IF4G3_MOUSE
ID IF4G3_MOUSE Reviewed; 1579 AA.
AC Q80XI3; Q6GQV5; Q80Y69; Q8BJ68; Q8BQF3; Q8C6Q3; Q8CIH0;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Eukaryotic translation initiation factor 4 gamma 3;
DE Short=eIF-4-gamma 3;
DE Short=eIF-4G 3;
DE Short=eIF4G 3;
DE AltName: Full=eIF-4-gamma II;
DE Short=eIF4GII;
GN Name=Eif4g3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-217 AND 807-1579 (ISOFORM 2),
RP AND NUCLEOTIDE SEQUENCE OF 1-135 (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Adipose tissue, Head, and Oviduct;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 164-492.
RG The MGC Project Team;
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
RC STRAIN=C57BL/6J, and FVB/N;
RC TISSUE=Brain, Colon, Kidney, Liver, and Mammary tumor;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-168; SER-267; SER-470 AND
RP SER-472, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-472, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-267; SER-436; SER-470 AND
RP SER-472, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Probable component of the protein complex eIF4F, which is
CC involved in the recognition of the mRNA cap, ATP-dependent unwinding of
CC 5'-terminal secondary structure and recruitment of mRNA to the
CC ribosome. Thought to be a functional homolog of EIF4G1 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with EIF4A, EIF4E, eIF3 and PABPC1. Part of a
CC complex with EIF4E. eIF4F is a multi-subunit complex, the composition
CC of which varies with external and internal environmental conditions. It
CC is composed of at least EIF4A, EIF4E and EIF4G1/EIF4G3. EIF4G1/EIF4G3
CC interacts through its C-terminus with the serine/threonine kinases
CC MKNK1, and with MKNK2. Appears to act as a scaffold protein, holding
CC these enzymes in place to phosphorylate eIF4E. Non-phosphorylated
CC EIF4EBP1 competes with EIF4G1/EIFG3 to interact with EIF4E; insulin
CC stimulated MAP-kinase (MAPK1 and MAPK3) phosphorylation of EIF4EBP1
CC causes dissociation of the complex allowing EIF4G1/EIF4G3 to bind and
CC consequent initiation of translation. EIF4G1/EIF4G3 interacts with
CC PABPC1 to bring about circularization of the mRNA (By similarity).
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q80XI3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80XI3-2; Sequence=VSP_010491;
CC Name=3;
CC IsoId=Q80XI3-3; Sequence=VSP_010490;
CC Name=4;
CC IsoId=Q80XI3-4; Sequence=VSP_026029, VSP_010491;
CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4G family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH23898.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH23898.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
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DR EMBL; AK029440; BAC26452.1; -; mRNA.
DR EMBL; AK050887; BAC34445.1; -; mRNA.
DR EMBL; AK054068; BAC35644.1; -; mRNA.
DR EMBL; CB522417; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CF743072; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC023898; AAH23898.1; ALT_INIT; mRNA.
DR EMBL; BC047531; AAH47531.1; -; mRNA.
DR EMBL; BC048848; AAH48848.1; -; mRNA.
DR EMBL; BC057913; AAH57913.1; -; mRNA.
DR EMBL; BC072600; AAH72600.1; -; mRNA.
DR CCDS; CCDS38926.1; -. [Q80XI3-4]
DR RefSeq; NP_766291.2; NM_172703.3.
DR AlphaFoldDB; Q80XI3; -.
DR SMR; Q80XI3; -.
DR BioGRID; 231042; 6.
DR ComplexPortal; CPX-5864; Eukaryotic translation initiation factor 4F, EIF4A2 and EIF4G3 variant.
DR ComplexPortal; CPX-5865; Eukaryotic translation initiation factor 4F, EIF4A1 and EIF4G3 variant.
DR IntAct; Q80XI3; 2.
DR STRING; 10090.ENSMUSP00000081233; -.
DR iPTMnet; Q80XI3; -.
DR PhosphoSitePlus; Q80XI3; -.
DR SwissPalm; Q80XI3; -.
DR EPD; Q80XI3; -.
DR jPOST; Q80XI3; -.
DR MaxQB; Q80XI3; -.
DR PaxDb; Q80XI3; -.
DR PeptideAtlas; Q80XI3; -.
DR PRIDE; Q80XI3; -.
