TPC11_HUMAN
ID TPC11_HUMAN Reviewed; 1133 AA.
AC Q7Z392; A4QPB8; B2RCD6; Q5U5I7; Q6FI73; Q86T25; Q9H0L1; Q9H5K9; Q9H8Q1;
AC Q9H9I7;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Trafficking protein particle complex subunit 11;
GN Name=TRAPPC11; Synonyms=C4orf41;
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] (ISOFORMS 1 AND 4).
RC TISSUE=Colon epithelium, and Endometrium;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 199-1133 (ISOFORM 1).
RC TISSUE=Ovary, and Trachea;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 319-1133 (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 298-1133 (ISOFORM 1).
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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-245, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [7]
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 [8]
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 [9]
RP VARIANT LGMDR18 ARG-980.
RX PubMed=23830518; DOI=10.1016/j.ajhg.2013.05.028;
RA Boegershausen N., Shahrzad N., Chong J.X., von Kleist-Retzow J.C.,
RA Stanga D., Li Y., Bernier F.P., Loucks C.M., Wirth R., Puffenberger E.G.,
RA Hegele R.A., Schreml J., Lapointe G., Keupp K., Brett C.L., Anderson R.,
RA Hahn A., Innes A.M., Suchowersky O., Mets M.B., Nuernberg G., McLeod D.R.,
RA Thiele H., Waggoner D., Altmueller J., Boycott K.M., Schoser B.,
RA Nuernberg P., Ober C., Heller R., Parboosingh J.S., Wollnik B., Sacher M.,
RA Lamont R.E.;
RT "Recessive TRAPPC11 mutations cause a disease spectrum of limb girdle
RT muscular dystrophy and myopathy with movement disorder and intellectual
RT disability.";
RL Am. J. Hum. Genet. 93:181-190(2013).
RN [10]
RP VARIANTS ALA-381 AND ALA-1104, INVOLVEMENT IN DISEASE, FUNCTION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=27862579; DOI=10.1002/humu.23145;
RA Matalonga L., Bravo M., Serra-Peinado C., Garcia-Pelegri E., Ugarteburu O.,
RA Vidal S., Llambrich M., Quintana E., Fuster-Jorge P., Gonzalez-Bravo M.N.,
RA Beltran S., Dopazo J., Garcia-Garcia F., Foulquier F., Matthijs G.,
RA Mills P., Ribes A., Egea G., Briones P., Tort F., Giros M.;
RT "Mutations in TRAPPC11 are associated with a congenital disorder of
RT glycosylation.";
RL Hum. Mutat. 38:148-151(2017).
CC -!- FUNCTION: Involved in endoplasmic reticulum to Golgi apparatus
CC trafficking at a very early stage. {ECO:0000269|PubMed:21525244,
CC ECO:0000269|PubMed:27862579}.
CC -!- SUBUNIT: Component of the multisubunit TRAPP (transport protein
CC particle) complex, which includes at least TRAPPC2, TRAPPC2L, TRAPPC3,
CC TRAPPC3L, TRAPPC4, TRAPPC5, TRAPPC8, TRAPPC9, TRAPPC10, TRAPPC11 and
CC TRAPPC12. {ECO:0000269|PubMed:21525244}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:27862579}.
CC Golgi apparatus, cis-Golgi network {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q7Z392-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z392-2; Sequence=VSP_035095, VSP_035098, VSP_035099;
CC Name=3;
CC IsoId=Q7Z392-3; Sequence=VSP_035098, VSP_035099;
CC Name=4;
CC IsoId=Q7Z392-4; Sequence=VSP_035096, VSP_035097;
CC -!- DISEASE: Muscular dystrophy, limb-girdle, autosomal recessive 18
CC (LGMDR18) [MIM:615356]: A form of limb-girdle muscular dystrophy
CC characterized by proximal muscle weakness with childhood onset,
CC resulting in gait abnormalities and scapular winging. Serum creatine
CC kinase is increased. A subset of patients may show a hyperkinetic
CC movement disorder with chorea, ataxia, or dystonia and global
CC developmental delay. {ECO:0000269|PubMed:23830518}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the TRAPPC11 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14240.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14556.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB15617.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG37533.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB66686.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAD91169.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAD97983.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL833571; CAD91169.1; ALT_INIT; mRNA.
