hepatocyte growth factor alpha chain

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Ligands
hepatocyte growth factor alpha chain (Human)

GtoPdb Ligand ID: 4950

Abbreviated name: HGF alpha chain

Compound class: Endogenous peptide in human, mouse or rat

Species: Human

Is a component of
hepatocyte growth factor

Is a component of

hepatocyte growth factor

Peptide Sequence
QRKRRNTIHEFKKSAKTTLIKIDPALKIKTKKVNTADQCANRCTRNKGLPFTCKAFVFDKARKQCLWFPFNSMSSGVKKE FGHEFDLYENKDYIRNCIIGKGRSYKGTVSITKSGIKCQPWSSMIPHEHSFLPSSYRGKDLQENYCRNPRGEEGGPWCFT SNPEVRYEVCDIPQCSEVECMTCNGESYRGLMDHTESGKICQRWDHQTPHRHKFLPERYPDKGFDDNYCRNPDGQPRPWC YTLDPHTRWEYCAIKTCADNTMNDTDVPLETTECIQGQGEGYRGTVNTIWNGIPCQRWDSQYPHEHDMTPENFKCKDLRE NYCRNPDGSESPWCFTTDPNIRVGYCSQIPNCDMSHGQDCYRGNGKNYMGNLSQTRSGLTCSMWDKNMEDLHRHIFWEPD ASKLNENYCRNPDDDAHGPWCYTGNPLIPWDYCPISRCEGDTTPTIVNLDHPVISCAKTKQLR

Peptide Sequence

QRKRRNTIHEFKKSAKTTLIKIDPALKIKTKKVNTADQCANRCTRNKGLPFTCKAFVFDKARKQCLWFPFNSMSSGVKKE
FGHEFDLYENKDYIRNCIIGKGRSYKGTVSITKSGIKCQPWSSMIPHEHSFLPSSYRGKDLQENYCRNPRGEEGGPWCFT
SNPEVRYEVCDIPQCSEVECMTCNGESYRGLMDHTESGKICQRWDHQTPHRHKFLPERYPDKGFDDNYCRNPDGQPRPWC
YTLDPHTRWEYCAIKTCADNTMNDTDVPLETTECIQGQGEGYRGTVNTIWNGIPCQRWDSQYPHEHDMTPENFKCKDLRE
NYCRNPDGSESPWCFTTDPNIRVGYCSQIPNCDMSHGQDCYRGNGKNYMGNLSQTRSGLTCSMWDKNMEDLHRHIFWEPD
ASKLNENYCRNPDDDAHGPWCYTGNPLIPWDYCPISRCEGDTTPTIVNLDHPVISCAKTKQLR

Post-translational Modification
N-terminal glutamine is pyrrolidone carboxylic acid; N-linked glycosylation of asparagine residues at positions 263 and 371; O-linked glycosylation of threonine at position 445. Disulphide bond formation between cysteine residues at positions 39 and 65; 43 and 53, 97 and 175, 118 and 158, and 146 and 170. Predicted disulphide bond formation between cysteine residues at positions 180 and 257, 201 and 240, 229 and 252, 274 and 352, 295 and 334, 323 and 346, 360 and 438, 381 and 431, and 409 and 433. Interchain disulphide bond between cysteine residue at position 456 of the alpha chain and 110 of the beta chain.

Post-translational Modification

N-terminal glutamine is pyrrolidone carboxylic acid; N-linked glycosylation of asparagine residues at positions 263 and 371; O-linked glycosylation of threonine at position 445. Disulphide bond formation between cysteine residues at positions 39 and 65; 43 and 53, 97 and 175, 118 and 158, and 146 and 170. Predicted disulphide bond formation between cysteine residues at positions 180 and 257, 201 and 240, 229 and 252, 274 and 352, 295 and 334, 323 and 346, 360 and 438, 381 and 431, and 409 and 433. Interchain disulphide bond between cysteine residue at position 456 of the alpha chain and 110 of the beta chain.