD RHRDFPDVLS GAYIIEVIPD 420 TPAEAGGLKE NDVIISINGQ SVVTANDVSD VIKKENTLNM VVRRGNEDIV ITVIPEEIDP 480 |
Gene Ontology | GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. GO:0031012; C:extracellular matrix; IEA:Compara. GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. GO:0008236; F:serine-type peptidase activity; IDA:UniProtKB. GO:0030514; P:negative regulation of BMP signaling pathway; IDA:MGI. GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IDA:MGI. GO:0006508; P:proteolysis; IDA:UniProtKB. GO:0001558; P:regulation of cell growth; IEA:InterPro. |
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