DR EMBL; BX538044; CAD97983.1; ALT_INIT; mRNA.
DR EMBL; BC051724; AAH51724.1; -; mRNA.
DR EMBL; BC139745; AAI39746.1; -; mRNA.
DR EMBL; AK022778; BAB14240.1; ALT_INIT; mRNA.
DR EMBL; AK023390; BAB14556.1; ALT_INIT; mRNA.
DR EMBL; AK026992; BAB15617.1; ALT_SEQ; mRNA.
DR EMBL; AK315057; BAG37533.1; ALT_INIT; mRNA.
DR EMBL; CR533553; CAG38584.1; -; mRNA.
DR EMBL; AL136752; CAB66686.1; ALT_INIT; mRNA.
DR CCDS; CCDS34112.1; -. [Q7Z392-1]
DR CCDS; CCDS47166.1; -. [Q7Z392-3]
DR RefSeq; NP_068761.4; NM_021942.5. [Q7Z392-1]
DR RefSeq; NP_951008.1; NM_199053.2. [Q7Z392-3]
DR AlphaFoldDB; Q7Z392; -.
DR SMR; Q7Z392; -.
DR BioGRID; 121957; 73.
DR ComplexPortal; CPX-4750; TRAPP III complex, TRAPPC2 variant.
DR ComplexPortal; CPX-6903; TRAPP III complex, TRAPPC2B variant.
DR CORUM; Q7Z392; -.
DR DIP; DIP-48282N; -.
DR IntAct; Q7Z392; 12.
DR STRING; 9606.ENSP00000335371; -.
DR iPTMnet; Q7Z392; -.
DR PhosphoSitePlus; Q7Z392; -.
DR BioMuta; TRAPPC11; -.
DR DMDM; 205696378; -.
DR EPD; Q7Z392; -.
DR jPOST; Q7Z392; -.
DR MassIVE; Q7Z392; -.
DR MaxQB; Q7Z392; -.
DR PaxDb; Q7Z392; -.
DR PeptideAtlas; Q7Z392; -.
DR PRIDE; Q7Z392; -.
DR ProteomicsDB; 69012; -. [Q7Z392-1]
DR ProteomicsDB; 69013; -. [Q7Z392-2]
DR ProteomicsDB; 69014; -. [Q7Z392-3]
DR ProteomicsDB; 69015; -. [Q7Z392-4]
DR Antibodypedia; 55746; 43 antibodies from 9 providers.
DR DNASU; 60684; -.
DR Ensembl; ENST00000334690.11; ENSP00000335371.6; ENSG00000168538.16. [Q7Z392-1]
DR Ensembl; ENST00000357207.8; ENSP00000349738.4; ENSG00000168538.16. [Q7Z392-3]
DR GeneID; 60684; -.
DR KEGG; hsa:60684; -.
DR MANE-Select; ENST00000334690.11; ENSP00000335371.6; NM_021942.6; NP_068761.4.
DR UCSC; uc003ivw.3; human. [Q7Z392-1]
DR CTD; 60684; -.
DR DisGeNET; 60684; -.
DR GeneCards; TRAPPC11; -.
DR HGNC; HGNC:25751; TRAPPC11.
DR HPA; ENSG00000168538; Low tissue specificity.
DR MalaCards; TRAPPC11; -.
DR MIM; 614138; gene.
DR MIM; 615356; phenotype.
DR neXtProt; NX_Q7Z392; -.
DR OpenTargets; ENSG00000168538; -.
DR Orphanet; 369847; Intellectual disability-hyperkinetic movement-truncal ataxia syndrome.
DR Orphanet; 369840; TRAPPC11-related limb-girdle muscular dystrophy R18.
DR Orphanet; 869; Triple A syndrome.
DR PharmGKB; PA162379849; -.
DR VEuPathDB; HostDB:ENSG00000168538; -.
DR eggNOG; KOG4386; Eukaryota.
DR GeneTree; ENSGT00390000006550; -.
