PSIP1_MOUSE
ID PSIP1_MOUSE Reviewed; 528 AA.
AC Q99JF8; A2BI10; A2BI11; Q3TEJ7; Q3TTD7; Q3UTA1; Q80WQ7; Q99JF7; Q99LR4;
AC Q9CT03;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=PC4 and SFRS1-interacting protein;
DE AltName: Full=Lens epithelium-derived growth factor;
DE Short=mLEDGF;
GN Name=Psip1; Synonyms=Ledgf;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Testis;
RA Bashein A.M., Brady G.;
RL Thesis (2000), University of Manchester, United Kingdom.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RA Yu L.;
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and Czech II; TISSUE=Brain, Limb, and Mammary gland;
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 [LARGE SCALE MRNA] OF 1-248.
RC STRAIN=C57BL/6J, and NOD; TISSUE=Egg, Embryo, Testis, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106; SER-176; SER-272 AND
RP SER-274, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106; SER-176; SER-272 AND
RP SER-274, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105; SER-106; THR-115;
RP THR-122; SER-129; THR-141; SER-176; SER-270; THR-271; SER-272; SER-274 AND
RP SER-520, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP CITRULLINATION AT ARG-515.
RX PubMed=24463520; DOI=10.1038/nature12942;
RA Christophorou M.A., Castelo-Branco G., Halley-Stott R.P., Oliveira C.S.,
RA Loos R., Radzisheuskaya A., Mowen K.A., Bertone P., Silva J.C.,
RA Zernicka-Goetz M., Nielsen M.L., Gurdon J.B., Kouzarides T.;
RT "Citrullination regulates pluripotency and histone H1 binding to
RT chromatin.";
RL Nature 507:104-108(2014).
CC -!- FUNCTION: Transcriptional coactivator involved in neuroepithelial stem
CC cell differentiation and neurogenesis. Involved in particular in lens
CC epithelial cell gene regulation and stress responses. May play an
CC important role in lens epithelial to fiber cell terminal
CC differentiation. May play a protective role during stress-induced
CC apoptosis (By similarity). {ECO:0000250|UniProtKB:O75475}.
CC -!- SUBUNIT: Monomer (By similarity). Interacts with IFRD1/PC4 (By
CC similarity). Interacts (via IBD domain) with POGZ (via IBM motif) and
CC CDCA7L (via IBM motifs) (By similarity). Interacts (via IBD domain)
CC with KMT2A (via IBM motifs) with a moderate affinity whereas interacts
CC with the KMT2A-MEN1 complex with a greater affinity; MEN1 enhances
CC interaction of KMT2A with PSIP1 (By similarity). Interacts (via IBD
CC domain) with IWS1 (via IBM motif), MED1 (via IBM motif) and DBF4 (via
CC IBM motifs) (By similarity). {ECO:0000250|UniProtKB:O75475}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O75475}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Ledgfa, p75;
CC IsoId=Q99JF8-1; Sequence=Displayed;
CC Name=2; Synonyms=Ledgfb, p52;
CC IsoId=Q99JF8-2; Sequence=VSP_014299, VSP_014300;
CC -!- PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}.
CC -!- SIMILARITY: Belongs to the HDGF family. {ECO:0000305}.
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DR EMBL; AJ308965; CAC34944.1; -; mRNA.
DR EMBL; AJ308966; CAC34945.1; -; mRNA.
DR EMBL; AF339082; AAO32949.1; -; mRNA.
DR EMBL; AF339083; AAO32950.1; -; mRNA.
DR EMBL; BX682545; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002260; AAH02260.1; -; mRNA.
DR EMBL; BC043079; AAH43079.1; -; mRNA.
DR EMBL; BC052177; AAH52177.1; -; mRNA.
DR EMBL; AK011572; BAB27707.3; -; mRNA.
DR EMBL; AK139598; BAE24079.1; -; mRNA.
DR EMBL; AK161426; BAE36388.1; -; mRNA.
DR EMBL; AK169600; BAE41251.1; -; mRNA.
DR CCDS; CCDS18299.1; -. [Q99JF8-1]
DR CCDS; CCDS71412.1; -. [Q99JF8-2]
DR RefSeq; NP_001277456.1; NM_001290527.1. [Q99JF8-2]
DR RefSeq; NP_598709.1; NM_133948.5. [Q99JF8-1]
DR AlphaFoldDB; Q99JF8; -.
DR BMRB; Q99JF8; -.
DR SMR; Q99JF8; -.
DR BioGRID; 221716; 13.
DR IntAct; Q99JF8; 3.
DR MINT; Q99JF8; -.
DR STRING; 10090.ENSMUSP00000030207; -.
DR iPTMnet; Q99JF8; -.
DR PhosphoSitePlus; Q99JF8; -.
DR EPD; Q99JF8; -.
DR jPOST; Q99JF8; -.
DR MaxQB; Q99JF8; -.
DR PaxDb; Q99JF8; -.
DR PeptideAtlas; Q99JF8; -.
DR PRIDE; Q99JF8; -.
DR ProteomicsDB; 301987; -. [Q99JF8-1]
DR ProteomicsDB; 301988; -. [Q99JF8-2]
DR Antibodypedia; 4436; 239 antibodies from 32 providers.
DR DNASU; 101739; -.
