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Cystatin C or cystatin 3 (formerly ... Cystatin C has a low molecular weight ... The glomerular sieving coefficients for 10–30 kDa plasma proteins in the human ...
These are cystatin-like proteins found in a range of organisms: plant phytocystatins, fetuin in mammals, insect cystatins, and a puff adder venom cystatin, which inhibits metalloproteases of the MEROPS peptidase family M12 (astacin/adamalysin). Also, a number of the cystatin-like proteins have been shown to be devoid of inhibitory activity.
13011 Ensembl ENSG00000077984 ENSMUSG00000068129 UniProt O76096 O89098 RefSeq (mRNA) NM_003650 NM_009977 RefSeq (protein) NP_003641 NP_034107 Location (UCSC) Chr 20: 24.95 – 24.96 Mb Chr 2: 150.41 – 150.42 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Cystatin-F is a protein that in humans is encoded by the CST7 gene. The cystatin superfamily encompasses proteins that contain ...
n/a Ensembl ENSG00000170369 n/a UniProt P09228 n/a RefSeq (mRNA) NM_001322 n/a RefSeq (protein) NP_001313 n/a Location (UCSC) Chr 20: 23.82 – 23.83 Mb n/a PubMed search n/a Wikidata View/Edit Human Cystatin-SA is a protein that in humans is encoded by the CST2 gene. The cystatin superfamily encompasses proteins that contain multiple cystatin-like sequences. Some of the members are active ...
Hereditary cystatin C amyloid angiopathy (HCCAA) is a rare, fatal type of hereditary cerebral amyloid angiopathy found almost exclusively in Iceland. A mutation in the protein cystatin C leads to amyloid (protein aggregate) dispositions in arteries in the brain, resulting in repeated brain hemorrhages .
Small soluble cytochrome c proteins with a molecular weight of 8-12 kDa and a single heme group belong to class I. [10] [11] It includes the low-spin soluble cytC of mitochondria and bacteria, with the heme-attachment site located towards the N-terminus, and the sixth ligand provided by a methionine residue about 40 residues further on towards the C-terminus.
Most of the type I keratins consist of acidic, low molecular weight proteins which in vivo are arranged in pairs of heterotypic Type I and Type II keratin chains, coexpressed during differentiation of simple and stratified epithelial tissues.
The first two alpha chains subunits of ColVI have a molecular weight of 140-150 KDa and the third polypeptide chain is larger with a molecular weight of 250-300kDa. [5] ColVI is also found in the skin, lungs, blood vessels, cornea and intervertebral disc. It also forms part of the peripheral nerves, brain, myocardium and adipose tissue. [5]