ID   FOXP4_HUMAN             Reviewed;         680 AA.
AC   Q8IVH2; Q5W098; Q7Z7F8; Q8IW55; Q96E19;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   24-JAN-2024, entry version 178.
DE   RecName: Full=Forkhead box protein P4;
DE   AltName: Full=Fork head-related protein-like A;
GN   Name=FOXP4; Synonyms=FKHLA;
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] (ISOFORM 1).
RA   Daigo Y., Takayama I., Fujino M.A.;
RT   "Isolation, mapping, and characterization of a novel human cDNA
RT   differentially expressed in the fundus of W/Wv mutant mice.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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 GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   TISSUE=Lung, and Skin;
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   [5]
RP   IDENTIFICATION BY 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   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-86 AND SER-554, AND
RP   IDENTIFICATION BY 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   [9]
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   [10]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-246, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25218447; DOI=10.1038/nsmb.2890;
RA   Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA   Vertegaal A.C.;
RT   "Uncovering global SUMOylation signaling networks in a site-specific
RT   manner.";
RL   Nat. Struct. Mol. Biol. 21:927-936(2014).
RN   [11]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-175; LYS-246 AND LYS-378, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
RN   [12]
RP   VARIANT [LARGE SCALE ANALYSIS] THR-464.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Transcriptional repressor that represses lung-specific
CC       expression. {ECO:0000250}.
CC   -!- SUBUNIT: Forms homodimers and heterodimers with FOXP1 and FOXP2.
CC       Dimerization is required for DNA-binding (By similarity).
CC       {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q8IVH2; Q9H334: FOXP1; NbExp=6; IntAct=EBI-1054619, EBI-983809;
CC       Q8IVH2; O15409: FOXP2; NbExp=6; IntAct=EBI-1054619, EBI-983612;
CC       Q8IVH2-2; Q92993: KAT5; NbExp=3; IntAct=EBI-25885364, EBI-399080;
CC       Q8IVH2-2; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-25885364, EBI-11742507;
CC       Q8IVH2-2; P17252: PRKCA; NbExp=3; IntAct=EBI-25885364, EBI-1383528;
CC       Q8IVH2-2; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-25885364, EBI-9090795;
CC       Q8IVH2-2; P61981: YWHAG; NbExp=3; IntAct=EBI-25885364, EBI-359832;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8IVH2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8IVH2-2; Sequence=VSP_043034;
CC       Name=3;
CC         IsoId=Q8IVH2-3; Sequence=VSP_043465, VSP_043466;
CC   -!- DOMAIN: The leucine-zipper is required for dimerization and
CC       transcriptional repression. {ECO:0000250}.
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DR   EMBL; AB080747; BAC53809.1; -; mRNA.
DR   EMBL; AL139331; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471081; EAX04047.1; -; Genomic_DNA.
DR   EMBL; CH471081; EAX04048.1; -; Genomic_DNA.
DR   EMBL; CH471081; EAX04049.1; -; Genomic_DNA.
DR   EMBL; BC013030; AAH13030.2; -; mRNA.
DR   EMBL; BC040962; AAH40962.1; -; mRNA.
DR   EMBL; BC052803; AAH52803.1; -; mRNA.
DR   CCDS; CCDS34447.1; -. [Q8IVH2-1]
DR   CCDS; CCDS34448.1; -. [Q8IVH2-2]
DR   CCDS; CCDS4856.1; -. [Q8IVH2-3]
DR   RefSeq; NP_001012426.1; NM_001012426.1. [Q8IVH2-1]
DR   RefSeq; NP_001012427.1; NM_001012427.1. [Q8IVH2-2]
DR   RefSeq; NP_612466.1; NM_138457.2. [Q8IVH2-3]
DR   PDB; 6XAT; X-ray; 2.20 A; A=464-550.
DR   PDBsum; 6XAT; -.
DR   AlphaFoldDB; Q8IVH2; -.
DR   SMR; Q8IVH2; -.
DR   BioGRID; 125474; 68.
DR   DIP; DIP-59301N; -.
