COPG_DROME
ID COPG_DROME Reviewed; 883 AA.
AC Q8I0G5; E1JJ29; Q8MYW4; Q9U677; Q9V9W9;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Coatomer subunit gamma {ECO:0000250|UniProtKB:P53620, ECO:0000312|EMBL:AAN14275.1};
DE AltName: Full=Gamma-coat protein {ECO:0000250|UniProtKB:P53620};
DE Short=Gamma-COP {ECO:0000250|UniProtKB:P53620};
GN Name=gammaCOP {ECO:0000312|FlyBase:FBgn0028968};
GN Synonyms=copg {ECO:0000312|EMBL:AAF05719.1}, gamma-Cop;
GN ORFNames=CG1528 {ECO:0000312|FlyBase:FBgn0028968};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAF05719.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RC STRAIN=Berkeley {ECO:0000269|PubMed:11018518};
RC TISSUE=Larva {ECO:0000269|PubMed:11018518}, and
RC Pupae {ECO:0000269|PubMed:11018518};
RX PubMed=11018518; DOI=10.1016/s0014-5793(00)02033-0;
RA Hahn Y., Lee Y.J., Yun J.H., Yang S.K., Park C.W., Mita K., Huh T.-L.,
RA Rhee M., Chung J.H.;
RT "Duplication of genes encoding non-clathrin coat protein gamma-COP in
RT vertebrate, insect and plant evolution.";
RL FEBS Lett. 482:31-36(2000).
RN [2] {ECO:0000312|EMBL:AAN14275.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAN14275.1}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAN71383.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS B AND C).
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5] {ECO:0000305}
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=16169286; DOI=10.1016/j.modgep.2005.06.001;
RA Grieder N.C., Kloter U., Gehring W.J.;
RT "Expression of COPI components during development of Drosophila
RT melanogaster.";
RL Gene Expr. Patterns 6:11-21(2005).
RN [6] {ECO:0000305}
RP FUNCTION.
RX PubMed=19067489; DOI=10.1371/journal.pbio.0060292;
RA Beller M., Sztalryd C., Southall N., Bell M., Jackle H., Auld D.S.,
RA Oliver B.;
RT "COPI complex is a regulator of lipid homeostasis.";
RL PLoS Biol. 6:E292-E292(2008).
RN [7] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=18398480; DOI=10.1371/journal.pone.0001964;
RA Jayaram S.A., Senti K.A., Tiklova K., Tsarouhas V., Hemphala J.,
RA Samakovlis C.;
RT "COPI vesicle transport is a common requirement for tube expansion in
RT Drosophila.";
RL PLoS ONE 3:E1964-E1964(2008).
RN [8] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=18802472; DOI=10.1371/journal.pone.0003241;
RA Grieder N.C., Caussinus E., Parker D.S., Cadigan K., Affolter M.,
RA Luschnig S.;
RT "gammaCOP is required for apical protein secretion and epithelial
RT morphogenesis in Drosophila melanogaster.";
RL PLoS ONE 3:E3241-E3241(2008).
CC -!- FUNCTION: The coatomer is a cytosolic protein complex that binds to
CC dilysine motifs and reversibly associates with Golgi non-clathrin-
CC coated vesicles, which further mediate biosynthetic protein transport
CC from the ER, via the Golgi up to the trans Golgi network. Coatomer
CC complex is required for budding from Golgi membranes, and is essential
CC for the retrograde Golgi-to-ER transport of dilysine-tagged proteins.
CC Required for limiting lipid storage in lipid droplets. Involved in the
CC expansion of luminal extracellular matrices and apical membrane during
CC tubulogenesis. Required in the tracheal epithelium for luminal protein
CC secretion and diametric tube growth. In salivary glands, required for
CC deposition of O-glycans and luminal extracellular matrix assembly.
CC Required for epidermal morphogenesis and cuticle development.
CC {ECO:0000269|PubMed:18398480, ECO:0000269|PubMed:18802472,
CC ECO:0000269|PubMed:19067489}.
CC -!- SUBUNIT: Oligomeric complex that consists of at least the alpha, beta,
CC beta', gamma, delta, epsilon and zeta subunits.