DR ProteomicsDB; 267100; -. [Q80XI3-1]
DR ProteomicsDB; 267101; -. [Q80XI3-2]
DR ProteomicsDB; 267102; -. [Q80XI3-3]
DR ProteomicsDB; 267103; -. [Q80XI3-4]
DR DNASU; 230861; -.
DR GeneID; 230861; -.
DR KEGG; mmu:230861; -.
DR UCSC; uc008vka.2; mouse. [Q80XI3-4]
DR UCSC; uc008vkb.2; mouse. [Q80XI3-2]
DR CTD; 8672; -.
DR MGI; MGI:1923935; Eif4g3.
DR eggNOG; KOG0401; Eukaryota.
DR InParanoid; Q80XI3; -.
DR OrthoDB; 594395at2759; -.
DR PhylomeDB; Q80XI3; -.
DR Reactome; R-MMU-1169408; ISG15 antiviral mechanism.
DR BioGRID-ORCS; 230861; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Eif4g3; mouse.
DR PRO; PR:Q80XI3; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q80XI3; protein.
DR GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0000339; F:RNA cap binding; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR GO; GO:0060903; P:positive regulation of meiosis I; IMP:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:MGI.
DR GO; GO:0045727; P:positive regulation of translation; IMP:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR GO; GO:0006412; P:translation; IMP:MGI.
DR GO; GO:0006413; P:translational initiation; IC:ComplexPortal.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR037585; EIF4G3.
DR InterPro; IPR045208; IF4G.
DR InterPro; IPR003891; Initiation_fac_eIF4g_MI.
DR InterPro; IPR003890; MIF4G-like_typ-3.
DR InterPro; IPR003307; W2_domain.
DR PANTHER; PTHR23253; PTHR23253; 1.
DR PANTHER; PTHR23253:SF23; PTHR23253:SF23; 1.
DR Pfam; PF02847; MA3; 1.
DR Pfam; PF02854; MIF4G; 1.
DR Pfam; PF02020; W2; 1.
DR SMART; SM00515; eIF5C; 1.
DR SMART; SM00544; MA3; 1.
DR SMART; SM00543; MIF4G; 1.
DR SUPFAM; SSF48371; SSF48371; 3.
DR PROSITE; PS51366; MI; 1.
DR PROSITE; PS51363; W2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Initiation factor; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; Repeat; RNA-binding;
KW Translation regulation.
FT CHAIN 1..1579
FT /note="Eukaryotic translation initiation factor 4 gamma 3"
FT /id="PRO_0000213330"
FT REPEAT 740..778
FT /note="HEAT 1"
FT DOMAIN 750..978
FT /note="MIF4G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT REPEAT 779..826
FT /note="HEAT 2"
FT REPEAT 827..900
FT /note="HEAT 3"
FT REPEAT 901..939
FT /note="HEAT 4"
FT REPEAT 940..979
FT /note="HEAT 5"
FT DOMAIN 1215..1337
FT /note="MI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT DOMAIN 1410..1579
FT /note="W2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00695"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..162
FT /note="PABPC1-binding"
FT /evidence="ECO:0000250"
FT REGION 454..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..625
FT /note="EIF4E-binding"
FT /evidence="ECO:0000250"
FT REGION 681..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..1014
FT /note="eIF3/EIF4A-binding"
FT /evidence="ECO:0000250"
FT REGION 724..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 855..875
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1009..1037
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1067..1214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1427..1579
FT /note="EIF4A-binding"
FT /evidence="ECO:0000250"
FT REGION 1565..1579
FT /note="Necessary but not sufficient for MKNK1-binding"
FT /evidence="ECO:0000250"
FT COILED 989..1018
FT /evidence="ECO:0000255"
FT COILED 1154..1176
FT /evidence="ECO:0000255"
FT COILED 1406..1438
FT /evidence="ECO:0000255"
FT COMPBIAS 20..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..187