DR   IntAct; Q8IVH2; 57.
DR   MINT; Q8IVH2; -.
DR   STRING; 9606.ENSP00000362151; -.
DR   GlyGen; Q8IVH2; 4 sites, 1 O-linked glycan (4 sites).
DR   iPTMnet; Q8IVH2; -.
DR   PhosphoSitePlus; Q8IVH2; -.
DR   BioMuta; FOXP4; -.
DR   DMDM; 46395887; -.
DR   EPD; Q8IVH2; -.
DR   jPOST; Q8IVH2; -.
DR   MassIVE; Q8IVH2; -.
DR   MaxQB; Q8IVH2; -.
DR   PaxDb; 9606-ENSP00000362151; -.
DR   PeptideAtlas; Q8IVH2; -.
DR   ProteomicsDB; 70705; -. [Q8IVH2-1]
DR   ProteomicsDB; 70706; -. [Q8IVH2-2]
DR   ProteomicsDB; 70707; -. [Q8IVH2-3]
DR   Pumba; Q8IVH2; -.
DR   ABCD; Q8IVH2; 2 sequenced antibodies.
DR   Antibodypedia; 1453; 300 antibodies from 35 providers.
DR   DNASU; 116113; -.
DR   Ensembl; ENST00000307972.10; ENSP00000309823.4; ENSG00000137166.18. [Q8IVH2-1]
DR   Ensembl; ENST00000373057.7; ENSP00000362148.3; ENSG00000137166.18. [Q8IVH2-2]
DR   Ensembl; ENST00000373063.7; ENSP00000362154.3; ENSG00000137166.18. [Q8IVH2-3]
DR   Ensembl; ENST00000704756.1; ENSP00000516024.1; ENSG00000137166.18. [Q8IVH2-1]
DR   GeneID; 116113; -.
DR   KEGG; hsa:116113; -.
DR   MANE-Select; ENST00000307972.10; ENSP00000309823.4; NM_001012426.2; NP_001012426.1.
DR   UCSC; uc003oql.4; human. [Q8IVH2-1]
DR   AGR; HGNC:20842; -.
DR   CTD; 116113; -.
DR   DisGeNET; 116113; -.
DR   GeneCards; FOXP4; -.
DR   HGNC; HGNC:20842; FOXP4.
DR   HPA; ENSG00000137166; Low tissue specificity.
DR   MalaCards; FOXP4; -.
DR   MIM; 608924; gene.
DR   neXtProt; NX_Q8IVH2; -.
DR   OpenTargets; ENSG00000137166; -.
DR   PharmGKB; PA134943098; -.
DR   VEuPathDB; HostDB:ENSG00000137166; -.
DR   eggNOG; KOG4385; Eukaryota.
DR   GeneTree; ENSGT00940000158700; -.
DR   HOGENOM; CLU_019502_3_1_1; -.
DR   InParanoid; Q8IVH2; -.
DR   OMA; KQQPKEX; -.
DR   OrthoDB; 5385885at2759; -.
DR   PhylomeDB; Q8IVH2; -.
DR   TreeFam; TF326978; -.
DR   PathwayCommons; Q8IVH2; -.
DR   SignaLink; Q8IVH2; -.
DR   BioGRID-ORCS; 116113; 24 hits in 1181 CRISPR screens.
DR   ChiTaRS; FOXP4; human.
DR   GeneWiki; FOXP4; -.
DR   GenomeRNAi; 116113; -.
DR   Pharos; Q8IVH2; Tbio.
DR   PRO; PR:Q8IVH2; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q8IVH2; Protein.
DR   Bgee; ENSG00000137166; Expressed in kidney epithelium and 166 other cell types or tissues.
DR   ExpressionAtlas; Q8IVH2; baseline and differential.
DR   GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd20067; FH_FOXP4; 1.
DR   Gene3D; 1.20.5.340; -; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR047414; FH_FOXP4.
DR   InterPro; IPR001766; Fork_head_dom.
DR   InterPro; IPR032354; FOXP-CC.
