TTL12_HUMAN
ID TTL12_HUMAN Reviewed; 644 AA.
AC Q14166; Q20WK5; Q9UGU3;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Tubulin--tyrosine ligase-like protein 12;
DE AltName: Full=Inactive tubulin--tyrosine ligase-like protein 12 {ECO:0000305};
GN Name=TTLL12; Synonyms=KIAA0153;
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 [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [3]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-644.
RC TISSUE=Bone marrow;
RX PubMed=8590280; DOI=10.1093/dnares/2.4.167;
RA Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. IV. The
RT coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 2:167-174(1995).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
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 FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=20162578; DOI=10.1002/ijc.25261;
RA Wasylyk C., Zambrano A., Zhao C., Brants J., Abecassis J., Schalken J.A.,
RA Rogatsch H., Schaefer G., Pycha A., Klocker H., Wasylyk B.;
RT "Tubulin tyrosine ligase like 12 links to prostate cancer through tubulin
RT posttranslational modification and chromosome ploidy.";
RL Int. J. Cancer 127:2542-2553(2010).
RN [11]
RP IDENTIFICATION BY 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 [12]
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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP FUNCTION, LACK OF TUBULIN TYROSINE LIGASE ACTIVITY, INTERACTION WITH CBX3;
RP HISTONE H3; HISTONE H4 AND TUBULIN ALPHA, AND SUBCELLULAR LOCATION.
RX PubMed=23251473; DOI=10.1371/journal.pone.0051258;
RA Brants J., Semenchenko K., Wasylyk C., Robert A., Carles A., Zambrano A.,
RA Pradeau-Aubreton K., Birck C., Schalken J.A., Poch O., de Mey J.,
RA Wasylyk B.;
RT "Tubulin tyrosine ligase like 12, a TTLL family member with SET- and TTL-
RT like domains and roles in histone and tubulin modifications and mitosis.";
RL PLoS ONE 7:E51258-E51258(2012).
RN [15]
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 [16]
RP FUNCTION, INTERACTION WITH MAVS; TBK1 AND IKBKE, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF TYR-244 AND GLU-605.
RX PubMed=28011935; DOI=10.4049/jimmunol.1601194;
RA Ju L.G., Zhu Y., Lei P.J., Yan D., Zhu K., Wang X., Li Q.L., Li X.J.,
RA Chen J.W., Li L.Y., Wu M.;
RT "TTLL12 Inhibits the Activation of Cellular Antiviral Signaling through
RT Interaction with VISA/MAVS.";
RL J. Immunol. 198:1274-1284(2017).
CC -!- FUNCTION: Negatively regulates post-translational modifications of
CC tubulin, including detyrosination of the C-terminus and
CC polyglutamylation of glutamate residues (PubMed:20162578,
CC PubMed:23251473). Also, indirectly promotes histone H4 trimethylation
CC at 'Lys-20' (H4K20me3) (PubMed:23251473). Probably by controlling
CC tubulin and/or histone H4 post-translational modifications, plays a
CC role in mitosis and in maintaining chromosome number stability
CC (PubMed:20162578, PubMed:23251473). During RNA virus-mediated
CC infection, acts as a negative regulator of the DDX58/RIG-I pathway by
CC preventing MAVS binding to TBK1 and IKBKE (PubMed:28011935).
CC {ECO:0000269|PubMed:20162578, ECO:0000269|PubMed:23251473,
CC ECO:0000269|PubMed:28011935}.
CC -!- SUBUNIT: Interacts with MAVS; the interaction prevents MAVS binding to
CC TBK1 and IKBKE (PubMed:28011935). Interacts (via N-terminus) with TBK1
CC (via protein kinase domain) (PubMed:28011935). Interacts (via TTL
CC domain) with IKBKE (via protein kinase domain) (PubMed:28011935).
CC Interacts with tubulin alpha (PubMed:23251473). Interacts with histone
CC H3 and histone H4 (when trimethylated at 'Lys-20' (H4K20me3))
CC (PubMed:23251473). Interacts with CBX3 (PubMed:23251473).
CC {ECO:0000269|PubMed:23251473, ECO:0000269|PubMed:28011935}.
