ELL_HUMAN
ID ELL_HUMAN Reviewed; 621 AA.
AC P55199;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=RNA polymerase II elongation factor ELL;
DE AltName: Full=Eleven-nineteen lysine-rich leukemia protein;
GN Name=ELL; Synonyms=C19orf17;
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], AND CHROMOSOMAL TRANSLOCATION.
RC TISSUE=Fetal brain;
RX PubMed=7991593; DOI=10.1073/pnas.91.25.12110;
RA Thirman M.J., Levitan D.A., Kobayashi H., Simon M.C., Rowley J.D.;
RT "Cloning of ELL, a gene that fuses to MLL in a t(11;19)(q23;p13.1) in acute
RT myeloid leukemia.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:12110-12114(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [3]
RP FUNCTION IN TRANSCRIPTION ELONGATION.
RX PubMed=8596958; DOI=10.1126/science.271.5257.1873;
RA Shilatifard A., Lane W.S., Jackson K.W., Conaway R.C., Conaway J.W.;
RT "An RNA polymerase II elongation factor encoded by the human ELL gene.";
RL Science 271:1873-1876(1996).
RN [4]
RP INTERACTION WITH EAF1, AND SUBCELLULAR LOCATION.
RX PubMed=11418481; DOI=10.1182/blood.v98.1.201;
RA Simone F., Polak P.E., Kaberlein J.J., Luo R.T., Levitan D.A.,
RA Thirman M.J.;
RT "EAF1, a novel ELL-associated factor that is delocalized by expression of
RT the MLL-ELL fusion protein.";
RL Blood 98:201-209(2001).
RN [5]
RP INTERACTION WITH EAF2, AND SUBCELLULAR LOCATION.
RX PubMed=12446457; DOI=10.1182/blood-2002-06-1664;
RA Simone F., Luo R.T., Polak P.E., Kaberlein J.J., Thirman M.J.;
RT "ELL-associated factor 2 (EAF2), a functional homolog of EAF1 with
RT alternative ELL binding properties.";
RL Blood 101:2355-2362(2003).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=12686606; DOI=10.1091/mbc.e02-07-0394;
RA Polak P.E., Simone F., Kaberlein J.J., Luo R.T., Thirman M.J.;
RT "ELL and EAF1 are Cajal body components that are disrupted in MLL-ELL
RT leukemia.";
RL Mol. Biol. Cell 14:1517-1528(2003).
RN [7]
RP FUNCTION IN TRANSCRIPTION.
RX PubMed=16006523; DOI=10.1073/pnas.0503017102;
RA Kong S.E., Banks C.A., Shilatifard A., Conaway J.W., Conaway R.C.;
RT "ELL-associated factors 1 and 2 are positive regulators of RNA polymerase
RT II elongation factor ELL.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:10094-10098(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-561, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309, 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 [10]
RP FUNCTION, AND IDENTIFICATION IN THE SEC COMPLEX.
RX PubMed=20471948; DOI=10.1016/j.molcel.2010.04.013;
RA He N., Liu M., Hsu J., Xue Y., Chou S., Burlingame A., Krogan N.J.,
RA Alber T., Zhou Q.;
RT "HIV-1 Tat and host AFF4 recruit two transcription elongation factors into
RT a bifunctional complex for coordinated activation of HIV-1 transcription.";
RL Mol. Cell 38:428-438(2010).
RN [11]
RP FUNCTION, AND IDENTIFICATION IN THE SEC COMPLEX.
RX PubMed=20159561; DOI=10.1016/j.molcel.2010.01.026;
RA Lin C., Smith E.R., Takahashi H., Lai K.C., Martin-Brown S., Florens L.,
RA Washburn M.P., Conaway J.W., Conaway R.C., Shilatifard A.;
RT "AFF4, a component of the ELL/P-TEFb elongation complex and a shared
RT subunit of MLL chimeras, can link transcription elongation to leukemia.";
RL Mol. Cell 37:429-437(2010).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309, AND IDENTIFICATION BY
RP 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 [13]
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE SEC COMPLEX,
RP IDENTIFICATION IN THE LEC COMPLEX, AND INTERACTION WITH ICE1 AND ICE2.
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 [14]
RP FUNCTION.
