TESP1_HUMAN
ID TESP1_HUMAN Reviewed; 521 AA.
AC A2RU30; B4DPM3; B4E048; B7Z9K7; O94849; Q4G0P2; Q9P0C4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Protein TESPA1;
DE AltName: Full=Thymocyte-expressed positive selection-associated protein 1;
GN Name=TESPA1; Synonyms=KIAA0748; ORFNames=HSPC257;
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), FUNCTION, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH PLCG1 AND GRB2.
RC TISSUE=T-cell;
RX PubMed=22561606; DOI=10.1038/ni.2301;
RA Wang D., Zheng M., Lei L., Ji J., Yao Y., Qiu Y., Ma L., Lou J., Ouyang C.,
RA Zhang X., He Y., Chi J., Wang L., Kuang Y., Wang J., Cao X., Lu L.;
RT "Tespa1 is involved in late thymocyte development through the regulation of
RT TCR-mediated signaling.";
RL Nat. Immunol. 13:560-568(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [3]
RP SEQUENCE REVISION.
RA Ohara O., Suyama M., Nagase T., Ishikawa K., Kikuno R.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Amygdala, Liver, and Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 349-521, AND VARIANT LYS-496.
RC TISSUE=Umbilical cord blood;
RA Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L.,
RA Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z.;
RT "Human partial CDS from CD34+ stem cells.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311, 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 INTERACTION WITH ITPR1, AND MUTAGENESIS OF PHE-185 AND PHE-186.
RX PubMed=23650607; DOI=10.1016/j.fob.2012.08.005;
RA Matsuzaki H., Fujimoto T., Ota T., Ogawa M., Tsunoda T., Doi K.,
RA Hamabashiri M., Tanaka M., Shirasawa S.;
RT "Tespa1 is a novel inositol 1,4,5-trisphosphate receptor binding protein in
RT T and B lymphocytes.";
RL FEBS Open Bio 2:255-259(2012).
RN [11]
RP INTERACTION WITH HSPA9, AND SUBCELLULAR LOCATION.
RX PubMed=23501103; DOI=10.1016/j.bbrc.2013.02.099;
RA Matsuzaki H., Fujimoto T., Tanaka M., Shirasawa S.;
RT "Tespa1 is a novel component of mitochondria-associated endoplasmic
RT reticulum membranes and affects mitochondrial calcium flux.";
RL Biochem. Biophys. Res. Commun. 433:322-326(2013).
CC -!- FUNCTION: Required for the development and maturation of T-cells, its
CC function being essential for the late stages of thymocyte development
CC (By similarity). Plays a role in T-cell antigen receptor (TCR)-mediated
CC activation of the ERK and NFAT signaling pathways, possibly by serving
CC as a scaffolding protein that promotes the assembly of the LAT
CC signalosome in thymocytes. May play a role in the regulation of
CC inositol 1,4,5-trisphosphate receptor-mediated Ca(2+) release and
CC mitochondrial Ca(2+) uptake via the mitochondria-associated endoplasmic
CC reticulum membrane (MAM) compartment. {ECO:0000250,
CC ECO:0000269|PubMed:22561606}.
CC -!- SUBUNIT: Interacts with PLCG1 and GRB2; the association is increased
CC with prolonged stimulation of the TCR and may facilitate the assembly
CC of the LAT signalosome. Interacts with ITPR1. Also interacts with ITPR3
CC (By similarity). Interacts with HSPA9. {ECO:0000250,
CC ECO:0000269|PubMed:22561606, ECO:0000269|PubMed:23501103,
CC ECO:0000269|PubMed:23650607}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22561606,
CC ECO:0000269|PubMed:23501103}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:23501103}. Note=May localize to mitochondria-
CC associated endoplasmic reticulum membrane (MAM).
CC {ECO:0000269|PubMed:23501103}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=A2RU30-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2RU30-2; Sequence=VSP_030488;
CC Name=3;
CC IsoId=A2RU30-3; Sequence=VSP_030488, VSP_030489;
CC -!- PTM: May be phosphorylated in response to store-operated Ca(+2) entry.
CC {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF28935.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB018291; BAA34468.2; -; mRNA.
DR EMBL; AK298405; BAG60635.1; -; mRNA.
