TROAP_HUMAN
ID TROAP_HUMAN Reviewed; 778 AA.
AC Q12815; F8VSF9; Q6PJU7; Q8N5B2;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 3.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Tastin;
DE AltName: Full=Trophinin-assisting protein;
DE AltName: Full=Trophinin-associated protein;
GN Name=TROAP;
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).
RX PubMed=7758945; DOI=10.1101/gad.9.10.1199;
RA Fukuda M.N., Sato T., Nakayama J., Klier G., Mikami M., Aoki D., Nozawa S.;
RT "Trophinin and tastin, a novel cell adhesion molecule complex with
RT potential involvement in embryo implantation.";
RL Genes Dev. 9:1199-1210(1995).
RN [2]
RP SEQUENCE REVISION TO 714 AND 742.
RA Fukuda M., Sato T.;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Lymph;
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-334 AND SER-344, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98; SER-334 AND SER-376, AND
RP IDENTIFICATION BY 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-324; SER-334; SER-362
RP AND THR-363, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334, AND IDENTIFICATION BY
RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-98; SER-170; SER-334
RP AND SER-376, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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).
CC -!- FUNCTION: Could be involved with bystin and trophinin in a cell
CC adhesion molecule complex that mediates an initial attachment of the
CC blastocyst to uterine epithelial cells at the time of the embryo
CC implantation.
CC -!- SUBUNIT: Directly binds bystin, and indirectly trophinin.
CC -!- INTERACTION:
CC Q12815; Q8N9N5: BANP; NbExp=3; IntAct=EBI-2349743, EBI-744695;
CC Q12815; Q13895: BYSL; NbExp=9; IntAct=EBI-2349743, EBI-358049;
CC Q12815; Q5BKX5-3: C19orf54; NbExp=3; IntAct=EBI-2349743, EBI-11976299;
CC Q12815; Q13627: DYRK1A; NbExp=4; IntAct=EBI-2349743, EBI-1053596;
CC Q12815; Q9Y463: DYRK1B; NbExp=7; IntAct=EBI-2349743, EBI-634187;
CC Q12815; Q15303: ERBB4; NbExp=3; IntAct=EBI-2349743, EBI-80371;
CC Q12815; O75420: GIGYF1; NbExp=3; IntAct=EBI-2349743, EBI-947774;
CC Q12815; Q15323: KRT31; NbExp=3; IntAct=EBI-2349743, EBI-948001;
CC Q12815; Q6A162: KRT40; NbExp=3; IntAct=EBI-2349743, EBI-10171697;
CC Q12815; Q15691: MAPRE1; NbExp=9; IntAct=EBI-2349743, EBI-1004115;
CC Q12815; Q9UPY8: MAPRE3; NbExp=7; IntAct=EBI-2349743, EBI-726739;
CC Q12815; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-2349743, EBI-22310682;
CC Q12815; O43482: OIP5; NbExp=3; IntAct=EBI-2349743, EBI-536879;
CC Q12815; Q05BL1: TP53BP2; NbExp=3; IntAct=EBI-2349743, EBI-11952721;
CC Q12815; Q12933: TRAF2; NbExp=5; IntAct=EBI-2349743, EBI-355744;
CC Q12815; P36406: TRIM23; NbExp=5; IntAct=EBI-2349743, EBI-740098;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q12815-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q12815-2; Sequence=VSP_042820, VSP_042821;
CC Name=3;
CC IsoId=Q12815-3; Sequence=VSP_055063;
CC -!- TISSUE SPECIFICITY: Strong expression at implantation sites. Was
CC exclusively localized to the apical side of the syncytiotrophoblast.
CC Also found in macrophages.
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DR EMBL; U04810; AAA79333.2; -; mRNA.
DR EMBL; AC125611; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471111; EAW58064.1; -; Genomic_DNA.
DR EMBL; BC011597; AAH11597.1; -; mRNA.
DR EMBL; BC018627; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC032583; AAH32583.1; -; mRNA.
DR CCDS; CCDS41779.1; -. [Q12815-2]
DR CCDS; CCDS61117.1; -. [Q12815-3]
DR CCDS; CCDS8784.1; -. [Q12815-1]
DR PIR; I38487; I38487.