CC {ECO:0000250|UniProtKB:P32074, ECO:0000250|UniProtKB:P53620,
CC ECO:0000250|UniProtKB:P53622}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P32074,
CC ECO:0000250|UniProtKB:P53620, ECO:0000250|UniProtKB:P53622}. Golgi
CC apparatus membrane {ECO:0000269|PubMed:18398480,
CC ECO:0000269|PubMed:18802472}; Peripheral membrane protein
CC {ECO:0000269|PubMed:18398480, ECO:0000269|PubMed:18802472}; Cytoplasmic
CC side {ECO:0000269|PubMed:18398480, ECO:0000269|PubMed:18802472}.
CC Cytoplasmic vesicle, COPI-coated vesicle membrane
CC {ECO:0000269|PubMed:18398480, ECO:0000269|PubMed:18802472}; Peripheral
CC membrane protein {ECO:0000269|PubMed:18398480,
CC ECO:0000269|PubMed:18802472}; Cytoplasmic side
CC {ECO:0000269|PubMed:18398480, ECO:0000269|PubMed:18802472}. Endoplasmic
CC reticulum {ECO:0000269|PubMed:18398480, ECO:0000269|PubMed:18802472}.
CC Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side
CC of the Golgi, as well as on the vesicles/buds originating from it.
CC {ECO:0000250|UniProtKB:P32074, ECO:0000250|UniProtKB:P53620,
CC ECO:0000250|UniProtKB:P53622, ECO:0000269|PubMed:18398480,
CC ECO:0000269|PubMed:18802472}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=B {ECO:0000269|PubMed:10731132, ECO:0000269|PubMed:12537569};
CC IsoId=Q8I0G5-1; Sequence=Displayed;
CC Name=A {ECO:0000269|PubMed:10731132, ECO:0000269|PubMed:11018518};
CC IsoId=Q8I0G5-2; Sequence=VSP_040672;
CC Name=C {ECO:0000269|PubMed:10731132, ECO:0000269|PubMed:12537569};
CC IsoId=Q8I0G5-3; Sequence=VSP_040672, VSP_040673;
CC -!- TISSUE SPECIFICITY: Expressed in ovary, testis, testis tip, young
CC spermatocytes, germ cells and follicle cells. Up-regulated expression
CC within centrally to posteriorly located germarial cysts and in
CC migrating follicle cells. Widespread expression in imaginal disks
CC including eye-antennal disk, wing disk, third leg and haltere disk.
CC {ECO:0000269|PubMed:16169286}.
CC -!- DEVELOPMENTAL STAGE: Expressed during spermatogenesis and at later
CC stages of oogenesis. During embryonic and larval development, expressed
CC ubiquitously. Starting at stage 10 embryos and lasting until the end of
CC embryonic development, strongly expressed in the salivary glands and in
CC cells of the presumptive proventriculus. Maternal expression abundant
CC in early embryos. Zygotic expression commences in the epidermis and
CC salivary glands from stage 11, initiates in the trachea at stage 13,
CC and at early stage 15 is also detected in the foregut and hindgut
CC tubes. {ECO:0000269|PubMed:16169286, ECO:0000269|PubMed:18398480}.
CC -!- DISRUPTION PHENOTYPE: Narrow tracheal tubes and thin salivary glands
CC with reduced tube diameter and impaired tube elongation. Fails to
CC complete dorsal closure. Fails to efficiently secrete luminal
CC components and assemble the luminal chitinous matrix during tracheal
CC tube expansion. In salivary glands, fails in the luminal deposition and
CC assembly of a distinct, transient intraluminal matrix. Disrupted
CC endoplasmic reticulum and Golgi in embryos. Null mutants die late in
CC embryogenesis with a poorly differentiated cuticle and denticle.
CC Defects in cell rearrangements, in branch elongation, in tube dilation
CC and tube fusion. {ECO:0000269|PubMed:18398480,
CC ECO:0000269|PubMed:18802472}.
CC -!- SIMILARITY: Belongs to the COPG family. {ECO:0000255}.
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DR EMBL; AF191563; AAF05719.1; -; mRNA.
DR EMBL; AE014297; AAN14275.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF57160.1; -; Genomic_DNA.
DR EMBL; AE014297; ACZ95077.1; -; Genomic_DNA.
DR EMBL; AY113545; AAM29550.1; -; mRNA.
