TANC1_HUMAN
ID TANC1_HUMAN Reviewed; 1861 AA.
AC Q9C0D5; C9JD88; Q49AI8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Protein TANC1;
DE AltName: Full=Tetratricopeptide repeat, ankyrin repeat and coiled-coil domain-containing protein 1;
GN Name=TANC1; Synonyms=KIAA1728;
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 GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-662 (ISOFORM 2), AND VARIANT
RP SER-251.
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 218-1861 (ISOFORM 1), AND
RP VARIANTS SER-251 AND ALA-1573.
RC TISSUE=Brain;
RX PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [4]
RP INTERACTION WITH TNIK, AND PHOSPHORYLATION.
RX PubMed=18930710; DOI=10.1016/j.bbrc.2008.10.038;
RA Nonaka H., Takei K., Umikawa M., Oshiro M., Kuninaka K., Bayarjargal M.,
RA Asato T., Yamashiro Y., Uechi Y., Endo S., Suzuki T., Kariya K.;
RT "MINK is a Rap2 effector for phosphorylation of the postsynaptic scaffold
RT protein TANC1.";
RL Biochem. Biophys. Res. Commun. 377:573-578(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66 AND SER-207, AND
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 [7]
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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63; SER-67; SER-270; SER-465
RP AND SER-1668, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
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).
CC -!- FUNCTION: May be a scaffold component in the postsynaptic density.
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts probably directly with DLG1, DLG4, HOMER1. Interacts
CC with DLGAP1, INA, CAMK2A, GRIN2B and GRIA1 (By similarity). Interacts
CC with TNIK. Interacts with MINK1 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q9C0D5; Q12959: DLG1; NbExp=3; IntAct=EBI-11023211, EBI-357481;
CC Q9C0D5; Q14160: SCRIB; NbExp=4; IntAct=EBI-11023211, EBI-357345;
CC -!- SUBCELLULAR LOCATION: Postsynaptic density {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9C0D5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C0D5-2; Sequence=VSP_030828;
CC -!- PTM: Phosphorylated; by MINK1 and TNIK upon stimulation by RAP2A.
CC {ECO:0000269|PubMed:18930710}.
CC -!- MISCELLANEOUS: [Isoform 2]: Incomplete sequence. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TANC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH37329.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH37329.1; Type=Miscellaneous discrepancy; Note=The cDNA sequence appears to be not correctly spliced at its 3'-end.; Evidence={ECO:0000305};
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DR EMBL; AC009307; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC010093; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC037329; AAH37329.1; ALT_SEQ; mRNA.
DR EMBL; AB051515; BAB21819.1; -; mRNA.
DR CCDS; CCDS42766.1; -. [Q9C0D5-1]
DR RefSeq; NP_001139381.1; NM_001145909.1.
DR RefSeq; NP_203752.2; NM_033394.2. [Q9C0D5-1]
DR RefSeq; XP_006712873.1; XM_006712810.3. [Q9C0D5-1]
DR RefSeq; XP_011510360.1; XM_011512058.2. [Q9C0D5-2]
DR AlphaFoldDB; Q9C0D5; -.
DR SMR; Q9C0D5; -.
DR BioGRID; 124545; 66.
DR IntAct; Q9C0D5; 16.
DR MINT; Q9C0D5; -.
DR STRING; 9606.ENSP00000263635; -.
DR GlyGen; Q9C0D5; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; Q9C0D5; -.
DR MetOSite; Q9C0D5; -.
DR PhosphoSitePlus; Q9C0D5; -.
DR BioMuta; TANC1; -.
DR DMDM; 296452941; -.
DR EPD; Q9C0D5; -.
DR jPOST; Q9C0D5; -.
DR MassIVE; Q9C0D5; -.
DR MaxQB; Q9C0D5; -.
DR PaxDb; Q9C0D5; -.
DR PeptideAtlas; Q9C0D5; -.
DR PRIDE; Q9C0D5; -.
DR ProteomicsDB; 80014; -. [Q9C0D5-1]
DR ProteomicsDB; 80015; -. [Q9C0D5-2]
DR Antibodypedia; 47958; 44 antibodies from 10 providers.
DR DNASU; 85461; -.
DR Ensembl; ENST00000263635.8; ENSP00000263635.6; ENSG00000115183.15. [Q9C0D5-1]
DR GeneID; 85461; -.
DR KEGG; hsa:85461; -.
