ELP5_HUMAN
ID ELP5_HUMAN Reviewed; 316 AA.
AC Q8TE02; A8K1M5; D3DTN9; Q659B6; Q7Z2T4; Q8TDR9; Q9BUB2; Q9Y2Q4;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Elongator complex protein 5 {ECO:0000303|PubMed:22854966};
DE AltName: Full=Dermal papilla-derived protein 6 {ECO:0000303|PubMed:16850183};
DE AltName: Full=S-phase 2 protein;
GN Name=ELP5 {ECO:0000303|PubMed:22854966, ECO:0000312|HGNC:HGNC:30617};
GN Synonyms=C17orf81, DERP6 {ECO:0000303|PubMed:16850183};
GN ORFNames=HSPC002, MSTP071;
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 SUBCELLULAR LOCATION.
RX PubMed=16850183; DOI=10.1007/s11033-006-6273-5;
RA Yuan J., Tang W., Luo K., Chen X., Gu X., Wan B., Yu L.;
RT "Cloning and characterization of the human gene DERP6, which activates
RT transcriptional activities of p53.";
RL Mol. Biol. Rep. 33:151-158(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT LYS-14.
RC TISSUE=Hair follicle dermal papilla;
RA Ikeda A., Yoshimoto M.;
RT "Molecular cloning of a dermal papilla derived gene.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Hippocampus;
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 GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
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), AND VARIANT TYR-303.
RC TISSUE=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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 10-316 (ISOFORM 3).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 24-316 (ISOFORM 2).
RC TISSUE=Aorta;
RA Zhao B., Xu Y.Y., Liu Y.Q., Wang X.Y., Liu B., Sheng H., Ye J., Song L.,
RA Gao Y., Zhang C.L., Zhang J., Gao R.L., Wu Q.Y., Hui R.T.;
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 149-316 (ISOFORM 4).
RC TISSUE=Amygdala;
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 [10]
RP IDENTIFICATION IN THE ELONGATOR COMPLEX, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [12]
RP REVIEW.
RX PubMed=29332244; DOI=10.1007/s00018-018-2747-6;
RA Dalwadi U., Yip C.K.;
RT "Structural insights into the function of Elongator.";
RL Cell. Mol. Life Sci. 75:1613-1622(2018).
RN [13]
RP PHOSPHORYLATION.
RX PubMed=31341009; DOI=10.1042/bcj20190106;
RA Li M.T., Liang J.Y., Sun Y.P., Jin J., Xiong Y., Guan K.L., Yuan H.X.;
RT "ELP3 Acetyltransferase is phosphorylated and regulated by the oncogenic
RT anaplastic lymphoma kinase (ALK).";
RL Biochem. J. 476:2239-2254(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) (PubMed:29332244). The elongator complex
CC catalyzes formation of carboxymethyluridine in the wobble base at
CC position 34 in tRNAs (PubMed:29332244). Involved in cell migration (By
CC similarity). {ECO:0000250|UniProtKB:Q99L85,
CC ECO:0000303|PubMed:29332244}.
CC -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC biosynthesis. {ECO:0000303|PubMed:29332244}.
CC -!- SUBUNIT: Component of the elongator complex which consists of ELP1,
CC ELP2, ELP3, ELP4, ELP5 and ELP6; in the complex, is required for
CC optimal binding of ELP3 to ELP4. {ECO:0000269|PubMed:22854966}.
CC -!- INTERACTION:
CC Q8TE02; P54253: ATXN1; NbExp=8; IntAct=EBI-946189, EBI-930964;
CC Q8TE02; Q96EB1: ELP4; NbExp=4; IntAct=EBI-946189, EBI-3951755;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22854966}. Cytoplasm
CC {ECO:0000269|PubMed:16850183, ECO:0000269|PubMed:22854966}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8TE02-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TE02-2; Sequence=VSP_023923;
CC Name=3;
CC IsoId=Q8TE02-3; Sequence=VSP_023920, VSP_023921;
CC Name=4;
CC IsoId=Q8TE02-4; Sequence=VSP_023922;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with high levels in heart,
CC brain, liver, skeletal muscle and testis.
CC -!- PTM: Tyrosine-phosphorylated. {ECO:0000269|PubMed:31341009}.