DR EMBL; BT001628; AAN71383.1; -; mRNA.
DR RefSeq; NP_001163784.1; NM_001170313.1. [Q8I0G5-3]
DR RefSeq; NP_524608.1; NM_079869.3. [Q8I0G5-2]
DR RefSeq; NP_733432.1; NM_170553.2. [Q8I0G5-1]
DR AlphaFoldDB; Q8I0G5; -.
DR SMR; Q8I0G5; -.
DR BioGRID; 68560; 6.
DR IntAct; Q8I0G5; 27.
DR STRING; 7227.FBpp0085155; -.
DR PaxDb; Q8I0G5; -.
DR PRIDE; Q8I0G5; -.
DR EnsemblMetazoa; FBtr0085793; FBpp0085154; FBgn0028968. [Q8I0G5-2]
DR EnsemblMetazoa; FBtr0085794; FBpp0085155; FBgn0028968. [Q8I0G5-1]
DR EnsemblMetazoa; FBtr0301290; FBpp0290505; FBgn0028968. [Q8I0G5-3]
DR GeneID; 43717; -.
DR KEGG; dme:Dmel_CG1528; -.
DR UCSC; CG1528-RA; d. melanogaster.
DR UCSC; CG1528-RB; d. melanogaster. [Q8I0G5-1]
DR CTD; 43717; -.
DR FlyBase; FBgn0028968; gammaCOP.
DR VEuPathDB; VectorBase:FBgn0028968; -.
DR eggNOG; KOG1078; Eukaryota.
DR GeneTree; ENSGT00390000016313; -.
DR InParanoid; Q8I0G5; -.
DR OMA; YMTQYHA; -.
DR PhylomeDB; Q8I0G5; -.
DR Reactome; R-DME-6807878; COPI-mediated anterograde transport.
DR Reactome; R-DME-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR BioGRID-ORCS; 43717; 1 hit in 3 CRISPR screens.
DR GenomeRNAi; 43717; -.
DR PRO; PR:Q8I0G5; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0028968; Expressed in spermathecum and 25 other tissues.
DR ExpressionAtlas; Q8I0G5; baseline and differential.
DR Genevisible; Q8I0G5; DM.
DR GO; GO:0036063; C:acroblast; IDA:FlyBase.
DR GO; GO:0005801; C:cis-Golgi network; IDA:FlyBase.
DR GO; GO:0030126; C:COPI vesicle coat; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:FlyBase.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:FlyBase.
DR GO; GO:0005794; C:Golgi apparatus; IDA:FlyBase.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0035147; P:branch fusion, open tracheal system; IMP:FlyBase.
DR GO; GO:0008362; P:chitin-based embryonic cuticle biosynthetic process; IMP:FlyBase.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0030198; P:extracellular matrix organization; IMP:FlyBase.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0007436; P:larval salivary gland morphogenesis; IMP:FlyBase.
DR GO; GO:0035149; P:lumen formation, open tracheal system; IMP:FlyBase.
DR GO; GO:0007112; P:male meiosis cytokinesis; IMP:FlyBase.
DR GO; GO:0007424; P:open tracheal system development; IMP:FlyBase.
DR GO; GO:0072384; P:organelle transport along microtubule; IBA:GO_Central.
DR GO; GO:0009306; P:protein secretion; IMP:FlyBase.
DR GO; GO:0010883; P:regulation of lipid storage; IDA:FlyBase.
DR GO; GO:0035158; P:regulation of tube diameter, open tracheal system; IMP:FlyBase.
DR Gene3D; 1.25.10.10; -; 2.
DR Gene3D; 2.60.40.1480; -; 1.
DR Gene3D; 3.30.310.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR InterPro; IPR013041; Clathrin_app_Ig-like_sf.
DR InterPro; IPR009028; Coatomer/calthrin_app_sub_C.
DR InterPro; IPR032154; Coatomer_g_Cpla.
DR InterPro; IPR017106; Coatomer_gsu.
DR InterPro; IPR013040; Coatomer_gsu_app_Ig-like_dom.
DR InterPro; IPR037067; Coatomer_gsu_app_sf.
DR InterPro; IPR012295; TBP_dom_sf.
DR PANTHER; PTHR10261; PTHR10261; 1.