DR MANE-Select; ENST00000263635.8; ENSP00000263635.6; NM_033394.3; NP_203752.2.
DR UCSC; uc002uag.4; human. [Q9C0D5-1]
DR CTD; 85461; -.
DR DisGeNET; 85461; -.
DR GeneCards; TANC1; -.
DR HGNC; HGNC:29364; TANC1.
DR HPA; ENSG00000115183; Low tissue specificity.
DR MIM; 611397; gene.
DR neXtProt; NX_Q9C0D5; -.
DR OpenTargets; ENSG00000115183; -.
DR PharmGKB; PA142670838; -.
DR VEuPathDB; HostDB:ENSG00000115183; -.
DR eggNOG; KOG0504; Eukaryota.
DR GeneTree; ENSGT00940000155655; -.
DR HOGENOM; CLU_001464_0_1_1; -.
DR InParanoid; Q9C0D5; -.
DR OMA; TSENQRP; -.
DR PhylomeDB; Q9C0D5; -.
DR TreeFam; TF323159; -.
DR PathwayCommons; Q9C0D5; -.
DR SignaLink; Q9C0D5; -.
DR SIGNOR; Q9C0D5; -.
DR BioGRID-ORCS; 85461; 6 hits in 1068 CRISPR screens.
DR ChiTaRS; TANC1; human.
DR GenomeRNAi; 85461; -.
DR Pharos; Q9C0D5; Tdark.
DR PRO; PR:Q9C0D5; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9C0D5; protein.
DR Bgee; ENSG00000115183; Expressed in upper arm skin and 185 other tissues.
DR Genevisible; Q9C0D5; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0043679; C:axon terminus; IEA:Ensembl.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0097062; P:dendritic spine maintenance; IEA:Ensembl.
DR GO; GO:0007520; P:myoblast fusion; IEA:Ensembl.
DR GO; GO:0099175; P:regulation of postsynapse organization; IBA:GO_Central.
DR GO; GO:0008542; P:visual learning; IEA:Ensembl.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 1.25.40.20; -; 3.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 3.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 10.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 6.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ANK repeat; Phosphoprotein;
KW Reference proteome; Repeat; Synapse; TPR repeat.
FT CHAIN 1..1861
FT /note="Protein TANC1"
FT /id="PRO_0000316959"
FT REPEAT 896..928
FT /note="ANK 1"
FT REPEAT 934..963
FT /note="ANK 2"
FT REPEAT 967..996
FT /note="ANK 3"
FT REPEAT 1000..1029
FT /note="ANK 4"
FT REPEAT 1040..1069
FT /note="ANK 5"
FT REPEAT 1078..1107
FT /note="ANK 6"
FT REPEAT 1111..1140
FT /note="ANK 7"
FT REPEAT 1144..1173
FT /note="ANK 8"
FT REPEAT 1177..1206
FT /note="ANK 9"
FT REPEAT 1210..1239
FT /note="ANK 10"
FT REPEAT 1243..1272
FT /note="ANK 11"
FT REPEAT 1289..1322
FT /note="TPR 1"
FT REPEAT 1336..1369
FT /note="TPR 2"
FT REPEAT 1371..1403
FT /note="TPR 3"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 63..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1421..1485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1636..1696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1422..1444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1446..1460
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1468..1485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1655..1693
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1439
