TTI1_HUMAN
ID TTI1_HUMAN Reviewed; 1089 AA.
AC O43156; D6W4K3; Q5JX67; Q96A38; Q9BR47; Q9H4K0;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2002, sequence version 3.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=TELO2-interacting protein 1 homolog;
DE AltName: Full=Protein SMG10;
GN Name=TTI1; Synonyms=KIAA0406, SMG10;
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].
RC TISSUE=Brain;
RX PubMed=9455477; DOI=10.1093/dnares/4.5.307;
RA Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VIII. 78
RT new cDNA clones from brain which code for large proteins in vitro.";
RL DNA Res. 4:307-313(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH TELO2; MTOR;
RP ATM; ATR; PRKDC; SMG1 AND TRRAP.
RX PubMed=20427287; DOI=10.1074/jbc.m110.121699;
RA Kaizuka T., Hara T., Oshiro N., Kikkawa U., Yonezawa K., Takehana K.,
RA Iemura S., Natsume T., Mizushima N.;
RT "Tti1 and Tel2 are critical factors in mammalian target of rapamycin
RT complex assembly.";
RL J. Biol. Chem. 285:20109-20116(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix, and Testis;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-459, AND IDENTIFICATION BY
RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-459, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP FUNCTION, INTERACTION WITH ATM; ATR; MTOR; PRKDC; SMG1; TELO2 AND TTI2, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20810650; DOI=10.1101/gad.1934210;
RA Hurov K.E., Cotta-Ramusino C., Elledge S.J.;
RT "A genetic screen identifies the Triple T complex required for DNA damage
RT signaling and ATM and ATR stability.";
RL Genes Dev. 24:1939-1950(2010).
RN [9]
RP FUNCTION, AND INTERACTION WITH TTI2 AND TELO2.
RX PubMed=20801936; DOI=10.1101/gad.1956410;
RA Takai H., Xie Y., de Lange T., Pavletich N.P.;
RT "Tel2 structure and function in the Hsp90-dependent maturation of mTOR and
RT ATR complexes.";
RL Genes Dev. 24:2019-2030(2010).
RN [10]
RP INTERACTION WITH RUVBL1 AND SMG1.
RX PubMed=20371770; DOI=10.1126/scisignal.2000468;
RA Izumi N., Yamashita A., Iwamatsu A., Kurata R., Nakamura H., Saari B.,
RA Hirano H., Anderson P., Ohno S.;
RT "AAA+ proteins RUVBL1 and RUVBL2 coordinate PIKK activity and function in
RT nonsense-mediated mRNA decay.";
RL Sci. Signal. 3:RA27-RA27(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-459, AND IDENTIFICATION BY
RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-459 AND SER-828, AND
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 [14]
RP IDENTIFICATION IN THE MTORC1 COMPLEX, IDENTIFICATION IN THE MTORC2 COMPLEX,
RP SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-828, UBIQUITINATION, AND
RP MUTAGENESIS OF SER-828.
RX PubMed=23263282; DOI=10.1038/ncb2651;
RA Fernandez-Saiz V., Targosz B.S., Lemeer S., Eichner R., Langer C.,
RA Bullinger L., Reiter C., Slotta-Huspenina J., Schroeder S., Knorn A.M.,
RA Kurutz J., Peschel C., Pagano M., Kuster B., Bassermann F.;
RT "SCF(Fbxo9) and CK2 direct the cellular response to growth factor
RT withdrawal via Tel2/Tti1 degradation and promote survival in multiple
RT myeloma.";
RL Nat. Cell Biol. 15:72-81(2013).
RN [15]
RP INTERACTION WITH WAC.
RX PubMed=26812014; DOI=10.1016/j.devcel.2015.12.019;
RA David-Morrison G., Xu Z., Rui Y.N., Charng W.L., Jaiswal M., Yamamoto S.,
RA Xiong B., Zhang K., Sandoval H., Duraine L., Zuo Z., Zhang S., Bellen H.J.;
RT "WAC regulates mTOR activity by acting as an adaptor for the TTT and
RT Pontin/Reptin complexes.";
RL Dev. Cell 36:139-151(2016).