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..474
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..536
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..570
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1009..1024
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1081..1100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1155..1169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1182..1196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 168
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43432"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43432"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 470
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 472
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43432"
FT MOD_RES 1150
FT /note="Phosphoserine; by CaMK1"
FT /evidence="ECO:0000250|UniProtKB:O43432"
FT MOD_RES 1212
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43432"
FT VAR_SEQ 10
FT /note="P -> PFAAGPRPAHHQGGFRPIQ (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026029"
FT VAR_SEQ 11
FT /note="F -> FAAGPRPAHHQF (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_010490"
FT VAR_SEQ 1084..1102
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_010491"
FT CONFLICT 183
FT /note="Missing (in Ref. 2; CF743072)"
FT /evidence="ECO:0000305"
FT CONFLICT 410
FT /note="A -> G (in Ref. 2; CF743072)"
FT /evidence="ECO:0000305"
FT CONFLICT 492
FT /note="A -> P (in Ref. 2; CB522417)"
FT /evidence="ECO:0000305"
FT CONFLICT 1324
FT /note="E -> G (in Ref. 1; BAC26452 and 3; AAH72600)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1579 AA; 174890 MW; EB4854590D250450 CRC64;
MNSQPQARSP FFQRPQIQPP RAAIPNSSPS IRPGVQTPTA VYQANQHIMM VNHLPMPYPV
TQGHQYCIPQ YRHSGPPYVG PPQQYPVQPP GPGPFYPGPG PGDFANAYGT PFYPSQPVYQ
SAPIIVPTQQ QPPPAKREKK TIRIRDPNQG GKDITEEIMS GGGSRNPTPP IGRPASTPTP
PQQLPSQVPE HSPVVYGTVE SAHLAASTPV TAASDQKQEE KPKPDPVFQS PSTVLRLVLS
GEKKEQAGQM PETAAGEPTP EPPRTSSPTS LPPLARSSLP SPMSAALSSQ PLFTAEDKCE
LPSSKEEDAP PVPSPTSCTA ASGPSLTDNS DICKKPCSVA PHDSQLISST ILINEMNGVG
EKLSAKENTV GMLRQEVLPL TLELEILEHP QEELKVECTP TPIAPSMLPA FSPAPPTPPT
SPPCPPVVLS AAIARSPAVA TEVQRVADEG ESLRTCLSKD AKEMQDKAES ESDGQAEETA
DPQSLHSGRS PAPVQTATTA PKSWKKTKEQ TRTPDEVLEA EAEPKAEEEL AVDSVLEPEQ
EKMSQGFPSE RDPSALKRGK AEEGNGEEAE PVRNGAESAS EGEGGDGNSG SADSSADGLT
FPFKAESWKP ADTEGKKQYD REFLLDIQFM PACIQKPEGL PPISDVVLDK INQPRLSMRT
LDPRILPRGP DFTPAFADFP RQTPGGRGVP LLNVGPRRSQ PGQRREPRKI ITVSVKEDVH
LRKAENAWKP SQKRDSHADD PESIKTQELF RKVRSILNKL TPQMFNQLMK QVSALTVDTE
ERLKGVIDLV FEKAIDEPSF SVAYANMCRC LVTLKVPMAD KPGNTVNFRK LLLNRCQKEF
EKDKADDDVF EKKQKELEAA SAPEERTRLH DELEEAKDKA RRRSIGNIKF IGELFKLKML
TEAIMHDCVV KLLKNHDEES LECLCRLLTT IGKDLDFEKA KPRMDQYFNQ MEKIVKERKT
SSRIRFMLQD VIDLRLCNWV SRRADQGPKT IEQIHKEAKI EEQEEQRKVQ QLMTKEKRRP
GVQRVDEGGW NTVQGAKNSR VLDPSKFLKI TKPTIDEKIQ LVPKAQLGSW GKGSSGGAKA
SESDALRSSA SSLNRFSPLQ PPAPSGSPSA TPLEFDSRRA LTSRGSMGRE KSDKPIPAGT
ARPNTFLRGS SKDLLDNQSQ EEQRREMLET VKQLTGGLDA ERASTEADRS KTRELAKSEM
CAVPAPDKPA LSEEEVERKS KSIIDEFLHI NDFKEATQCI EELSAQGPLH VFVKVGVEFT
LERSQITRDH MGHLLYQLVQ SEKLSKQDFF KGFSETLELA DDMAIDIPHI WLYLAELVTP
MLKEGGISMR ELIVEFSKPL LPVGRAGVLL SEILHLLCRQ MSHKKVGALW READLSWKDF
LPEGEDVHHF LLEQKLDFTE SEGPCSSEAL SKKELSAEEL SQRLEKLIME EKADDERIFD
WVEANLDESQ MSSPTFLRAL MTAVCKAAII ADCSTFRVDT AVIKQRVPIL LKYLDSDTEK
ELQALYALQA SIVKLDQPAN LLRMFFDCLY DEEVISEDAF YKWESSKDPA EQAGKGVALK
SVTAFFTWLR EAEEESEDN
