TPPC8_HUMAN
ID TPPC8_HUMAN Reviewed; 1435 AA.
AC Q9Y2L5; A0JP15; B3KME5; Q9H0L2;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Trafficking protein particle complex subunit 8;
DE AltName: Full=Protein TRS85 homolog;
GN Name=TRAPPC8; Synonyms=KIAA1012;
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] (ISOFORM 1), AND VARIANTS SER-137
RP AND ALA-1146.
RC TISSUE=Brain;
RX PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:63-70(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT SER-137.
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 54-1435 (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 427-1435 (ISOFORM 1).
RC TISSUE=Teratocarcinoma;
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 [6]
RP IDENTIFICATION IN TRAPP COMPLEX.
RX PubMed=11805826; DOI=10.1038/415141a;
RA Gavin A.-C., Boesche M., Krause R., Grandi P., Marzioch M., Bauer A.,
RA Schultz J., Rick J.M., Michon A.-M., Cruciat C.-M., Remor M., Hoefert C.,
RA Schelder M., Brajenovic M., Ruffner H., Merino A., Klein K., Hudak M.,
RA Dickson D., Rudi T., Gnau V., Bauch A., Bastuck S., Huhse B., Leutwein C.,
RA Heurtier M.-A., Copley R.R., Edelmann A., Querfurth E., Rybin V.,
RA Drewes G., Raida M., Bouwmeester T., Bork P., Seraphin B., Kuster B.,
RA Neubauer G., Superti-Furga G.;
RT "Functional organization of the yeast proteome by systematic analysis of
RT protein complexes.";
RL Nature 415:141-147(2002).
RN [7]
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 [8]
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 [9]
RP FUNCTION, AND IDENTIFICATION IN TRAPP COMPLEX.
RX PubMed=21525244; DOI=10.1091/mbc.e10-11-0873;
RA Scrivens P.J., Noueihed B., Shahrzad N., Hul S., Brunet S., Sacher M.;
RT "C4orf41 and TTC-15 are mammalian TRAPP components with a role at an early
RT stage in ER-to-Golgi trafficking.";
RL Mol. Biol. Cell 22:2083-2093(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-273, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279 AND SER-309, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-273, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP FUNCTION, INTERACTION WITH TBC1D14, AND SUBCELLULAR LOCATION.
RX PubMed=26711178; DOI=10.15252/embj.201592695;
RA Lamb C.A., Nuehlen S., Judith D., Frith D., Snijders A.P., Behrends C.,
RA Tooze S.A.;
RT "TBC1D14 regulates autophagy via the TRAPP complex and ATG9 traffic.";
RL EMBO J. 35:281-301(2016).
RN [14]
RP VARIANT [LARGE SCALE ANALYSIS] GLN-537.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Plays a role in endoplasmic reticulum to Golgi apparatus
CC trafficking at a very early stage (PubMed:21525244). Maintains together
CC with TBC1D14 the cycling pool of ATG9 required for initiation of
CC autophagy (PubMed:26711178). {ECO:0000269|PubMed:21525244,
CC ECO:0000269|PubMed:26711178}.
CC -!- SUBUNIT: Component of the multisubunit TRAPP (transport protein
CC particle) complex, which includes TRAPPC2, TRAPPC2L, TRAPPC3, TRAPPC3L,
CC TRAPPC4, TRAPPC5, TRAPPC8, TRAPPC9, TRAPPC10, TRAPPC11 and TRAPPC12.
CC Interacts with TBC1D14 (PubMed:26711178). {ECO:0000269|PubMed:11805826,
CC ECO:0000269|PubMed:21525244, ECO:0000269|PubMed:26711178}.
CC -!- INTERACTION:
CC Q9Y2L5; A5PLN9: TRAPPC13; NbExp=2; IntAct=EBI-2820056, EBI-2857298;
CC Q9Y2L5; O43617: TRAPPC3; NbExp=2; IntAct=EBI-2820056, EBI-743566;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y2L5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y2L5-2; Sequence=VSP_014454, VSP_004000;
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TRS85 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI27110.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI27111.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA76856.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG50957.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB023229; BAA76856.2; ALT_INIT; mRNA.
DR EMBL; AL136749; CAB66683.2; -; mRNA.
DR EMBL; AC009831; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC022960; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC127109; AAI27110.1; ALT_INIT; mRNA.
DR EMBL; BC127110; AAI27111.1; ALT_INIT; mRNA.
DR EMBL; AK001662; BAG50957.1; ALT_INIT; mRNA.
DR CCDS; CCDS11901.1; -. [Q9Y2L5-1]
DR RefSeq; NP_055754.2; NM_014939.3. [Q9Y2L5-1]
DR AlphaFoldDB; Q9Y2L5; -.
DR SMR; Q9Y2L5; -.
DR BioGRID; 116545; 65.
DR ComplexPortal; CPX-4750; TRAPP III complex, TRAPPC2 variant.
