INT6_HUMAN
ID INT6_HUMAN Reviewed; 887 AA.
AC Q9UL03; Q0P664; Q6PJP4; Q9UFK0; Q9Y5M9;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Integrator complex subunit 6;
DE Short=Int6;
DE AltName: Full=DBI-1;
DE AltName: Full=Protein DDX26;
DE AltName: Full=Protein deleted in cancer 1;
DE Short=DICE1;
GN Name=INTS6; Synonyms=DBI1, DDX26, DDX26A;
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), AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10467397; DOI=10.1038/sj.onc.1202806;
RA Wieland I., Arden K.C., Michels D., Klein-Hitpass L., Boehm M., Viars C.S.,
RA Weidle U.H.;
RT "Isolation of DICE1: a gene frequently affected by LOH and downregulated in
RT lung carcinomas.";
RL Oncogene 18:4530-4537(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 415-887 (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, Lung, and Placenta;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 273-887 (ISOFORM 1).
RC TISSUE=Lung;
RA Hoff H.B. III, Oh C., Sell C.;
RT "Human DBI-1 homolog.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=11939413; DOI=10.3727/096504001108747503;
RA Wieland I., Roepke A., Stumm M., Sell C., Weidle U.H., Wieacker P.F.;
RT "Molecular characterization of the DICE1 (DDX26) tumor suppressor gene in
RT lung carcinoma cells.";
RL Oncol. Res. 12:491-500(2001).
RN [7]
RP FUNCTION.
RX PubMed=15254679;
RA Wieland I., Sell C., Weidle U.H., Wieacker P.;
RT "Ectopic expression of DICE1 suppresses tumor cell growth.";
RL Oncol. Rep. 12:207-211(2004).
RN [8]
RP INDUCTION.
RX PubMed=16007164; DOI=10.1038/sj.onc.1208824;
RA Roepke A., Buhtz P., Boehm M., Seger J., Wieland I., Allhoff E.P.,
RA Wieacker P.F.;
RT "Promoter CpG hypermethylation and downregulation of DICE1 expression in
RT prostate cancer.";
RL Oncogene 24:6667-6675(2005).
RN [9]
RP LACK OF INVOLVEMENT IN CANCER.
RX PubMed=16271964; DOI=10.1016/j.cancergencyto.2005.04.014;
RA Hernandez M., Papadopoulos N., Almeida T.A.;
RT "Absence of mutations in DICE1/DDX26 gene in human cancer cell lines with
RT frequent 13q14 deletions.";
RL Cancer Genet. Cytogenet. 163:91-92(2005).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND IDENTIFICATION IN THE
RP INTEGRATOR COMPLEX.
RX PubMed=16239144; DOI=10.1016/j.cell.2005.08.019;
RA Baillat D., Hakimi M.-A., Naeaer A.M., Shilatifard A., Cooch N.,
RA Shiekhattar R.;
RT "Integrator, a multiprotein mediator of small nuclear RNA processing,
RT associates with the C-terminal repeat of RNA polymerase II.";
RL Cell 123:265-276(2005).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-804, 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 [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23904267; DOI=10.1091/mbc.e13-05-0254;
RA Jodoin J.N., Sitaram P., Albrecht T.R., May S.B., Shboul M., Lee E.,
RA Reversade B., Wagner E.J., Lee L.A.;
RT "Nuclear-localized Asunder regulates cytoplasmic dynein localization via
RT its role in the integrator complex.";
RL Mol. Biol. Cell 24:2954-2965(2013).
CC -!- FUNCTION: Component of the Integrator (INT) complex, a complex involved
CC in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their
CC 3'-box-dependent processing. The Integrator complex is associated with
CC the C-terminal domain (CTD) of RNA polymerase II largest subunit
CC (POLR2A) and is recruited to the U1 and U2 snRNAs genes (Probable).