CC -!- FUNCTION: Regulator of the DNA damage response (DDR). Part of the TTT
CC complex that is required to stabilize protein levels of the
CC phosphatidylinositol 3-kinase-related protein kinase (PIKK) family
CC proteins. The TTT complex is involved in the cellular resistance to DNA
CC damage stresses, like ionizing radiation (IR), ultraviolet (UV) and
CC mitomycin C (MMC). Together with the TTT complex and HSP90 may
CC participate in the proper folding of newly synthesized PIKKs. Promotes
CC assembly, stabilizes and maintains the activity of mTORC1 and mTORC2
CC complexes, which regulate cell growth and survival in response to
CC nutrient and hormonal signals. {ECO:0000269|PubMed:20427287,
CC ECO:0000269|PubMed:20801936, ECO:0000269|PubMed:20810650}.
CC -!- SUBUNIT: Component of the TTT complex composed of TELO2, TTI1 and TTI2
CC (PubMed:20801936). Interacts with ATM, ATR, MTOR, PRKDC, RUVBL1, SMG1,
CC TELO2, TRRAP AND TTI2 (PubMed:20371770, PubMed:20427287,
CC PubMed:20810650). Component of the mTORC1 and mTORC2 complexes
CC (PubMed:23263282). Interacts with WAC; WAC positively regulates MTOR
CC activity by promoting the assembly of the TTT complex and the RUVBL
CC complex composed of RUVBL1 and RUVBL2 into the TTT-RUVBL complex which
CC leads to the dimerization of the mTORC1 complex and its subsequent
CC activation (PubMed:26812014). {ECO:0000269|PubMed:20371770,
CC ECO:0000269|PubMed:20427287, ECO:0000269|PubMed:20801936,
CC ECO:0000269|PubMed:20810650, ECO:0000269|PubMed:23263282,
CC ECO:0000269|PubMed:26812014}.
CC -!- INTERACTION:
CC O43156; Q13315: ATM; NbExp=5; IntAct=EBI-1055680, EBI-495465;
CC O43156; Q13535: ATR; NbExp=2; IntAct=EBI-1055680, EBI-968983;
CC O43156; Q9UK97: FBXO9; NbExp=5; IntAct=EBI-1055680, EBI-2869927;
CC O43156; Q9Y4R8: TELO2; NbExp=7; IntAct=EBI-1055680, EBI-1043674;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23263282}.
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- PTM: Phosphorylated at Ser-828 by CK2 following growth factor
CC deprivation, leading to its subsequent ubiquitination by the SCF(FBXO9)
CC complex. Phosphorylation by CK2 only takes place when TELO2 is bound to
CC mTORC1, not mTORC2; leading to selective ubiquitination of mTORC1-
CC associated protein. {ECO:0000269|PubMed:23263282}.
CC -!- PTM: Ubiquitinated by the SCF(FBXO9) complex following phosphorylation
CC by CK2 in response to growth factor deprivation, leading to its
CC degradation by the proteasome. Only mTORC1-associated protein is
CC ubiquitinated and degraded, leading to selective inactivation of mTORC1
CC to restrain cell growth and protein translation, while mTORC2 is
CC activated due to the relief of feedback inhibition by mTORC1.
CC {ECO:0000269|PubMed:23263282}.
CC -!- SIMILARITY: Belongs to the tti1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA23702.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB007866; BAA23702.2; ALT_INIT; mRNA.
DR EMBL; BR000854; FAA00688.1; -; mRNA.
DR EMBL; AL109823; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW76047.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76048.1; -; Genomic_DNA.
DR EMBL; BC013121; AAH13121.1; -; mRNA.