DR ComplexPortal; CPX-6903; TRAPP III complex, TRAPPC2B variant.
DR CORUM; Q9Y2L5; -.
DR DIP; DIP-48280N; -.
DR IntAct; Q9Y2L5; 21.
DR MINT; Q9Y2L5; -.
DR STRING; 9606.ENSP00000283351; -.
DR GlyConnect; 1829; 3 N-Linked glycans (1 site).
DR GlyGen; Q9Y2L5; 1 site, 4 N-linked glycans (1 site).
DR iPTMnet; Q9Y2L5; -.
DR PhosphoSitePlus; Q9Y2L5; -.
DR BioMuta; TRAPPC8; -.
DR DMDM; 296452850; -.
DR EPD; Q9Y2L5; -.
DR jPOST; Q9Y2L5; -.
DR MassIVE; Q9Y2L5; -.
DR MaxQB; Q9Y2L5; -.
DR PaxDb; Q9Y2L5; -.
DR PeptideAtlas; Q9Y2L5; -.
DR PRIDE; Q9Y2L5; -.
DR ProteomicsDB; 85834; -. [Q9Y2L5-1]
DR ProteomicsDB; 85835; -. [Q9Y2L5-2]
DR Antibodypedia; 48760; 13 antibodies from 9 providers.
DR DNASU; 22878; -.
DR Ensembl; ENST00000283351.10; ENSP00000283351.4; ENSG00000153339.15. [Q9Y2L5-1]
DR GeneID; 22878; -.
DR KEGG; hsa:22878; -.
DR MANE-Select; ENST00000283351.10; ENSP00000283351.4; NM_014939.5; NP_055754.3.
DR UCSC; uc002kxc.5; human. [Q9Y2L5-1]
DR CTD; 22878; -.
DR DisGeNET; 22878; -.
DR GeneCards; TRAPPC8; -.
DR HGNC; HGNC:29169; TRAPPC8.
DR HPA; ENSG00000153339; Low tissue specificity.
DR MIM; 614136; gene.
DR neXtProt; NX_Q9Y2L5; -.
DR OpenTargets; ENSG00000153339; -.
DR PharmGKB; PA165429149; -.
DR VEuPathDB; HostDB:ENSG00000153339; -.
DR eggNOG; KOG1938; Eukaryota.
DR GeneTree; ENSGT00390000000568; -.
DR HOGENOM; CLU_004823_2_0_1; -.
DR InParanoid; Q9Y2L5; -.
DR OMA; NPNVWAN; -.
DR OrthoDB; 625387at2759; -.
DR PhylomeDB; Q9Y2L5; -.
DR TreeFam; TF106128; -.
DR PathwayCommons; Q9Y2L5; -.
DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR SignaLink; Q9Y2L5; -.
DR BioGRID-ORCS; 22878; 776 hits in 1087 CRISPR screens.
DR ChiTaRS; TRAPPC8; human.
DR GeneWiki; KIAA1012; -.
DR GenomeRNAi; 22878; -.
DR Pharos; Q9Y2L5; Tdark.
DR PRO; PR:Q9Y2L5; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q9Y2L5; protein.
DR Bgee; ENSG00000153339; Expressed in hair follicle and 209 other tissues.
DR ExpressionAtlas; Q9Y2L5; baseline and differential.
DR Genevisible; Q9Y2L5; HS.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000407; C:phagophore assembly site; IBA:GO_Central.
DR GO; GO:0030008; C:TRAPP complex; IDA:UniProtKB.
DR GO; GO:1990072; C:TRAPPIII protein complex; IBA:GO_Central.
DR GO; GO:0048208; P:COPII vesicle coating; IC:ComplexPortal.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
DR GO; GO:0034497; P:protein localization to phagophore assembly site; IBA:GO_Central.
DR GO; GO:0099022; P:vesicle tethering; IC:ComplexPortal.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR024420; TRAPP_III_complex_Trs85.
DR PANTHER; PTHR12975; PTHR12975; 1.
DR Pfam; PF12739; TRAPPC-Trs85; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ER-Golgi transport; Golgi apparatus; Phosphoprotein;
KW Reference proteome; Transport.
