RRAGC_MOUSE
ID RRAGC_MOUSE Reviewed; 398 AA.
AC Q99K70; A2A7K7; Q3TL69; Q6IQZ6; Q8CFT7; Q9Z124;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Ras-related GTP-binding protein C;
DE Short=Rag C;
DE Short=RagC;
DE EC=3.6.5.- {ECO:0000250|UniProtKB:Q9HB90};
DE AltName: Full=GTPase-interacting protein 2;
DE AltName: Full=TIB929;
GN Name=Rragc {ECO:0000312|MGI:MGI:1858751};
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] {ECO:0000305, ECO:0000312|EMBL:BAA75671.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAA75671.1};
RX PubMed=10660099; DOI=10.1016/s0304-3835(99)00285-2;
RA Nakaji T., Kataoka T.R., Watabe K., Nishiyama K., Nojima H., Shimada Y.,
RA Sato F., Matsushima H., Endo Y., Kuroda Y., Kitamura Y., Ito A., Maeda S.;
RT "A new member of the GTPase superfamily that is upregulated in highly
RT metastatic cells.";
RL Cancer Lett. 147:139-147(1999).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAE35013.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE35013.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:BAE38923.1};
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 [3]
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 [4] {ECO:0000305, ECO:0000312|EMBL:AAH05417.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, Czech II {ECO:0000312|EMBL:AAH05417.1}, and
RC FVB/N {ECO:0000312|EMBL:AAH71245.1};
RC TISSUE=Liver {ECO:0000312|EMBL:AAH71245.1},
RC Mammary gland {ECO:0000312|EMBL:AAH05417.1}, and Retina;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-95, 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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC 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 [7]
RP INTERACTION WITH SESN1; SESN2 AND SESN3.
RX PubMed=25259925; DOI=10.1016/j.cell.2014.08.038;
RA Peng M., Yin N., Li M.O.;
RT "Sestrins function as guanine nucleotide dissociation inhibitors for Rag
RT GTPases to control mTORC1 signaling.";
RL Cell 159:122-133(2014).
RN [8]
RP INTERACTION WITH PIP4P1.
RX PubMed=29644770; DOI=10.1111/gtc.12583;
RA Hashimoto Y., Shirane M., Nakayama K.I.;
RT "TMEM55B contributes to lysosomal homeostasis and amino acid-induced mTORC1
RT activation.";
RL Genes Cells 23:418-434(2018).
RN [9]
RP INTERACTION WITH TFE3.
RX PubMed=30595499; DOI=10.1016/j.stem.2018.11.021;
RA Villegas F., Lehalle D., Mayer D., Rittirsch M., Stadler M.B., Zinner M.,
RA Olivieri D., Vabres P., Duplomb-Jego L., De Bont E.S.J.M., Duffourd Y.,
RA Duijkers F., Avila M., Genevieve D., Houcinat N., Jouan T., Kuentz P.,
RA Lichtenbelt K.D., Thauvin-Robinet C., St-Onge J., Thevenon J.,
RA van Gassen K.L.I., van Haelst M., van Koningsbruggen S., Hess D.,
RA Smallwood S.A., Riviere J.B., Faivre L., Betschinger J.;
RT "Lysosomal signaling licenses embryonic stem cell differentiation via
RT inactivation of Tfe3.";
RL Cell Stem Cell 24:257-270(2019).
CC -!- FUNCTION: Guanine nucleotide-binding protein that plays a crucial role
CC in the cellular response to amino acid availability through regulation
CC of the mTORC1 signaling cascade. Forms heterodimeric Rag complexes with
CC RRAGA or RRAGB and cycles between an inactive GTP-bound and an active
CC GDP-bound form. In its active form participates in the relocalization
CC of mTORC1 to the lysosomes and its subsequent activation by the GTPase
CC RHEB. This is a crucial step in the activation of the TOR signaling
CC cascade by amino acids. {ECO:0000250|UniProtKB:Q9HB90}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000250|UniProtKB:Q9HB90};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000250|UniProtKB:Q9HB90};
CC -!- ACTIVITY REGULATION: In high-amino acid conditions, activated by GTPase
CC activating protein (GAP) FLCN that stimulates RRAGC GTPase activity to
CC turn it into its active GDP-bound form. {ECO:0000250|UniProtKB:Q9HB90}.
CC -!- SUBUNIT: Forms a heterodimer with RRAGA, in a sequence-independent
CC manner, and RRAGB (By similarity). Heterodimerization stabilizes
CC proteins of the heterodimer (By similarity). In complex with RRAGA or
CC RRAGB, interacts with RPTOR; this interaction is particularly efficient
CC with GTP-loaded RRAGB and GDP-loaded RRAGC (By similarity). Component
CC of the lysosomal folliculin complex (LFC), composed of FLCN, FNIP1 (or
CC FNIP2), RRAGA/RagA or RRAGB/RagB GDP-bound, RRAGC/RagC or RRAGD/RagD
CC GTP-bound, and Ragulator (By similarity). Interacts with NOL8 (By
CC similarity). Interacts with SH3BP4; the interaction with this negative
CC regulator is most probably direct, preferentially occurs with the
CC inactive GDP-bound form of RRAGB, is negatively regulated by amino
CC acids and prevents interaction with RPTOR (By similarity). The Rag
CC heterodimer interacts with SLC38A9; the probable amino acid sensor (By
CC similarity). Interacts with SESN1, SESN2 and SESN3 (PubMed:25259925).
