ICE2_HUMAN
ID ICE2_HUMAN Reviewed; 982 AA.
AC Q659A1; B2RU08; Q05CT1; Q3B7W6; Q63HP4; Q658Q0; Q68CN8; Q6IPW7; Q6UX23;
AC Q71H65; Q96CY5; Q9HAA2;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Little elongation complex subunit 2;
DE AltName: Full=Interactor of little elongator complex ELL subunit 2;
DE AltName: Full=NMDA receptor-regulated protein 2;
GN Name=ICE2; Synonyms=BRCC1, NARG2; ORFNames=UNQ3101/PRO10100;
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).
RC TISSUE=Mammary cancer;
RA Gokhale P.C., Dritschilo A., Rahman A., Ahmad I., Kasid U.N.;
RT "Novel transcript in human breast cancer cells.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryo, and Kidney;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Adipose tissue, Bone marrow, Fetal kidney, and Heart;
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 [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone, Brain, Ovary, and 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 [7]
RP IDENTIFICATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15606750; DOI=10.1111/j.1432-1033.2004.04414.x;
RA Sugiura N., Dadashev V., Corriveau R.A.;
RT "NARG2 encodes a novel nuclear protein with (S/T)PXX motifs that is
RT expressed during development.";
RL Eur. J. Biochem. 271:4629-4637(2004).
RN [8]
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP IDENTIFICATION IN THE LEC COMPLEX, AND INTERACTION WITH ELL.
RX PubMed=22195968; DOI=10.1016/j.molcel.2011.12.008;
RA Smith E.R., Lin C., Garrett A.S., Thornton J., Mohaghegh N., Hu D.,
RA Jackson J., Saraf A., Swanson S.K., Seidel C., Florens L., Washburn M.P.,
RA Eissenberg J.C., Shilatifard A.;
RT "The little elongation complex regulates small nuclear RNA transcription.";
RL Mol. Cell 44:954-965(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-326, 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 [13]
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE LEC COMPLEX, AND
RP INTERACTION WITH ICE1.
RX PubMed=23932780; DOI=10.1016/j.molcel.2013.07.003;
RA Hu D., Smith E.R., Garruss A.S., Mohaghegh N., Varberg J.M., Lin C.,
RA Jackson J., Gao X., Saraf A., Florens L., Washburn M.P., Eissenberg J.C.,
RA Shilatifard A.;
RT "The little elongation complex functions at initiation and elongation
RT phases of snRNA gene transcription.";
RL Mol. Cell 51:493-505(2013).
RN [14]
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).
CC -!- FUNCTION: Component of the little elongation complex (LEC), a complex
CC required to regulate small nuclear RNA (snRNA) gene transcription by
CC RNA polymerase II and III. {ECO:0000269|PubMed:23932780}.
CC -!- SUBUNIT: Component of the little elongation complex (LEC), at least
CC composed of ELL (ELL, ELL2 or ELL3), ZC3H8, ICE1 and ICE2. Interacts
CC with ICE1 (via C-terminus domain). Interacts with ELL.
CC {ECO:0000269|PubMed:22195968, ECO:0000269|PubMed:23932780}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23932780}.
CC Note=Colocalizes with COIL in subnuclear Cajal and histone locus
CC bodies. Translocates in the LEC complex to Cajal and histone locus
CC bodies at snRNA genes in a ICE1-dependent manner. Associates to
CC transcriptionally active chromatin at snRNA genes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q659A1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q659A1-2; Sequence=VSP_041612, VSP_041613;
CC -!- TISSUE SPECIFICITY: Expressed at low levels in lung and testis.
CC {ECO:0000269|PubMed:15606750}.
CC -!- DEVELOPMENTAL STAGE: Expressed in fetal brain, kidney, liver and lung.
CC {ECO:0000269|PubMed:15606750}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ICE2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH13684.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH20918.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAI07428.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC Sequence=AAQ88910.1; Type=Miscellaneous discrepancy; Note=Unlikely isoform. Aberrant splice sites.; Evidence={ECO:0000305};
CC Sequence=BAB13948.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAH18700.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
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DR EMBL; AF502591; AAQ07460.1; -; mRNA.
DR EMBL; AY358546; AAQ88910.1; ALT_SEQ; mRNA.
DR EMBL; CR749852; CAH18700.1; ALT_SEQ; mRNA.
