GNAS1_RAT
ID GNAS1_RAT Reviewed; 1144 AA.
AC Q63803;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 3.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Guanine nucleotide-binding protein G(s) subunit alpha isoforms XLas;
DE AltName: Full=Adenylate cyclase-stimulating G alpha protein;
DE AltName: Full=Extra large alphas protein;
DE Short=XLalphas;
DE AltName: Full=G-alpha-8;
GN Name=Gnas {ECO:0000312|RGD:2716}; Synonyms=Gnas1 {ECO:0000312|RGD:2716};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000269|PubMed:15057822};
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAC39211.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 284-1144, AND TISSUE SPECIFICITY.
RX PubMed=7997272; DOI=10.1038/372804a0;
RA Kehlenbach R.H., Matthey J., Huttner W.B.;
RT "XLas is a new type of G protein.";
RL Nature 372:804-809(1994).
RN [3]
RP ERRATUM OF PUBMED:7997272.
RA Kehlenbach R.H., Matthey J., Huttner W.B.;
RL Nature 375:253-253(1995).
RN [4] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10931823; DOI=10.1074/jbc.m001335200;
RA Pasolli H.A., Klemke M., Kehlenbach R.H., Wang Y., Huttner W.B.;
RT "Characterization of the extra-large G protein alpha-subunit XLalphas. I.
RT Tissue distribution and subcellular localization.";
RL J. Biol. Chem. 275:33622-33632(2000).
RN [5] {ECO:0000305}
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF GLN-977.
RX PubMed=10931851; DOI=10.1074/jbc.m006594200;
RA Klemke M., Pasolli H.A., Kehlenbach R.H., Offermanns S., Schultz G.,
RA Huttner W.B.;
RT "Characterization of the extra-large G protein alpha-subunit XLalphas. II.
RT Signal transduction properties.";
RL J. Biol. Chem. 275:33633-33640(2000).
RN [6] {ECO:0000305}
RP INTERACTION WITH ALEX.
RX PubMed=11447126; DOI=10.1093/emboj/20.14.3849;
RA Klemke M., Kehlenbach R.H., Huttner W.B.;
RT "Two overlapping reading frames in a single exon encode interacting
RT proteins -- a novel way of gene usage.";
RL EMBO J. 20:3849-3860(2001).
RN [7] {ECO:0000305}
RP IDENTIFICATION.
RX PubMed=15148396; DOI=10.1073/pnas.0308758101;
RA Abramowitz J., Grenet D., Birnbaumer M., Torres H.N., Birnbaumer L.;
RT "XL alpha-s, the extra-long form of the alpha subunit of the Gs G protein,
RT is significantly longer than suspected, and so is its companion Alex.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:8366-8371(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1102, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) function as
CC transducers in numerous signaling pathways controlled by G protein-
CC coupled receptors (GPCRs). Signaling involves the activation of
CC adenylyl cyclases, resulting in increased levels of the signaling
CC molecule cAMP. GNAS functions downstream of several GPCRs, including
CC beta-adrenergic receptors. XLas isoforms interact with the same set of
CC receptors as Gnas isoforms. {ECO:0000269|PubMed:10931851}.
CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The
CC alpha chain contains the guanine nucleotide binding site. Interacts
CC through its N-terminal region with ALEX which is produced from the same
CC locus in a different open reading frame. This interaction may inhibit
CC its adenylyl cyclase-stimulating activity. Interacts with MAGED2.
CC {ECO:0000250|UniProtKB:Q5JWF2, ECO:0000269|PubMed:10931851,
CC ECO:0000269|PubMed:11447126}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10931823};
CC Peripheral membrane protein {ECO:0000269|PubMed:10931823}. Apical cell
CC membrane {ECO:0000250|UniProtKB:Q5JWF2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=XLas-1;
CC IsoId=Q63803-1; Sequence=Displayed;
CC Name=Gnas-1 {ECO:0000305};
CC IsoId=P63095-1; Sequence=External;
CC Name=Gnas-2 {ECO:0000305};
CC IsoId=P63095-2; Sequence=External;
CC Name=Gnas-3 {ECO:0000305}; Synonyms=GsaN1 {ECO:0000305};
CC IsoId=P63095-3; Sequence=External;
CC Name=Nesp55 {ECO:0000305};
CC IsoId=Q792G6-1; Sequence=External;
CC -!- TISSUE SPECIFICITY: Enriched in neuroendocrine tissues with a
CC particularly high level of expression in pituitary where it is abundant
CC in intermediate and anterior lobes. In adrenal gland, found in central
CC region containing medullary chromaffin cells but not in cortex. In
CC cerebellum, strongly expressed in perikarya of Purkinje cells. Not
CC detected in liver, kidney or neurohypophysis.
CC {ECO:0000269|PubMed:10931823, ECO:0000269|PubMed:7997272}.
CC -!- MISCELLANEOUS: This protein is produced by a bicistronic gene which
CC also produces the ALEX protein from an overlapping reading frame.
