ID   NFYA_HUMAN              Reviewed;         347 AA.
AC   P23511; Q8IXU0;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 2.
DT   24-JAN-2024, entry version 207.
DE   RecName: Full=Nuclear transcription factor Y subunit alpha;
DE   AltName: Full=CAAT box DNA-binding protein subunit A;
DE   AltName: Full=Nuclear transcription factor Y subunit A;
DE            Short=NF-YA;
GN   Name=NFYA;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1549471; DOI=10.1093/nar/20.5.1087;
RA   Li X.-Y., Mantovani R., Hooft van Huijsduijnen R., Andre I., Benoist C.,
RA   Mathis D.;
RT   "Evolutionary variation of the CCAAT-binding transcription factor NF-Y.";
RL   Nucleic Acids Res. 20:1087-1091(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 91-347.
RX   PubMed=2000400; DOI=10.1073/pnas.88.5.1968;
RA   Becker D.M., Fikes J.D., Guarente L.;
RT   "A cDNA encoding a human CCAAT-binding protein cloned by functional
RT   complementation in yeast.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:1968-1972(1991).
RN   [5]
RP   INTERACTION WITH ZHX1.
RX   PubMed=10441475; DOI=10.1006/bbrc.1999.1087;
RA   Yamada K., Printz R.L., Osawa H., Granner D.K.;
RT   "Human ZHX1: cloning, chromosomal location, and interaction with
RT   transcription factor NF-Y.";
RL   Biochem. Biophys. Res. Commun. 261:614-621(1999).
RN   [6]
RP   INTERACTION WITH ZHX1.
RX   PubMed=10571058; DOI=10.1016/s0014-5793(99)01311-3;
RA   Yamada K., Osawa H., Granner D.K.;
RT   "Identification of proteins that interact with NF-YA.";
RL   FEBS Lett. 460:41-45(1999).
RN   [7]
RP   INTERACTION WITH ZFX3.
RC   TISSUE=Testis;
RX   PubMed=12659632; DOI=10.1042/bj20021866;
RA   Yamada K., Kawata H., Shou Z., Hirano S., Mizutani T., Yazawa T.,
RA   Sekiguchi T., Yoshino M., Kajitani T., Miyamoto K.;
RT   "Analysis of zinc-fingers and homeoboxes (ZHX)-1-interacting proteins:
RT   molecular cloning and characterization of a member of the ZHX family,
RT   ZHX3.";
RL   Biochem. J. 373:167-178(2003).
RN   [8]
RP   FUNCTION, AND INTERACTION WITH ZHX2.
RC   TISSUE=Testis;
RX   PubMed=12741956; DOI=10.1042/bj20030171;
RA   Kawata H., Yamada K., Shou Z., Mizutani T., Yazawa T., Yoshino M.,
RA   Sekiguchi T., Kajitani T., Miyamoto K.;
RT   "Zinc-fingers and homeoboxes (ZHX) 2, a novel member of the ZHX family,
RT   functions as a transcriptional repressor.";
RL   Biochem. J. 373:747-757(2003).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [10]
RP   INTERACTION WITH SP1.
RX   PubMed=19302979; DOI=10.1016/j.bbrc.2009.03.075;
RA   Lim K., Chang H.I.;
RT   "O-GlcNAcylation of Sp1 interrupts Sp1 interaction with NF-Y.";
RL   Biochem. Biophys. Res. Commun. 382:593-597(2009).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (3.08 ANGSTROMS) OF 262-332 IN COMPLEX WITH NYFB;
RP   NYFC AND PROMOTER DNA, AND SUBUNIT.
RX   PubMed=23332751; DOI=10.1016/j.cell.2012.11.047;
RA   Nardini M., Gnesutta N., Donati G., Gatta R., Forni C., Fossati A.,
RA   Vonrhein C., Moras D., Romier C., Bolognesi M., Mantovani R.;
RT   "Sequence-specific transcription factor NF-Y displays histone-like DNA
RT   binding and H2B-like ubiquitination.";
RL   Cell 152:132-143(2013).