DR EMBL; BC013755; AAH13755.1; -; mRNA.
DR CCDS; CCDS13300.1; -.
DR PIR; T00052; T00052.
DR RefSeq; NP_001290386.1; NM_001303457.1.
DR RefSeq; NP_055472.1; NM_014657.2.
DR PDB; 7OLE; EM; 3.41 A; H=1-1089.
DR PDBsum; 7OLE; -.
DR AlphaFoldDB; O43156; -.
DR BioGRID; 115030; 120.
DR ComplexPortal; CPX-6148; TTT complex.
DR DIP; DIP-50660N; -.
DR IntAct; O43156; 40.
DR MINT; O43156; -.
DR STRING; 9606.ENSP00000362547; -.
DR iPTMnet; O43156; -.
DR PhosphoSitePlus; O43156; -.
DR BioMuta; TTI1; -.
DR EPD; O43156; -.
DR jPOST; O43156; -.
DR MassIVE; O43156; -.
DR MaxQB; O43156; -.
DR PaxDb; O43156; -.
DR PeptideAtlas; O43156; -.
DR PRIDE; O43156; -.
DR ProteomicsDB; 48776; -.
DR Antibodypedia; 57267; 133 antibodies from 22 providers.
DR DNASU; 9675; -.
DR Ensembl; ENST00000373447.8; ENSP00000362546.3; ENSG00000101407.13.
DR Ensembl; ENST00000373448.6; ENSP00000362547.2; ENSG00000101407.13.
DR Ensembl; ENST00000449821.1; ENSP00000407270.1; ENSG00000101407.13.
DR GeneID; 9675; -.
DR KEGG; hsa:9675; -.
DR MANE-Select; ENST00000373447.8; ENSP00000362546.3; NM_001303457.2; NP_001290386.1.
DR UCSC; uc002xhl.4; human.
DR CTD; 9675; -.
DR DisGeNET; 9675; -.
DR GeneCards; TTI1; -.
DR HGNC; HGNC:29029; TTI1.
DR HPA; ENSG00000101407; Low tissue specificity.
DR MIM; 614425; gene.
DR neXtProt; NX_O43156; -.
DR OpenTargets; ENSG00000101407; -.
DR PharmGKB; PA165392722; -.
DR VEuPathDB; HostDB:ENSG00000101407; -.
DR eggNOG; KOG4524; Eukaryota.
DR GeneTree; ENSGT00390000009748; -.
DR HOGENOM; CLU_004815_0_0_1; -.
DR InParanoid; O43156; -.
DR OMA; GAHTCQV; -.
DR OrthoDB; 89960at2759; -.
DR PhylomeDB; O43156; -.
DR TreeFam; TF315296; -.
DR PathwayCommons; O43156; -.
DR SignaLink; O43156; -.
DR SIGNOR; O43156; -.
DR BioGRID-ORCS; 9675; 624 hits in 1088 CRISPR screens.
DR ChiTaRS; TTI1; human.
DR GenomeRNAi; 9675; -.
DR Pharos; O43156; Tbio.
DR PRO; PR:O43156; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; O43156; protein.
DR Bgee; ENSG00000101407; Expressed in secondary oocyte and 208 other tissues.
DR ExpressionAtlas; O43156; baseline and differential.
DR Genevisible; O43156; HS.
DR GO; GO:0070209; C:ASTRA complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0031931; C:TORC1 complex; IDA:UniProtKB.
DR GO; GO:0031932; C:TORC2 complex; IDA:UniProtKB.
DR GO; GO:0110078; C:TTT complex; IPI:ComplexPortal.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:2000003; P:positive regulation of DNA damage checkpoint; IC:ComplexPortal.
DR GO; GO:0050821; P:protein stabilization; IC:ComplexPortal.
DR GO; GO:0032006; P:regulation of TOR signaling; IMP:UniProtKB.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR016441; Tti1.