DR EMBL; BX647873; CAH56197.1; -; mRNA.
DR EMBL; AK021958; BAB13948.1; ALT_INIT; mRNA.
DR EMBL; AK055752; BAG51567.1; -; mRNA.
DR EMBL; AL833122; CAH56202.1; -; mRNA.
DR EMBL; AL832046; CAH56220.1; -; mRNA.
DR EMBL; CH471082; EAW77589.1; -; Genomic_DNA.
DR EMBL; BC013684; AAH13684.1; ALT_INIT; mRNA.
DR EMBL; BC020918; AAH20918.1; ALT_SEQ; mRNA.
DR EMBL; BC071685; AAH71685.1; -; mRNA.
DR EMBL; BC107427; AAI07428.1; ALT_SEQ; mRNA.
DR EMBL; BC140894; AAI40895.1; -; mRNA.
DR CCDS; CCDS10176.1; -. [Q659A1-1]
DR RefSeq; NP_001018099.1; NM_001018089.2.
DR RefSeq; NP_078887.2; NM_024611.5. [Q659A1-1]
DR RefSeq; XP_005254718.1; XM_005254661.1. [Q659A1-1]
DR RefSeq; XP_011520311.1; XM_011522009.1. [Q659A1-1]
DR RefSeq; XP_016878058.1; XM_017022569.1. [Q659A1-1]
DR AlphaFoldDB; Q659A1; -.
DR BioGRID; 122789; 73.
DR IntAct; Q659A1; 35.
DR STRING; 9606.ENSP00000261520; -.
DR iPTMnet; Q659A1; -.
DR PhosphoSitePlus; Q659A1; -.
DR BioMuta; ICE2; -.
DR DMDM; 156632596; -.
DR EPD; Q659A1; -.
DR jPOST; Q659A1; -.
DR MassIVE; Q659A1; -.
DR MaxQB; Q659A1; -.
DR PaxDb; Q659A1; -.
DR PeptideAtlas; Q659A1; -.
DR PRIDE; Q659A1; -.
DR ProteomicsDB; 65932; -. [Q659A1-1]
DR ProteomicsDB; 65933; -. [Q659A1-2]
DR Antibodypedia; 25471; 125 antibodies from 20 providers.
DR DNASU; 79664; -.
DR Ensembl; ENST00000261520.9; ENSP00000261520.4; ENSG00000128915.12. [Q659A1-1]
DR Ensembl; ENST00000558181.5; ENSP00000453593.1; ENSG00000128915.12. [Q659A1-2]
DR Ensembl; ENST00000560668.5; ENSP00000453303.1; ENSG00000128915.12. [Q659A1-2]
DR GeneID; 79664; -.
DR KEGG; hsa:79664; -.
DR MANE-Select; ENST00000261520.9; ENSP00000261520.4; NM_024611.6; NP_078887.2.
DR UCSC; uc002agp.5; human. [Q659A1-1]
DR CTD; 79664; -.
DR DisGeNET; 79664; -.
DR GeneCards; ICE2; -.
DR HGNC; HGNC:29885; ICE2.
DR HPA; ENSG00000128915; Tissue enhanced (parathyroid).
DR MIM; 610835; gene.
DR neXtProt; NX_Q659A1; -.
DR OpenTargets; ENSG00000128915; -.
DR PharmGKB; PA134960292; -.
DR VEuPathDB; HostDB:ENSG00000128915; -.
DR eggNOG; ENOG502QUWA; Eukaryota.
DR GeneTree; ENSGT00390000006883; -.
DR HOGENOM; CLU_327237_0_0_1; -.
DR InParanoid; Q659A1; -.
DR OMA; FHEIPMD; -.
DR PhylomeDB; Q659A1; -.
DR TreeFam; TF106272; -.
DR PathwayCommons; Q659A1; -.
DR Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
DR SignaLink; Q659A1; -.
DR SIGNOR; Q659A1; -.
DR BioGRID-ORCS; 79664; 347 hits in 1081 CRISPR screens.
DR ChiTaRS; ICE2; human.
DR GenomeRNAi; 79664; -.
DR Pharos; Q659A1; Tbio.
DR PRO; PR:Q659A1; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q659A1; protein.
DR Bgee; ENSG00000128915; Expressed in colonic epithelium and 187 other tissues.