CC -!- INTERACTION:
CC Q14166; P25685: DNAJB1; NbExp=4; IntAct=EBI-923010, EBI-357034;
CC Q14166; P68104: EEF1A1; NbExp=4; IntAct=EBI-923010, EBI-352162;
CC Q14166; Q05639: EEF1A2; NbExp=4; IntAct=EBI-923010, EBI-354943;
CC Q14166; Q8WU58: FAM222B; NbExp=3; IntAct=EBI-923010, EBI-2807642;
CC Q14166; P0CG20: PRR35; NbExp=3; IntAct=EBI-923010, EBI-11986293;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20162578,
CC ECO:0000269|PubMed:28011935}. Midbody {ECO:0000305|PubMed:20162578}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000305|PubMed:20162578}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000305|PubMed:20162578}. Nucleus {ECO:0000269|PubMed:23251473}.
CC Note=Predominantly localizes in the cytoplasm (PubMed:28011935).
CC Partially colocalizes with vimentin in prostate cancer cells
CC (PubMed:20162578). {ECO:0000269|PubMed:20162578,
CC ECO:0000269|PubMed:28011935}.
CC -!- TISSUE SPECIFICITY: Expressed in the basal layer of prostate and
CC endothelial cells. Increased expression in prostatic intraepithelial
CC neoplasia and metastatic lesions. {ECO:0000269|PubMed:20162578}.
CC -!- SIMILARITY: Belongs to the tubulin--tyrosine ligase family.
CC {ECO:0000305}.
CC -!- CAUTION: Although it belongs to the tubulin--tyrosine ligase family,
CC the TTL domain lacks some of the ATP binding sites predicted to be
CC essential for TTL activity (PubMed:23251473). Lacks tyrosine ligase
CC activity in vitro (PubMed:23251473). Lacks glutamylation activity in
CC vitro (By similarity). Although TTLL12 contains a potential SET-like
CC domain in the N-terminus, it does not have lysine methyltransferase
CC activity towards histone in vitro (PubMed:23251473).
CC {ECO:0000250|UniProtKB:Q3UDE2, ECO:0000269|PubMed:23251473}.
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DR EMBL; CT841516; CAJ86446.1; -; mRNA.
DR EMBL; Z82214; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471138; EAW73291.1; -; Genomic_DNA.
DR EMBL; BC001070; AAH01070.1; -; mRNA.
DR EMBL; D63487; BAA09774.1; -; mRNA.
DR CCDS; CCDS14047.1; -.
DR RefSeq; NP_055955.1; NM_015140.3.
DR AlphaFoldDB; Q14166; -.
DR SMR; Q14166; -.
DR BioGRID; 116782; 105.
DR IntAct; Q14166; 24.
DR STRING; 9606.ENSP00000216129; -.
DR GlyGen; Q14166; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q14166; -.
DR PhosphoSitePlus; Q14166; -.
DR SwissPalm; Q14166; -.
DR BioMuta; TTLL12; -.
DR DMDM; 20455527; -.
DR EPD; Q14166; -.
DR jPOST; Q14166; -.
DR MassIVE; Q14166; -.
DR MaxQB; Q14166; -.
DR PaxDb; Q14166; -.
DR PeptideAtlas; Q14166; -.
DR PRIDE; Q14166; -.
DR ProteomicsDB; 59894; -.
DR Antibodypedia; 27494; 265 antibodies from 17 providers.
DR DNASU; 23170; -.
DR Ensembl; ENST00000216129.7; ENSP00000216129.6; ENSG00000100304.13.
DR GeneID; 23170; -.
DR KEGG; hsa:23170; -.
DR MANE-Select; ENST00000216129.7; ENSP00000216129.6; NM_015140.4; NP_055955.1.
DR UCSC; uc003bdq.4; human.
DR CTD; 23170; -.
DR DisGeNET; 23170; -.
DR GeneCards; TTLL12; -.
DR HGNC; HGNC:28974; TTLL12.
DR HPA; ENSG00000100304; Tissue enhanced (esophagus).
DR MIM; 619410; gene.
DR neXtProt; NX_Q14166; -.
DR OpenTargets; ENSG00000100304; -.
DR PharmGKB; PA143485663; -.
DR VEuPathDB; HostDB:ENSG00000100304; -.
DR eggNOG; KOG2155; Eukaryota.
DR GeneTree; ENSGT00390000006760; -.
DR HOGENOM; CLU_018324_0_0_1; -.