DR Pfam; PF01602; Adaptin_N; 1.
DR Pfam; PF16381; Coatomer_g_Cpla; 1.
DR Pfam; PF08752; COP-gamma_platf; 1.
DR PIRSF; PIRSF037093; Coatomer_gamma_subunit; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF49348; SSF49348; 1.
DR SUPFAM; SSF55711; SSF55711; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; Cytoplasmic vesicle;
KW Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus; Membrane;
KW Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1..883
FT /note="Coatomer subunit gamma"
FT /id="PRO_0000405327"
FT REPEAT 69..106
FT /note="HEAT 1"
FT REPEAT 292..329
FT /note="HEAT 2"
FT REPEAT 331..364
FT /note="HEAT 3"
FT REPEAT 365..401
FT /note="HEAT 4"
FT REPEAT 404..439
FT /note="HEAT 5"
FT REPEAT 476..513
FT /note="HEAT 6"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 2..17
FT /note="NYFSLTSHKKHRGHPS -> GSFRREKDDEED (in isoform A and
FT isoform C)"
FT /evidence="ECO:0000303|PubMed:10731132,
FT ECO:0000303|PubMed:11018518, ECO:0000303|PubMed:12537569"
FT /id="VSP_040672"
FT VAR_SEQ 18
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|PubMed:10731132,
FT ECO:0000303|PubMed:12537569"
FT /id="VSP_040673"
FT CONFLICT 280
FT /note="A -> V (in Ref. 1; AAF05719)"
FT /evidence="ECO:0000305"
FT CONFLICT 546
FT /note="S -> W (in Ref. 4; AAM29550)"
FT /evidence="ECO:0000305"
FT CONFLICT 724
FT /note="A -> T (in Ref. 4; AAM29550)"
FT /evidence="ECO:0000305"
FT CONFLICT 729
FT /note="T -> A (in Ref. 4; AAM29550)"
FT /evidence="ECO:0000305"
FT CONFLICT 771
FT /note="I -> V (in Ref. 4; AAM29550)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 883 AA; 97690 MW; 7C610B0F7A39692F CRC64;
MNYFSLTSHK KHRGHPSAGP SNAYQNLEKT SVLQETRTFN ETPVNPRKCI HILTKILYLI
NQGEQLVARE ATDCFFAMTK LFQSKDVVLR RMVYLGIKEL SSIAEDVIIV TSSLTKDMTG
KEDLYRAAAI RALCSITDNT MLQAVERYMK QCIVDKNAAV SCAALVSSLR LANTAGDVVK
RWANEAQEAL NSDNIMVQYH ALGLLYHIRK SDRLAVSKLV NKLTRGSLKS PYAVCMLIRI
ACKLIEEEDI PSEELSDSPL FTFIESCLRH KSEMVIYEAA HAIVNLKNTN PRMLSPAFSI
LQLFCSSPKA TLRFAAVRTL NKVAMTHPAA VTTCNLDLEG LITDSNRSVA TLAITTLLKT
GAESSVERLM KQISTFVAEI SDEFKVVVVQ AICALCTKYP RKHTVLMNFL SGMLREEGGL
EYKTSIVDTI ITIIEENADA KESGLSHLCE FIEDCEHVSL AVRILHLLGK EGPFAATPSK
YIRFIYNRVI LESPIVRAAA VTAMAQFGAS CPALLSNILV LLGRCQMDPD DEVRDRATYY
LSILNSERPE LYKNYIIERE NCSLALLEKS LVEHLNGDVD TRFDISIVPK AAIVKPVIAN
DVMLVTSSAP RPPKITREEE SAARLAQLPG IQVLGPIHRS TAPIQLTESE TEYTVQCIKH
IFGQHVVFQF DCLNTLSDQI LENVRVELTL PEGFTTRAVI PCPKLPYNDL QTTFVIVEFP
PDAANSIATF GATLRFVVKD CDPNTGEPES EEGYDDEYML EDLELTVADQ IQKTRKNNFQ
VSWDAADSEE WLQAEDTFVL SAVTTLQDAV NTIVKILGLG AANLSENVPE GTHLHTLLCS
GTFRGGAEIL VRAKLALSEG VTLNLTVRST DQDVAELITA AIG