DR HOGENOM; CLU_003649_0_0_1; -.
DR InParanoid; Q7Z392; -.
DR OMA; VFEGCLR; -.
DR OrthoDB; 1065648at2759; -.
DR PhylomeDB; Q7Z392; -.
DR TreeFam; TF314022; -.
DR PathwayCommons; Q7Z392; -.
DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR SignaLink; Q7Z392; -.
DR BioGRID-ORCS; 60684; 740 hits in 1087 CRISPR screens.
DR ChiTaRS; TRAPPC11; human.
DR GenomeRNAi; 60684; -.
DR Pharos; Q7Z392; Tbio.
DR PRO; PR:Q7Z392; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q7Z392; protein.
DR Bgee; ENSG00000168538; Expressed in calcaneal tendon and 187 other tissues.
DR ExpressionAtlas; Q7Z392; baseline and differential.
DR Genevisible; Q7Z392; HS.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0030008; C:TRAPP complex; IMP:UniProtKB.
DR GO; GO:1990072; C:TRAPPIII protein complex; IC:ComplexPortal.
DR GO; GO:0045054; P:constitutive secretory pathway; IMP:UniProtKB.
DR GO; GO:0048208; P:COPII vesicle coating; IC:ComplexPortal.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
DR GO; GO:0061635; P:regulation of protein complex stability; IMP:UniProtKB.
DR GO; GO:0099022; P:vesicle tethering; IC:ComplexPortal.
DR InterPro; IPR021773; TPC11.
DR InterPro; IPR025876; TRAPPC11_C.
DR Pfam; PF11817; Foie-gras_1; 1.
DR Pfam; PF12742; Gryzun-like; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Disease variant; ER-Golgi transport;
KW Golgi apparatus; Limb-girdle muscular dystrophy; Reference proteome;
KW Transport.
FT CHAIN 1..1133
FT /note="Trafficking protein particle complex subunit 11"
FT /id="PRO_0000348072"
FT MOD_RES 245
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 1..656
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_035095"
FT VAR_SEQ 962..1018
FT /note="CFCLQCPSLGNIEGGVATGHYIISWKRTSAMENIPIITTVITLPHVIVENIP
FT LHVNA -> LYYLLEKDLSNGEYPHHHNCHHSAARDCGEYPSPCECRSAVIWACQRVVT
FT CQVSPTE (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_035096"
FT VAR_SEQ 1019..1133
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_035097"
FT VAR_SEQ 1067..1086
FT /note="RILPGTEQEMLYNFYPLMAG -> PAQAFYTYQYFCQATGSTHG (in
FT isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_035098"
FT VAR_SEQ 1087..1133
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_035099"
FT VARIANT 381
FT /note="P -> A (found in a patient with congenital disorder
FT of glycosylation; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:27862579"
FT /id="VAR_078126"
FT VARIANT 980
FT /note="G -> R (in LGMDR18; dbSNP:rs397509417)"
FT /evidence="ECO:0000269|PubMed:23830518"
FT /id="VAR_070158"
FT VARIANT 1104
FT /note="T -> A (found in a patient with congenital disorder
FT of glycosylation; unknown pathological significance;
FT dbSNP:rs78663235)"
FT /evidence="ECO:0000269|PubMed:27862579"
FT /id="VAR_078127"
FT CONFLICT 70
