RGS3_MOUSE
ID RGS3_MOUSE Reviewed; 966 AA.
AC Q9DC04; Q5SRB1; Q5SRB4; Q5SRB8; Q8CEE3; Q8VI25; Q925G9; Q9JL22; Q9JL23;
AC Q9QXA2;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Regulator of G-protein signaling 3;
DE Short=RGS3;
DE AltName: Full=C2PA;
GN Name=Rgs3;
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 [MRNA] (ISOFORM 3), AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=11034339; DOI=10.1016/s0014-5793(00)01942-6;
RA Linares J.-L., Wendling C., Tomasetto C., Rio M.-C.;
RT "C2PA, a new protein expressed during mouse spermatogenesis.";
RL FEBS Lett. 480:249-254(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH EPHRINS,
RP AND SUBCELLULAR LOCATION.
RC TISSUE=Embryo;
RX PubMed=11301003; DOI=10.1016/s0092-8674(01)00297-5;
RA Lu Q., Sun E.E., Klein R.S., Flanagan J.G.;
RT "Ephrin-B reverse signaling is mediated by a novel PDZ-RGS protein and
RT selectively inhibits G protein-coupled chemoattraction.";
RL Cell 105:69-79(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RA Huang W.-Y., Izumo S.;
RT "EPP1, a novel PDZ protein expressed in the arterial endothelial cells
RT binding to B ephrins.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
RC STRAIN=C57BL/6J; TISSUE=Lung;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [7]
RP PARTIAL NUCLEOTIDE SEQUENCE (ISOFORMS 5 AND 6).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=10779778; DOI=10.4049/jimmunol.164.9.4720;
RA Reif K., Cyster J.G.;
RT "RGS molecule expression in murine B lymphocytes and ability to down-
RT regulate chemotaxis to lymphoid chemokines.";
RL J. Immunol. 164:4720-4729(2000).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12210723; DOI=10.1002/jcb.10279;
RA Hirabayashi S., Ohno H., Iida J., Hata Y.;
RT "C2PA is a nuclear protein implicated in the heat shock response.";
RL J. Cell. Biochem. 87:65-74(2002).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-712; SER-715; SER-747 AND
RP SER-776, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
RC 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 [10]
RP STRUCTURE BY NMR OF 10-94.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the PDZ domain of RGS3.";
RL Submitted (NOV-2004) to the PDB data bank.
CC -!- FUNCTION: Down-regulates signaling from heterotrimeric G-proteins by
CC increasing the GTPase activity of the alpha subunits, thereby driving
CC them into their inactive GDP-bound form. Down-regulates G-protein-
CC mediated release of inositol phosphates and activation of MAP kinases.
CC {ECO:0000269|PubMed:11301003, ECO:0000269|PubMed:12210723}.
CC -!- SUBUNIT: Binds the GNB1-GNG2 heterodimer (By similarity). Binds EFNB1
CC and EFNB2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Cell membrane
CC {ECO:0000250|UniProtKB:P49796}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P49796}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P49796}. Note=Long isoforms are cytoplasmic and
CC associated with the plasma membrane. Short isoforms are nuclear.
CC {ECO:0000250|UniProtKB:P49796}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:11301003}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Nucleus
CC {ECO:0000269|PubMed:12210723}.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q9DC04-3; Sequence=Displayed;
CC Name=5; Synonyms=Long;
CC IsoId=Q9DC04-1; Sequence=VSP_013966;
CC Name=6; Synonyms=Short;
CC IsoId=Q9DC04-2; Sequence=VSP_005663, VSP_005664;
CC Name=2;
CC IsoId=Q9DC04-4; Sequence=VSP_013970;
CC Name=3; Synonyms=C2PA;
CC IsoId=Q9DC04-5; Sequence=VSP_013967, VSP_013968, VSP_013969;
CC Name=4;
CC IsoId=Q9DC04-6; Sequence=VSP_013968, VSP_013969;
CC -!- TISSUE SPECIFICITY: Detected in embryos from E8.5-16.5 in cortical
CC ventricular zone, dorsal root ganglia and cerebellar primordia. Isoform
CC 3 is detected in testis and in spermatocytes from newborn mice. Levels
CC increase and reach a maximum after 21 days; after this they decrease
CC again. Long isoforms are widely expressed.
CC {ECO:0000269|PubMed:11034339}.
CC -!- PTM: Phosphorylated by cyclic GMP-dependent protein kinase.
CC {ECO:0000250}.
CC -!- PTM: ISGylated. {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 3]: Nuclear. {ECO:0000269|PubMed:12210723}.
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DR EMBL; AJ250999; CAB66146.1; -; mRNA.
DR EMBL; AF350047; AAK38878.1; -; mRNA.
DR EMBL; AF319519; AAL37173.1; -; mRNA.
DR EMBL; AK004648; BAB23439.1; -; mRNA.
DR EMBL; AK028445; BAC25954.1; -; mRNA.
DR EMBL; AL672272; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC033449; AAH33449.1; -; mRNA.
