ID ELP5_HUMAN Reviewed; 300 AA. AC Q8TE02; A8K1M5; D3DTN9; Q659B6; Q7Z2T4; Q8TDR9; Q9BUB2; Q9Y2Q4; DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2024, sequence version 3. DT 24-JUL-2024, entry version 148. 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 (ISOFORM 1). 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 [MRNA] (ISOFORM 5). RA Yu L.; RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases. RN [4] 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 [5] 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 [6] 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT TYR-287. 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 [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (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 [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-300 (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 [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 133-300 (ISOFORM 2). 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 [11] 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, 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 [13] 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 [14] 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=3; 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, Alternative initiation; Named isoforms=4; CC Name=5; CC IsoId=Q8TE02-5; Sequence=Displayed; CC Name=1; CC IsoId=Q8TE02-1; Sequence=VSP_062149; CC Name=2; CC IsoId=Q8TE02-2; Sequence=VSP_062152, VSP_062153; CC Name=3; CC IsoId=Q8TE02-3; Sequence=VSP_062150, VSP_062151; 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 -!- MISCELLANEOUS: [Isoform 1]: Produced by alternative initiation at Met-1 CC of isoform 5. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 5]: Major isoform. {ECO:0000305}. 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 -!- SEQUENCE CAUTION: CC Sequence=AAM10496.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAQ13591.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=CAH56280.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305}; 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; AB013910; BAB87800.1; -; mRNA. DR EMBL; AF087868; AAM10496.1; ALT_INIT; 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; -; mRNA. DR EMBL; AF163262; AAQ13591.1; ALT_INIT; mRNA. DR EMBL; AL713741; CAH56280.1; ALT_SEQ; mRNA. DR CCDS; CCDS11094.2; -. [Q8TE02-5] DR CCDS; CCDS11095.2; -. [Q8TE02-2] DR RefSeq; NP_056177.3; NM_015362.4. [Q8TE02-5] DR RefSeq; NP_981958.1; NM_203413.2. [Q8TE02-2] DR RefSeq; NP_981959.1; NM_203414.2. [Q8TE02-5] DR RefSeq; NP_981960.1; NM_203415.2. [Q8TE02-5] DR RefSeq; XP_011522081.1; XM_011523779.2. [Q8TE02-1] DR AlphaFoldDB; Q8TE02; -. DR BioGRID; 117122; 25. DR ComplexPortal; CPX-1949; Elongator holoenzyme complex. DR CORUM; Q8TE02; -. DR IntAct; Q8TE02; 8. DR STRING; 9606.ENSP00000379869; -. DR iPTMnet; Q8TE02; -. DR PhosphoSitePlus; Q8TE02; -. DR BioMuta; ELP5; -. DR DMDM; 134034093; -. DR jPOST; Q8TE02; -. DR MassIVE; Q8TE02; -. DR PaxDb; 9606-ENSP00000379869; -. DR PeptideAtlas; Q8TE02; -. DR ProteomicsDB; 74381; -. [Q8TE02-1] DR ProteomicsDB; 74382; -. [Q8TE02-2] DR ProteomicsDB; 74383; -. [Q8TE02-3] DR Pumba; Q8TE02; -. DR Antibodypedia; 11862; 84 antibodies from 20 providers. DR DNASU; 23587; -. DR Ensembl; ENST00000354429.7; ENSP00000346412.3; ENSG00000170291.16. [Q8TE02-5] DR Ensembl; ENST00000356683.7; ENSP00000349111.3; ENSG00000170291.16. [Q8TE02-2] DR Ensembl; ENST00000396627.7; ENSP00000379868.3; ENSG00000170291.16. [Q8TE02-5] DR Ensembl; ENST00000396628.7; ENSP00000379869.3; ENSG00000170291.16. [Q8TE02-5] DR Ensembl; ENST00000573657.6; ENSP00000459633.2; ENSG00000170291.16. [Q8TE02-3] DR Ensembl; ENST00000574255.6; ENSP00000461489.2; ENSG00000170291.16. [Q8TE02-3] DR Ensembl; ENST00000574993.6; ENSP00000459835.2; ENSG00000170291.16. [Q8TE02-2] DR Ensembl; ENST00000671820.1; ENSP00000500470.1; ENSG00000288485.1. [Q8TE02-1] DR Ensembl; ENST00000671829.1; ENSP00000500574.1; ENSG00000288485.1. [Q8TE02-1] DR Ensembl; ENST00000673570.1; ENSP00000500315.1; ENSG00000288485.1. [Q8TE02-1] DR GeneID; 23587; -. DR KEGG; hsa:23587; -. DR MANE-Select; ENST00000396628.7; ENSP00000379869.3; NM_203414.3; NP_981959.2. DR UCSC; uc002gfg.2; human. [Q8TE02-5] DR AGR; HGNC:30617; -. 