FT /note="T -> A (in Ref. 2; AAH51724)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="Q -> L (in Ref. 2; AAH51724)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="S -> F (in Ref. 2; AAH51724)"
FT /evidence="ECO:0000305"
FT CONFLICT 397
FT /note="W -> R (in Ref. 3; BAG37533)"
FT /evidence="ECO:0000305"
FT CONFLICT 467
FT /note="K -> E (in Ref. 2; AAH51724)"
FT /evidence="ECO:0000305"
FT CONFLICT 544
FT /note="N -> K (in Ref. 3; BAB15617)"
FT /evidence="ECO:0000305"
FT CONFLICT 660
FT /note="V -> L (in Ref. 2; AAH51724)"
FT /evidence="ECO:0000305"
FT CONFLICT 661
FT /note="P -> L (in Ref. 3; BAB15617)"
FT /evidence="ECO:0000305"
FT CONFLICT 697
FT /note="R -> K (in Ref. 4; CAG38584)"
FT /evidence="ECO:0000305"
FT CONFLICT 723..744
FT /note="Missing (in Ref. 3; BAB14556)"
FT /evidence="ECO:0000305"
FT CONFLICT 812
FT /note="T -> P (in Ref. 1; CAD91169, 4; CAG38584 and 5;
FT CAB66686)"
FT /evidence="ECO:0000305"
FT CONFLICT 842
FT /note="Y -> C (in Ref. 3; BAB15617)"
FT /evidence="ECO:0000305"
FT CONFLICT 865
FT /note="V -> I (in Ref. 3; BAB14240)"
FT /evidence="ECO:0000305"
FT CONFLICT 869
FT /note="E -> G (in Ref. 3; BAB14556)"
FT /evidence="ECO:0000305"
FT CONFLICT 1011
FT /note="N -> S (in Ref. 3; BAB14240)"
FT /evidence="ECO:0000305"
FT CONFLICT 1030
FT /note="L -> S (in Ref. 3; BAB14556)"
FT /evidence="ECO:0000305"
FT CONFLICT 1112
FT /note="I -> L (in Ref. 1; CAD97983)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1133 AA; 128881 MW; 6048FB396E946D4A CRC64;
MSPTQWDFPV ELCCRPMAFV TLTGLDVVYN AVHRAVWDAF CANRRADRVP ISFKVLPGDH
EYPKCRPKRT SYEWYIPKGI LKTGWMNKHL NLVPALVVVF YELDWDEPQW KEKQSECATR
VEIVRQSLQG RNTKVAVVLI QKKTPLPPGE DVIASERAAA LCNACELSGK SLFVLPHTDH
LVGYIIRLEN AFYEHAQTYY YTEIRRVKSH KEFLNKTTHQ LLFVRHQFKI AFFSELKQDT
QNALKNYRTA YNLVHELRAH ETNILEIKTM AGFINYKICR LCFQHNTPLD AIAQFRKHID
LCKKKIGSAE LSFEHDAWMS KQFQAFGDLF DEAIKLGLTA IQTQNPGFYY QQAAYYAQER
KQLAKTLCNH EASVMYPNPD PLETQTGVLD FYGQRSWRQG ILSFDLSDPE KEKVGILAIQ
LKERNVVHSE IIITLLSNAV AQFKKYKCPR MKSHLMVQMG EEYYYAKDYT KALKLLDYVM
CDYRSEGWWT LLTSVLTTAL KCSYLMAQLK DYITYSLELL GRASTLKDDQ KSRIEKNLIN
VLMNESPDPE PDCDILAVKT AQKLWADRIS LAGSNIFTIG VQDFVPFVQC KAKFHAPSFH
VDVPVQFDIY LKADCPHPIR FSKLCVSFNN QEYNQFCVIE EASKANEVLE NLTQGKMCLV
PGKTRKLLFK FVAKTEDVGK KIEITSVDLA LGNETGRCVV LNWQGGGGDA ASSQEALQAA
RSFKRRPKLP DNEVHWDSII IQASTMIISR VPNISVHLLH EPPALTNEMY CLVVTVQSHE
KTQIRDVKLT AGLKPGQDAN LTQKTHVTLH GTELCDESYP ALLTDIPVGD LHPGEQLEKM
LYVRCGTVGS RMFLVYVSYL INTTVEEKEI VCKCHKDETV TIETVFPFDV AVKFVSTKFE
HLERVYADIP FLLMTDLLSA SPWALTIVSS ELQLAPSMTT VDQLESQVDN VILQTGESAS
ECFCLQCPSL GNIEGGVATG HYIISWKRTS AMENIPIITT VITLPHVIVE NIPLHVNADL
PSFGRVRESL PVKYHLQNKT DLVQDVEISV EPSDAFMFSG LKQIRLRILP GTEQEMLYNF
YPLMAGYQQL PSLNINLLRF PNFTNQLLRR FIPTSIFVKP QGRLMDDTSI AAA
