ID PFKA_DROME Reviewed; 788 AA.
AC P52034; Q8IH94; Q8MKV4; Q9V5G7; Q9Y100;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 27-MAR-2024, entry version 170.
DE RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_03184};
DE Short=ATP-PFK {ECO:0000255|HAMAP-Rule:MF_03184};
DE Short=Phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_03184};
DE EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_03184};
DE AltName: Full=Phosphohexokinase {ECO:0000255|HAMAP-Rule:MF_03184};
GN Name=Pfk; ORFNames=CG4001;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM B), AND FUNCTION.
RC STRAIN=Oregon-R;
RX PubMed=7929140; DOI=10.1016/s0021-9258(17)31444-8;
RA Currie P.D., Sullivan D.T.;
RT "Structure and expression of the gene encoding phosphofructokinase (PFK) in
RT Drosophila melanogaster.";
RL J. Biol. Chem. 269:24679-24687(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=10731138; DOI=10.1126/science.287.5461.2222;
RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., Stapleton M.,
RA Harvey D.A.;
RT "A Drosophila complementary DNA resource.";
RL Science 287:2222-2224(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 101-788 (ISOFORM C).
RC STRAIN=Berkeley; TISSUE=Testis;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=2935142; DOI=10.1007/bf00499933;
RA Munneke L.R., Collier G.E.;
RT "Genetic and biochemical characterization of phosphofructokinase from
RT Drosophila melanogaster.";
RL Biochem. Genet. 23:847-857(1985).
CC -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to
CC fructose 1,6-bisphosphate by ATP, the first committing step of
CC glycolysis. {ECO:0000255|HAMAP-Rule:MF_03184,
CC ECO:0000269|PubMed:2935142, ECO:0000269|PubMed:7929140}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-
CC bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634,
CC ChEBI:CHEBI:456216; EC=2.7.1.11; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03184};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03184};
CC -!- ACTIVITY REGULATION: Allosterically activated by ADP, AMP, or fructose
CC 2,6-bisphosphate, and allosterically inhibited by ATP or citrate.
CC {ECO:0000255|HAMAP-Rule:MF_03184}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 3/4.
CC {ECO:0000255|HAMAP-Rule:MF_03184}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_03184}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=B;
CC IsoId=P52034-1; Sequence=Displayed;
CC Name=A;
CC IsoId=P52034-2; Sequence=VSP_014950;
CC Name=C;
CC IsoId=P52034-3; Sequence=VSP_014951;
CC -!- TISSUE SPECIFICITY: Nearly 90% of the PFK activity in adults is
CC localized to the thorax. {ECO:0000269|PubMed:2935142}.
CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC ATP-dependent PFK group I subfamily. Eukaryotic two domain clade 'E'
CC sub-subfamily. {ECO:0000255|HAMAP-Rule:MF_03184}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN71109.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L27653; AAA62385.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF58840.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF58841.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM71065.2; -; Genomic_DNA.
DR EMBL; AF145673; AAD38648.1; -; mRNA.
DR EMBL; BT001354; AAN71109.1; ALT_FRAME; mRNA.
DR PIR; A55034; A55034.
DR RefSeq; NP_523676.1; NM_078952.3. [P52034-2]
DR RefSeq; NP_724890.1; NM_165746.3. [P52034-1]
DR RefSeq; NP_724891.2; NM_165747.4. [P52034-3]
DR AlphaFoldDB; P52034; -.
DR SMR; P52034; -.
DR BioGRID; 61888; 4.
DR IntAct; P52034; 3.
DR MINT; P52034; -.
DR STRING; 7227.FBpp0087506; -.
DR PaxDb; 7227-FBpp0087506; -.
DR DNASU; 36060; -.
DR EnsemblMetazoa; FBtr0088420; FBpp0087506; FBgn0003071. [P52034-2]
DR EnsemblMetazoa; FBtr0088421; FBpp0087507; FBgn0003071. [P52034-3]
DR EnsemblMetazoa; FBtr0088422; FBpp0087508; FBgn0003071. [P52034-1]
DR GeneID; 36060; -.
DR KEGG; dme:Dmel_CG4001; -.
DR UCSC; CG4001-RA; d. melanogaster. [P52034-1]
DR AGR; FB:FBgn0003071; -.
DR CTD; 36060; -.
DR FlyBase; FBgn0003071; Pfk.