CC Mediates recruitment of cytoplasmic dynein to the nuclear envelope,
CC probably as component of the INT complex (PubMed:23904267). May have a
CC tumor suppressor role; an ectopic expression suppressing tumor cell
CC growth (PubMed:15254679, PubMed:16239144).
CC {ECO:0000269|PubMed:15254679, ECO:0000269|PubMed:16239144,
CC ECO:0000269|PubMed:23904267, ECO:0000305|PubMed:16239144}.
CC -!- SUBUNIT: Belongs to the multiprotein complex Integrator, at least
CC composed of INTS1, INTS2, INTS3, INTS4, INTS5, INTS6, INTS7, INTS8,
CC INTS9/RC74, INTS10, INTS11/CPSF3L and INTS12.
CC {ECO:0000269|PubMed:16239144}.
CC -!- INTERACTION:
CC Q9UL03; P33993: MCM7; NbExp=10; IntAct=EBI-1381827, EBI-355924;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11939413,
CC ECO:0000269|PubMed:23904267}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9UL03-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UL03-2; Sequence=VSP_021457, VSP_021458;
CC Name=3;
CC IsoId=Q9UL03-3; Sequence=VSP_041356;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in heart, brain,
CC placenta, lung, liver, skeletal muscle, kidney and pancreas.
CC {ECO:0000269|PubMed:10467397}.
CC -!- INDUCTION: Frequently down-regulated in nonsmall cell lung carcinomas
CC and prostate cancers. Down-regulation in prostate cancer is due to CpG
CC hypermethylation of its promoter. However, some involvement in cancer
CC is unclear. {ECO:0000269|PubMed:16007164}.
CC -!- SIMILARITY: Belongs to the Integrator subunit 6 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH13358.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AL833524; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB56020.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/INTS6ID40287ch13q14.html";
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DR EMBL; AF097645; AAF03046.1; -; mRNA.
DR EMBL; AL833524; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL354820; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL137780; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC013358; AAH13358.1; ALT_SEQ; mRNA.
DR EMBL; BC018725; AAH18725.1; -; mRNA.
DR EMBL; BC032386; AAH32386.1; -; mRNA.
DR EMBL; BC039829; AAH39829.1; -; mRNA.
DR EMBL; AF141326; AAD39481.1; -; mRNA.
DR EMBL; AL117626; CAB56020.1; ALT_INIT; mRNA.
DR EMBL; BK005730; DAA05730.1; -; mRNA.
DR CCDS; CCDS41890.1; -. [Q9UL03-3]
DR CCDS; CCDS45048.1; -. [Q9UL03-2]
DR CCDS; CCDS9428.1; -. [Q9UL03-1]
DR PIR; T17330; T17330.
DR RefSeq; NP_001035026.1; NM_001039937.1. [Q9UL03-3]
DR RefSeq; NP_001035027.1; NM_001039938.1. [Q9UL03-2]
DR RefSeq; NP_001293020.1; NM_001306091.1.
DR RefSeq; NP_036273.1; NM_012141.2. [Q9UL03-1]
DR RefSeq; XP_011533342.1; XM_011535040.2. [Q9UL03-1]
DR PDB; 7BV7; X-ray; 2.40 A; C=800-887.
DR PDB; 7CUN; EM; 3.50 A; F=1-887.
DR PDB; 7PKS; EM; 3.60 A; f=1-887.
DR PDBsum; 7BV7; -.
DR PDBsum; 7CUN; -.
DR PDBsum; 7PKS; -.
DR AlphaFoldDB; Q9UL03; -.
DR SMR; Q9UL03; -.
DR BioGRID; 117717; 89.
DR ComplexPortal; CPX-6441; Integrator complex.
DR CORUM; Q9UL03; -.
DR DIP; DIP-38627N; -.
DR IntAct; Q9UL03; 32.
DR MINT; Q9UL03; -.
DR STRING; 9606.ENSP00000310260; -.