DR EMBL; AF215670; AAF34627.1; -; mRNA.
DR EMBL; AF215669; AAF34626.1; -; mRNA.
DR CCDS; CCDS18246.1; -. [Q9DC04-5]
DR CCDS; CCDS38776.1; -. [Q9DC04-6]
DR CCDS; CCDS51202.1; -. [Q9DC04-3]
DR CCDS; CCDS80110.1; -. [Q9DC04-1]
DR RefSeq; NP_001075119.1; NM_001081650.2. [Q9DC04-6]
DR RefSeq; NP_001297635.1; NM_001310706.1. [Q9DC04-1]
DR RefSeq; NP_062365.2; NM_019492.3.
DR RefSeq; NP_599018.3; NM_134257.3. [Q9DC04-3]
DR RefSeq; XP_006538130.1; XM_006538067.3.
DR RefSeq; XP_006538131.1; XM_006538068.3. [Q9DC04-1]
DR RefSeq; XP_006538132.1; XM_006538069.3. [Q9DC04-1]
DR RefSeq; XP_006538133.1; XM_006538070.3. [Q9DC04-1]
DR RefSeq; XP_017175797.1; XM_017320308.1.
DR PDB; 1WHD; NMR; -; A=18-94.
DR PDBsum; 1WHD; -.
DR AlphaFoldDB; Q9DC04; -.
DR SMR; Q9DC04; -.
DR BioGRID; 206112; 2.
DR IntAct; Q9DC04; 1.
DR MINT; Q9DC04; -.
DR STRING; 10090.ENSMUSP00000081569; -.
DR iPTMnet; Q9DC04; -.
DR PhosphoSitePlus; Q9DC04; -.
DR EPD; Q9DC04; -.
DR jPOST; Q9DC04; -.
DR MaxQB; Q9DC04; -.
DR PaxDb; Q9DC04; -.
DR PeptideAtlas; Q9DC04; -.
DR PRIDE; Q9DC04; -.
DR ProteomicsDB; 254953; -. [Q9DC04-3]
DR ProteomicsDB; 254954; -. [Q9DC04-1]
DR ProteomicsDB; 254955; -. [Q9DC04-2]
DR ProteomicsDB; 254956; -. [Q9DC04-4]
DR ProteomicsDB; 254957; -. [Q9DC04-5]
DR ProteomicsDB; 254958; -. [Q9DC04-6]
DR Antibodypedia; 15339; 176 antibodies from 30 providers.
DR DNASU; 50780; -.
DR Ensembl; ENSMUST00000084521; ENSMUSP00000081569; ENSMUSG00000059810. [Q9DC04-3]
DR Ensembl; ENSMUST00000107420; ENSMUSP00000103043; ENSMUSG00000059810. [Q9DC04-1]
DR Ensembl; ENSMUST00000107424; ENSMUSP00000103047; ENSMUSG00000059810. [Q9DC04-6]
DR GeneID; 50780; -.
DR KEGG; mmu:50780; -.
DR UCSC; uc008tfe.2; mouse. [Q9DC04-6]
DR UCSC; uc008tfg.1; mouse. [Q9DC04-1]
DR UCSC; uc008tfh.2; mouse. [Q9DC04-3]
DR CTD; 5998; -.
DR MGI; MGI:1354734; Rgs3.
DR VEuPathDB; HostDB:ENSMUSG00000059810; -.
DR eggNOG; KOG3589; Eukaryota.
DR GeneTree; ENSGT00940000154416; -.
DR HOGENOM; CLU_005574_0_0_1; -.
DR InParanoid; Q9DC04; -.
DR OrthoDB; 201302at2759; -.
DR PhylomeDB; Q9DC04; -.
DR TreeFam; TF351952; -.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR BioGRID-ORCS; 50780; 1 hit in 58 CRISPR screens.
DR ChiTaRS; Rgs3; mouse.
DR EvolutionaryTrace; Q9DC04; -.
DR PRO; PR:Q9DC04; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9DC04; protein.
DR Bgee; ENSMUSG00000059810; Expressed in animal zygote and 152 other tissues.
DR ExpressionAtlas; Q9DC04; baseline and differential.
DR Genevisible; Q9DC04; MM.
DR GO; GO:0005737; C:cytoplasm; TAS:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005096; F:GTPase activator activity; TAS:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:MGI.
DR GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; ISO:MGI.
DR CDD; cd08713; RGS_RGS3; 1.
DR Gene3D; 1.10.167.10; -; 1.
DR Gene3D; 1.10.196.10; -; 2.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR034951; RGS_RGS3.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR024066; RGS_subdom1/3.
DR InterPro; IPR044926; RGS_subdomain_2.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF00615; RGS; 1.
DR PRINTS; PR01301; RGSPROTEIN.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00315; RGS; 1.
DR SUPFAM; SSF48097; SSF48097; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50132; RGS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cytoplasm; Membrane;
KW Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Signal transduction inhibitor; Ubl conjugation.