DR ExpressionAtlas; Q659A1; baseline and differential.
DR Genevisible; Q659A1; HS.
DR GO; GO:0015030; C:Cajal body; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0000791; C:euchromatin; IDA:UniProtKB.
DR GO; GO:0035363; C:histone locus body; IDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0008023; C:transcription elongation factor complex; IDA:UniProtKB.
DR GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; IMP:UniProtKB.
DR GO; GO:0042795; P:snRNA transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0042796; P:snRNA transcription by RNA polymerase III; IMP:UniProtKB.
DR InterPro; IPR019535; ICE2_C.
DR Pfam; PF10505; NARG2_C; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..982
FT /note="Little elongation complex subunit 2"
FT /id="PRO_0000297964"
FT REGION 410..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 930..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..493
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..968
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 571
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UZ18"
FT MOD_RES 573
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q3UZ18"
FT VAR_SEQ 50..73
FT /note="RIGENLNASASSVENEPAVSSATQ -> ESRGVMWTCWLNTQRFLQIPKLLE
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_041612"
FT VAR_SEQ 74..982
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_041613"
FT CONFLICT 272
FT /note="L -> P (in Ref. 4; CAH18700)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="S -> L (in Ref. 4; CAH18700)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="T -> P (in Ref. 4; CAH56220)"
FT /evidence="ECO:0000305"
FT CONFLICT 621
FT /note="T -> S (in Ref. 4; CAH56220)"
FT /evidence="ECO:0000305"
FT CONFLICT 753
FT /note="T -> A (in Ref. 4; CAH18700)"
FT /evidence="ECO:0000305"
FT CONFLICT 906
FT /note="W -> R (in Ref. 3; BAB13948)"
FT /evidence="ECO:0000305"
FT CONFLICT 947
FT /note="P -> S (in Ref. 4; CAH56197)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 982 AA; 110011 MW; 09B36E742FC77597 CRC64;
MSSKMVISEP GLNWDISPKN GLKTFFSREN YKDHSMAPSL KELRVLSNRR IGENLNASAS
SVENEPAVSS ATQAKEKVKT TIGMVLLPKP RVPYPRFSRF SQREQRSYVD LLVKYAKIPA
NSKAVGINKN DYLQYLDMKK HVNEEVTEFL KFLQNSAKKC AQDYNMLSDD ARLFTEKILR
ACIEQVKKYS EFYTLHEVTS LMGFFPFRVE MGLKLEKTLL ALGSVKYVKT VFPSMPIKLQ
LSKDDIATIE TSEQTAEAMH YDISKDPNAE KLVSRYHPQI ALTSQSLFTL LNNHGPTYKE
QWEIPVCIQV IPVAGSKPVK VIYINSPLPQ KKMTMRERNQ IFHEVPLKFM MSKNTSVPVS
AVFMDKPEEF ISEMDMSCEV NECRKIESLE NLYLDFDDDV TELETFGVTT TKVSKSPSPA
STSTVPNMTD APTAPKAGTT TVAPSAPDIS ANSRSLSQIL MEQLQKEKQL VTGMDGGPEE
CKNKDDQGFE SCEKVSNSDK PLIQDSDLKT SDALQLENSQ EIETSNKNDM TIDILHADGE
RPNVLENLDN SKEKTVGSEA AKTEDTVLCS SDTDEECLII DTECKNNSDG KTAVVGSNLS
SRPASPNSSS GQASVGNQTN TACSPEESCV LKKPIKRVYK KFDPVGEILK MQDELLKPIS
RKVPELPLMN LENSKQPSVS EQLSGPSDSS SWPKSGWPSA FQKPKGRLPY ELQDYVEDTS
EYLAPQEGNF VYKLFSLQDL LLLVRCSVQR IETRPRSKKR KKIRRQFPVY VLPKVEYQAC
YGVEALTESE LCRLWTESLL HSNSSFYVGH IDAFTSKLFL LEEITSEELK EKLSALKISN
LFNILQHILK KLSSLQEGSY LLSHAAEDSS LLIYKASDGK VTRTAYNLYK THCGLPGVPS
SLSVPWVPLD PSLLLPYHIH HGRIPCTFPP KSLDTTTQQK IGGTRMPTRS HRNPVSMETK
SSCLPAQQVE TEGVAPHKRK IT