DR iPTMnet; Q9UL03; -.
DR PhosphoSitePlus; Q9UL03; -.
DR BioMuta; INTS6; -.
DR DMDM; 74753376; -.
DR EPD; Q9UL03; -.
DR jPOST; Q9UL03; -.
DR MassIVE; Q9UL03; -.
DR MaxQB; Q9UL03; -.
DR PaxDb; Q9UL03; -.
DR PeptideAtlas; Q9UL03; -.
DR PRIDE; Q9UL03; -.
DR ProteomicsDB; 84922; -. [Q9UL03-1]
DR ProteomicsDB; 84923; -. [Q9UL03-2]
DR ProteomicsDB; 84924; -. [Q9UL03-3]
DR TopDownProteomics; Q9UL03-2; -. [Q9UL03-2]
DR Antibodypedia; 730; 153 antibodies from 26 providers.
DR DNASU; 26512; -.
DR Ensembl; ENST00000311234.9; ENSP00000310260.4; ENSG00000102786.15. [Q9UL03-1]
DR Ensembl; ENST00000398119.6; ENSP00000381187.2; ENSG00000102786.15. [Q9UL03-3]
DR Ensembl; ENST00000442263.4; ENSP00000411245.3; ENSG00000102786.15. [Q9UL03-2]
DR GeneID; 26512; -.
DR KEGG; hsa:26512; -.
DR MANE-Select; ENST00000311234.9; ENSP00000310260.4; NM_012141.3; NP_036273.1.
DR UCSC; uc001vfj.4; human. [Q9UL03-1]
DR CTD; 26512; -.
DR DisGeNET; 26512; -.
DR GeneCards; INTS6; -.
DR HGNC; HGNC:14879; INTS6.
DR HPA; ENSG00000102786; Low tissue specificity.
DR MIM; 604331; gene.
DR neXtProt; NX_Q9UL03; -.
DR OpenTargets; ENSG00000102786; -.
DR PharmGKB; PA27212; -.
DR VEuPathDB; HostDB:ENSG00000102786; -.
DR eggNOG; KOG3768; Eukaryota.
DR GeneTree; ENSGT00390000016655; -.
DR HOGENOM; CLU_006789_0_0_1; -.
DR InParanoid; Q9UL03; -.
DR OMA; QDFTLPM; -.
DR PhylomeDB; Q9UL03; -.
DR TreeFam; TF323386; -.
DR PathwayCommons; Q9UL03; -.
DR Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
DR SignaLink; Q9UL03; -.
DR SIGNOR; Q9UL03; -.
DR BioGRID-ORCS; 26512; 568 hits in 1100 CRISPR screens.
DR ChiTaRS; INTS6; human.
DR GeneWiki; INTS6; -.
DR GenomeRNAi; 26512; -.
DR Pharos; Q9UL03; Tbio.
DR PRO; PR:Q9UL03; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q9UL03; protein.
DR Bgee; ENSG00000102786; Expressed in secondary oocyte and 184 other tissues.
DR ExpressionAtlas; Q9UL03; baseline and differential.
DR Genevisible; Q9UL03; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
DR GO; GO:0032039; C:integrator complex; IDA:HGNC-UCL.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:ProtInc.
DR GO; GO:0034243; P:regulation of transcription elongation from RNA polymerase II promoter; IC:ComplexPortal.
DR GO; GO:0034472; P:snRNA 3'-end processing; IBA:GO_Central.
DR GO; GO:0016180; P:snRNA processing; IDA:HGNC-UCL.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR029307; INT_SG_DDX_CT_C.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF15300; INT_SG_DDX_CT_C; 1.