DR   InterPro; IPR030456; TF_fork_head_CS_2.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR45796; FORKHEAD BOX P, ISOFORM C; 1.
DR   PANTHER; PTHR45796:SF7; FORKHEAD BOX PROTEIN P4; 1.
DR   Pfam; PF00250; Forkhead; 1.
DR   Pfam; PF16159; FOXP-CC; 1.
DR   PRINTS; PR00053; FORKHEAD.
DR   SMART; SM00339; FH; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS00658; FORK_HEAD_2; 1.
DR   PROSITE; PS50039; FORK_HEAD_3; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR   Genevisible; Q8IVH2; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; DNA-binding; Isopeptide bond;
KW   Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW   Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..680
FT                   /note="Forkhead box protein P4"
FT                   /id="PRO_0000091889"
FT   ZN_FING         307..332
FT                   /note="C2H2-type"
FT   DNA_BIND        467..559
FT                   /note="Fork-head"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT   REGION          1..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          262..306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          349..370
FT                   /note="Leucine-zipper"
FT   REGION          407..445
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          602..680
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        274..288
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         52
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         86
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         554
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   CROSSLNK        175
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        246
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25218447,
FT                   ECO:0007744|PubMed:28112733"
FT   CROSSLNK        378
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VAR_SEQ         141..142
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_043034"
FT   VAR_SEQ         220
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_043465"
FT   VAR_SEQ         384..395
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_043466"
FT   VARIANT         464
FT                   /note="A -> T (in a breast cancer sample; somatic mutation;
FT                   dbSNP:rs867245225)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036219"
FT   HELIX           472..482
FT                   /evidence="ECO:0007829|PDB:6XAT"
FT   HELIX           490..500
FT                   /evidence="ECO:0007829|PDB:6XAT"
FT   HELIX           502..506
FT                   /evidence="ECO:0007829|PDB:6XAT"
FT   HELIX           509..521
FT                   /evidence="ECO:0007829|PDB:6XAT"
FT   STRAND          525..528
FT                   /evidence="ECO:0007829|PDB:6XAT"
FT   STRAND          535..538
FT                   /evidence="ECO:0007829|PDB:6XAT"
SQ   SEQUENCE   680 AA;  73488 MW;  A63826ED85B24752 CRC64;
     MMVESASETI RSAPSGQNGV GSLSGQADGS SGGATGTTAS GTGREVTTGA DSNGEMSPAE
     LLHFQQQQAL QVARQFLLQQ ASGLSSPGNN DSKQSASAVQ VPVSVAMMSP QMLTPQQMQQ
     ILSPPQLQAL LQQQQALMLQ QLQEYYKKQQ EQLHLQLLTQ QQAGKPQPKE ALGNKQLAFQ
     QQLLQMQQLQ QQHLLNLQRQ GLVSLQPNQA SGPLQTLPQA AVCPTDLPQL WKGEGAPGQP
     AEDSVKQEGL DLTGTAATAT SFAAPPKVSP PLSHHTLPNG QPTVLTSRRD SSSHEETPGS
     HPLYGHGECK WPGCETLCED LGQFIKHLNT EHALDDRSTA QCRVQMQVVQ QLEIQLAKES
     ERLQAMMAHL HMRPSEPKPF SQPLNPVPGS SSFSKVTVSA ADSFPDGLVH PPTSAAAPVT
     PLRPPGLGSA SLHGGGPARR RSSDKFCSPI SSELAQNHEF YKNADVRPPF TYASLIRQAI
     LETPDRQLTL NEIYNWFTRM FAYFRRNTAT WKNAVRHNLS LHKCFVRVEN VKGAVWTVDE
     REYQKRRPPK MTGSPTLVKN MISGLSYGAL NASYQAALAE SSFPLLNSPG MLNPGSASSL
     LPLSHDDVGA PVEPLPSNGS SSPPRLSPPQ YSHQVQVKEE PAEAEEDRQP GPPLGAPNPS
     ASGPPEDRDL EEELPGEELS
//