CC   -!- FUNCTION: Component of the sequence-specific heterotrimeric
CC       transcription factor (NF-Y) which specifically recognizes a 5'-CCAAT-3'
CC       box motif found in the promoters of its target genes. NF-Y can function
CC       as both an activator and a repressor, depending on its interacting
CC       cofactors. NF-YA positively regulates the transcription of the core
CC       clock component BMAL1. {ECO:0000269|PubMed:12741956}.
CC   -!- SUBUNIT: Heterotrimeric transcription factor composed of three
CC       components, NF-YA, NF-YB and NF-YC. NF-YB and NF-YC must interact and
CC       dimerize for NF-YA association and DNA binding. Interacts with SP1; the
CC       interaction is inhibited by glycosylation of SP1. Interacts with ZHX1.
CC       Interacts (via N-terminus) with ZHX2 (via homeobox domain). Interacts
CC       with ZFX3. {ECO:0000269|PubMed:10441475, ECO:0000269|PubMed:10571058,
CC       ECO:0000269|PubMed:12659632, ECO:0000269|PubMed:12741956,
CC       ECO:0000269|PubMed:19302979, ECO:0000269|PubMed:23332751}.
CC   -!- INTERACTION:
CC       P23511; Q92624: APPBP2; NbExp=3; IntAct=EBI-389739, EBI-743771;
CC       P23511; P68400: CSNK2A1; NbExp=4; IntAct=EBI-389739, EBI-347804;
CC       P23511; P52655: GTF2A1; NbExp=3; IntAct=EBI-389739, EBI-389518;
CC       P23511; Q9Y383: LUC7L2; NbExp=4; IntAct=EBI-389739, EBI-352851;
CC       P23511; P25208: NFYB; NbExp=8; IntAct=EBI-389739, EBI-389728;
CC       P23511; Q13952: NFYC; NbExp=6; IntAct=EBI-389739, EBI-389755;
CC       P23511; Q7Z3K3: POGZ; NbExp=3; IntAct=EBI-389739, EBI-1389308;
CC       P23511; Q07955: SRSF1; NbExp=5; IntAct=EBI-389739, EBI-398920;
CC       P23511; P04637: TP53; NbExp=11; IntAct=EBI-389739, EBI-366083;
CC       P23511-2; P54253: ATXN1; NbExp=3; IntAct=EBI-11061759, EBI-930964;
CC       P23511-2; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-11061759, EBI-11524452;
CC       P23511-2; P68400: CSNK2A1; NbExp=3; IntAct=EBI-11061759, EBI-347804;
CC       P23511-2; Q92997: DVL3; NbExp=3; IntAct=EBI-11061759, EBI-739789;
CC       P23511-2; P52655: GTF2A1; NbExp=3; IntAct=EBI-11061759, EBI-389518;
CC       P23511-2; Q9Y383: LUC7L2; NbExp=3; IntAct=EBI-11061759, EBI-352851;
CC       P23511-2; P25208: NFYB; NbExp=6; IntAct=EBI-11061759, EBI-389728;
CC       P23511-2; Q13952-2: NFYC; NbExp=4; IntAct=EBI-11061759, EBI-11956831;
CC       P23511-2; Q7Z3K3: POGZ; NbExp=3; IntAct=EBI-11061759, EBI-1389308;
CC       P23511-2; P14859-6: POU2F1; NbExp=5; IntAct=EBI-11061759, EBI-11526590;
CC       P23511-2; Q2TAL8: QRICH1; NbExp=3; IntAct=EBI-11061759, EBI-2798044;
CC       P23511-2; Q9Y4C2-2: TCAF1; NbExp=3; IntAct=EBI-11061759, EBI-11974855;
CC       P23511-2; Q9BZL1: UBL5; NbExp=3; IntAct=EBI-11061759, EBI-607755;
CC       P23511-2; Q14119: VEZF1; NbExp=3; IntAct=EBI-11061759, EBI-11980193;
CC       P23511-2; Q96K80: ZC3H10; NbExp=3; IntAct=EBI-11061759, EBI-742550;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Long;
CC         IsoId=P23511-1; Sequence=Displayed;
CC       Name=Short;
CC         IsoId=P23511-2; Sequence=VSP_000849;
CC   -!- SIMILARITY: Belongs to the NFYA/HAP2 subunit family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00966}.
