ELP1_MOUSE
ID ELP1_MOUSE Reviewed; 1333 AA.
AC Q7TT37; Q3UHY6; Q7TQH1; Q8C6B3; Q8CBI3; Q8CH82; Q8VHU5; Q8VHV9; Q9CT81;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Elongator complex protein 1;
DE Short=ELP1;
DE AltName: Full=IkappaB kinase complex-associated protein;
DE Short=IKK complex-associated protein;
GN Name=Elp1; Synonyms=Ikap, Ikbkap;
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], DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ;
RX PubMed=11747609; DOI=10.1089/104454901317094990;
RA Cuajungco M.P., Leyne M., Mull J., Gill S.P., Gusella J.F.,
RA Slaugenhaupt S.A.;
RT "Cloning, characterization, and genomic structure of the mouse Ikbkap
RT gene.";
RL DNA Cell Biol. 20:579-586(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=129/SvJ; TISSUE=Spleen;
RX PubMed=11722848; DOI=10.1016/s0378-1119(01)00737-5;
RA Coli R., Anderson S.L., Volpi S.A., Rubin B.Y.;
RT "Genomic organization and chromosomal localization of the mouse IKBKAP
RT gene.";
RL Gene 279:81-89(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6 X CBA;
RA Shirane M., Hatakeyama S., Nakayama K.;
RT "Molecular cloning and biochemical analysis of murine IKAP.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Head;
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Eye;
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 [7]
RP FUNCTION IN NEUROGENESIS, AND SUBCELLULAR LOCATION.
RX PubMed=19185337; DOI=10.1016/j.cell.2008.11.043;
RA Creppe C., Malinouskaya L., Volvert M.L., Gillard M., Close P., Malaise O.,
RA Laguesse S., Cornez I., Rahmouni S., Ormenese S., Belachew S.,
RA Malgrange B., Chapelle J.P., Siebenlist U., Moonen G., Chariot A.,
RA Nguyen L.;
RT "Elongator controls the migration and differentiation of cortical neurons
RT through acetylation of alpha-tubulin.";
RL Cell 136:551-564(2009).
RN [8]
RP 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 [9]
RP FUNCTION.
RX PubMed=22854966; DOI=10.1074/jbc.m112.402727;
RA Close P., Gillard M., Ladang A., Jiang Z., Papuga J., Hawkes N., Nguyen L.,
RA Chapelle J.P., Bouillenne F., Svejstrup J., Fillet M., Chariot A.;
RT "DERP6 (ELP5) and C3ORF75 (ELP6) regulate tumorigenicity and migration of
RT melanoma cells as subunits of Elongator.";
RL J. Biol. Chem. 287:32535-32545(2012).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=23717213; DOI=10.1371/journal.pgen.1003516;
RA Lin F.J., Shen L., Jang C.W., Falnes P.O., Zhang Y.;
RT "Ikbkap/Elp1 deficiency causes male infertility by disrupting meiotic
RT progression.";
RL PLoS Genet. 9:e1003516-e1003516(2013).
RN [11]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=31827135; DOI=10.1038/s41598-019-55090-1;
RA Yang K.T., Inoue A., Lee Y.J., Jiang C.L., Lin F.J.;
RT "Loss of Ikbkap/Elp1 in mouse oocytes causes spindle disorganization,
RT developmental defects in preimplantation embryos and impaired female
RT fertility.";
RL Sci. Rep. 9:18875-18875(2019).
CC -!- FUNCTION: Component of the elongator complex which is required for
CC multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl
CC uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U
CC (5-carbamoylmethyl uridine) (By similarity). The elongator complex
CC catalyzes the formation of carboxymethyluridine in the wobble base at
CC position 34 in tRNAs (PubMed:23717213). Regulates the migration and
CC branching of projection neurons in the developing cerebral cortex,
CC through a process depending on alpha-tubulin acetylation
CC (PubMed:22854966). ELP1 binds to tRNA, mediating interaction of the
CC elongator complex with tRNA (By similarity). May act as a scaffold
CC protein that assembles active IKK-MAP3K14 complexes (IKKA, IKKB and
CC MAP3K14/NIK) (By similarity). {ECO:0000250|UniProtKB:O95163,
CC ECO:0000250|UniProtKB:Q06706, ECO:0000269|PubMed:22854966}.