DR RefSeq; NP_001094090.1; NM_001100620.1. [Q12815-2]
DR RefSeq; NP_001265253.1; NM_001278324.1. [Q12815-3]
DR RefSeq; NP_005471.3; NM_005480.3. [Q12815-1]
DR RefSeq; XP_011536027.1; XM_011537725.2.
DR AlphaFoldDB; Q12815; -.
DR SMR; Q12815; -.
DR BioGRID; 115341; 59.
DR DIP; DIP-52951N; -.
DR IntAct; Q12815; 38.
DR MINT; Q12815; -.
DR STRING; 9606.ENSP00000257909; -.
DR GlyGen; Q12815; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q12815; -.
DR PhosphoSitePlus; Q12815; -.
DR BioMuta; TROAP; -.
DR DMDM; 223634724; -.
DR EPD; Q12815; -.
DR jPOST; Q12815; -.
DR MassIVE; Q12815; -.
DR MaxQB; Q12815; -.
DR PaxDb; Q12815; -.
DR PeptideAtlas; Q12815; -.
DR PRIDE; Q12815; -.
DR ProteomicsDB; 28603; -.
DR ProteomicsDB; 58966; -. [Q12815-1]
DR ProteomicsDB; 58967; -. [Q12815-2]
DR Antibodypedia; 25932; 79 antibodies from 20 providers.
DR DNASU; 10024; -.
DR Ensembl; ENST00000257909.8; ENSP00000257909.3; ENSG00000135451.13. [Q12815-1]
DR Ensembl; ENST00000380327.9; ENSP00000369684.5; ENSG00000135451.13. [Q12815-2]
DR Ensembl; ENST00000548311.5; ENSP00000448313.1; ENSG00000135451.13. [Q12815-3]
DR GeneID; 10024; -.
DR KEGG; hsa:10024; -.
DR MANE-Select; ENST00000257909.8; ENSP00000257909.3; NM_005480.4; NP_005471.3.
DR UCSC; uc001rtv.5; human. [Q12815-1]
DR CTD; 10024; -.
DR DisGeNET; 10024; -.
DR GeneCards; TROAP; -.
DR HGNC; HGNC:12327; TROAP.
DR HPA; ENSG00000135451; Tissue enhanced (bone marrow, lymphoid tissue, testis).
DR MIM; 603872; gene.
DR neXtProt; NX_Q12815; -.
DR OpenTargets; ENSG00000135451; -.
DR PharmGKB; PA37003; -.
DR VEuPathDB; HostDB:ENSG00000135451; -.
DR eggNOG; ENOG502S991; Eukaryota.
DR GeneTree; ENSGT00390000012132; -.
DR HOGENOM; CLU_020167_0_0_1; -.
DR InParanoid; Q12815; -.
DR PhylomeDB; Q12815; -.
DR TreeFam; TF338049; -.
DR PathwayCommons; Q12815; -.
DR SignaLink; Q12815; -.
DR BioGRID-ORCS; 10024; 41 hits in 1081 CRISPR screens.
DR ChiTaRS; TROAP; human.
DR GeneWiki; TROAP; -.
DR GenomeRNAi; 10024; -.
DR Pharos; Q12815; Tbio.
DR PRO; PR:Q12815; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q12815; protein.
DR Bgee; ENSG00000135451; Expressed in oocyte and 137 other tissues.
DR ExpressionAtlas; Q12815; baseline and differential.
DR Genevisible; Q12815; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR InterPro; IPR026133; Tastin.
