TCPA_MOUSE
ID TCPA_MOUSE Reviewed; 556 AA.
AC P11983; P11984; Q3TJ96; Q3TKU1; Q3U5T8; Q3U7I8; Q3UAA8; Q3UB80; Q3UE48;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 3.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=T-complex protein 1 subunit alpha;
DE Short=TCP-1-alpha;
DE AltName: Full=CCT-alpha;
DE AltName: Full=Tailless complex polypeptide 1A;
DE Short=TCP-1-A;
DE AltName: Full=Tailless complex polypeptide 1B;
DE Short=TCP-1-B;
GN Name=Tcp1; Synonyms=Cct1, Ccta;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=3753900; DOI=10.1016/0092-8674(86)90839-1;
RA Willison K.R., Dudley K., Potter J.;
RT "Molecular cloning and sequence analysis of a haploid expressed gene
RT encoding t complex polypeptide 1.";
RL Cell 44:727-738(1986).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=2377466; DOI=10.1093/nar/18.14.4247;
RA Kirchhoff C., Willison K.R.;
RT "Nucleotide and amino-acid sequence of human testis-derived TCP1.";
RL Nucleic Acids Res. 18:4247-4247(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1937024; DOI=10.1016/0378-1119(91)90162-5;
RA Kubota H., Morita T., Nagata T., Takemoto Y., Nozaki M., Gachelin G.,
RA Matsushiro A.;
RT "Nucleotide sequence of mouse Tcp-1a cDNA.";
RL Gene 105:269-273(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=1383093; DOI=10.1016/0378-1119(92)90095-7;
RA Kubota H., Willison K., Ashworth A., Nozaki M., Miyamoto H., Yamamoto H.,
RA Matsushiro A., Morita T.;
RT "Structure and expression of the gene encoding mouse T-complex polypeptide
RT (Tcp-1).";
RL Gene 120:207-215(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Placenta;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 PROTEIN SEQUENCE OF 1-11; 34-43; 64-73; 190-199; 234-243; 371-378; 434-466
RP AND 485-496, ACETYLATION AT MET-1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryonic fibroblast;
RA Bienvenut W.V., Sandilands E., Serrels B., Brunton V.G., Frame M.C.;
RL Submitted (FEB-2008) to UniProtKB.
RN [8]
RP PROTEIN SEQUENCE OF 19-63; 112-122; 131-145; 190-199; 234-243; 248-259;
RP 299-309; 434-443; 469-480; 500-510 AND 516-526, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [9]
RP PROTEIN SEQUENCE OF 485-496.
RC TISSUE=Brain;
RA Lubec G., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544 AND SER-551, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-400 AND LYS-494, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Component of the chaperonin-containing T-complex (TRiC), a
CC molecular chaperone complex that assists the folding of proteins upon
CC ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1,
CC thereby regulating telomere maintenance. As part of the TRiC complex
CC may play a role in the assembly of BBSome, a complex involved in
CC ciliogenesis regulating transports vesicles to the cilia. The TRiC
CC complex plays a role in the folding of actin and tubulin.
CC {ECO:0000250|UniProtKB:P17987}.
CC -!- SUBUNIT: Component of the chaperonin-containing T-complex (TRiC), a
CC heterooligomeric complex of about 850 to 900 kDa that forms two stacked
CC rings, 12 to 16 nm in diameter. Interacts with PACRG. Interacts with
CC GBA (By similarity). Interacts with DLEC1 (By similarity).
CC {ECO:0000250|UniProtKB:P17987}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P17987}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:P17987}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P11983-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P11983-2; Sequence=VSP_024734, VSP_024735;
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA40337.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAA40338.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M20130; AAA40337.1; ALT_FRAME; mRNA.
DR EMBL; M12899; AAA40338.1; ALT_FRAME; mRNA.
DR EMBL; D90344; BAA14356.1; -; mRNA.
DR EMBL; D10606; BAA01461.1; -; Genomic_DNA.
DR EMBL; S46763; AAB23855.1; -; Genomic_DNA.
DR EMBL; AK149611; BAE28989.1; -; mRNA.
DR EMBL; AK149755; BAE29063.1; -; mRNA.
DR EMBL; AK151068; BAE30084.1; -; mRNA.
DR EMBL; AK151445; BAE30407.1; -; mRNA.
DR EMBL; AK152641; BAE31381.1; -; mRNA.
DR EMBL; AK153430; BAE31988.1; -; mRNA.
DR EMBL; AK165665; BAE38327.1; -; mRNA.
DR EMBL; AK166828; BAE39052.1; -; mRNA.
DR EMBL; AK166966; BAE39149.1; -; mRNA.
DR EMBL; AK167529; BAE39599.1; -; mRNA.
DR EMBL; BC003809; AAH03809.1; -; mRNA.
