PFKA2_PICPA
ID PFKA2_PICPA Reviewed; 941 AA.
AC Q8TGA0;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=ATP-dependent 6-phosphofructokinase subunit beta {ECO:0000255|HAMAP-Rule:MF_03184};
DE EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_03184};
DE AltName: Full=ATP-dependent 6-phosphofructokinase 2 {ECO:0000255|HAMAP-Rule:MF_03184};
DE Short=ATP-PFK 2 {ECO:0000255|HAMAP-Rule:MF_03184};
DE Short=Phosphofructokinase 2 {ECO:0000255|HAMAP-Rule:MF_03184};
DE AltName: Full=Phosphohexokinase 2 {ECO:0000255|HAMAP-Rule:MF_03184};
GN Name=PFK2;
OS Komagataella pastoris (Yeast) (Pichia pastoris).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Komagataella.
OX NCBI_TaxID=4922;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-16.
RC STRAIN=MH458;
RX PubMed=12125051; DOI=10.1002/yea.889;
RA Edelmann A., Baer J.;
RT "Molecular genetics of 6-phosphofructokinase in Pichia pastoris.";
RL Yeast 19:949-956(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, AND SUBUNIT.
RC STRAIN=ATCC 28485 / BCRC 21531 / CBS 704 / DSM 70382 / JCM 3650 / NBRC
RC 10777 / NRRLY-1603;
RX PubMed=12125050; DOI=10.1002/yea.885;
RA Kirchberger J., Baer J., Schellenberger W., Dihazi H., Kopperschlaeger G.;
RT "6-phosphofructokinase from Pichia pastoris: purification, kinetic and
RT molecular characterization of the enzyme.";
RL Yeast 19:933-947(2002).
RN [3]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=17522059; DOI=10.1074/jbc.m611547200;
RA Tanneberger K., Kirchberger J., Baer J., Schellenberger W., Rothemund S.,
RA Kamprad M., Otto H., Schoeneberg T., Edelmann A.;
RT "A novel form of 6-phosphofructokinase. Identification and functional
RT relevance of a third type of subunit in Pichia pastoris.";
RL J. Biol. Chem. 282:23687-23697(2007).
RN [4]
RP STRUCTURE BY ELECTRON MICROSCOPY, AND SUBUNIT.
RX PubMed=19559794; DOI=10.1016/j.jsb.2009.06.014;
RA Benjamin S., Radermacher M., Kirchberger J., Schoeneberg T., Edelmann A.,
RA Ruiz T.;
RT "3D structure of phosphofructokinase from Pichia pastoris: Localization of
RT the novel gamma-subunits.";
RL J. Struct. Biol. 168:345-351(2009).
RN [5] {ECO:0007744|PDB:3OPY}
RP X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) IN COMPLEX WITH ALLOSTERIC INHIBITOR
RP ATP.
RX PubMed=20833871; DOI=10.1096/fj.10-163865;
RA Straeter N., Marek S., Kuettner E.B., Kloos M., Keim A., Brueser A.,
RA Kirchberger J., Schoeneberg T.;
RT "Molecular architecture and structural basis of allosteric regulation of
RT eukaryotic phosphofructokinases.";
RL FASEB J. 25:89-98(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 ECO:0000269|PubMed:12125050}.
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, ECO:0000269|PubMed:12125050};
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, ECO:0000269|PubMed:12125050}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.971 mM for D-fructose 6-phosphate {ECO:0000269|PubMed:12125050};
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: Heterododecamer of 4 alpha, 4 beta and 4 gamma chains.
CC {ECO:0000269|PubMed:12125050, ECO:0000269|PubMed:17522059,
CC ECO:0000269|PubMed:19559794, ECO:0000269|PubMed:20833871}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184,
CC ECO:0000269|PubMed:17522059}.
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; AF395078; AAL82590.2; -; Genomic_DNA.
DR PDB; 3OPY; X-ray; 3.05 A; B/D/F/H=1-941.
DR PDBsum; 3OPY; -.
DR AlphaFoldDB; Q8TGA0; -.
DR SMR; Q8TGA0; -.
DR UniPathway; UPA00109; UER00182.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
DR Gene3D; 3.10.180.10; -; 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; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
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 SUPFAM; SSF54593; SSF54593; 1.
DR TIGRFAMs; TIGR02478; 6PF1K_euk; 1.
DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Allosteric enzyme; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Glycolysis; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12125051"
FT CHAIN 2..941
FT /note="ATP-dependent 6-phosphofructokinase subunit beta"
FT /id="PRO_0000429716"
FT REGION 2..558
FT /note="N-terminal catalytic PFK domain 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184,
FT ECO:0000305|PubMed:20833871"
FT REGION 559..572
FT /note="Interdomain linker"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184,
FT ECO:0000305|PubMed:20833871"
FT REGION 573..941
FT /note="C-terminal regulatory PFK domain 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184,
FT ECO:0000305|PubMed:20833871"
FT ACT_SITE 333
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 191
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /ligand_note="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 255..256
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /ligand_note="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 285..288
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /ligand_note="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 286
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 331..333
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /ligand_label="2"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 368
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /ligand_label="1"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 375..377
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /ligand_label="2"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 395
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000269|PubMed:20833871,
FT ECO:0007744|PDB:3OPY"
FT BINDING 400..405
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000269|PubMed:20833871,
FT ECO:0007744|PDB:3OPY"
FT BINDING 410
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000269|PubMed:20833871,
FT ECO:0007744|PDB:3OPY"
FT BINDING 432
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /ligand_label="2"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 460
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /ligand_label="1"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 466..469
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /ligand_label="2"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 557..558
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000269|PubMed:20833871,
FT ECO:0007744|PDB:3OPY"
FT BINDING 643
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_label="2"
FT /ligand_note="allosteric activator; ligand shared with
FT subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 701..705
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_label="2"
FT /ligand_note="allosteric activator; ligand shared with
FT subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 739
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_label="1"
FT /ligand_note="allosteric activator; ligand shared with
FT subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 746..748
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_label="2"
FT /ligand_note="allosteric activator; ligand shared with
FT subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 806
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_label="2"
FT /ligand_note="allosteric activator; ligand shared with
FT subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 832
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_label="1"
FT /ligand_note="allosteric activator; ligand shared with
FT subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 838..841
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_label="2"
FT /ligand_note="allosteric activator; ligand shared with
FT subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 918
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_label="2"
FT /ligand_note="allosteric activator; ligand shared with
FT subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT STRAND 9..16
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 24..32
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 70..80
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 97..103
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 105..113
FT /evidence="ECO:0007829|PDB:3OPY"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 196..209
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 220..226
FT /evidence="ECO:0007829|PDB:3OPY"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 237..240
FT /evidence="ECO:0007829|PDB:3OPY"
FT TURN 241..245
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 262..275
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 279..284
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 286..297
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 315..319
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 324..333
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 345..360
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 367..373
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 381..389
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 393..396
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 407..421
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 426..430
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 444..453
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 458..463
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 465..468
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 475..494
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 502..509
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 511..515
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 516..531
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 535..541
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 544..557
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 568..570
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 573..581
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 586..600
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 603..607
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 610..617
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 620..622
FT /evidence="ECO:0007829|PDB:3OPY"
FT TURN 625..630
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 631..633
FT /evidence="ECO:0007829|PDB:3OPY"
FT TURN 646..648
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 651..660
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 664..671
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 672..683
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 684..686
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 689..691
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 695..700
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 715..735
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 739..745
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 752..761
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 764..767
FT /evidence="ECO:0007829|PDB:3OPY"
FT TURN 769..771
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 775..790
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 800..805
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 806..808
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 810..812
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 814..825
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 828..834
FT /evidence="ECO:0007829|PDB:3OPY"
FT TURN 838..841
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 847..875
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 884..887
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 890..895
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 900..904
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 905..910
FT /evidence="ECO:0007829|PDB:3OPY"
FT TURN 915..918
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 926..936
FT /evidence="ECO:0007829|PDB:3OPY"
SQ SEQUENCE 941 AA; 103733 MW; BA5FCF3DE48C5899 CRC64;
MPDASLFNGT SFITLFAPNI SLLQASIDFY TNFLGFAIRK NSNQKLFWLQ LEEDQNNVSI
QLILDPEHAA SVSQIDQNIR NLTRSLYRKD WRSIQSNIAF KSSSLSKLVK LLKDGGHPVQ
QSPNEISPFE VYTVDPLGSL IGFSGFKNPF AVNERSLLPK VSEEKAYRAE DDSEKLLNPV
RKTIGVMTSG GDSPGMNPFV RAVVRAGIYK GCKVFCIHEG YEGLVRGGEK YIKETQWHDV
RGWLVEGGTN IGTARCKEFR ERSGRLKACK NMIDMGIDAL IVCGGDGSLT GADRFRSEWP
SLIEELLQTE QISQQQFNTH QNLNICGAVG SIDNDMSSTD ATIGAFSSLD RICRAIDYID
ATANSHSRAF IVEVMGRHCG WLGLLAGLAT SADYILIPEK PASSREWQDQ MCDIVGKHRA
RGKRKTIVIV AEGAISNDLS PISCDQVKDV LVNRLGLDTR VTTLGHVQRG GTAVAFDRIY
ATLQGVEAVN AVLECDADTP SPMIAIKEDQ ITRVPLVDAV ELTQQVAKSI ESRNFKKAIS
LRDSEFVEHM KNFISTNSAD HVPPSLPLEK RKKIAIINVG APAGGMNSAV YSMATYCMSR
GHVPYAIHNG FSGLARHESV RSINWLDIEG WGSLGGSEIG TNRTLPNDAD IGMIAYFFEK
YGFDGLILVG GFEAFISLHQ LERARINYPS LRIPLVLIPA TISNNVPGTE YSLGSDTCLN
SFMEYCDVIK QSAAATRNRV FVVEVQGGNS GYIATHAQLA CGAQISYVPE EGISLAQLEM
DINSLKESFA NDQGKTKSGR LILKSENASK VLTTEVISTI IDDEASGRFD SKTAIPGHVQ
QGGIPSPMDR VRASRFAIRA VSFIERHSDR CQTFKNSISF RQTDEITSTA VVLGIHKSQL
RFTPIRQLYD FESDVPRRMR KNIFWSNVRE ISDMLSGRTS L