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DR   EMBL; X59711; CAA42231.1; -; mRNA.
DR   EMBL; AL031778; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC039244; AAH39244.1; -; mRNA.
DR   EMBL; M59079; AAA35950.1; -; mRNA.
DR   CCDS; CCDS4849.1; -. [P23511-1]
DR   CCDS; CCDS4850.1; -. [P23511-2]
DR   PIR; S22816; A39123.
DR   RefSeq; NP_002496.1; NM_002505.4. [P23511-1]
DR   RefSeq; NP_068351.1; NM_021705.3. [P23511-2]
DR   PDB; 4AWL; X-ray; 3.08 A; A=262-332.
DR   PDB; 6QMP; X-ray; 2.00 A; A=267-295.
DR   PDB; 6QMQ; X-ray; 2.50 A; A=267-285.
DR   PDB; 6QMS; X-ray; 1.80 A; A=267-285.
DR   PDBsum; 4AWL; -.
DR   PDBsum; 6QMP; -.
DR   PDBsum; 6QMQ; -.
DR   PDBsum; 6QMS; -.
DR   AlphaFoldDB; P23511; -.
DR   SASBDB; P23511; -.
DR   SMR; P23511; -.
DR   BioGRID; 110866; 99.
DR   ComplexPortal; CPX-1956; CCAAT-binding factor complex.
DR   CORUM; P23511; -.
DR   IntAct; P23511; 40.
DR   MINT; P23511; -.
DR   STRING; 9606.ENSP00000345702; -.
DR   GlyCosmos; P23511; 4 sites, 2 glycans.
DR   GlyGen; P23511; 6 sites, 2 O-linked glycans (6 sites).
DR   iPTMnet; P23511; -.
DR   PhosphoSitePlus; P23511; -.
DR   BioMuta; NFYA; -.
DR   DMDM; 115844; -.
DR   EPD; P23511; -.
DR   jPOST; P23511; -.
DR   MassIVE; P23511; -.
DR   MaxQB; P23511; -.
DR   PaxDb; 9606-ENSP00000345702; -.
DR   PeptideAtlas; P23511; -.
DR   ProteomicsDB; 54123; -. [P23511-1]
DR   ProteomicsDB; 54124; -. [P23511-2]
DR   Pumba; P23511; -.
DR   Antibodypedia; 3982; 267 antibodies from 35 providers.
DR   DNASU; 4800; -.
DR   Ensembl; ENST00000341376.11; ENSP00000345702.6; ENSG00000001167.15. [P23511-1]
DR   Ensembl; ENST00000353205.5; ENSP00000229418.6; ENSG00000001167.15. [P23511-2]
DR   GeneID; 4800; -.
DR   KEGG; hsa:4800; -.
DR   MANE-Select; ENST00000341376.11; ENSP00000345702.6; NM_002505.5; NP_002496.1.
DR   UCSC; uc003opo.4; human. [P23511-1]
DR   AGR; HGNC:7804; -.
DR   CTD; 4800; -.
DR   DisGeNET; 4800; -.
DR   GeneCards; NFYA; -.
DR   HGNC; HGNC:7804; NFYA.
DR   HPA; ENSG00000001167; Low tissue specificity.
DR   MIM; 189903; gene.
DR   neXtProt; NX_P23511; -.
DR   OpenTargets; ENSG00000001167; -.
DR   PharmGKB; PA31609; -.
DR   VEuPathDB; HostDB:ENSG00000001167; -.
DR   eggNOG; KOG1561; Eukaryota.
DR   GeneTree; ENSGT00390000015714; -.
DR   HOGENOM; CLU_071609_1_0_1; -.
DR   InParanoid; P23511; -.
DR   OMA; VAHMIRV; -.
DR   OrthoDB; 5490901at2759; -.
DR   PhylomeDB; P23511; -.
DR   TreeFam; TF323257; -.
DR   PathwayCommons; P23511; -.
DR   Reactome; R-HSA-1989781; PPARA activates gene expression.
DR   Reactome; R-HSA-2426168; Activation of gene expression by SREBF (SREBP).