DR VEuPathDB; VectorBase:FBgn0003071; -.
DR eggNOG; KOG2440; Eukaryota.
DR GeneTree; ENSGT00940000171778; -.
DR HOGENOM; CLU_011053_1_0_1; -.
DR InParanoid; P52034; -.
DR OMA; EWQDQMC; -.
DR PhylomeDB; P52034; -.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR Reactome; R-DME-70171; Glycolysis.
DR SignaLink; P52034; -.
DR UniPathway; UPA00109; UER00182.
DR BioGRID-ORCS; 36060; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 36060; -.
DR PRO; PR:P52034; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0003071; Expressed in adult hindgut (Drosophila) and 29 other cell types or tissues.
DR ExpressionAtlas; P52034; baseline and differential.
DR Genevisible; P52034; DM.
DR GO; GO:0005945; C:6-phosphofructokinase complex; IBA:GO_Central.
DR GO; GO:0003872; F:6-phosphofructokinase activity; IMP:FlyBase.
DR GO; GO:0016208; F:AMP binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0070095; F:fructose-6-phosphate binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048029; F:monosaccharide binding; IBA:GO_Central.
DR GO; GO:0061621; P:canonical glycolysis; IBA:GO_Central.
DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0042593; P:glucose homeostasis; IMP:FlyBase.
DR GO; GO:0006096; P:glycolytic process; IMP:FlyBase.
DR GO; GO:0009744; P:response to sucrose; IMP:FlyBase.
DR Gene3D; 3.40.50.450; -; 2.
DR Gene3D; 3.40.50.460; Phosphofructokinase domain; 2.
DR HAMAP; MF_03184; Phosphofructokinase_I_E; 1.
DR InterPro; IPR009161; 6-Pfructokinase_euk.
DR InterPro; IPR022953; ATP_PFK.
DR InterPro; IPR015912; Phosphofructokinase_CS.
DR InterPro; IPR000023; Phosphofructokinase_dom.
DR InterPro; IPR035966; PKF_sf.
DR NCBIfam; TIGR02478; 6PF1K_euk; 1.
DR PANTHER; PTHR13697:SF4; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE; 1.
DR PANTHER; PTHR13697; PHOSPHOFRUCTOKINASE; 1.
DR Pfam; PF00365; PFK; 2.
DR PIRSF; PIRSF000533; ATP_PFK_euk; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; Phosphofructokinase; 2.
DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 2.
PE 2: Evidence at transcript level;
KW Allosteric enzyme; Alternative splicing; ATP-binding; Cytoplasm;
KW Glycolysis; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..788
FT /note="ATP-dependent 6-phosphofructokinase"
FT /id="PRO_0000112031"
FT REGION 1..392
FT /note="N-terminal catalytic PFK domain 1"
FT REGION 393..410
FT /note="Interdomain linker"
FT REGION 411..788
FT /note="C-terminal regulatory PFK domain 2"
FT ACT_SITE 168
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 27
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 90..91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 120..123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 121
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 166..168
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 203
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 210..212
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 266
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 294
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 300..303
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 480
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 537..541
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 575
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 582..584
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 638