CC {ECO:0000269|PubMed:11447126}.
CC -!- MISCELLANEOUS: The GNAS locus is imprinted in a complex manner, giving
CC rise to distinct paternally, maternally and biallelically expressed
CC proteins. The XLas isoforms are paternally derived, the Gnas isoforms
CC are biallelically derived and the Nesp55 isoforms are maternally
CC derived.
CC -!- SIMILARITY: Belongs to the G-alpha family. G(s) subfamily.
CC {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC39211.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AABR03134399; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03134465; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X84047; CAC39211.1; ALT_INIT; mRNA.
DR AlphaFoldDB; Q63803; -.
DR SMR; Q63803; -.
DR IntAct; Q63803; 1.
DR STRING; 10116.ENSRNOP00000066164; -.
DR iPTMnet; Q63803; -.
DR SwissPalm; Q63803; -.
DR jPOST; Q63803; -.
DR PaxDb; Q63803; -.
DR PRIDE; Q63803; -.
DR ABCD; Q63803; 1 sequenced antibody.
DR RGD; 2716; Gnas.
DR eggNOG; KOG0099; Eukaryota.
DR InParanoid; Q63803; -.
DR Reactome; R-RNO-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR Reactome; R-RNO-420092; Glucagon-type ligand receptors.
DR Reactome; R-RNO-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030142; C:COPI-coated Golgi to ER transport vesicle; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0030425; C:dendrite; ISO:RGD.
DR GO; GO:0005768; C:endosome; IDA:RGD.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IDA:RGD.
DR GO; GO:0031224; C:intrinsic component of membrane; ISO:RGD.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0045121; C:membrane raft; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0055037; C:recycling endosome; IDA:RGD.
DR GO; GO:0001726; C:ruffle; IDA:RGD.
DR GO; GO:0032588; C:trans-Golgi network membrane; ISO:RGD.
DR GO; GO:0010856; F:adenylate cyclase activator activity; IDA:UniProtKB.
DR GO; GO:0043014; F:alpha-tubulin binding; IDA:RGD.
DR GO; GO:0031698; F:beta-2 adrenergic receptor binding; IPI:RGD.
DR GO; GO:0051430; F:corticotropin-releasing hormone receptor 1 binding; IPI:RGD.
DR GO; GO:0031748; F:D1 dopamine receptor binding; IPI:RGD.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; IPI:RGD.
DR GO; GO:0031681; F:G-protein beta-subunit binding; IDA:RGD.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IDA:RGD.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0005159; F:insulin-like growth factor receptor binding; IPI:RGD.
DR GO; GO:0035255; F:ionotropic glutamate receptor binding; IPI:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031852; F:mu-type opioid receptor binding; IDA:RGD.
DR GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
DR GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; ISO:RGD.
DR GO; GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; ISO:RGD.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:RGD.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0060348; P:bone development; ISO:RGD.
DR GO; GO:0055074; P:calcium ion homeostasis; IMP:RGD.
DR GO; GO:0051216; P:cartilage development; ISO:RGD.
DR GO; GO:0050890; P:cognition; ISO:RGD.
DR GO; GO:0048589; P:developmental growth; ISO:RGD.
DR GO; GO:0006306; P:DNA methylation; ISO:RGD.
DR GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; ISO:RGD.
DR GO; GO:0035116; P:embryonic hindlimb morphogenesis; ISO:RGD.
DR GO; GO:0001958; P:endochondral ossification; ISO:RGD.
DR GO; GO:0006112; P:energy reserve metabolic process; ISO:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:RGD.
DR GO; GO:0071514; P:genomic imprinting; ISO:RGD.
DR GO; GO:0060789; P:hair follicle placode formation; ISO:RGD.
DR GO; GO:0035264; P:multicellular organism growth; ISO:RGD.
DR GO; GO:0045776; P:negative regulation of blood pressure; IMP:RGD.
DR GO; GO:0040015; P:negative regulation of multicellular organism growth; ISO:RGD.
DR GO; GO:0035814; P:negative regulation of renal sodium excretion; IMP:RGD.
DR GO; GO:0070527; P:platelet aggregation; ISO:RGD.
DR GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:RGD.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:RGD.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISO:RGD.
DR GO; GO:0045672; P:positive regulation of osteoclast differentiation; ISO:RGD.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:RGD.
DR GO; GO:0010765; P:positive regulation of sodium ion transport; IMP:RGD.
DR GO; GO:0040032; P:post-embryonic body morphogenesis; ISO:RGD.
DR GO; GO:0009791; P:post-embryonic development; ISO:RGD.
DR GO; GO:2000828; P:regulation of parathyroid hormone secretion; ISO:RGD.
DR GO; GO:0009966; P:regulation of signal transduction; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:RGD.
DR GO; GO:0071107; P:response to parathyroid hormone; ISO:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:RGD.
DR GO; GO:0007606; P:sensory perception of chemical stimulus; IBA:GO_Central.