CC -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC biosynthesis. {ECO:0000250|UniProtKB:O95163}.
CC -!- SUBUNIT: Homodimer; dimerization promotes ELP1 stability and elongator
CC complex formation. Component of the elongator complex which consists of
CC ELP1, ELP2, ELP3, ELP4, ELP5 and ELP6. Interacts preferentially with
CC MAP3K14/NIK followed by IKK-alpha and IKK-beta.
CC {ECO:0000250|UniProtKB:O95163}.
CC -!- INTERACTION:
CC Q7TT37; P23242: Gja1; NbExp=3; IntAct=EBI-8418161, EBI-298630;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19185337,
CC ECO:0000269|PubMed:23717213, ECO:0000269|PubMed:31827135}. Nucleus
CC {ECO:0000250|UniProtKB:O95163}.
CC -!- TISSUE SPECIFICITY: In the testis, expression is restricted to germ
CC cells during spermatogenesis with no expression detected in somatic
CC cells such as Sertoli cells or Leydig cells (at protein level)
CC (PubMed:23717213). In the ovary, expressed in oocytes of primary,
CC secondary and antral follicles (at protein level) (PubMed:31827135).
CC Widely expressed in adult tissues with highest levels in brain and also
CC expressed at all embryonic stages (PubMed:11747609).
CC {ECO:0000269|PubMed:11747609, ECO:0000269|PubMed:23717213,
CC ECO:0000269|PubMed:31827135}.
CC -!- DEVELOPMENTAL STAGE: During spermatogenesis, expressed in the testis in
CC all male germ cell stages except elongated spermatids (at protein
CC level) (PubMed:23717213). Highly expressed in fully-grown germinal
CC vesicle oocytes and modest expression throughout the preimplantation
CC stage with a slight down-regulation at the 2-cell stage
CC (PubMed:31827135). In the embryo, expressed at embryonic days 7, 11, 15
CC and 17 with the highest expression at embryonic day 11
CC (PubMed:11747609). {ECO:0000269|PubMed:11747609,
CC ECO:0000269|PubMed:23717213, ECO:0000269|PubMed:31827135}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Conditional knockout in male germ cells results
CC in defects in wobble uridine tRNA modification and defects in synapsis
CC and meiotic recombination which result in increased apoptosis and
CC complete arrest of gametogenesis, leading to male infertility
CC (PubMed:23717213). Conditional knockout in female germ cells results in
CC female subfertility with reduced litter size although ovaries are
CC morphologically and histologically indistinguishable from those of
CC controls (PubMed:31827135). Oocytes show aneuploidy, reduced alpha-
CC tubulin acetylation and are unable to complete meiosis with defects in
CC meiotic spindle organization, chromosome alignment and kinetochore
CC function (PubMed:31827135). Embryos derived from Elp1-deficient oocytes
CC exhibit digyny, progressive delays in preimplantation development and
CC severe degeneration before reaching the blastocyst stage
CC (PubMed:31827135). {ECO:0000269|PubMed:23717213,
CC ECO:0000269|PubMed:31827135}.
CC -!- SIMILARITY: Belongs to the ELP1/IKA1 family. {ECO:0000305}.
CC -!- CAUTION: The elongator complex was originally thought to play a role in
CC transcription elongation. However, it is no longer thought to play a
CC direct role in this process and its primary function is thought to be
CC in tRNA modification. {ECO:0000250|UniProtKB:O95163}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL36025.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAO15309.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF367244; AAL36025.1; ALT_FRAME; mRNA.
DR EMBL; AF387811; AAL40925.1; -; mRNA.
DR EMBL; AF140786; AAO15309.1; ALT_FRAME; mRNA.
DR EMBL; AK004402; BAB23291.1; -; mRNA.
DR EMBL; AK076152; BAC36221.1; -; mRNA.
DR EMBL; AK035944; BAC29252.1; -; mRNA.
DR EMBL; AK147153; BAE27720.1; -; mRNA.
DR EMBL; AL807762; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL929577; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC052387; AAH52387.2; -; mRNA.