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6F6B3"
FT MOD_RES 1668
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1676
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q0VGY8"
FT MOD_RES 1677
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q0VGY8"
FT VAR_SEQ 122..227
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030828"
FT VARIANT 30
FT /note="P -> S (in dbSNP:rs34588551)"
FT /id="VAR_061022"
FT VARIANT 251
FT /note="N -> S (in dbSNP:rs12466551)"
FT /evidence="ECO:0000269|PubMed:11214970,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_038435"
FT VARIANT 1511
FT /note="G -> S (in dbSNP:rs13421084)"
FT /id="VAR_038436"
FT VARIANT 1573
FT /note="T -> A (in dbSNP:rs4664277)"
FT /evidence="ECO:0000269|PubMed:11214970"
FT /id="VAR_038437"
SQ SEQUENCE 1861 AA; 202219 MW; E9BE1083E5FB9413 CRC64;
MLKAVLKKSR EGGKGGKKEA GSDFGPETSP VLHLDHSADS PVSSLPTAED TYRVSLAKGV
SMSLPSSPLL PRQSHLVQSR VNKKSPGPVR KPKYVESPRV PGDAVIMPFR EVAKPTEPDE
HEAKADNEPS CSPAAQELLT RLGFLLGEGI PSATHITIED KNETMCTALS QGISPCSTLT
SSTASPSTDS PCSTLNSCVS KTAANKSPCE TISSPSSTLE SKDSGIIATI TSSSENDDRS
GSSLEWNKDG NLRLGVQKGV LHDRRADNCS PVAEEETTGS AESTLPKAES SAGDGPVPYS
QGSSSLIMPR PNSVAATSST KLEDLSYLDG QRNAPLRTSI RLPWHNTAGG RAQEVKARFA
PYKPQDILLK PLLFEVPSIT TDSVFVGRDW LFHQIEENLR NTELAENRGA VVVGNVGFGK
TAIISKLVAL SCHGSRMRQI ASNSPGSSPK TSDPTQDLHF TPLLSPSSST SASSTAKTPL
GSISAENQRP REDAVKYLAS KVVAYHYCQA DNTYTCLVPE FVHSIAALLC RSHQLAAYRD
LLIKEPQLQS MLSLRSCVQD PVAAFKRGVL EPLTNLRNEQ KIPEEEYIIL IDGLNEAEFH
KPDYGDTLSS FITKIISKFP AWLKLIVTVR ANFQEIISAL PFVKLSLDDF PDNKDIHSDL
HAYVQHRVHS SQDILSNISL NGKADATLIG KVSSHLVLRS LGSYLYLKLT LDLFQRGHLV
IKSASYKVVP VSLSELYLLQ CNMKFMTQSA FERALPILNV ALASLHPMTD EQIFQAINAG
HIQGEQGWED FQQRMDALSC FLIKRRDKTR MFCHPSFREW LVWRADGENT AFLCEPRNGH
ALLAFMFSRQ EGKLNRQQTM ELGHHILKAH IFKGLSKKTG ISSSHLQALW IGYSTEGLSA
ALASLRNLYT PNVKVSRLLI LGGANVNYRT EVLNNAPILC VQSHLGHEEV VTLLLEFGAC
LDGTSENGMT ALCYAAAAGH MKLVCLLTKK GVRVDHLDKK GQCALVHSAL RGHGDILQYL
LTCEWSPGPP QPGTLRKSHA LQQALTAAAS MGHSSVVQCL LGMEKEHEVE VNGTDTLWGE
TALTAAAGRG KLEVCELLLG HGAAVSRTNR RGVPPLFCAA RQGHWQIVRL LLERGCDVNL
SDKQGRTPLM VAACEGHLST VEFLLSKGAA LSSLDKEGLS ALSWACLKGH RAVVQYLVEE
GAAIDQTDKN GRTPLDLAAF YGDAETVLYL VEKGAVIEHV DHSGMRPLDR AIGCRNTSVV
VALLRKGAKL GNAAWAMATS KPDILIILLQ KLMEEGNVMY KKGKMKEAAQ RYQYALRKFP
REGFGEDMRP FNELRVSLYL NLSRCRRKTN DFGMAEEFAS KALELKPKSY EAFYARARAK
RNSRQFVAAL ADLQEAVKLC PTNQEVKRLL ARVEEECKQL QRSQQQKQQG PLPAPLNDSE
NEEDTPTPGL SDHFHSEETE EEETSPQEES VSPTPRSQPS SSVPSSYIRN LQEGLQSKGR
PVSPQSRAGI GKSLREPVAQ PGLLLQPSKQ AQIVKTSQHL GSGQSAVRNG SMKVQISSQN
PPPSPMPGRI AATPAGSRTQ HLEGTGTFTT RAGCGHFGDR LGPSQNVRLQ CGENGPAHPL
PSKTKTTERL LSHSSVAVDA APPNQGGLAT CSDVRHPASL TSSGSSGSPS SSIKMSSSTS
SLTSSSSFSD GFKVQGPDTR IKDKVVTHVQ SGTAEHRPRN TPFMGIMDKT ARFQQQSNPP
SRSWHCPAPE GLLTNTSSAA GLQSANTEKP SLMQVGGYNN QAKTCSVSTL SASVHNGAQV
KELEESKCQI PVHSQENRIT KTVSHLYQES ISKQQPHISN EAHRSHLTAA KPKRSFIESN
V