DR Pfam; PF13519; VWA_2; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR PROSITE; PS50234; VWFA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..887
FT /note="Integrator complex subunit 6"
FT /id="PRO_0000259543"
FT DOMAIN 3..227
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT MOD_RES 804
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 1..13
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_041356"
FT VAR_SEQ 114..115
FT /note="GR -> VG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021457"
FT VAR_SEQ 116..887
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021458"
FT CONFLICT 273
FT /note="N -> R (in Ref. 5; AAD39481)"
FT /evidence="ECO:0000305"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 12..15
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 19..23
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 24..39
FT /evidence="ECO:0007829|PDB:7CUN"
FT TURN 43..46
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 58..61
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 70..78
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 88..99
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:7CUN"
FT TURN 104..109
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:7CUN"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 196..203
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 213..223
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:7CUN"
FT TURN 245..247
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 306..310
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 335..338
FT /evidence="ECO:0007829|PDB:7CUN"
FT TURN 339..342
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 349..352
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 356..361
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 363..367
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 375..377
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 386..389
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 412..415
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 424..431
FT /evidence="ECO:0007829|PDB:7CUN"
FT TURN 432..434
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 440..442
FT /evidence="ECO:0007829|PDB:7CUN"
FT TURN 447..449
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 454..469
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 470..472
FT /evidence="ECO:0007829|PDB:7CUN"
FT TURN 540..542
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 553..563
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 584..589
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 809..820
FT /evidence="ECO:0007829|PDB:7BV7"
FT STRAND 822..824
FT /evidence="ECO:0007829|PDB:7BV7"
FT HELIX 828..834
FT /evidence="ECO:0007829|PDB:7BV7"
FT HELIX 841..857
FT /evidence="ECO:0007829|PDB:7BV7"
FT HELIX 861..880
FT /evidence="ECO:0007829|PDB:7BV7"
SQ SEQUENCE 887 AA; 100390 MW; FCD3FD61B7767E03 CRC64;
MPILLFLIDT SASMNQRSHL GTTYLDTAKG AVETFMKLRA RDPASRGDRY MLVTFEEPPY
AIKAGWKENH ATFMNELKNL QAEGLTTLGQ SLRTAFDLLN LNRLVTGIDN YGQGRNPFFL
EPAIIITITD GSKLTTTSGV QDELHLPLNS PLPGSELTKE PFRWDQRLFA LVLRLPGTMS
VESEQLTGVP LDDSAITPMC EVTGGRSYSV CSPRMLNQCL ESLVQKVQSG VVINFEKAGP
DPSPVEDGQP DISRPFGSQP WHSCHKLIYV RPNPKTGVPI GHWPVPESFW PDQNSPTLPP
RTSHPVVKFS CTDCEPMVID KLPFDKYELE PSPLTQFILE RKSPQTCWQV YVSNSAKYSE
LGHPFGYLKA STALNCVNLF VMPYNYPVLL PLLDDLFKVH KAKPTLKWRQ SFESYLKTMP
PYYLGPLKKA VRMMGAPNLI ADSMEYGLSY SVISYLKKLS QQAKIESDRV IGSVGKKVVQ
ETGIKVRSRS HGLSMAYRKD FQQLLQGISE DVPHRLLDLN MKEYTGFQVA LLNKDLKPQT
FRNAYDIPRR NLLDHLTRMR SNLLKSTRRF LKGQDEDQVH SVPIAQMGNY QEYLKQVPSP
LRELDPDQPR RLHTFGNPFK LDKKGMMIDE ADEFVAGPQN KHKRPGEPNM QGIPKRRRCM
SPLLRGRQQN PVVNNHIGGK GPPAPTTQAQ PDLIKPLPLH KISETTNDSI IHDVVENHVA
DQLSSDITPN AMDTEFSASS PASLLERPTN HMEALGHDHL GTNDLTVGGF LENHEEPRDK
EQCAEENIPA SSLNKGKKLM HCRSHEEVNT ELKAQIMKEI RKPGRKYERI FTLLKHVQGS
LQTRLIFLQN VIKEASRFKK RMLIEQLENF LDEIHRRANQ INHINSN