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 664
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 670..673
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 745
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT VAR_SEQ 1..15
FT /note="MNSEINQRFLARGSQ -> MHSIKFRVFTKLKPIFLEINGRIPICRHFHGPT
FT TFRLEISNKTPPIRQKLTFPNIGIQCTRSHHLCCPRDISGNTLLSVKFNCKRHCIKLRS
FT DSGDQKNDSPGEKNIQKDKSAQRCGKPINNLHNGFLNAVNYSEKNAVKKKKSAPKRKCG
FT KSVDELRKCLRTMQDVIDFVHPVKPF (in isoform A)"
FT /evidence="ECO:0000303|PubMed:10731138"
FT /id="VSP_014950"
FT VAR_SEQ 219..250
FT /note="LVGGLACEADFIFIPEMPPKVDWPDRLCSQLA -> ISAAIATEADFMFIPE
FT EPVSVNWKDEICVKLH (in isoform C)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_014951"
FT CONFLICT 68..70
FT /note="QEA -> RKS (in Ref. 1; AAA62385)"
FT /evidence="ECO:0000305"
FT CONFLICT 80..92
FT /note="HRGGTIIGSARCQ -> PFVGWHHPLLRPLP (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 130..131
FT /note="FR -> LP (in Ref. 1; AAA62385)"
FT /evidence="ECO:0000305"
FT CONFLICT 160..161
FT /note="IV -> ML (in Ref. 1; AAA62385)"
FT /evidence="ECO:0000305"
FT CONFLICT 190..199
FT /note="AIDAISSTAY -> QSKAKVQSPVQPN (in Ref. 1; AAA62385)"
FT /evidence="ECO:0000305"
FT CONFLICT 209..212
FT /note="VMGR -> GQVS (in Ref. 1; AAA62385)"
FT /evidence="ECO:0000305"
FT CONFLICT 228..252
FT /note="DFIFIPEMPPKVDWPDRLCSQLAQE -> IHIHPNAPGRLGQTGSALSWTQ
FT (in Ref. 1; AAA62385)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="I -> F (in Ref. 1; AAA62385)"
FT /evidence="ECO:0000305"
FT CONFLICT 322..325
FT /note="ATLA -> PLWP (in Ref. 1; AAA62385)"
FT /evidence="ECO:0000305"
FT CONFLICT 360..361
FT /note="VA -> G (in Ref. 1; AAA62385)"
FT /evidence="ECO:0000305"
FT CONFLICT 374..375
FT /note="KL -> NV (in Ref. 1; AAA62385)"
FT /evidence="ECO:0000305"
FT CONFLICT 455
FT /note="G -> R (in Ref. 1; AAA62385)"
FT /evidence="ECO:0000305"
FT CONFLICT 478
FT /note="T -> S (in Ref. 1; AAA62385)"
FT /evidence="ECO:0000305"
FT CONFLICT 522..526
FT /note="DNYPQ -> TTTHS (in Ref. 1; AAA62385)"
FT /evidence="ECO:0000305"
FT CONFLICT 590..591
FT /note="AT -> PP (in Ref. 1; AAA62385)"
FT /evidence="ECO:0000305"
FT CONFLICT 613
FT /note="D -> E (in Ref. 1; AAA62385)"
FT /evidence="ECO:0000305"
FT CONFLICT 622..636
FT /note="ASKMAEGVSRGLILR -> PPRWPRRLPRSNPA (in Ref. 1;
FT AAA62385)"
FT /evidence="ECO:0000305"
FT CONFLICT 695..705
FT /note="WLAAQIKANID -> CWPPRSRRTST (in Ref. 1; AAA62385)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 788 AA; 86648 MW; BE45A03013299B75 CRC64;
MNSEINQRFL ARGSQKDKGL AVFTSGGDSQ GMNAAVRACV RMAIYLGCKV YFIREGYQGM
VDGGDCIQEA NWASVSSIIH RGGTIIGSAR CQDFRERQGR LKAANNLIQR GITNLVVIGG
DGSLTGANLF RQEWSSLLDE LVKNKTITTE QQEKFNVLHI VGLVGSIDND FCGTDMTIGT
DTALHRIIEA IDAISSTAYS HQRTFIMEVM GRHCGYLALV GGLACEADFI FIPEMPPKVD
WPDRLCSQLA QERSAGQRLN IVIVAEGAMD REGHPITAED VKKVIDERLK HDARITVLGH
VQRGGNPSAF DRILACRMGA EATLALMEAT KDSVPVVISL DGNQAVRVPL MECVERTQAV
AKAMAEKRWA DAVKLRGRSF ERNLETYKML TRLKPPKENF DADGKGIEGY RLAVMHIGAP
ACGMNAAVRS FVRNAIYRGD VVYGINDGVE GLIAGNVREL GWSDVSGWVG QGGAYLGTKR
TLPEGKFKEI AARLKEFKIQ GLLIIGGFES YHAAGQIADQ RDNYPQFCIP IVVIPSTISN
NVPGTEFSLG CDTGLNEITE ICDRIRQSAQ GTKRRVFVIE TMGGYCGYLA TLAGLAGGAD
AAYIYEEKFS IKDLQQDVYH MASKMAEGVS RGLILRNEKA SENYSTDFIY RLYSEEGKGL
FTCRMNILGH MQQGGSPTPF DRNMGTKMAA KCVDWLAAQI KANIDANGVV NCKSPDTATL
LGIVSRQYRF SPLVDLIAET NFDQRIPKKQ WWLRLRPLLR ILAKHDSAYE EEGMYITVEE
ECDTDAVA
//