DR GO; GO:0001501; P:skeletal system development; ISO:RGD.
DR GO; GO:0043588; P:skin development; ISO:RGD.
DR GO; GO:0001894; P:tissue homeostasis; ISO:RGD.
DR CDD; cd00066; G-alpha; 1.
DR Gene3D; 1.10.400.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR000367; Gprotein_alpha_S.
DR InterPro; IPR001019; Gprotein_alpha_su.
DR InterPro; IPR011025; GproteinA_insert.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10218; PTHR10218; 1.
DR Pfam; PF00503; G-alpha; 1.
DR PRINTS; PR00318; GPROTEINA.
DR PRINTS; PR00443; GPROTEINAS.
DR SMART; SM00275; G_alpha; 1.
DR SUPFAM; SSF47895; SSF47895; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51882; G_ALPHA; 1.
PE 1: Evidence at protein level;
KW ADP-ribosylation; Alternative splicing; Cell membrane; Coiled coil;
KW GTP-binding; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transducer.
FT CHAIN 1..1144
FT /note="Guanine nucleotide-binding protein G(s) subunit
FT alpha isoforms XLas"
FT /id="PRO_0000253986"
FT DOMAIN 789..1144
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 1..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 622..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 735..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 792..805
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 818..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 946..954
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 969..978
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 1038..1045
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 1114..1119
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT COILED 745..772
FT /evidence="ECO:0000255"
FT COILED 837..863
FT /evidence="ECO:0000255"
FT COMPBIAS 358..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..654
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..772
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 797..805
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P04896"
FT BINDING 804
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P04896"
FT BINDING 947..954
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P04896"
FT BINDING 954
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P04896"
FT BINDING 973..977
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P63096"
FT BINDING 1042..1045
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P63096"
FT BINDING 1116
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P04896"
FT MOD_RES 951
FT /note="ADP-ribosylarginine; by cholera toxin"
FT /evidence="ECO:0000250"
FT MOD_RES 1102
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MUTAGEN 977
FT /note="Q->L: Large increase in adenylyl cyclase activity."
FT /evidence="ECO:0000269|PubMed:10931851"
SQ SEQUENCE 1144 AA; 122887 MW; 8B151D85E76ABFA1 CRC64;
MGMLNCLHGN NMSGQHDIPP EVGDQPEQEP LEAQGAAAPG AGVGPAEEME TEPSNNEPIP
DETDSEVCGP PEDSKSDIQS PSQAFEEVQV GGDYSPPPEE AMPFEIQQPS LGDFWPTLEQ
PGPSGTPSGI KAFNPAILEP GTPTGAHPGL GAYSPPPEEA MPFEFNEPAQ EDRCQPPLQV
PDLAPGGPEA WVSRALPAEP GNLGFENTGF REDYSPPPEE SVPFQLDGEE FGGDSPPPGL
PRVTPQIGIG GEFPTVAVPS TLCLAPAANA PPLWVQGAIG RPFREAVRSP NFAYDISPME
ITRPLLEIGR ASTGVDDDTA VNMDSPPIAS DGPPIEVSGA PVKSEHAKRP PLERQAAETG
NSPISSTTAE EAKVPSLERG EGSPTQPETV HIKPAPVAES GTDSSKADPD SATHAVLQIG
PEEVGGVPTM PTDLPPASED AGPDVRAEPD GGTAPATPAE SEDNREPAAA AAAEPAAEPA
AEPAAEPAAE PAAEPAAEAV PDTEAESASG AVPDTQEEPA AAAASATPAE PAARAAPVTP
TEPATRAVPS ARAHPAAGAV PGASAMSAAA RAAAARAAYA GPLVWGARSL SATPAARASL
PARAAAAARA ASAARAVAAG RSASAAPSRA HLRPPSPEIQ VADPPTPRPA PRPSAWPDKY
ERGRSCCRYE AASGICEIES SSDESEEGAT GCFQWLLRRN RRPGQPRSHT VGSNPVRNFF
ARAFGSCFGL SECTRSRSLS PGKAKDPMEE RRKQMRKEAM EMREQKRADK KRSKLIDKQL
EEEKMDYMCT HRLLLLGAGE SGKSTIVKQM RILHVNGFNG EGGEEDPQAA RSNSDGEKAT
KVQDIKNNLK EAIETIVAAM SNLVPPVELA NPENQFRVDY ILSVMNVPNF DFPPEFYEHA
KALWEDEGVR ACYERSNEYQ LIDCAQYFLD KIDVIKQADY VPSDQDLPRC RVLTSGIFET
KFQVDKVNFH MFDVGGQRDE RRKWIQCFND VTAIIFVVAS SSYNMVIRED NQTNRLQEAL
NLFKSIWNNR WLRTISVILF LNKQDLLAEK VLAGKSKIED YFPEFARYTT PEDATPEPGE
DPRVTRAKYF IRDEFLRIST ASGDGRHYCY PHFTCAVDTE NIRRVFNDCR DIIQRMHLRQ
YELL