RX PubMed=22252557; DOI=10.1038/ncomms1652;
RA Byun J.S., Fufa T.D., Wakano C., Fernandez A., Haggerty C.M., Sung M.H.,
RA Gardner K.;
RT "ELL facilitates RNA polymerase II pause site entry and release.";
RL Nat. Commun. 3:633-633(2012).
RN [15]
RP REVIEW ON THE SUPER ELONGATION COMPLEX.
RX PubMed=22895430; DOI=10.1038/nrm3417;
RA Luo Z., Lin C., Shilatifard A.;
RT "The super elongation complex (SEC) family in transcriptional control.";
RL Nat. Rev. Mol. Cell Biol. 13:543-547(2012).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-180 AND SER-309, 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 [18]
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 [19]
RP INTERACTION WITH USPL1.
RX PubMed=24413172; DOI=10.1242/jcs.141788;
RA Hutten S., Chachami G., Winter U., Melchior F., Lamond A.I.;
RT "A role for the Cajal-body-associated SUMO isopeptidase USPL1 in snRNA
RT transcription mediated by RNA polymerase II.";
RL J. Cell Sci. 127:1065-1078(2014).
RN [20]
RP STRUCTURE BY NMR OF 197-297.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the helical domain in human eleven-nineteen lysine-
RT rich leukemia protein ELL.";
RL Submitted (MAY-2007) to the PDB data bank.
CC -!- FUNCTION: Elongation factor component of the super elongation complex
CC (SEC), a complex required to increase the catalytic rate of RNA
CC polymerase II transcription by suppressing transient pausing by the
CC polymerase at multiple sites along the DNA. Elongation factor component
CC of the little elongation complex (LEC), a complex required to regulate
CC small nuclear RNA (snRNA) gene transcription by RNA polymerase II and
CC III (PubMed:22195968, PubMed:23932780). Specifically required for
CC stimulating the elongation step of RNA polymerase II- and III-dependent
CC snRNA gene transcription (PubMed:23932780). ELL also plays an early
CC role before its assembly into in the SEC complex by stabilizing RNA
CC polymerase II recruitment/initiation and entry into the pause site.
CC Required to stabilize the pre-initiation complex and early elongation.
CC {ECO:0000269|PubMed:16006523, ECO:0000269|PubMed:20159561,
CC ECO:0000269|PubMed:20471948, ECO:0000269|PubMed:22195968,
CC ECO:0000269|PubMed:22252557, ECO:0000269|PubMed:23932780,
CC ECO:0000269|PubMed:8596958}.
CC -!- SUBUNIT: Component of the super elongation complex (SEC), at least
CC composed of EAF1, EAF2, CDK9, MLLT3/AF9, AFF (AFF1 or AFF4), the P-TEFb
CC complex and ELL (ELL, ELL2 or ELL3). Component of the little elongation
CC complex (LEC), at least composed of ELL (ELL, ELL2 or ELL3), ZC3H8,
CC ICE1 and ICE2. Interacts with AFF4; the interaction is direct.
CC Interacts with EAF1 and EAF2. Interacts with ICE1 (via N-terminus
CC domain). Interacts with ICE2. Interacts with USPL1 (PubMed:24413172).
CC {ECO:0000269|PubMed:11418481, ECO:0000269|PubMed:12446457,
CC ECO:0000269|PubMed:20159561, ECO:0000269|PubMed:20471948,
CC ECO:0000269|PubMed:22195968, ECO:0000269|PubMed:23932780,
CC ECO:0000269|PubMed:24413172}.
CC -!- INTERACTION:
CC P55199; P62136: PPP1CA; NbExp=2; IntAct=EBI-1245868, EBI-357253;
CC P55199; Q96H20: SNF8; NbExp=3; IntAct=EBI-1245868, EBI-747719;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11418481,
CC ECO:0000269|PubMed:12446457}. Nucleus speckle
CC {ECO:0000269|PubMed:11418481, ECO:0000269|PubMed:12446457}. Nucleus,
CC Cajal body {ECO:0000269|PubMed:12686606, ECO:0000269|PubMed:22195968,
CC ECO:0000269|PubMed:23932780}. Note=Colocalizes with EAF2 to nuclear
CC speckles (PubMed:12446457). Colocalizes with coilin in subnuclear cajal
CC and histone locus bodies (PubMed:12686606). Translocates in the LEC
CC complex to cajal and histone locus bodies at snRNA genes in a ICE1-
CC dependent manner. Associates to transcriptionally active chromatin at
CC snRNA genes(PubMed:23932780). {ECO:0000269|PubMed:12446457,
CC ECO:0000269|PubMed:12686606, ECO:0000269|PubMed:23932780}.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested. Highest levels
CC found in placenta, skeletal muscle, testis and peripheral blood
CC leukocytes.