DR   Reactome; R-HSA-380994; ATF4 activates genes in response to endoplasmic reticulum stress.
DR   Reactome; R-HSA-381183; ATF6 (ATF6-alpha) activates chaperone genes.
DR   Reactome; R-HSA-9614657; FOXO-mediated transcription of cell death genes.
DR   SignaLink; P23511; -.
DR   SIGNOR; P23511; -.
DR   BioGRID-ORCS; 4800; 184 hits in 1179 CRISPR screens.
DR   ChiTaRS; NFYA; human.
DR   GeneWiki; NFYA; -.
DR   GenomeRNAi; 4800; -.
DR   Pharos; P23511; Tbio.
DR   PRO; PR:P23511; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; P23511; Protein.
DR   Bgee; ENSG00000001167; Expressed in cortical plate and 186 other cell types or tissues.
DR   ExpressionAtlas; P23511; baseline and differential.
DR   GO; GO:0016602; C:CCAAT-binding factor complex; IDA:UniProtKB.
DR   GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0032993; C:protein-DNA complex; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IDA:NTNU_SB.
DR   GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:ProtInc.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISS:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:UniProtKB.
DR   GO; GO:0035065; P:regulation of histone acetylation; IDA:ComplexPortal.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
DR   Gene3D; 6.10.250.2430; -; 1.
DR   InterPro; IPR018362; CCAAT-binding_factor_CS.
DR   InterPro; IPR001289; NFYA.
DR   PANTHER; PTHR12632:SF6; NUCLEAR TRANSCRIPTION FACTOR Y SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR12632; TRANSCRIPTION FACTOR NF-Y ALPHA-RELATED; 1.
DR   Pfam; PF02045; CBFB_NFYA; 1.
DR   PRINTS; PR00616; CCAATSUBUNTB.
DR   SMART; SM00521; CBF; 1.
DR   PROSITE; PS00686; NFYA_HAP2_1; 1.
DR   PROSITE; PS51152; NFYA_HAP2_2; 1.
DR   Genevisible; P23511; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Alternative splicing; Biological rhythms;
KW   DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..347
FT                   /note="Nuclear transcription factor Y subunit alpha"
FT                   /id="PRO_0000198768"
FT   DNA_BIND        296..321
FT                   /note="NFYA/HAP2-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00966"
FT   REGION          299..347
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           266..289
FT                   /note="Subunit association domain (SAD)"
FT   COMPBIAS        312..332
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         326
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         26..54
FT                   /note="Missing (in isoform Short)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_000849"
FT   CONFLICT        273
FT                   /note="H -> N (in Ref. 3; AAH39244)"
FT                   /evidence="ECO:0000305"
FT   STRAND          264..267
FT                   /evidence="ECO:0007829|PDB:4AWL"
FT   TURN            269..271
FT                   /evidence="ECO:0007829|PDB:6QMS"
FT   HELIX           275..278
FT                   /evidence="ECO:0007829|PDB:6QMS"
FT   HELIX           301..309
FT                   /evidence="ECO:0007829|PDB:4AWL"
FT   HELIX           314..316
FT                   /evidence="ECO:0007829|PDB:4AWL"
SQ   SEQUENCE   347 AA;  36877 MW;  D00BE17041EB1A9E CRC64;
     MEQYTANSNS STEQIVVQAG QIQQQQQGGV TAVQLQTEAQ VASASGQQVQ TLQVVQGQPL
     MVQVSGGQLI TSTGQPIMVQ AVPGGQGQTI MQVPVSGTQG LQQIQLVPPG QIQIQGGQAV
     QVQGQQGQTQ QIIIQQPQTA VTAGQTQTQQ QIAVQGQQVA QTAEGQTIVY QPVNADGTIL
     QQVTVPVSGM ITIPAASLAG AQIVQTGANT NTTSSGQGTV TVTLPVAGNV VNSGGMVMMV
     PGAGSVPAIQ RIPLPGAEML EEEPLYVNAK QYHRILKRRQ ARAKLEAEGK IPKERRKYLH
     ESRHRHAMAR KRGEGGRFFS PKEKDSPHMQ DPNQADEEAM TQIIRVS
//