DR Ensembl; ENSMUST00000030207; ENSMUSP00000030207; ENSMUSG00000028484. [Q99JF8-1]
DR Ensembl; ENSMUST00000107215; ENSMUSP00000102833; ENSMUSG00000028484. [Q99JF8-2]
DR GeneID; 101739; -.
DR KEGG; mmu:101739; -.
DR UCSC; uc008tkw.2; mouse. [Q99JF8-1]
DR UCSC; uc008tkx.2; mouse. [Q99JF8-2]
DR CTD; 11168; -.
DR MGI; MGI:2142116; Psip1.
DR VEuPathDB; HostDB:ENSMUSG00000028484; -.
DR eggNOG; KOG1904; Eukaryota.
DR GeneTree; ENSGT00940000154706; -.
DR HOGENOM; CLU_034054_1_0_1; -.
DR InParanoid; Q99JF8; -.
DR OMA; NLRVGMN; -.
DR OrthoDB; 530959at2759; -.
DR PhylomeDB; Q99JF8; -.
DR TreeFam; TF105385; -.
DR BioGRID-ORCS; 101739; 4 hits in 77 CRISPR screens.
DR ChiTaRS; Psip1; mouse.
DR PRO; PR:Q99JF8; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q99JF8; protein.
DR Bgee; ENSMUSG00000028484; Expressed in embryonic post-anal tail and 268 other tissues.
DR ExpressionAtlas; Q99JF8; baseline and differential.
DR Genevisible; Q99JF8; MM.
DR GO; GO:0000791; C:euchromatin; ISS:UniProtKB.
DR GO; GO:0000792; C:heterochromatin; ISS:UniProtKB.
DR GO; GO:0034399; C:nuclear periphery; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISS:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0097100; F:supercoiled DNA binding; ISS:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0000395; P:mRNA 5'-splice site recognition; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0009408; P:response to heat; IDA:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IDA:UniProtKB.
DR CDD; cd05834; HDGF_related; 1.
DR Gene3D; 1.20.930.10; -; 1.
DR InterPro; IPR035496; HDGF-rel_PWWP.
DR InterPro; IPR036218; HIVI-bd_sf.
DR InterPro; IPR021567; LEDGF_IBD.
DR InterPro; IPR000313; PWWP_dom.
DR InterPro; IPR035441; TFIIS/LEDGF_dom_sf.
DR Pfam; PF11467; LEDGF; 1.
DR Pfam; PF00855; PWWP; 1.
DR SMART; SM00293; PWWP; 1.
DR SUPFAM; SSF140576; SSF140576; 1.
DR PROSITE; PS50812; PWWP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Citrullination; Coiled coil; DNA-binding;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..528
FT /note="PC4 and SFRS1-interacting protein"
FT /id="PRO_0000191709"
FT DOMAIN 7..64
FT /note="PWWP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT REGION 61..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..415
FT /note="Integrase-binding domain (IBD)"
FT /evidence="ECO:0000250|UniProtKB:O75475"
FT REGION 444..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 306..332
FT /evidence="ECO:0000255"
FT COILED 369..393
FT /evidence="ECO:0000255"
FT MOTIF 146..156
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:O75475"
FT COMPBIAS 61..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..471
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..528
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q812D1"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 115
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 122
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 141
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75475"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 271
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75475"
FT MOD_RES 435
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75475"
FT MOD_RES 441
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75475"
FT MOD_RES 515
FT /note="Citrulline"
FT /evidence="ECO:0000269|PubMed:24463520"
FT MOD_RES 520
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 525
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75475"
FT CROSSLNK 75
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75475"
FT VAR_SEQ 324..331
FT /note="QQNKDEGK -> HQTTCNLQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1,
FT ECO:0000303|Ref.2"
FT /id="VSP_014299"
FT VAR_SEQ 332..528
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1,
FT ECO:0000303|Ref.2"
FT /id="VSP_014300"
FT CONFLICT Q99JF8-2:324..331
FT /note="HQTTCNLQ -> QLKALIQ (in Ref. 4; AAH52177)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 528 AA; 59697 MW; 4A9AE28245843AB6 CRC64;
MTRDFKPGDL IFAKMKGYPH WPARVDEVPD GAVKPPTNKL PIFFFGTHET AFLGPKDIFP
YSENKEKYGK PNKRKGFNEG LWEIDNNPKV KFSSQQASTK QSNASSDVEV EEKETNVSKE
DTDQEEKASN EDVTKAVDIT TPKAARRGRK RKAEKQVDTE EAGMVTAATA SNVKASPKRG
RPAATEVKIP KPRGRPKVVK QPCPSDGDMV IDEDKSKKKG PEEKQPKKQL KKEEEGQKEE
EKPRKEPDKK EGKKEVESKR KNLAKPGVTS TSDSEDEDDQ EGEKKRKGGR NFQAAHRRNM
LKGQHEKEAG DRKRKQEEQM ETEQQNKDEG KKPEVKKVEK KRETSMDSRL QRIHAEIKNS
LKIDNLDVNR CIEALDELAS LQVTMQQAQK HTEMITTLKK IRRFKVSQVI MEKSTMLYNK
FKNMFLVGEG DSVITQVLNK SLAEQRQHEE ANKTKDQGKK GPNKKLEKEP TGTKSLNGGS
DAQESNHPQH NGDSNEDGKD SREASSKTKP PGEEREAEIS LKESTLDN