DR PIRSF; PIRSF005250; UCP005250; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..1089
FT /note="TELO2-interacting protein 1 homolog"
FT /id="PRO_0000050751"
FT REGION 826..852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 835..851
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 459
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 828
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:23263282,
FT ECO:0007744|PubMed:23186163"
FT VARIANT 450
FT /note="R -> H (in dbSNP:rs36059660)"
FT /id="VAR_034033"
FT VARIANT 671
FT /note="A -> V (in dbSNP:rs1057238)"
FT /id="VAR_014082"
FT VARIANT 751
FT /note="K -> E (in dbSNP:rs6091654)"
FT /id="VAR_049509"
FT VARIANT 979
FT /note="A -> T (in dbSNP:rs1064275)"
FT /id="VAR_014083"
FT VARIANT 1028
FT /note="R -> K (in dbSNP:rs34900517)"
FT /id="VAR_034034"
FT MUTAGEN 828
FT /note="S->A: Abolishes phosphorylation by CK2 in response
FT to growth factor deprivation and subsequent ubiquitination
FT and degradation."
FT /evidence="ECO:0000269|PubMed:23263282"
SQ SEQUENCE 1089 AA; 122069 MW; 27F4D3EFAC18A54E CRC64;
MAVFDTPEEA FGVLRPVCVQ LTKTQTVENV EHLQTRLQAV SDSALQELQQ YILFPLRFTL
KTPGPKRERL IQSVVECLTF VLSSTCVKEQ ELLQELFSEL SACLYSPSSQ KPAAVSEELK
LAVIQGLSTL MHSAYGDIIL TFYEPSILPR LGFAVSLLLG LAEQEKSKQI KIAALKCLQV
LLLQCDCQDH PRSLDELEQK QLGDLFASFL PGISTALTRL ITGDFKQGHS IVVSSLKIFY
KTVSFIMADE QLKRISKVQA KPAVEHRVAE LMVYREADWV KKTGDKLTIL IKKIIECVSV
HPHWKVRLEL VELVEDLLLK CSQSLVECAG PLLKALVGLV NDESPEIQAQ CNKVLRHFAD
QKVVVGNKAL ADILSESLHS LATSLPRLMN SQDDQGKFST LSLLLGYLKL LGPKINFVLN
SVAHLQRLSK ALIQVLELDV ADIKIVEERR WNSDDLNASP KTSATQPWNR IQRRYFRFFT
DERIFMLLRQ VCQLLGYYGN LYLLVDHFME LYHQSVVYRK QAAMILNELV TGAAGLEVED
LHEKHIKTNP EELREIVTSI LEEYTSQENW YLVTCLETEE MGEELMMEHP GLQAITSGEH
TCQVTSFLAF SKPSPTICSM NSNIWQICIQ LEGIGQFAYA LGKDFCLLLM SALYPVLEKA
GDQTLLISQV ATSTMMDVCR ACGYDSLQHL INQNSDYLVN GISLNLRHLA LHPHTPKVLE
VMLRNSDANL LPLVADVVQD VLATLDQFYD KRAASFVSVL HALMAALAQW FPDTGNLGHL
QEQSLGEEGS HLNQRPAALE KSTTTAEDIE QFLLNYLKEK DVADGNVSDF DNEEEEQSVP
PKVDENDTRP DVEPPLPLQI QIAMDVMERC IHLLSDKNLQ IRLKVLDVLD LCVVVLQSHK
NQLLPLAHQA WPSLVHRLTR DAPLAVLRAF KVLRTLGSKC GDFLRSRFCK DVLPKLAGSL
VTQAPISARA GPVYSHTLAF KLQLAVLQGL GPLCERLDLG EGDLNKVADA CLIYLSVKQP
VKLQEAARSV FLHLMKVDPD STWFLLNELY CPVQFTPPHP SLHPVQLHGA SGQQNPYTTN
VLQLLKELQ