DR EMBL; AK303223; BAG64310.1; -; mRNA.
DR EMBL; AK315972; BAH14343.1; -; mRNA.
DR EMBL; AC079842; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW96796.1; -; Genomic_DNA.
DR EMBL; CH471054; EAW96799.1; -; Genomic_DNA.
DR EMBL; BC044578; AAH44578.1; -; mRNA.
DR EMBL; BC132732; AAI32733.2; -; mRNA.
DR EMBL; BC132734; AAI32735.2; -; mRNA.
DR EMBL; AF161375; AAF28935.1; ALT_FRAME; mRNA.
DR CCDS; CCDS44913.1; -. [A2RU30-1]
DR CCDS; CCDS58240.1; -. [A2RU30-2]
DR RefSeq; NP_001092285.1; NM_001098815.2. [A2RU30-1]
DR RefSeq; NP_001129502.1; NM_001136030.2. [A2RU30-1]
DR RefSeq; NP_001248773.1; NM_001261844.1. [A2RU30-2]
DR RefSeq; NP_055611.1; NM_014796.2. [A2RU30-2]
DR RefSeq; XP_005269304.1; XM_005269247.2. [A2RU30-2]
DR RefSeq; XP_006719778.1; XM_006719715.3. [A2RU30-1]
DR RefSeq; XP_011537337.1; XM_011539035.2. [A2RU30-1]
DR RefSeq; XP_011537338.1; XM_011539036.1.
DR RefSeq; XP_011537339.1; XM_011539037.2. [A2RU30-1]
DR RefSeq; XP_016875751.1; XM_017020262.1. [A2RU30-1]
DR RefSeq; XP_016875752.1; XM_017020263.1. [A2RU30-1]
DR AlphaFoldDB; A2RU30; -.
DR BioGRID; 115176; 15.
DR IntAct; A2RU30; 14.
DR STRING; 9606.ENSP00000400892; -.
DR iPTMnet; A2RU30; -.
DR PhosphoSitePlus; A2RU30; -.
DR BioMuta; TESPA1; -.
DR MassIVE; A2RU30; -.
DR PaxDb; A2RU30; -.
DR PeptideAtlas; A2RU30; -.
DR PRIDE; A2RU30; -.
DR ProteomicsDB; 492; -. [A2RU30-1]
DR ProteomicsDB; 493; -. [A2RU30-2]
DR ProteomicsDB; 494; -. [A2RU30-3]
DR Antibodypedia; 48438; 86 antibodies from 24 providers.
DR DNASU; 9840; -.
DR Ensembl; ENST00000316577.12; ENSP00000312679.8; ENSG00000135426.16. [A2RU30-1]
DR Ensembl; ENST00000449076.6; ENSP00000400892.1; ENSG00000135426.16. [A2RU30-1]
DR Ensembl; ENST00000524622.5; ENSP00000435622.1; ENSG00000135426.16. [A2RU30-2]
DR Ensembl; ENST00000531122.5; ENSP00000433098.1; ENSG00000135426.16. [A2RU30-2]
DR Ensembl; ENST00000532804.5; ENSP00000432030.1; ENSG00000135426.16. [A2RU30-2]
DR GeneID; 9840; -.
DR KEGG; hsa:9840; -.
DR MANE-Select; ENST00000449076.6; ENSP00000400892.1; NM_001136030.3; NP_001129502.1.
DR UCSC; uc001sgl.5; human. [A2RU30-1]
DR CTD; 9840; -.
DR DisGeNET; 9840; -.
DR GeneCards; TESPA1; -.
DR HGNC; HGNC:29109; TESPA1.
DR HPA; ENSG00000135426; Tissue enhanced (brain, lymphoid tissue).
DR MIM; 615664; gene.
DR neXtProt; NX_A2RU30; -.
DR OpenTargets; ENSG00000135426; -.
DR PharmGKB; PA128394561; -.
DR VEuPathDB; HostDB:ENSG00000135426; -.
DR eggNOG; ENOG502QWSR; Eukaryota.
DR GeneTree; ENSGT00940000160763; -.
DR HOGENOM; CLU_040123_0_0_1; -.
DR InParanoid; A2RU30; -.
DR OMA; KAPCCTH; -.
DR PhylomeDB; A2RU30; -.