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 OpenTargets; ENSG00000170291; -. DR PharmGKB; PA143485405; -. DR VEuPathDB; HostDB:ENSG00000170291; -. DR eggNOG; ENOG502QQ2R; Eukaryota. DR GeneTree; ENSGT00390000009210; -. DR HOGENOM; CLU_076374_0_0_1; -. DR InParanoid; Q8TE02; -. DR OMA; DEEIFCI; -. DR OrthoDB; 9395at2759; -. DR PhylomeDB; Q8TE02; -. DR TreeFam; TF314636; -. DR BioCyc; MetaCyc:ENSG00000170291-MONOMER; -. DR PathwayCommons; Q8TE02; -. DR Reactome; R-HSA-3214847; HATs acetylate histones. DR SignaLink; Q8TE02; -. DR SIGNOR; Q8TE02; -. DR UniPathway; UPA00988; -. DR BioGRID-ORCS; 23587; 650 hits in 1192 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 99 other cell types or tissues. DR ExpressionAtlas; Q8TE02; baseline and differential. 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; NAS:ComplexPortal. DR GO; GO:0006400; P:tRNA modification; IBA:GO_Central. DR GO; GO:0002098; P:tRNA wobble uridine modification; NAS:ComplexPortal. DR CDD; cd19496; Elp5; 1. DR InterPro; IPR019519; Elp5. DR PANTHER; PTHR15641; ELONGATOR COMPLEX PROTEIN 5; 1. DR PANTHER; PTHR15641:SF1; ELONGATOR COMPLEX PROTEIN 5; 1. DR Pfam; PF10483; Elong_Iki1; 2. PE 1: Evidence at protein level; KW Alternative initiation; Alternative splicing; Cytoplasm; Nucleus; KW Phosphoprotein; Reference proteome; tRNA processing. FT CHAIN 1..300 FT /note="Elongator complex protein 5" FT /id="PRO_0000280817" FT REGION 264..300 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 286..300 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 252 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 1 FT /note="M -> MTPSEGARAGTGRELEM (in isoform 1)" FT /id="VSP_062149" FT VAR_SEQ 138..163 FT /note="DSSSVGKVSVLGLLHEELHGPGPVGA -> ETPPSLFPLIHLPLPRSVPLFL FT STLE (in isoform 3)" FT /id="VSP_062150" FT VAR_SEQ 164..300 FT /note="Missing (in isoform 3)" FT /id="VSP_062151" FT VAR_SEQ 231..263 FT /note="DPTTHLTFNLHLSKKEREARDSLILPFQFSSEK -> SKNAKARTRKCSLVS FT GHGRENKSCRGWGWGQGF (in isoform 2)" FT /id="VSP_062152" FT VAR_SEQ 264..300 FT /note="Missing (in isoform 2)" FT /id="VSP_062153" FT VARIANT 287 FT /note="D -> Y (in dbSNP:rs17849664)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_031205" FT CONFLICT 135 FT /note="C -> R (in Ref. 3; AAM10496)" FT /evidence="ECO:0000305" FT CONFLICT 159 FT /note="G -> S (in Ref. 3; AAM10496)" FT /evidence="ECO:0000305" FT CONFLICT 165 FT /note="S -> N (in Ref. 3; AAM10496)" FT /evidence="ECO:0000305" FT CONFLICT 212 FT /note="Q -> K (in Ref. 3; AAM10496)" FT /evidence="ECO:0000305" FT CONFLICT 229 FT /note="P -> R (in Ref. 3; AAM10496)" FT /evidence="ECO:0000305" FT VARIANT Q8TE02-1:14 FT /note="E -> K (in dbSNP:rs2521988)" FT /evidence="ECO:0000269|Ref.2" FT /id="VAR_088548" FT CONFLICT Q8TE02-2:247 FT /note="H -> Q (in Ref. 9; AAQ13591)" FT /evidence="ECO:0000305" SQ SEQUENCE 300 AA; 33197 MW; 2443B829343D72EF CRC64; MLDSLLALGG LVLLRDSVEW EGRSLLKALV KKSALCGEQV HILGCEVSEE EFREGFDSDI NNRLVYHDFF RDPLNWSKTE EAFPGGPLGA LRAMCKRTDP VPVTIALDSL SWLLLRLPCT TLCQVLHAVS HQDSCPGDSS SVGKVSVLGL LHEELHGPGP VGALSSLAQT EVTLGGTMGQ ASAHILCRRP RQRPTDQTQW FSILPDFSLD LQEGPSVESQ PYSDPHIPPV DPTTHLTFNL HLSKKEREAR DSLILPFQFS SEKQQALLRP RPGQATSHIF YEPDAYDDLD QEDPDDDLDI //