FT CHAIN 1..966
FT /note="Regulator of G-protein signaling 3"
FT /id="PRO_0000204183"
FT DOMAIN 18..95
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 841..966
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT REGION 115..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 637..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 806..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..448
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..675
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 167
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P49796"
FT MOD_RES 712
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 715
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 747
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 776
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..398
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_013966"
FT VAR_SEQ 1..17
FT /note="MNRFNGLCKVCSERRYR -> MERPHQDASLSKKDACTQTYPPRRRIRHAQV
FT QDAGQLKLSIDAQDRVLLPHIIEGKGLMSREPGICDPYVKVSLIPEDSQLPCQTTQIIP
FT DCRDPAFHEHFFFPVPEEGDQKRLLVTVWNRASETRQHTLIGCMSFGVRSLLTPDKEIS
FT GWYYLLGEDLGRTKHLKVARRRLQPLRDMLLRMPGEGDPENGEKL (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:11034339"
FT /id="VSP_013967"
FT VAR_SEQ 399..773
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_005663"
FT VAR_SEQ 399..433
FT /note="MFETEADEKEMPLVEGKGPGAEEPAPSKNPSPGQE -> KLHPYGSLQQEMG
FT PVTSISATQDRSFTSSGQTLIG (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:11034339,
FT ECO:0000303|PubMed:16141072, ECO:0000303|Ref.3"
FT /id="VSP_013968"
FT VAR_SEQ 434..966
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:11034339,
FT ECO:0000303|PubMed:16141072, ECO:0000303|Ref.3"
FT /id="VSP_013969"
FT VAR_SEQ 455..490
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11301003"
FT /id="VSP_013970"
FT VAR_SEQ 774..795
FT /note="KMSGTDLTECDEASRKRKSKNI -> MLRGMYLTRNGNLQRRHTMKE (in
FT isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_005664"
FT CONFLICT 179
FT /note="T -> A (in Ref. 3; AAL37173)"
FT /evidence="ECO:0000305"
FT CONFLICT 501
FT /note="S -> P (in Ref. 1; AAK38878)"
FT /evidence="ECO:0000305"
FT STRAND 18..22
FT /evidence="ECO:0007829|PDB:1WHD"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:1WHD"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:1WHD"
FT HELIX 48..52
FT /evidence="ECO:0007829|PDB:1WHD"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:1WHD"
FT HELIX 73..82
FT /evidence="ECO:0007829|PDB:1WHD"
FT STRAND 84..93
FT /evidence="ECO:0007829|PDB:1WHD"
SQ SEQUENCE 966 AA; 106219 MW; 20B6B2BB7A9C8BB2 CRC64;
MNRFNGLCKV CSERRYRQIT IRRGKDGFGF TICCDSPVRV QAVDSGGPAE RAGLQQLDTV
LQLNERPVEH WKCVELAHEI RSCPSEIILL VWRVVPQIKP GPDGGVLRRA SCKSTHDLLS
PPNKREKNCT HGAPVRPEQR HSCHLVCDSS DGLLLGGWER YTEVGKRSGQ HTLPALSRTT
TPTDPNYIIL APLNPGSQLL RPVYQEDTIP EEPGTTTKGK SYTGLGKKSR LMKTVQTMKG
HSNYQDCSAL RPHIPHSSYG TYVTLAPKVL VFPVFVQPLD LCNPARTLLL SEELLLYEGR
NKTSQVTLFA YSDLLLFTKE EEPGRCDVLR NPLYLQSVKL QEGSSEDLKF CVLYLAEKAE
CLFTLEAHSQ EQKKRVCWCL SENIAKQQQL AAPPTERKMF ETEADEKEMP LVEGKGPGAE
EPAPSKNPSP GQELPPGQDL PPSKDPSPSQ ELPAGQDLPP SKDPSPSQEL PAGQDLPPSK
DPSPSQELPV GQDLPPRKDS SGQEAAPGPE SPSSEDIATC PKPPQSPETS TSKDSPPGQG
SSPTTELPSC QGLPAGQEST SQDPLLSQEP PVIPESSASV QKRLPSQESP SSLGSLPEKD
LAEQTISSGE PPVATGAVLP ASRPNFVIPE VRLDNAYSQL DGAHGGSSGE DEDAEEGEEG
GEGEEDEEDD TSDDNYGDRS EAKRSSLIET GQGAEGGFSL RVQNSLRRRT HSEGSLLQES
RGPCFASDTT LHCSDGEGAT STWAIPSPRT LKKELGRNGG SMHHLSLFFT GHRKMSGTDL
TECDEASRKR KSKNIAKDMK NKLAIFRRRN ESPGAQPASK TDKTTKSFKP TSEEALKWSE
SLEKLLLHKY GLEVFQAFLR TEFSEENLEF WLACEDFKKV KSQSKMAAKA KKIFAEFIAI
QACKEVNLDS YTREHTKENL QSITRGCFDL AQKRIFGLME KDSYPRFLRS DLYLDLINQK
KMSPPL