DR InParanoid; Q14166; -.
DR OMA; CKRACDY; -.
DR OrthoDB; 611643at2759; -.
DR PhylomeDB; Q14166; -.
DR TreeFam; TF313037; -.
DR PathwayCommons; Q14166; -.
DR Reactome; R-HSA-8955332; Carboxyterminal post-translational modifications of tubulin.
DR SignaLink; Q14166; -.
DR BioGRID-ORCS; 23170; 11 hits in 1079 CRISPR screens.
DR ChiTaRS; TTLL12; human.
DR GenomeRNAi; 23170; -.
DR Pharos; Q14166; Tbio.
DR PRO; PR:Q14166; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q14166; protein.
DR Bgee; ENSG00000100304; Expressed in lower esophagus mucosa and 181 other tissues.
DR ExpressionAtlas; Q14166; baseline and differential.
DR Genevisible; Q14166; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:1990889; F:H4K20me3 modified histone binding; IDA:UniProtKB.
DR GO; GO:0015631; F:tubulin binding; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0060339; P:negative regulation of type I interferon-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:UniProtKB.
DR InterPro; IPR004344; TTL/TTLL_fam.
DR InterPro; IPR027749; TTLL12.
DR PANTHER; PTHR46088; PTHR46088; 1.
DR Pfam; PF03133; TTL; 1.
DR PROSITE; PS51221; TTL; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Cytoskeleton; Immunity; Innate immunity;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..644
FT /note="Tubulin--tyrosine ligase-like protein 12"
FT /id="PRO_0000212446"
FT DOMAIN 300..644
FT /note="TTL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00568"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 450..453
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6ZT98"
FT BINDING 468
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6ZT98"
FT BINDING 470
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6ZT98"
FT VARIANT 84
FT /note="R -> W (in dbSNP:rs138951)"
FT /id="VAR_052413"
FT VARIANT 95
FT /note="N -> S (in dbSNP:rs13058467)"
FT /id="VAR_052414"
FT VARIANT 297
FT /note="V -> M (in dbSNP:rs11704935)"
FT /id="VAR_052415"
FT VARIANT 464
FT /note="V -> M (in dbSNP:rs34074034)"
FT /id="VAR_052416"
FT MUTAGEN 244
FT /note="Y->A: Decreases expression of IFNB1 mRNA following
FT infection with Sendai virus."
FT /evidence="ECO:0000269|PubMed:28011935"
FT MUTAGEN 605
FT /note="E->A: Decreases expression of IFNB1 mRNA following
FT infection with Sendai virus."
FT /evidence="ECO:0000269|PubMed:28011935"
SQ SEQUENCE 644 AA; 74404 MW; BFF552774DF500EF CRC64;
MEAERGPERR PAERSSPGQT PEEGAQALAE FAALHGPALR ASGVPERYWG RLLHKLEHEV
FDAGEVFGIM QVEEVEEEED EAAREVRKQQ PNPGNELCYK VIVTRESGLQ AAHPNSIFLI
DHAWTCRVEH ARQQLQQVPG LLHRMANLMG IEFHGELPST EAVALVLEEM WKFNQTYQLA
HGTAEEKMPV WYIMDEFGSR IQHADVPSFA TAPFFYMPQQ VAYTLLWPLR DLDTGEEVTR
DFAYGETDPL IRKCMLLPWA PTDMLDLSSC TPEPPAEHYQ AILEENKEKL PLDINPVVHP
HGHIFKVYTD VQQVASSLTH PRFTLTQSEA DADILFNFSH FKDYRKLSQE RPGVLLNQFP
CENLLTVKDC LASIARRAGG PEGPPWLPRT FNLRTELPQF VSYFQQRERW GEDNHWICKP
WNLARSLDTH VTKSLHSIIR HRESTPKVVS KYIESPVLFL REDVGKVKFD IRYIVLLRSV
RPLRLFVYDV FWLRFSNRAF ALNDLDDYEK HFTVMNYDPD VVLKQVHCEE FIPEFEKQYP
EFPWTDVQAE IFRAFTELFQ VACAKPPPLG LCDYPSSRAM YAVDLMLKWD NGPDGRRVMQ
PQILEVNFNP DCERACRYHP TFFNDVFSTL FLDQPGGCHV TCLV