DR CCDS; CCDS28397.1; -. [P11983-1]
DR CCDS; CCDS70760.1; -. [P11983-2]
DR PIR; B24059; B24059.
DR PIR; JC1443; JC1443.
DR RefSeq; NP_001277641.1; NM_001290712.1. [P11983-2]
DR RefSeq; NP_038714.2; NM_013686.4. [P11983-1]
DR AlphaFoldDB; P11983; -.
DR SMR; P11983; -.
DR BioGRID; 204044; 55.
DR CORUM; P11983; -.
DR DIP; DIP-32342N; -.
DR IntAct; P11983; 13.
DR MINT; P11983; -.
DR STRING; 10090.ENSMUSP00000116108; -.
DR iPTMnet; P11983; -.
DR PhosphoSitePlus; P11983; -.
DR SwissPalm; P11983; -.
DR REPRODUCTION-2DPAGE; IPI00459493; -.
DR REPRODUCTION-2DPAGE; P11983; -.
DR EPD; P11983; -.
DR jPOST; P11983; -.
DR MaxQB; P11983; -.
DR PaxDb; P11983; -.
DR PeptideAtlas; P11983; -.
DR PRIDE; P11983; -.
DR ProteomicsDB; 263264; -. [P11983-1]
DR ProteomicsDB; 263265; -. [P11983-2]
DR Antibodypedia; 20023; 699 antibodies from 39 providers.
DR DNASU; 21454; -.
DR Ensembl; ENSMUST00000089024; ENSMUSP00000086418; ENSMUSG00000068039. [P11983-2]
DR Ensembl; ENSMUST00000151287; ENSMUSP00000116108; ENSMUSG00000068039. [P11983-1]
DR GeneID; 21454; -.
DR KEGG; mmu:21454; -.
DR UCSC; uc008all.2; mouse. [P11983-1]
DR UCSC; uc008alm.2; mouse. [P11983-2]
DR CTD; 6950; -.
DR MGI; MGI:98535; Tcp1.
DR VEuPathDB; HostDB:ENSMUSG00000068039; -.
DR eggNOG; KOG0360; Eukaryota.
DR GeneTree; ENSGT00550000074878; -.
DR HOGENOM; CLU_008891_5_1_1; -.
DR InParanoid; P11983; -.
DR OMA; KNYKNYG; -.
DR OrthoDB; 335406at2759; -.
DR PhylomeDB; P11983; -.
DR TreeFam; TF106331; -.
DR BRENDA; 3.6.4.B10; 3474.
DR Reactome; R-MMU-390471; Association of TriC/CCT with target proteins during biosynthesis.
DR Reactome; R-MMU-5620922; BBSome-mediated cargo-targeting to cilium.
DR Reactome; R-MMU-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR BioGRID-ORCS; 21454; 32 hits in 73 CRISPR screens.
DR ChiTaRS; Tcp1; mouse.
DR PRO; PR:P11983; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P11983; protein.
DR Bgee; ENSMUSG00000068039; Expressed in spermatid and 68 other tissues.
DR ExpressionAtlas; P11983; baseline and differential.
DR Genevisible; P11983; MM.
DR GO; GO:0001669; C:acrosomal vesicle; IDA:MGI.
DR GO; GO:0044297; C:cell body; IDA:MGI.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005832; C:chaperonin-containing T-complex; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0000792; C:heterochromatin; IDA:MGI.
DR GO; GO:0005874; C:microtubule; ISO:MGI.
DR GO; GO:0005815; C:microtubule organizing center; IDA:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0000242; C:pericentriolar material; IDA:MGI.
DR GO; GO:0002199; C:zona pellucida receptor complex; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0044183; F:protein folding chaperone; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IDA:MGI.
DR GO; GO:0061077; P:chaperone-mediated protein folding; ISO:MGI.
DR GO; GO:1904851; P:positive regulation of establishment of protein localization to telomere; ISO:MGI.
DR GO; GO:0051973; P:positive regulation of telomerase activity; ISO:MGI.
DR GO; GO:1904874; P:positive regulation of telomerase RNA localization to Cajal body; ISO:MGI.
DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; ISO:MGI.
DR GO; GO:0006457; P:protein folding; ISO:MGI.
DR GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR GO; GO:2000109; P:regulation of macrophage apoptotic process; IMP:MGI.
DR GO; GO:0090666; P:scaRNA localization to Cajal body; ISO:MGI.
DR GO; GO:1901998; P:toxin transport; IMP:MGI.
DR GO; GO:0044053; P:translocation of peptides or proteins into host cell cytoplasm; IMP:MGI.
DR CDD; cd03335; TCP1_alpha; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR012715; Chap_CCT_alpha.
DR InterPro; IPR017998; Chaperone_TCP-1.