CC -!- SIMILARITY: Belongs to the ELP5 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:0000305|PubMed:29332244}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-17 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD20964.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAQ13591.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF087868; AAM10496.1; -; mRNA.
DR EMBL; AB013910; BAB87800.1; -; mRNA.
DR EMBL; AK289940; BAF82629.1; -; mRNA.
DR EMBL; AC003688; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471108; EAW90230.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90231.1; -; Genomic_DNA.
DR EMBL; BC002762; AAH02762.2; -; mRNA.
DR EMBL; AF070658; AAD20964.1; ALT_INIT; mRNA.
DR EMBL; AF163262; AAQ13591.1; ALT_INIT; mRNA.
DR EMBL; AL713741; CAH56280.1; -; mRNA.
DR RefSeq; NP_056177.3; NM_015362.4. [Q8TE02-1]
DR RefSeq; NP_981958.1; NM_203413.2. [Q8TE02-2]
DR RefSeq; NP_981959.1; NM_203414.2. [Q8TE02-1]
DR RefSeq; NP_981960.1; NM_203415.2. [Q8TE02-1]
DR RefSeq; XP_011522081.1; XM_011523779.2. [Q8TE02-1]
DR AlphaFoldDB; Q8TE02; -.
DR BioGRID; 117122; 21.
DR ComplexPortal; CPX-1949; Elongator holoenzyme complex.
DR CORUM; Q8TE02; -.
DR IntAct; Q8TE02; 9.
DR MINT; Q8TE02; -.
DR STRING; 9606.ENSP00000379869; -.
DR iPTMnet; Q8TE02; -.
DR PhosphoSitePlus; Q8TE02; -.
DR BioMuta; ELP5; -.
DR DMDM; 134034093; -.
DR EPD; Q8TE02; -.
DR jPOST; Q8TE02; -.
DR MassIVE; Q8TE02; -.
DR MaxQB; Q8TE02; -.
DR PaxDb; Q8TE02; -.
DR PeptideAtlas; Q8TE02; -.
DR PRIDE; Q8TE02; -.
DR ProteomicsDB; 74381; -. [Q8TE02-1]
DR ProteomicsDB; 74382; -. [Q8TE02-2]
DR ProteomicsDB; 74383; -. [Q8TE02-3]
DR ProteomicsDB; 74384; -. [Q8TE02-4]
DR Antibodypedia; 11862; 84 antibodies from 20 providers.
DR DNASU; 23587; -.
DR Ensembl; ENST00000354429.7; ENSP00000346412.3; ENSG00000170291.16.
DR Ensembl; ENST00000356683.7; ENSP00000349111.3; ENSG00000170291.16.
DR Ensembl; ENST00000396627.7; ENSP00000379868.3; ENSG00000170291.16.
DR Ensembl; ENST00000396628.7; ENSP00000379869.3; ENSG00000170291.16.
DR Ensembl; ENST00000573657.6; ENSP00000459633.2; ENSG00000170291.16.
DR Ensembl; ENST00000574255.6; ENSP00000461489.2; ENSG00000170291.16.
DR Ensembl; ENST00000574993.6; ENSP00000459835.2; ENSG00000170291.16.
DR Ensembl; ENST00000671820.1; ENSP00000500470.1; ENSG00000288485.1. [Q8TE02-1]
DR Ensembl; ENST00000671829.1; ENSP00000500574.1; ENSG00000288485.1. [Q8TE02-1]
DR Ensembl; ENST00000672545.1; ENSP00000500755.1; ENSG00000288485.1. [Q8TE02-2]
DR Ensembl; ENST00000673019.1; ENSP00000500212.1; ENSG00000288485.1. [Q8TE02-2]
DR Ensembl; ENST00000673277.1; ENSP00000499930.1; ENSG00000288485.1. [Q8TE02-3]
DR Ensembl; ENST00000673309.1; ENSP00000500054.1; ENSG00000288485.1. [Q8TE02-3]
DR Ensembl; ENST00000673570.1; ENSP00000500315.1; ENSG00000288485.1. [Q8TE02-1]
DR GeneID; 23587; -.
DR KEGG; hsa:23587; -.
DR UCSC; uc002gfg.2; human. [Q8TE02-1]
DR CTD; 23587; -.