DR EMBL; BC054468; AAH54468.1; -; mRNA.
DR CCDS; CCDS38765.1; -.
DR RefSeq; NP_080355.2; NM_026079.3.
DR AlphaFoldDB; Q7TT37; -.
DR SMR; Q7TT37; -.
DR BioGRID; 230947; 7.
DR IntAct; Q7TT37; 4.
DR MINT; Q7TT37; -.
DR STRING; 10090.ENSMUSP00000030140; -.
DR iPTMnet; Q7TT37; -.
DR PhosphoSitePlus; Q7TT37; -.
DR EPD; Q7TT37; -.
DR MaxQB; Q7TT37; -.
DR PaxDb; Q7TT37; -.
DR PeptideAtlas; Q7TT37; -.
DR PRIDE; Q7TT37; -.
DR ProteomicsDB; 277853; -.
DR Antibodypedia; 14913; 273 antibodies from 32 providers.
DR DNASU; 230233; -.
DR Ensembl; ENSMUST00000030140; ENSMUSP00000030140; ENSMUSG00000028431.
DR GeneID; 230233; -.
DR KEGG; mmu:230233; -.
DR UCSC; uc012del.1; mouse.
DR CTD; 8518; -.
DR MGI; MGI:1914544; Elp1.
DR VEuPathDB; HostDB:ENSMUSG00000028431; -.
DR eggNOG; KOG1920; Eukaryota.
DR GeneTree; ENSGT00390000013344; -.
DR HOGENOM; CLU_001477_1_0_1; -.
DR InParanoid; Q7TT37; -.
DR OMA; DMNILHD; -.
DR OrthoDB; 180136at2759; -.
DR PhylomeDB; Q7TT37; -.
DR TreeFam; TF300402; -.
DR UniPathway; UPA00988; -.
DR BioGRID-ORCS; 230233; 25 hits in 76 CRISPR screens.
DR ChiTaRS; Epb41; mouse.
DR PRO; PR:Q7TT37; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q7TT37; protein.
DR Bgee; ENSMUSG00000028431; Expressed in pharyngeal arch 2 and 249 other tissues.
DR Genevisible; Q7TT37; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0033588; C:elongator holoenzyme complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0004672; F:protein kinase activity; ISO:MGI.
DR GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR GO; GO:0007252; P:I-kappaB phosphorylation; ISO:MGI.
DR GO; GO:0002926; P:tRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation; IBA:GO_Central.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IMP:UniProtKB.
DR InterPro; IPR006849; Elp1.
DR PANTHER; PTHR12747; PTHR12747; 1.
DR Pfam; PF04762; IKI3; 1.
DR PIRSF; PIRSF017233; IKAP; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; tRNA processing.
FT CHAIN 1..1333
FT /note="Elongator complex protein 1"
FT /id="PRO_0000283995"
FT REGION 886..1333
FT /note="Mediates dimerization"
FT /evidence="ECO:0000250|UniProtKB:O95163"
FT REGION 1175..1209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1192..1210
FT /note="Required for binding to tRNA"
FT /evidence="ECO:0000250|UniProtKB:Q06706"
FT COMPBIAS 1175..1191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 805
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95163"
FT MOD_RES 1172
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95163"
FT MOD_RES 1175
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95163"
FT CONFLICT 42
