PFKAM_RABIT
ID PFKAM_RABIT Reviewed; 780 AA.
AC P00511;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=ATP-dependent 6-phosphofructokinase, muscle type {ECO:0000255|HAMAP-Rule:MF_03184};
DE Short=ATP-PFK {ECO:0000255|HAMAP-Rule:MF_03184};
DE Short=PFK-M;
DE EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_03184};
DE AltName: Full=6-phosphofructokinase type A;
DE AltName: Full=Phosphofructo-1-kinase isozyme A;
DE Short=PFK-A;
DE AltName: Full=Phosphohexokinase {ECO:0000255|HAMAP-Rule:MF_03184};
GN Name=PFKM;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Muscle;
RX PubMed=2951385; DOI=10.1016/s0021-9258(18)61332-8;
RA Lee C.P., Kao M.C., French B.A., Putney S.D., Chang S.H.;
RT "The rabbit muscle phosphofructokinase gene. Implications for protein
RT structure, function, and tissue specificity.";
RL J. Biol. Chem. 262:4195-4199(1987).
RN [2]
RP PROTEIN SEQUENCE OF 2-780, AND ACETYLATION AT THR-2.
RX PubMed=6233492; DOI=10.1038/309467a0;
RA Poorman R.A., Randolph A., Kemp R.G., Heinrikson R.L.;
RT "Evolution of phosphofructokinase -- gene duplication and creation of new
RT effector sites.";
RL Nature 309:467-469(1984).
RN [3]
RP PROTEIN SEQUENCE OF 768-780, AND PHOSPHORYLATION AT SER-775.
RX PubMed=2539199; DOI=10.1016/0167-4838(89)90079-4;
RA Valaitis A.P., Foe L.G., Kwiatkowska D., Latshaw S.P., Kemp R.G.;
RT "The sites of phosphorylation of rabbit brain phosphofructo-1-kinase by
RT cyclic AMP-dependent protein kinase.";
RL Biochim. Biophys. Acta 995:187-194(1989).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 194-959.
RX PubMed=21241708; DOI=10.1016/j.jmb.2011.01.019;
RA Banaszak K., Mechin I., Obmolova G., Oldham M., Chang S.H., Ruiz T.,
RA Radermacher M., Kopperschlager G., Rypniewski W.;
RT "The crystal structures of eukaryotic phosphofructokinases from baker's
RT yeast and rabbit skeletal muscle.";
RL J. Mol. Biol. 407:284-297(2011).
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 -!- 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 -!- 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: Homo- and heterotetramers (By similarity). Phosphofructokinase
CC (PFK) enzyme functions as a tetramer composed of different combinations
CC of 3 types of subunits, called PFKM (M), PFKL (L) and PFKP (P). The
CC composition of the PFK tetramer differs according to the tissue type it
CC is present in. The kinetic and regulatory properties of the tetrameric
CC enzyme are dependent on the subunit composition, hence can vary across
CC tissues (Probable). Interacts (via C-terminus) with HK1 (via N-terminal
CC spermatogenic cell-specific region) (By similarity).
CC {ECO:0000250|UniProtKB:P47857, ECO:0000255|HAMAP-Rule:MF_03184,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184}.
CC -!- PTM: GlcNAcylation decreases enzyme activity. {ECO:0000250}.
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}.
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DR EMBL; M14477; AAA31441.1; -; Genomic_DNA.
DR EMBL; M14456; AAA31441.1; JOINED; Genomic_DNA.
DR EMBL; M14457; AAA31441.1; JOINED; Genomic_DNA.
DR EMBL; M14458; AAA31441.1; JOINED; Genomic_DNA.
DR EMBL; M14459; AAA31441.1; JOINED; Genomic_DNA.
DR EMBL; M14460; AAA31441.1; JOINED; Genomic_DNA.
DR EMBL; M14461; AAA31441.1; JOINED; Genomic_DNA.
DR EMBL; M14462; AAA31441.1; JOINED; Genomic_DNA.
DR EMBL; M14463; AAA31441.1; JOINED; Genomic_DNA.
DR EMBL; M14464; AAA31441.1; JOINED; Genomic_DNA.
DR EMBL; M14465; AAA31441.1; JOINED; Genomic_DNA.
DR EMBL; M14466; AAA31441.1; JOINED; Genomic_DNA.
DR EMBL; M14467; AAA31441.1; JOINED; Genomic_DNA.
DR EMBL; M14468; AAA31441.1; JOINED; Genomic_DNA.
DR EMBL; M14469; AAA31441.1; JOINED; Genomic_DNA.
DR EMBL; M14470; AAA31441.1; JOINED; Genomic_DNA.
DR EMBL; M14471; AAA31441.1; JOINED; Genomic_DNA.
DR EMBL; M14472; AAA31441.1; JOINED; Genomic_DNA.
DR EMBL; M14473; AAA31441.1; JOINED; Genomic_DNA.
DR EMBL; M14474; AAA31441.1; JOINED; Genomic_DNA.
DR EMBL; M14475; AAA31441.1; JOINED; Genomic_DNA.