DR DisGeNET; 23587; -.
DR GeneCards; ELP5; -.
DR HGNC; HGNC:30617; ELP5.
DR HPA; ENSG00000170291; Tissue enhanced (testis).
DR MIM; 615019; gene.
DR neXtProt; NX_Q8TE02; -.
DR PharmGKB; PA143485405; -.
DR VEuPathDB; HostDB:ENSG00000170291; -.
DR eggNOG; ENOG502QQ2R; Eukaryota.
DR HOGENOM; CLU_076374_0_0_1; -.
DR InParanoid; Q8TE02; -.
DR OMA; SICHLAT; -.
DR OrthoDB; 805928at2759; -.
DR PhylomeDB; Q8TE02; -.
DR TreeFam; TF314636; -.
DR PathwayCommons; Q8TE02; -.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR SignaLink; Q8TE02; -.
DR UniPathway; UPA00988; -.
DR BioGRID-ORCS; 23587; 615 hits in 1103 CRISPR screens.
DR ChiTaRS; ELP5; human.
DR GeneWiki; C17orf81; -.
DR GenomeRNAi; 23587; -.
DR Pharos; Q8TE02; Tbio.
DR PRO; PR:Q8TE02; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q8TE02; protein.
DR Bgee; ENSG00000170291; Expressed in right testis and 97 other tissues.
DR ExpressionAtlas; Q8TE02; baseline and differential.
DR Genevisible; Q8TE02; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0033588; C:elongator holoenzyme complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0006417; P:regulation of translation; IC:ComplexPortal.
DR GO; GO:0006400; P:tRNA modification; IBA:GO_Central.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IC:ComplexPortal.
DR InterPro; IPR019519; Elp5.
DR PANTHER; PTHR15641; PTHR15641; 1.
DR Pfam; PF10483; Elong_Iki1; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome; tRNA processing.
FT CHAIN 1..316
FT /note="Elongator complex protein 5"
FT /id="PRO_0000280817"
FT REGION 280..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..316
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 154..179
FT /note="DSSSVGKVSVLGLLHEELHGPGPVGA -> ETPPSLFPLIHLPLPRSVPLFL
FT STLE (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11042152"
FT /id="VSP_023920"
FT VAR_SEQ 180..316
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11042152"
FT /id="VSP_023921"
FT VAR_SEQ 246
FT /note="V -> VHPLYLQV (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_023922"
FT VAR_SEQ 247..316
FT /note="DPTTHLTFNLHLSKKEREARDSLILPFQFSSEKQQALLRPRPGQATSHIFYE
FT PDAYDDLDQEDPDDDLDI -> SKNAKARTRKCSLVSGHGRENKSCRGWGWGQGF (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.8"
FT /id="VSP_023923"
FT VARIANT 14
FT /note="E -> K (in dbSNP:rs2521988)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_053882"
FT VARIANT 303
FT /note="D -> Y (in dbSNP:rs17849664)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_031205"
FT CONFLICT 151
FT /note="C -> R (in Ref. 1; AAM10496)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="G -> S (in Ref. 1; AAM10496)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="S -> N (in Ref. 1; AAM10496)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="Q -> K (in Ref. 1; AAM10496)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="P -> R (in Ref. 1; AAM10496)"
FT /evidence="ECO:0000305"
FT CONFLICT Q8TE02-2:263
FT /note="H -> Q (in Ref. 8; AAQ13591)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 316 AA; 34841 MW; C96F86C6B99CE7CE CRC64;
MTPSEGARAG TGRELEMLDS LLALGGLVLL RDSVEWEGRS LLKALVKKSA LCGEQVHILG
CEVSEEEFRE GFDSDINNRL VYHDFFRDPL NWSKTEEAFP GGPLGALRAM CKRTDPVPVT
IALDSLSWLL LRLPCTTLCQ VLHAVSHQDS CPGDSSSVGK VSVLGLLHEE LHGPGPVGAL
SSLAQTEVTL GGTMGQASAH ILCRRPRQRP TDQTQWFSIL PDFSLDLQEG PSVESQPYSD
PHIPPVDPTT HLTFNLHLSK KEREARDSLI LPFQFSSEKQ QALLRPRPGQ ATSHIFYEPD
AYDDLDQEDP DDDLDI