CC -!- DISEASE: Note=A chromosomal aberration involving ELL is found in acute
CC leukemias. Translocation t(11;19)(q23;p13.1) with KMT2A/MLL1. The
CC result is a rogue activator protein. {ECO:0000269|PubMed:7991593}.
CC -!- SIMILARITY: Belongs to the ELL/occludin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ELLID10.html";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U16282; AAA57120.1; -; mRNA.
DR EMBL; BC049195; AAH49195.1; -; mRNA.
DR CCDS; CCDS12380.1; -.
DR PIR; I38880; I38880.
DR RefSeq; NP_006523.1; NM_006532.3.
DR PDB; 2DOA; NMR; -; A=200-292.
DR PDBsum; 2DOA; -.
DR AlphaFoldDB; P55199; -.
DR SMR; P55199; -.
DR BioGRID; 113828; 72.
DR CORUM; P55199; -.
DR IntAct; P55199; 35.
DR MINT; P55199; -.
DR STRING; 9606.ENSP00000262809; -.
DR iPTMnet; P55199; -.
DR PhosphoSitePlus; P55199; -.
DR BioMuta; ELL; -.
DR DMDM; 1706635; -.
DR EPD; P55199; -.
DR jPOST; P55199; -.
DR MassIVE; P55199; -.
DR MaxQB; P55199; -.
DR PaxDb; P55199; -.
DR PeptideAtlas; P55199; -.
DR PRIDE; P55199; -.
DR ProteomicsDB; 56805; -.
DR Antibodypedia; 15081; 399 antibodies from 33 providers.
DR DNASU; 8178; -.
DR Ensembl; ENST00000262809.9; ENSP00000262809.3; ENSG00000105656.13.
DR GeneID; 8178; -.
DR KEGG; hsa:8178; -.
DR MANE-Select; ENST00000262809.9; ENSP00000262809.3; NM_006532.4; NP_006523.1.
DR UCSC; uc002njh.3; human.
DR CTD; 8178; -.
DR DisGeNET; 8178; -.
DR GeneCards; ELL; -.
DR HGNC; HGNC:23114; ELL.
DR HPA; ENSG00000105656; Low tissue specificity.
DR MIM; 600284; gene.
DR neXtProt; NX_P55199; -.
DR OpenTargets; ENSG00000105656; -.
DR PharmGKB; PA134939610; -.
DR VEuPathDB; HostDB:ENSG00000105656; -.
DR eggNOG; KOG4796; Eukaryota.
DR GeneTree; ENSGT00940000155914; -.
DR HOGENOM; CLU_021268_0_0_1; -.
DR InParanoid; P55199; -.
DR OMA; THNGRDC; -.
DR OrthoDB; 335949at2759; -.
DR PhylomeDB; P55199; -.
DR TreeFam; TF326161; -.
DR PathwayCommons; P55199; -.
DR Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-HSA-167152; Formation of HIV elongation complex in the absence of HIV Tat.
DR Reactome; R-HSA-167200; Formation of HIV-1 elongation complex containing HIV-1 Tat.
DR Reactome; R-HSA-167238; Pausing and recovery of Tat-mediated HIV elongation.
DR Reactome; R-HSA-167243; Tat-mediated HIV elongation arrest and recovery.
DR Reactome; R-HSA-167246; Tat-mediated elongation of the HIV-1 transcript.
DR Reactome; R-HSA-167287; HIV elongation arrest and recovery.
DR Reactome; R-HSA-167290; Pausing and recovery of HIV elongation.
DR Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-HSA-6781827; Transcription-Coupled Nucleotide Excision Repair (TC-NER).
DR Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-HSA-75955; RNA Polymerase II Transcription Elongation.
DR SignaLink; P55199; -.
DR SIGNOR; P55199; -.
DR BioGRID-ORCS; 8178; 746 hits in 1082 CRISPR screens.
