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CHPF

Gene
CHPF
Protein
Chondroitin sulfate synthase 2
Organism
Homo sapiens
Length
775 amino acids
Function
Has both beta-1,3-glucuronic acid and beta-1,4-N-acetylgalactosamine transferase activity. Transfers glucuronic acid (GlcUA) from UDP-GlcUA and N-acetylgalactosamine (GalNAc) from UDP-GalNAc to the non-reducing end of the elongating chondroitin polymer. Isoform 2 may facilitate PRKN transport into the mitochondria. In collaboration with PRKN, isoform 2 may enhance cell viability and protect cells from oxidative stress.
Similarity
Belongs to the chondroitin N-acetylgalactosaminyltransferase family.
Mass
85.467 kDa
Sequence
MRASLLLSVLRPAGPVAVGISLGFTLSLLSVTWVEEPCGPGPPQPGDSELPPRGNTNAARRPNSVQPGAEREKPGAGEGAGENWEPRVLPYHPAQPGQAAKKAVRTRYISTELGIRQRLLVAVLTSQTTLPTLGVAVNRTLGHRLERVVFLTGARGRRAPPGMAVVTLGEERPIGHLHLALRHLLEQHGDDFDWFFLVPDTTYTEAHGLARLTGHLSLASAAHLYLGRPQDFIGGEPTPGRYCHGGFGVLLSRMLLQQLRPHLEGCRNDIVSARPDEWLGRCILDATGVGCTGDHEGVHYSHLELSPGEPVQEGDPHFRSALTAHPVRDPVHMYQLHKAFARAELERTYQEIQELQWEIQNTSHLAVDGDQAAAWPVGIPAPSRPASRFEVLRWDYFTEQHAFSCADGSPRCPLRGADRADVADVLGTALEELNRRYHPALRLQKQQLVNGYRRFDPARGMEYTLDLQLEALTPQGGRRPLTRRVQLLRPLSRVEILPVPYVTEASRLTVLLPLAAAERDLAPGFLEAFATAALEPGDAAAALTLLLLYEPRQAQRVAHADVFAPVKAHVAELERRFPGARVPWLSVQTAAPSPLRLMDLLSKKHPLDTLFLLAGPDTVLTPDFLNRCRMHAISGWQAFFPMHFQAFHPAVAPPQGPGPPELGRDTGRFDRQAASEACFYNSDYVAARGRLAAASEQEEELLESLDVYELFLHFSSLHVLRAVEPALLQRYRAQTCSARLSEDLYHRCLQSVLEGLGSRTQLAMLLFEQEQGNST

Gene
Chpf
Protein
Chondroitin sulfate synthase 2
Organism
Mus musculus
Length
774 amino acids
Function
Has both beta-1,3-glucuronic acid and beta-1,4-N-acetylgalactosamine transferase activity. Transfers glucuronic acid (GlcUA) from UDP-GlcUA and N-acetylgalactosamine (GalNAc) from UDP-GalNAc to the non-reducing end of the elongating chondroitin polymer (By similarity). Isoform 2 may facilitate PRKN transport into the mitochondria. In collaboration with PRKN, isoform 2 may enhance cell viability and protect cells from oxidative stress (By similarity).
Similarity
Belongs to the chondroitin N-acetylgalactosaminyltransferase family.
Mass
85.534 kDa
Sequence
MRASLLLSVLRPAGPVAVGISLGFTLSLLSVTWVEEPCGPGPPQPGDSELPPRGNTNAARRPNSVQPGSERERPGAGAGTGESWEPRVLPYHPAQPGQATKKAVRTRYISTELGIRQKLLVAVLTSQATLPTLGVAVNRTLGHRLEHVVFLTGARGRRTPSGMAVVALGEERPIGHLHLALRHLLEQHGDDFDWFFLVPDATYTEAHGLDRLAGHLSLASATHLYLGRPQDFIGGDTTPGRYCHGGFGVLLSRTLLQQLRPHLESCRNDIVSARPDEWLGRCILDATGVGCTGDHEGMHYNYLELSPGEPVQEGDPRFRSALTAHPVRDPVHMYQLHKAFARAELDRTYQEIQELQWEIQNTSRLAADGERASAWPVGIPAPSRPASRFEVLRWDYFTEQYAFSCADGSPRCPLRGADQADVADVLGTALEELNRRYQPALQLQKQQLVNGYRRFDPARGMEYTLDLQLEALTPQGGRWPLTRRVQLLRPLSRVEILPVPYVTEASRLTVLLPLAAAERDLASGFLEAFATAALEPGDAAALTLLLLYEPRQAQRAAHSDVFAPVKAHVAELERRFPGARVPWLSVQTAAPSPLRLMDLLSKKHPLDTLFLLAGPDTVLTPDFLNRCRMHAISGWQAFFPMHFQAFHPAVAPPQGPGPPELGRDTGHFDRQAASEACFYNSDYVAARGRLVAASEQEEELLESLDVYELFLRFSNLHVLRAVEPALLQRYRAQPCSARLSEDLYHRCRQSVLEGLGSRTQLAMLLFEQEQGNST

Gene
chpF
Protein
Chaplin-F
Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Length
88 amino acids
Function
One of 8 partially redundant surface-active proteins required for efficient formation of aerial mycelium; the short chaplins assemble into a hydrophobic, amyloidal fibrillar surface layer that envelopes and protects aerial hyphae and spores, presumably anchored to the long chaplins (PubMed:12832396, PubMed:12832397, PubMed:15228525, PubMed:17462011). Chaplins have an overlapping function with the surface-active SapB peptide; chaplins are essential on minimal medium while on rich medium both chaplins and SapB are required for efficient aerial hyphae formation (PubMed:17462011). Chaplins are also involved in cell attachment to a hydrophobic surface (PubMed:19682261). Forms amyloid fibrils in vitro probably composed of stacked beta-sheets, at low extracellular concentrations individually restores the ability to form aerial hyphae to a chaplin-deficient strain (PubMed:21526199). A small chaplin extract (ChpD, ChpE, ChpF, ChpG and ChpH) self-assembles into 2 different amyloids; small fibrils at the air-water interface form an amiphipathic membrane that resembles spore-surface structures involved in aerial hyphae formation, and hydrophilic fibrils in solution that resemble the fibers that attach cells to a hydrophobic surface. At the air-water interface the hydrophilic surface is in contact with water (probably equivalent to the peptidoglycan layer), while the hydrophobic face is exposed to the air, making the surface of the aerial hyphae hydrophobic (PubMed:24012833). A small chaplin extract applied to a chaplin-deficient strain restores aerial hyphae formation (PubMed:12832396, PubMed:12832397). The small chaplin extract forms an amyloid-like structure similar to that seen on the surface of cells without rodlets (rdlA-rdlB deletions), and is highly surface active, reducing surface tension from 72 to 26 mJ/m(2), which probably allows escape of hyphae from an aqueous environment into air (PubMed:12832396). ChpF alone is less surface active at pH 3.0 than at pH 10.0, it reduces the surface tension of water from 72.8 mN/m to 50 mN/m at pH 3.0 or to 37 mN/m at pH 10.0 (PubMed:28925983). ChpF and ChpG are sufficient to restore the rodlet layer and hydrophobicity to a strain deleted for the other 6 chaplin genes (PubMed:15228525).
Similarity
Belongs to the chaplin family. Short chaplin subfamily.
Mass
8.698 kDa
Sequence
MYNPKEHFSMSRIAKGLALTSVAAAAVAGTAGVAAADSGAQAAAAHSPGVLSGNVVQVPVHIPVNVCGNTIDVIGLLNPAFGNECEND