FA9_CANLF
ID FA9_CANLF Reviewed; 452 AA.
AC P19540;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Coagulation factor IX;
DE EC=3.4.21.22 {ECO:0000250|UniProtKB:P00740};
DE AltName: Full=Christmas factor;
DE Contains:
DE RecName: Full=Coagulation factor IXa light chain;
DE Contains:
DE RecName: Full=Coagulation factor IXa heavy chain;
DE Flags: Precursor;
GN Name=F9;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Liver;
RX PubMed=2367529; DOI=10.1073/pnas.87.13.5173;
RA Axelrod J.H., Read M.S., Brinkhous K.M., Verma I.M.;
RT "Phenotypic correction of factor IX deficiency in skin fibroblasts of
RT hemophilic dogs.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:5173-5177(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=2752110;
RA Evans J.P., Watzke H.H., Ware J.L., Stafford D.W., High K.A.;
RT "Molecular cloning of a cDNA encoding canine factor IX.";
RL Blood 74:207-212(1989).
RN [3]
RP VARIANT HEMB GLU-418, ROLE IN DISEASE, AND FUNCTION.
RX PubMed=2481310; DOI=10.1073/pnas.86.24.10095;
RA Evans J.P., Brinkhous K.M., Brayer G.D., Reisner H.M., High K.A.;
RT "Canine hemophilia B resulting from a point mutation with unusual
RT consequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:10095-10099(1989).
CC -!- FUNCTION: Factor IX is a vitamin K-dependent plasma protein that
CC participates in the intrinsic pathway of blood coagulation by
CC converting factor X to its active form in the presence of Ca(2+) ions,
CC phospholipids, and factor VIIIa. {ECO:0000250|UniProtKB:P00740,
CC ECO:0000269|PubMed:2367529, ECO:0000269|PubMed:2481310}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Selective cleavage of Arg-|-Ile bond in factor X to form
CC factor Xa.; EC=3.4.21.22; Evidence={ECO:0000250|UniProtKB:P00740};
CC -!- SUBUNIT: Heterodimer of a light chain and a heavy chain; disulfide-
CC linked. Interacts with SERPINC1. {ECO:0000250|UniProtKB:P00740}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2367529}.
CC -!- TISSUE SPECIFICITY: Detected in the liver.
CC {ECO:0000269|PubMed:2752110}.
CC -!- DOMAIN: Calcium binds to the gamma-carboxyglutamic acid (Gla) residues
CC in the Gla domain. Calcium can also bind, with stronger affinity, to
CC another site beyond the Gla domain. Under physiological ion
CC concentrations, Ca(2+) is displaced by Mg(2+) from some of the
CC gammaglutamate residues in the N-terminal Gla domain. This leads to a
CC subtle conformation change that may affect the interaction with its
CC binding protein. {ECO:0000250|UniProtKB:P00741}.
CC -!- PTM: Activated by factor XIa, which excises the activation peptide. The
CC propeptide can also be removed by snake venom protease.
CC {ECO:0000250|UniProtKB:P00740}.
CC -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate
CC and asparagine is (R) stereospecific within EGF domains.
CC {ECO:0000250|UniProtKB:P00740}.
CC -!- PTM: Predominantly O-glucosylated at Ser-92 by POGLUT1 in vitro.
CC {ECO:0000250|UniProtKB:P00740}.
CC -!- DISEASE: Note=Defects in F9 are the cause of hemophilia B (HEMB).
CC {ECO:0000269|PubMed:2481310}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; M21757; AAA75006.1; -; mRNA.
DR EMBL; M33826; AAA30844.1; -; mRNA.
DR PIR; A30351; A30351.
DR RefSeq; NP_001003323.1; NM_001003323.2.
DR AlphaFoldDB; P19540; -.
DR SMR; P19540; -.
DR STRING; 9612.ENSCAFP00000028031; -.
DR MEROPS; S01.214; -.
DR PaxDb; P19540; -.
DR GeneID; 404015; -.
DR KEGG; cfa:404015; -.
DR CTD; 2158; -.
DR eggNOG; ENOG502QUEV; Eukaryota.
DR InParanoid; P19540; -.
DR OrthoDB; 1314811at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0004175; F:endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0007596; P:blood coagulation; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR GO; GO:0031638; P:zymogen activation; ISS:UniProtKB.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 4.10.740.10; -; 1.
DR InterPro; IPR017857; Coagulation_fac-like_Gla_dom.
DR InterPro; IPR035694; Coagulation_factor_IX.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR035972; GLA-like_dom_SF.