DR ChiTaRS; ELL; human.
DR EvolutionaryTrace; P55199; -.
DR GeneWiki; ELL_(gene); -.
DR GenomeRNAi; 8178; -.
DR Pharos; P55199; Tbio.
DR PRO; PR:P55199; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P55199; protein.
DR Bgee; ENSG00000105656; Expressed in right testis and 108 other tissues.
DR ExpressionAtlas; P55199; baseline and differential.
DR Genevisible; P55199; 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:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0008023; C:transcription elongation factor complex; IDA:UniProtKB.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0019902; F:phosphatase binding; IDA:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0032786; P:positive regulation of DNA-templated transcription, elongation; TAS:ProtInc.
DR GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; IMP:UniProtKB.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; 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 GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; TAS:ProtInc.
DR Gene3D; 1.10.10.2670; -; 1.
DR InterPro; IPR042065; E3_ELL-like.
DR InterPro; IPR031184; ELL.
DR InterPro; IPR031176; ELL/occludin.
DR InterPro; IPR019464; ELL_N.
DR InterPro; IPR010844; Occludin_ELL.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR23288; PTHR23288; 1.
DR PANTHER; PTHR23288:SF9; PTHR23288:SF9; 1.
DR Pfam; PF10390; ELL; 1.
DR Pfam; PF07303; Occludin_ELL; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS51980; OCEL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chromosomal rearrangement; Nucleus;
KW Phosphoprotein; Proto-oncogene; Reference proteome; Transcription;
KW Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..621
FT /note="RNA polymerase II elongation factor ELL"
FT /id="PRO_0000146733"
FT DOMAIN 507..617
FT /note="OCEL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01324"
FT REGION 296..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 445..459
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 490..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 46
FT /note="KMT2A/MLL1 fusion point (in acute myeloid leukemia
FT patient)"
FT /evidence="ECO:0000269|PubMed:7991593"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 180
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 561
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT VARIANT 297
FT /note="S -> N (in dbSNP:rs2303694)"
FT /id="VAR_053072"
FT VARIANT 387
FT /note="R -> W (in dbSNP:rs35245196)"
FT /id="VAR_053073"
FT HELIX 207..217
FT /evidence="ECO:0007829|PDB:2DOA"
FT HELIX 222..232
FT /evidence="ECO:0007829|PDB:2DOA"
FT HELIX 236..248
FT /evidence="ECO:0007829|PDB:2DOA"
FT STRAND 249..252
FT /evidence="ECO:0007829|PDB:2DOA"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:2DOA"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:2DOA"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:2DOA"
FT HELIX 279..291
FT /evidence="ECO:0007829|PDB:2DOA"
SQ SEQUENCE 621 AA; 68265 MW; EB4A3F94CA8A411F CRC64;
MAALKEDRSY GLSCGRVSDG SKVSVFHVKL TDSALRAFES YRARQDSVSL RPSIRFQGSQ
GHISIPQPDC PAEARTFSFY LSNIGRDNPQ GSFDCIQQYV SSHGEVHLDC LGSIQDKITV
CATDDSYQKA RQSMAQAEEE TRSRSAIVIK AGGRYLGKKV QFRKPAPGAT DAVPSRKRAT
PINLASAIRK SGASAVSGGS GVSQRPFRDR VLHLLALRPY RKAELLLRLQ KDGLTQADKD
ALDGLLQQVA NMSAKDGTCT LQDCMYKDVQ KDWPGYSEGD QQLLKRVLVR KLCQPQSTGS
LLGDPAASSP PGERGRSASP PQKRLQPPDF IDPLANKKPR ISHFTQRAQP AVNGKLGVPN
GREALLPTPG PPASTDTLSS STHLPPRLEP PRAHDPLADV SNDLGHSGRD CEHGEAAAPA
PTVRLGLPLL TDCAQPSRPH GSPSRSKPKK KSKKHKDKER AAEDKPRAQL PDCAPATHAT
PGAPADTPGL NGTCSVSSVP TSTSETPDYL LKYAAISSSE QRQSYKNDFN AEYSEYRDLH
ARIERITRRF TQLDAQLRQL SQGSEEYETT RGQILQEYRK IKKTNTNYSQ EKHRCEYLHS
KLAHIKRLIA EYDQRQLQAW P