DR EMBL; M14476; AAA31441.1; JOINED; Genomic_DNA.
DR PIR; A26550; KIRBF.
DR PDB; 3O8L; X-ray; 3.20 A; A/B=1-762.
DR PDB; 3O8N; X-ray; 3.20 A; A/B=1-762.
DR PDBsum; 3O8L; -.
DR PDBsum; 3O8N; -.
DR AlphaFoldDB; P00511; -.
DR SMR; P00511; -.
DR STRING; 9986.ENSOCUP00000014991; -.
DR ChEMBL; CHEMBL1075312; -.
DR iPTMnet; P00511; -.
DR PRIDE; P00511; -.
DR eggNOG; KOG2440; Eukaryota.
DR InParanoid; P00511; -.
DR BRENDA; 2.7.1.11; 1749.
DR SABIO-RK; P00511; -.
DR UniPathway; UPA00109; UER00182.
DR EvolutionaryTrace; P00511; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003872; F:6-phosphofructokinase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
DR CDD; cd00764; Eukaryotic_PFK; 1.
DR Gene3D; 3.40.50.460; -; 2.
DR HAMAP; MF_03184; Phosphofructokinase_I_E; 1.
DR InterPro; IPR009161; 6-Pfructokinase_euk.
DR InterPro; IPR022953; ATP_PFK.
DR InterPro; IPR041914; PFK_vert-type.
DR InterPro; IPR015912; Phosphofructokinase_CS.
DR InterPro; IPR000023; Phosphofructokinase_dom.
DR InterPro; IPR035966; PKF_sf.
DR Pfam; PF00365; PFK; 2.
DR PIRSF; PIRSF000533; ATP_PFK_euk; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; SSF53784; 2.
DR TIGRFAMs; TIGR02478; 6PF1K_euk; 1.
DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Allosteric enzyme; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Glycolysis; Glycoprotein; Hydroxylation; Kinase;
KW Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6233492"
FT CHAIN 2..780
FT /note="ATP-dependent 6-phosphofructokinase, muscle type"
FT /id="PRO_0000112019"
FT REGION 2..390
FT /note="N-terminal catalytic PFK domain 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184,
FT ECO:0000305|PubMed:21241708"
FT REGION 391..401
FT /note="Interdomain linker"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184,
FT ECO:0000305|PubMed:21241708"
FT REGION 402..780
FT /note="C-terminal regulatory PFK domain 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184,
FT ECO:0000305|PubMed:21241708"
FT ACT_SITE 166
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 25
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 88..89
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 118..121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 119
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 164..166
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 201
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 208..210
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 264
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 292
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 298..301
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 471
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 528..532
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 566
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 573..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 /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 629
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 655
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 661..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 /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 735
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 MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000269|PubMed:6233492"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47858"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47857"
FT MOD_RES 557
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P08237"
FT MOD_RES 667
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08237"
FT MOD_RES 775
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:2539199"
FT CARBOHYD 530
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT CONFLICT 269
FT /note="R -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 480..508
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 559
FT /note="S -> I (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 566
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT TURN 10..13
FT /evidence="ECO:0007829|PDB:3O8L"
FT STRAND 17..21
FT /evidence="ECO:0007829|PDB:3O8L"
FT HELIX 30..43
FT /evidence="ECO:0007829|PDB:3O8L"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:3O8L"
FT HELIX 54..59