FT CHAIN 1..1435
FT /note="Trafficking protein particle complex subunit 8"
FT /id="PRO_0000065641"
FT REGION 301..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 916..926
FT /note="VFFIHFPTGLL -> TLALAQEVNQR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11230166"
FT /id="VSP_014454"
FT VAR_SEQ 927..1002
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11230166"
FT /id="VSP_004000"
FT VARIANT 74
FT /note="N -> S (in dbSNP:rs34292533)"
FT /id="VAR_057814"
FT VARIANT 137
FT /note="L -> S (in dbSNP:rs6506948)"
FT /evidence="ECO:0000269|PubMed:10231032,
FT ECO:0000269|PubMed:11230166"
FT /id="VAR_060250"
FT VARIANT 517
FT /note="S -> G (in dbSNP:rs17857486)"
FT /id="VAR_060251"
FT VARIANT 537
FT /note="R -> Q (in a breast cancer sample; somatic mutation;
FT dbSNP:rs754569032)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036270"
FT VARIANT 708
FT /note="Q -> E (in dbSNP:rs16962530)"
FT /id="VAR_057815"
FT VARIANT 954
FT /note="R -> H (in dbSNP:rs2170562)"
FT /id="VAR_060252"
FT VARIANT 1146
FT /note="T -> A (in dbSNP:rs3737374)"
FT /evidence="ECO:0000269|PubMed:10231032"
FT /id="VAR_060253"
FT VARIANT 1189
FT /note="I -> V (in dbSNP:rs36034613)"
FT /id="VAR_057816"
FT VARIANT 1298
FT /note="S -> P (in dbSNP:rs633500)"
FT /id="VAR_060254"
FT CONFLICT 251
FT /note="K -> E (in Ref. 2; CAB66683)"
FT /evidence="ECO:0000305"
FT CONFLICT 631
FT /note="E -> G (in Ref. 5; BAG50957)"
FT /evidence="ECO:0000305"
FT CONFLICT 1060
FT /note="P -> T (in Ref. 5; BAG50957)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1435 AA; 160997 MW; A6D60A7C9E65F46D CRC64;
MAQCVQSVQE LIPDSFVPCV AALCSDEAER LTRLNHLSFA ELLKPFSRLT SEVHMRDPNN
QLHVIKNLKI AVSNIVTQPP QPGAIRKLLN DVVSGSQPAE GLVANVITAG DYDLNISATT
PWFESYRETF LQSMPALDHE FLNHYLACML VASSSEAEPV EQFSKLSQEQ HRIQHNSDYS
YPKWFIPNTL KYYVLLHDVS AGDEQRAESI YEEMKQKYGT QGCYLLKINS RTSNRASDEQ
IPDPWSQYLQ KNSIQNQESY EDGPCTITSN KNSDNNLLSL DGLDNEVKDG LPNNFRAHPL
QLEQSSDPSN SIDGPDHLRS ASSLHETKKG NTGIIHGACL TLTDHDRIRQ FIQEFTFRGL
LPHIEKTIRQ LNDQLISRKG LSRSLFSATK KWFSGSKVPE KSINDLKNTS GLLYPPEAPE
LQIRKMADLC FLVQHYDLAY SCYHTAKKDF LNDQAMLYAA GALEMAAVSA FLQPGAPRPY
PAHYMDTAIQ TYRDICKNMV LAERCVLLSA ELLKSQSKYS EAAALLIRLT SEDSDLRSAL
LLEQAAHCFI NMKSPMVRKY AFHMILAGHR FSKAGQKKHA LRCYCQAMQV YKGKGWSLAE
DHINFTIGRQ SYTLRQLDNA VSAFRHILIN ESKQSAAQQG AFLREYLYVY KNVSQLSPDG
PLPQLPLPYI NSSATRVFFG HDRRPADGEK QAATHVSLDQ EYDSESSQQW RELEEQVVSV
VNKGVIPSNF HPTQYCLNSY SDNSRFPLAV VEEPITVEVA FRNPLKVLLL LTDLSLLWKF
HPKDFSGKDN EEVKQLVTSE PEMIGAEVIS EFLINGEESK VARLKLFPHH IGELHILGVV
YNLGTIQGSM TVDGIGALPG CHTGKYSLSM SVRGKQDLEI QGPRLNNTKE EKTSVKYGPD
RRLDPIITEE MPLLEVFFIH FPTGLLCGEI RKAYVEFVNV SKCPLTGLKV VSKRPEFFTF
GGNTAVLTPL SPSASENCSA YKTVVTDATS VCTALISSAS SVDFGIGTGS QPEVIPVPLP
DTVLLPGASV QLPMWLRGPD EEGVHEINFL FYYESVKKQP KIRHRILRHT AIICTSRSLN
VRATVCRSNS LENEEGRGGN MLVFVDVENT NTSEAGVKEF HIVQVSSSSK HWKLQKSVNL
SENKDTKLAS REKGKFCFKA IRCEKEEAAT QSSEKYTFAD IIFGNEQIIS SASPCADFFY
RSLSSELKKP QAHLPVHTEK QSTEDAVRLI QKCSEVDLNI VILWKAYVVE DSKQLILEGQ
HHVILRTIGK EAFSYPQKQE PPEMELLKFF RPENITVSSR PSVEQLSSLI KTSLHYPESF
NHPFHQKSLC LVPVTLLLSN CSKADVDVIV DLRHKTTSPE ALEIHGSFTW LGQTQYKLQL
KSQEIHSLQL KACFVHTGVY NLGTPRVFAK LSDQVTVFET SQQNSMPALI IISNV
