Gene: [0Xq271/F9] coagulation factor IX (plasma thromboplastic component); hemophilia B (Christmas disease; coagulation factor IX deficiency);

FUN	[1] Converts coagulation factor X to Xa. [2] Systematic name: not known. [3] Catalyzes hydrolysis one arg-|-ile bond in factor X to form factor Xa."
MOP	The molecular product is a serum glycoprotein (MM 56 kD). It is synthesized by hepatocytes as a single-strand polypeptide. N-terminal region of the primary translation product contains 46 amino acids and two domains: the signal peptide (28 amino acids), which is necessary for transferring the protein through membrane, and the (Thr...Arg) propeptide (18 amino acids), which serves for post-translational modification and (PTM) and the consequent secretion of inactive F(IX) into the blood flow. The PTM occurs after the splitting of the signal peptide and includes the vitamin K-dependent gamma-carboxylation of the first 12 Glu in the catalytical peptide, beta-carboxylation of Asp in position <64>, and propeptide splitting. The mature enzyme consists of two peptide chains, light and heavy (L and H) ones, which arises from the splitting of the inactive catalytic polypeptide."
MUT	The mutant forms include F(IX)-Chapel Hill (substitution of Arg for Hys at position 145 (Noyes-1983), that prevents the peptide splitting and hence the enzyme activation), F(IX)-Alabama (substitution of Asp for Gly at position 47 (Davis-1984)), 'splicing' mutations (see Rees-1985), large deletions (see Giannelli-1983 and Hassan-1985), and F(IX)-Campbridge (substitution of Arg (codon ag) for Ser (codons ag or ag) at position <-1>, see Diuguid-1986 and a similar example in Bentley-1986: substitution of Arg for Glu in position <-4>). As for the latter case, the mutation does not prevent the signal peptide splitting at position <-19,-18> but makes it impossible to split the propeptide from the catalytic one, F(IX), at position <-1,+1>, thus disturbing the F(IX) processing. As a result, the F(IX)-Campbridge is 18 amino acids longer than the normal protein and has only seven of 12 gamma-carboxylated Asp."
REF	MUT "Bentley AK &: Cell, 45, (May), 343-348, 1986 LOC "Boyd &: Ann Hum Genet, 48, 145-152, 1984 LOC,POL "Camerino &: PNAS, 81, 498-502, 1984 CLO,SEQ "Choo KH &: Nature, 299, (9 Sep), 178-180, 1982 POL,PND "Connor &: J Med Genet, 22, 441-446, 1985 MUT "Davis &: Blood, 64, (Suppl), 262, 1984 MUT,POG "de la Salle C &: Clin Genet, 38, N6, 434-440, 1990 MUT "Diuguid &: PNAS, 83, N16, 5803-5807, 1986 POL,PND "Giannelli F &: Lancet, 1, N8371, 239-241, 1984 MUT "Giannelli F &: Nature, 303, (12 May), 181-182, 1983 MUT "Hassan &: Blood, 66, N3, 728-730, 1985 POL,PND "Hay CW &: Blood, 67, N5, 1508-1511, 1986 SEQ,POL "Jagadeeswaran P &: Somat Cell Mol Genet, 10, N5, 465-473, 1984 SEQ,PEP "Kurachi K, Davie: PNAS, 79, 6461-6464, 1982 POL,PND "Lillicrap &: Brit J Haematol, 62, 557-565, 1986 POL,PND "Lubahn DB &: AJHG, 40, 527-536, 1987 POL,PND "Mulligan L &: Hum Genet, 75, 381-383, 1987 EXP,PND "Nisen &: New Engl J Med, 315, N18, 1139-1142, 1986 MUT "Noyes CM &: PNAS, 80, 4200-4202, 1983 LOC "Purrello M &: EMBO J, 4, 725-729, 1985 LOC "Quirk S &: CCG, 39, 121-124, 1985 MOP,EXP,EVO "Rees DJ &: EMBO J, 7, N7, 2053-2061, 1988 MUT "Rees DJ &: Nature, 316, 643-645, 1985 EVO,MAM,GEN,MOP,SEQ "Sarkar &: Genomics, 6, N1, 133-143, 1990 LOC "Schwartz &: Hum Genet, 76, 64-67, 1987 ENG,EXP "Simpson PJ &: Gene, 61, 373-383, 1987
KEY	hem, clot
CLA	coding, basic
LOC	0X q27.1
MIM	MIM: 306900
EZN	ENZYME: 3.4.21.22

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Ген коагуляционного фактора IX