FT /evidence="ECO:0007829|PDB:3O8L"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:3O8L"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:3O8L"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:3O8L"
FT HELIX 95..108
FT /evidence="ECO:0007829|PDB:3O8L"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:3O8L"
FT HELIX 119..130
FT /evidence="ECO:0007829|PDB:3O8L"
FT HELIX 133..138
FT /evidence="ECO:0007829|PDB:3O8L"
FT TURN 139..143
FT /evidence="ECO:0007829|PDB:3O8L"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:3O8L"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:3O8L"
FT STRAND 157..163
FT /evidence="ECO:0007829|PDB:3O8L"
FT HELIX 178..193
FT /evidence="ECO:0007829|PDB:3O8L"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:3O8L"
FT HELIX 214..223
FT /evidence="ECO:0007829|PDB:3O8L"
FT HELIX 240..252
FT /evidence="ECO:0007829|PDB:3O8L"
FT STRAND 256..260
FT /evidence="ECO:0007829|PDB:3O8N"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:3O8L"
FT HELIX 276..286
FT /evidence="ECO:0007829|PDB:3O8L"
FT STRAND 291..294
FT /evidence="ECO:0007829|PDB:3O8L"
FT HELIX 307..325
FT /evidence="ECO:0007829|PDB:3O8L"
FT STRAND 334..339
FT /evidence="ECO:0007829|PDB:3O8L"
FT STRAND 342..347
FT /evidence="ECO:0007829|PDB:3O8L"
FT HELIX 348..363
FT /evidence="ECO:0007829|PDB:3O8L"
FT HELIX 367..374
FT /evidence="ECO:0007829|PDB:3O8L"
FT HELIX 377..389
FT /evidence="ECO:0007829|PDB:3O8L"
FT STRAND 402..410
FT /evidence="ECO:0007829|PDB:3O8L"
FT HELIX 415..428
FT /evidence="ECO:0007829|PDB:3O8L"
FT STRAND 432..438
FT /evidence="ECO:0007829|PDB:3O8L"
FT HELIX 441..445
FT /evidence="ECO:0007829|PDB:3O8L"
FT STRAND 448..450
FT /evidence="ECO:0007829|PDB:3O8L"
FT TURN 453..456
FT /evidence="ECO:0007829|PDB:3O8L"
FT HELIX 475..477
FT /evidence="ECO:0007829|PDB:3O8L"
FT HELIX 478..487
FT /evidence="ECO:0007829|PDB:3O8L"
FT STRAND 493..498
FT /evidence="ECO:0007829|PDB:3O8L"
FT HELIX 499..514
FT /evidence="ECO:0007829|PDB:3O8L"
FT STRAND 522..527
FT /evidence="ECO:0007829|PDB:3O8L"
FT HELIX 542..556
FT /evidence="ECO:0007829|PDB:3O8L"
FT TURN 557..560
FT /evidence="ECO:0007829|PDB:3O8L"
FT STRAND 562..564
FT /evidence="ECO:0007829|PDB:3O8L"
FT STRAND 566..572
FT /evidence="ECO:0007829|PDB:3O8L"
FT HELIX 579..587
FT /evidence="ECO:0007829|PDB:3O8L"
FT STRAND 591..594
FT /evidence="ECO:0007829|PDB:3O8L"
FT STRAND 596..598
FT /evidence="ECO:0007829|PDB:3O8L"
FT HELIX 602..616
FT /evidence="ECO:0007829|PDB:3O8L"
FT STRAND 621..628
FT /evidence="ECO:0007829|PDB:3O8L"
FT STRAND 633..635
FT /evidence="ECO:0007829|PDB:3O8L"
FT HELIX 637..647
FT /evidence="ECO:0007829|PDB:3O8L"
FT TURN 648..651
FT /evidence="ECO:0007829|PDB:3O8L"
FT STRAND 653..658
FT /evidence="ECO:0007829|PDB:3O8L"
FT HELIX 670..692
FT /evidence="ECO:0007829|PDB:3O8L"
FT STRAND 697..700
FT /evidence="ECO:0007829|PDB:3O8L"
FT STRAND 708..714
FT /evidence="ECO:0007829|PDB:3O8L"
FT STRAND 717..722
FT /evidence="ECO:0007829|PDB:3O8L"
FT HELIX 723..726
FT /evidence="ECO:0007829|PDB:3O8L"
FT HELIX 727..729
FT /evidence="ECO:0007829|PDB:3O8L"
FT TURN 732..735
FT /evidence="ECO:0007829|PDB:3O8L"
FT STRAND 736..739
FT /evidence="ECO:0007829|PDB:3O8L"
FT HELIX 741..744
FT /evidence="ECO:0007829|PDB:3O8L"
FT HELIX 746..751
FT /evidence="ECO:0007829|PDB:3O8L"
FT TURN 752..754
FT /evidence="ECO:0007829|PDB:3O8N"
SQ SEQUENCE 780 AA; 85203 MW; ACDDF38C36F48EDB CRC64;
MTHEEHHAAR TLGVGKAIAV LTSGGDAQGM NAAVRAVVRV GIFTGARVFF VHEGYQGLVD
GGDHIREATW ESVSMMLQLG GTVIGSARCK DFREREGRLR AAHNLVKRGI TNLCVIGGDG
SLTGADTFRS EWSDLLSDLQ KAGKITAEEA TRSSYLNIVG LVGSIDNDFC GTDMTIGTDS
ALHRITEIVD AITTTAQSHQ RTFVLEVMGR HCGYLALVTS LSCGADWVFI PECPPDDNWE
DHLCRRLSET RTRGSRLNII IVAEGAIDRN GKPITSEGVK DLVVRRLGYD TRVTVLGHVQ
RGGTPSAFDR ILGSRMGVEA VMALLEGTPD TPACVVSLSG NQAVRLPLME CVQVTKDVTK
AMDEKRFDEA MKLRGRSFMN NWEVYKLLAH IRPPAPKSGS YTVAVMNVGA PAAGMNAAVR
STVRIGLIQG NRVLVVHDGF EGPAKGQIEE AGWSYVGGWT GQGGSKLGSK RTLPKKSFEQ
ISANITKFNI QGLVIIGGFE AYTGGLELME GRKQFDELCI PFVVIPATVS NNVPGSDFSV
GADTALNTIC TTCDRIKQSA AGTKRRVFII ETMGGYCGYL ATMAGLAAGA DAAYIFEEPF
TIRDLQANVE HLVQKMKTTV KRGLVLRNEK CNENYTTDFI FNLYSEEGKG IFDSRKNVLG
HMQQGGSPTP FDRNFATKMG AKAMNWMAGK IKESYRNGRI FANTPDSGCV LGMRKRALVF
QPVTELQNQT DFEHRIPKEQ WWLKLRPILK ILAKYEIDLD TSEHAHLEHI SRKRSGEATV