DR PANTHER; PTHR15289; PTHR15289; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cytoplasm; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..778
FT /note="Tastin"
FT /id="PRO_0000065636"
FT REPEAT 516..548
FT /note="1"
FT REPEAT 549..581
FT /note="2"
FT REPEAT 582..614
FT /note="3"
FT REPEAT 615..647
FT /note="4"
FT REGION 1..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..647
FT /note="4 X 33 AA approximate tandem repeats"
FT REGION 600..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..529
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..572
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..631
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 363
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 113..778
FT /note="EAPGTIEFVADPAALATILSGEGVKSCHLGRQPSLAKRVLVRGSQGGTTQRV
FT QGVRASAYLAPRTPTHRLDPARASCFSRLEGPGPRGRTLCPQRLQALISPSGPSFHPST
FT RPSFQELRRETAGSSRTSVSQASGLLLETPVQPAFSLPKGEREVVTHSDEGGVASLGLA
FT QRVPLRENREMSHTRDSHDSHLMPSPAPVAQPLPGHVVPCPSPFGRAQRVPSPGPPTLT
FT SYSVLRRLTVQPKTRFTPMPSTPRVQQAQWLRGVSPQSCSEDPALPWEQVAVRLFDQES
FT CIRSLEGSGKPPVATPSGPHSNRTPSLQEVKIQRIGILQQLLRQEVEGLVGGQCVPLNG
FT GSSLDMVELQPLLTEISRTLNATEHNSGTSHLPGLLKHSGLPKPCLPEECGEPQPCPPA
FT EPGPPEAFCRSEPEIPEPSLQEQLEVPEPYPPAEPRPLESCCRSEPEIPESSRQEQLEV
FT PEPCPPAEPRPLESYCRIEPEIPESSRQEQLEVPEPCPPAEPGPLQPSTQGQSGPPGPC
FT PRVELGASEPCTLEHRSLESSLPPCCSQWAPATTSLIFSSQHPLCASPPICSLQSLRPP
FT AGQAGLSNLAPRTLALRERLKSCLTAIHCFHEARLDDECAFYTSRAPPSGPTRVCTNPV
FT ATLLEWQDALCFIPVGSAAPQGSP -> GAMACTCNHSYSGG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055063"
FT VAR_SEQ 113..144
FT /note="EAPGTIEFVADPAALATILSGEGVKSCHLGRQ -> VLVPAPGKLFALRRSP
FT FPPAKCHLARCHGLYL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042820"
FT VAR_SEQ 145..778
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042821"
FT CONFLICT 224
FT /note="R -> H (in Ref. 1; AAA79333)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 778 AA; 83857 MW; 530B0481EC8D7E02 CRC64;
MTTRQATKDP LLRGVSPTPS KIPVRSQKRT PFPTVTSCAV DQENQDPRRW VQKPPLNIQR
PLVDSAGPRP KARHQAETSQ RLVGISQPRN PLEELRPSPR GQNVGPGPPA QTEAPGTIEF
VADPAALATI LSGEGVKSCH LGRQPSLAKR VLVRGSQGGT TQRVQGVRAS AYLAPRTPTH
RLDPARASCF SRLEGPGPRG RTLCPQRLQA LISPSGPSFH PSTRPSFQEL RRETAGSSRT
SVSQASGLLL ETPVQPAFSL PKGEREVVTH SDEGGVASLG LAQRVPLREN REMSHTRDSH
DSHLMPSPAP VAQPLPGHVV PCPSPFGRAQ RVPSPGPPTL TSYSVLRRLT VQPKTRFTPM
PSTPRVQQAQ WLRGVSPQSC SEDPALPWEQ VAVRLFDQES CIRSLEGSGK PPVATPSGPH
SNRTPSLQEV KIQRIGILQQ LLRQEVEGLV GGQCVPLNGG SSLDMVELQP LLTEISRTLN
ATEHNSGTSH LPGLLKHSGL PKPCLPEECG EPQPCPPAEP GPPEAFCRSE PEIPEPSLQE
QLEVPEPYPP AEPRPLESCC RSEPEIPESS RQEQLEVPEP CPPAEPRPLE SYCRIEPEIP
ESSRQEQLEV PEPCPPAEPG PLQPSTQGQS GPPGPCPRVE LGASEPCTLE HRSLESSLPP
CCSQWAPATT SLIFSSQHPL CASPPICSLQ SLRPPAGQAG LSNLAPRTLA LRERLKSCLT
AIHCFHEARL DDECAFYTSR APPSGPTRVC TNPVATLLEW QDALCFIPVG SAAPQGSP