DR TreeFam; TF331566; -.
DR PathwayCommons; A2RU30; -.
DR SignaLink; A2RU30; -.
DR BioGRID-ORCS; 9840; 10 hits in 1078 CRISPR screens.
DR ChiTaRS; TESPA1; human.
DR GenomeRNAi; 9840; -.
DR Pharos; A2RU30; Tbio.
DR PRO; PR:A2RU30; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; A2RU30; protein.
DR Bgee; ENSG00000135426; Expressed in prefrontal cortex and 118 other tissues.
DR ExpressionAtlas; A2RU30; baseline and differential.
DR Genevisible; A2RU30; HS.
DR GO; GO:0008180; C:COP9 signalosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0036398; C:TCR signalosome; IEA:Ensembl.
DR GO; GO:0043274; F:phospholipase binding; IEA:Ensembl.
DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR GO; GO:0010387; P:COP9 signalosome assembly; ISS:UniProtKB.
DR GO; GO:0033089; P:positive regulation of T cell differentiation in thymus; ISS:UniProtKB.
DR GO; GO:0050862; P:positive regulation of T cell receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0008104; P:protein localization; IEA:Ensembl.
DR GO; GO:0033077; P:T cell differentiation in thymus; IEA:Ensembl.
DR GO; GO:0036399; P:TCR signalosome assembly; IEA:Ensembl.
DR InterPro; IPR029325; ITPR-bd.
DR InterPro; IPR026647; TESPA1.
DR InterPro; IPR043444; TESPA1-like.
DR PANTHER; PTHR17469; PTHR17469; 1.
DR PANTHER; PTHR17469:SF1; PTHR17469:SF1; 1.
DR Pfam; PF14722; KRAP_IP3R_bind; 1.
DR SMART; SM01257; KRAP_IP3R_bind; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Endoplasmic reticulum; Membrane;
KW Phosphoprotein; Reference proteome; Signalosome.
FT CHAIN 1..521
FT /note="Protein TESPA1"
FT /id="PRO_0000315219"
FT REGION 331..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 311
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT VAR_SEQ 1..138
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:9872452"
FT /id="VSP_030488"
FT VAR_SEQ 520..521
FT /note="DS -> FVKLSPPPQQHVV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030489"
FT VARIANT 496
FT /note="E -> K (in dbSNP:rs997173)"
FT /evidence="ECO:0000269|Ref.8"
FT /id="VAR_049513"
FT MUTAGEN 185
FT /note="F->A: Loss of ITPR1-binding."
FT /evidence="ECO:0000269|PubMed:23650607"
FT MUTAGEN 186
FT /note="F->A: Strong decrease in ITPR1-binding. Complete
FT loss of ITPR1-binding; when associated with A-185."
FT /evidence="ECO:0000269|PubMed:23650607"
FT CONFLICT 475
FT /note="R -> Q (in Ref. 7; AAH44578)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 521 AA; 59213 MW; E10A8FC0056909F3 CRC64;
MEASVLSPTS WEKRRAWLRQ SRNWQTQVLE EEAAAALQDV PDPEPSSLDD VFQEGNPINK
IEDWLQDCGY SEEGFSEEAG QFIYNGFCSH GTSFEDDLTL GAEATLLAAN GKLFSRSFLE
TARPCQLLDL GCSLASSSMT GGTNKTSSSI SEILDKVQED AEDVLFSLGF GQEDHKDTSR
IPARFFTTPS QAKGIDFQLF LKSQVRRIEM EDPCLMLASR FKQVQTLAVT ADAFFCLYSY
VSKTPVQKFT PSHMFWNCNH PTDVPSIRIL SREPEPQSPR DRLRKAISKM CLYTCPRDRP
PPPHNTPKRN SLDQVVLEVM DKVKEEKQFL QQDSDLGQFS QEDPVPPAEG KKLPTSPYPC
VFCCEEETQQ RMSTVLAPSQ TLDSNPKVPC CTHSLPIEDP QWSTDPAQIR RELCSLPATN
TETHPAKDET FWKRKSRARK SLFQKNLMGR KVKSLDLSIT QQKWKQSVDR PELRRSLSQQ
PQDTFDLEEV QSNSEEEQSQ SRWPSRPRHP HHHQTFAGKD S