DR InterPro; IPR000294; GLA_domain.
DR InterPro; IPR012224; Pept_S1A_FX.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24278:SF31; PTHR24278:SF31; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF00594; Gla; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF001143; Factor_X; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR PRINTS; PR00001; GLABLOOD.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 1.
DR SMART; SM00069; GLA; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF57630; SSF57630; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS00011; GLA_1; 1.
DR PROSITE; PS50998; GLA_2; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW Blood coagulation; Calcium; Cleavage on pair of basic residues;
KW Disease variant; Disulfide bond; EGF-like domain;
KW Gamma-carboxyglutamic acid; Glycoprotein; Hemophilia; Hemostasis;
KW Hydrolase; Hydroxylation; Magnesium; Metal-binding; Phosphoprotein;
KW Protease; Reference proteome; Repeat; Secreted; Serine protease; Signal;
KW Sulfation; Zymogen.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..39
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT /id="PRO_0000027745"
FT CHAIN 40..452
FT /note="Coagulation factor IX"
FT /id="PRO_0000027746"
FT CHAIN 40..185
FT /note="Coagulation factor IXa light chain"
FT /id="PRO_0000027747"
FT PROPEP 186..217
FT /note="Activation peptide"
FT /id="PRO_0000027748"
FT CHAIN 218..452
FT /note="Coagulation factor IXa heavy chain"
FT /id="PRO_0000027749"
FT DOMAIN 40..85
FT /note="Gla"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT DOMAIN 86..122
FT /note="EGF-like 1; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 123..164
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 218..450
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 258
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT ACT_SITE 306
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT ACT_SITE 402
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 40
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 41
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 46
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 46
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 54
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 54
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 56
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 56
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 56
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 59
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 59
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 60
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 65
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 65
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 69
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 69
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 69
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 75
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 79
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 79
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 86
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 87
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 89
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 103
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 104
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 272
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="8"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 274
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="8"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 279
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="8"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 282
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="8"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT SITE 185..186
FT /note="Cleavage; by factor XIa"
FT /evidence="ECO:0000250"
FT SITE 217..218
FT /note="Cleavage; by factor XIa"
FT /evidence="ECO:0000250"
FT MOD_RES 46
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00741,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 47
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00741,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 54
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00741,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 56
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00741,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 59
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00741,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 60
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00741,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 65
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00741,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 66
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00741,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 69
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00741,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 72
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00741,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 75
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00741,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 79
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00741,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 103
FT /note="(3R)-3-hydroxyaspartate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT MOD_RES 195
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT MOD_RES 199
FT /note="Phosphothreonine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT CARBOHYD 78
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT CARBOHYD 92
FT /note="O-linked (Glc...) serine"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 199
FT /note="O-linked (GalNAc...) threonine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 209
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT CARBOHYD 216
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 57..62
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT DISULFID 90..101
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT DISULFID 95..110
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT DISULFID 112..121
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT DISULFID 127..138
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT DISULFID 134..148
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT DISULFID 150..163
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT DISULFID 171..326
FT /note="Interchain (between light and heavy chains)"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT DISULFID 243..259
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT DISULFID 373..387
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT DISULFID 398..426
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT VARIANT 418
FT /note="G -> E (in HEMB)"
FT /evidence="ECO:0000269|PubMed:2481310"
SQ SEQUENCE 452 AA; 50828 MW; 1F6537C46A6960ED CRC64;
MAEASGLVTV CLLGYLLSAE CAVFLDRENA TKILSRPKRY NSGKLEEFVR GNLERECIEE
KCSFEEAREV FENTEKTTEF WKQYVDGDQC ESNPCLNDGV CKDDINSYEC WCRAGFEGKN
CELDVTCNIK NGRCKQFCKL GPDNKVVCSC TTGYQLAEDQ RSCEPAVPFP CGRVSVPHIS
MTRTRAETLF SNMDYENSTE VEKILDNVTQ PLNDFTRVVG GKDAKPGQFP WQVLLNGKVD
AFCGGSIINE KWVVTAAHCI EPDVKITIVA GEHNTEKREH TEQKRNVIRT ILHHSYNATI
NKYNHDIALL ELDEPLTLNS YVTPICIADR EYSNIFLKFG SGYVSGWGRV FNKGRSASIL
QYLKVPLVDR ATCLRSTKFT IYNNMFCAGF HEGGKDSCQG DSGGPHVTEV EGISFLTGII
SWGEECAMKG KYGIYTKVSR YVNWIKEKTK LT