FT /note="T -> P (in Ref. 3; AAO15309)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="D -> G (in Ref. 4; BAE27720)"
FT /evidence="ECO:0000305"
FT CONFLICT 215..216
FT /note="QT -> HS (in Ref. 3; AAO15309)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="I -> V (in Ref. 2; AAL40925)"
FT /evidence="ECO:0000305"
FT CONFLICT 346
FT /note="I -> V (in Ref. 2; AAL40925 and 3; AAO15309)"
FT /evidence="ECO:0000305"
FT CONFLICT 582
FT /note="Y -> I (in Ref. 1; AAL36025)"
FT /evidence="ECO:0000305"
FT CONFLICT 634..635
FT /note="ND -> LV (in Ref. 1; AAL36025)"
FT /evidence="ECO:0000305"
FT CONFLICT 649
FT /note="D -> A (in Ref. 2; AAL40925)"
FT /evidence="ECO:0000305"
FT CONFLICT 663
FT /note="V -> G (in Ref. 1; AAL36025, 2; AAL40925 and 3;
FT AAO15309)"
FT /evidence="ECO:0000305"
FT CONFLICT 693..694
FT /note="ER -> VW (in Ref. 1; AAL36025)"
FT /evidence="ECO:0000305"
FT CONFLICT 773
FT /note="K -> F (in Ref. 1; AAL36025)"
FT /evidence="ECO:0000305"
FT CONFLICT 1110
FT /note="V -> I (in Ref. 1; AAL36025, 2; AAL40925 and 3;
FT AAO15309)"
FT /evidence="ECO:0000305"
FT CONFLICT 1159
FT /note="A -> G (in Ref. 4; BAB23291)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1333 AA; 149584 MW; C40E0098DD4DF63C CRC64;
MRNLKLHRTL EFRDIQAPGK PQCFCLRAEQ GTVLIGSERG LTEVDPVRRE VKTEISLVAE
GFLPEDGSGC IVGIQDLLDQ ESVCVATASG DVIVCNLSTQ QLECVGSVAS GISVMSWSPD
QELLLLATAQ QTLIMMTKDF EVIAEEQIHQ DDFGEGKFVT VGWGSKQTQF HGSEGRPTAF
PVQLPENALP WDDRRPHITW RGDGQYFAVS VVCRQTEARK IRVWNREFAL QSTSESVPGL
GPALAWKPSG SLIASTQDKP NQQDVVFFEK NGLLHGHFTL PFLKDEVKVN DLLWNADSSV
LAIWLEDLPK EDSSTLKSYV QLWTVGNYHW YLKQSLPFST TGKNQIVSLL WDPVTPCRLH
VLCTGWRYLC CDWHWTTDRS SGNSANDLAN VAVIDGNRVL VTVFRQTVVP PPMCTYRLLI
PHPVNQVIFS AHLGNDLAVL DASNQISVYK CGDKPNMDST VKLGAVGGNG FKVPLTTPHL
EKRYSIQFGN NEEEEEEEVN ALQLSFLTWV EDDTFLAISY SHSSSQSIIH HLTVTHSEVD
EEQGQLDVSS SVTVDGVVIG LCCCSKTKSL AVQLADGQVL KYLWESPSLA VEPWKNSEGI
PVRFVHPCTQ MEVATIGGEE CVLGLTDRCR FFINDTEVAS NITSFAVCDD FLLVTTHSHT
CQVFSLSGAS LKMLQAALSG SHEASGEILR KVERGSRIVT VVPQDTKLIL QMPRGNLEVV
HHRALVLAQI RKWLDKLMFK EAFECMRKLR INLNLIHDHN PKVFLENVET FVKQIDSVNH
INLFFTELRE EDVTKTMYPP PITKSVQVST HPDGKKLDLI CDAMRAAMEA INPRKFCLSI
LTSHVKKTTP ELEIVLQKVQ ELQGNLPFDP ESVSVEEALK YLLLLVDVNE LFNHSLGTYD
FNLVLMVAEK SQKDPKEYLP FLNTLKKMET NYQRFTIDKY LKRYEKALGH LSKCGPEYFT
ECLNLIKDKN LYKEALKLYR PDSPQYQAVS MAYGEHLMQE HLYEPAGLVF ARCGAQEKAL
EAFLACGSWQ QALCVAAQLQ MSKDKVAGLA RTLAGKLVEQ RKHSEAATVL EQYAQDYEEA
VLLLLEGSAW EEALRLVYKY DRVDIIETSV KPSILEAQKN YMDFLDSETA TFIRHKNRLQ
VVRALRRQAP QVHVDHEVAH GPESDLFSET SSIMSGSEMS GRYSHSNSRI SARSSKNRRK
AERKKHSLKE GSPLEGLALL EALSEVVQSV EKLKDEVRAI LKVLFLFEFE EQAKELQRAF
ESTLQLMERA VPEIWTPAGQ QSSTTPVLGP SSTANSITAS YQQQKTCVPA LDAGVYMPPK
MDPRSQWKLS LLE