DR InterPro; IPR002194; Chaperonin_TCP-1_CS.
DR InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR InterPro; IPR027413; GROEL-like_equatorial_sf.
DR InterPro; IPR027410; TCP-1-like_intermed_sf.
DR PANTHER; PTHR11353; PTHR11353; 1.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR PRINTS; PR00304; TCOMPLEXTCP1.
DR SUPFAM; SSF48592; SSF48592; 1.
DR SUPFAM; SSF52029; SSF52029; 1.
DR SUPFAM; SSF54849; SSF54849; 1.
DR TIGRFAMs; TIGR02340; chap_CCT_alpha; 1.
DR PROSITE; PS00750; TCP1_1; 1.
DR PROSITE; PS00751; TCP1_2; 1.
DR PROSITE; PS00995; TCP1_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Chaperone; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Nucleotide-binding;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..556
FT /note="T-complex protein 1 subunit alpha"
FT /id="PRO_0000128305"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|Ref.7"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17987"
FT MOD_RES 181
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P17987"
FT MOD_RES 199
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P17987"
FT MOD_RES 400
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 494
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 544
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 551
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..49
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024734"
FT VAR_SEQ 50
FT /note="G -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024735"
FT CONFLICT 17
FT /note="V -> I (in Ref. 1; AAA40337, 3; BAA14356 and 5;
FT BAE30084)"
FT /evidence="ECO:0000305"
FT CONFLICT 36
FT /note="F -> L (in Ref. 1; AAA40337 and 3; BAA14356)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="T -> A (in Ref. 1; AAA40337 and 3; BAA14356)"
FT /evidence="ECO:0000305"
FT CONFLICT 149..151
FT /note="INA -> TNT (in Ref. 1; AAA40337 and 3; BAA14356)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="A -> T (in Ref. 1; AAA40338)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="L -> H (in Ref. 5; BAE31381)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="V -> I (in Ref. 1; AAA40337 and 3; BAA14356)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="N -> D (in Ref. 5; BAE39599)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="K -> E (in Ref. 5; BAE31381)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="Y -> C (in Ref. 1; AAA40337 and 3; BAA14356)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="H -> C (in Ref. 1; AAA40337 and 3; BAA14356)"
FT /evidence="ECO:0000305"
FT CONFLICT 326
FT /note="S -> T (in Ref. 1; AAA40337 and 3; BAA14356)"
FT /evidence="ECO:0000305"
FT CONFLICT 378
FT /note="R -> Q (in Ref. 5; BAE30084)"
FT /evidence="ECO:0000305"
FT CONFLICT 402
FT /note="V -> I (in Ref. 5; BAE30407/BAE31988)"
FT /evidence="ECO:0000305"
FT CONFLICT 405
FT /note="L -> S (in Ref. 1; AAA40337 and 3; BAA14356)"
FT /evidence="ECO:0000305"
FT CONFLICT 429
FT /note="S -> N (in Ref. 1; AAA40338)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="A -> V (in Ref. 5; BAE31381)"
FT /evidence="ECO:0000305"
FT CONFLICT 454
FT /note="V -> M (in Ref. 5; BAE39052)"
FT /evidence="ECO:0000305"
FT CONFLICT 494
FT /note="K -> N (in Ref. 5; BAE30407)"
FT /evidence="ECO:0000305"
FT CONFLICT 537
FT /note="S -> C (in Ref. 1; AAA40337 and 3; BAA14356)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 556 AA; 60449 MW; 48F2387BE0F909A4 CRC64;
MEGPLSVFGD RSTGEAVRSQ NVMAAASIAN IVKSSFGPVG LDKMLVDDIG DVTITNDGAT
ILKLLEVEHP AAKVLCELAD LQDKEVGDGT TSVVIIAAEL LKNADELVKQ KIHPTSVISG
YRLACKEAVR YINENLIINT DELGRDCLIN AAKTSMSSKI IGINGDYFAN MVVDAVLAVK
YTDARGQPRY PVNSVNILKA HGRSQIESML INGYALNCVV GSQGMPKRIV NAKIACLDFS
LQKTKMKLGV QVVITDPEKL DQIRQRESDI TKERIQKILA TGANVILTTG GIDDMYLKYF
VEAGAMAVRR VLKRDLKHVA KASGASILST LANLEGEETF EVTMLGQAEE VVQERICDDE
LILIKNTKAR TSASIILRGA NDFMCDEMER SLHDALCVVK RVLELKSVVP GGGAVEAALS
IYLENYATSM GSREQLAIAE FARSLLVIPN TLAVNAAQDS TDLVAKLRAF HNEAQVNPER
KNLKWIGLDL VHGKPRDNKQ AGVFEPTIVK VKSLKFATEA AITILRIDDL IKLHPESKDD
KHGSYENAVH SGALDD