CC Interacts with PIP4P1 (PubMed:29644770). The GDP-bound form interacts
CC with TFE3 (PubMed:30595499). {ECO:0000250|UniProtKB:Q9HB90,
CC ECO:0000269|PubMed:25259925, ECO:0000269|PubMed:29644770,
CC ECO:0000269|PubMed:30595499}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9HB90}. Nucleus
CC {ECO:0000250|UniProtKB:Q9HB90}. Lysosome
CC {ECO:0000250|UniProtKB:Q9HB90}. Note=Predominantly cytoplasmic. May
CC shuttle between the cytoplasm and nucleus, depending on the bound
CC nucleotide state of associated RRAGA. {ECO:0000250|UniProtKB:Q9HB90}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000303|PubMed:10660099};
CC IsoId=Q99K70-1; Sequence=Displayed;
CC Name=2 {ECO:0000303|PubMed:15489334};
CC IsoId=Q99K70-2; Sequence=VSP_052076, VSP_052077;
CC -!- TISSUE SPECIFICITY: Expressed most abundantly in kidney. Moderately
CC expressed in brain, ovary, and testis, and detected at lower levels in
CC heart, liver, and muscle. Not detected in lung, spleen, and small
CC intestine. Widely expressed in tumor cells, with expression being
CC specifically up-regulated in highly metastatic cells.
CC {ECO:0000269|PubMed:10660099}.
CC -!- SIMILARITY: Belongs to the GTR/RAG GTP-binding protein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA75671.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB017616; BAA75671.1; ALT_FRAME; mRNA.
DR EMBL; AK159355; BAE35013.1; -; mRNA.
DR EMBL; AK166658; BAE38923.1; -; mRNA.
DR EMBL; AL606962; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005417; AAH05417.1; -; mRNA.
DR EMBL; BC037732; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC071245; AAH71245.1; -; mRNA.
DR CCDS; CCDS18622.1; -. [Q99K70-1]
DR RefSeq; NP_059503.2; NM_017475.2. [Q99K70-1]
DR PDB; 5X6V; X-ray; 2.02 A; G=238-375.
DR PDBsum; 5X6V; -.
DR AlphaFoldDB; Q99K70; -.
DR SMR; Q99K70; -.
DR BioGRID; 207590; 11.
DR STRING; 10090.ENSMUSP00000030399; -.
DR iPTMnet; Q99K70; -.
DR PhosphoSitePlus; Q99K70; -.
DR EPD; Q99K70; -.
DR jPOST; Q99K70; -.
DR MaxQB; Q99K70; -.
DR PaxDb; Q99K70; -.
DR PeptideAtlas; Q99K70; -.
DR PRIDE; Q99K70; -.
DR ProteomicsDB; 260936; -. [Q99K70-1]
DR ProteomicsDB; 260937; -. [Q99K70-2]
DR Antibodypedia; 17665; 289 antibodies from 28 providers.
DR DNASU; 54170; -.
DR Ensembl; ENSMUST00000030399; ENSMUSP00000030399; ENSMUSG00000028646. [Q99K70-1]
DR Ensembl; ENSMUST00000155757; ENSMUSP00000115232; ENSMUSG00000028646. [Q99K70-2]
DR GeneID; 54170; -.
DR KEGG; mmu:54170; -.
DR UCSC; uc008uqm.1; mouse. [Q99K70-1]
DR CTD; 64121; -.
DR MGI; MGI:1858751; Rragc.
DR VEuPathDB; HostDB:ENSMUSG00000028646; -.
DR eggNOG; KOG3887; Eukaryota.
DR GeneTree; ENSGT00950000183031; -.
DR HOGENOM; CLU_047421_1_1_1; -.
DR InParanoid; Q99K70; -.
DR OMA; RACSHQA; -.
DR OrthoDB; 1216811at2759; -.
DR PhylomeDB; Q99K70; -.
DR TreeFam; TF300659; -.
DR Reactome; R-MMU-1632852; Macroautophagy.
DR Reactome; R-MMU-165159; MTOR signalling.
DR Reactome; R-MMU-166208; mTORC1-mediated signalling.
DR Reactome; R-MMU-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR Reactome; R-MMU-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-MMU-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-MMU-9639288; Amino acids regulate mTORC1.
DR BioGRID-ORCS; 54170; 26 hits in 75 CRISPR screens.
DR ChiTaRS; Rragc; mouse.
DR PRO; PR:Q99K70; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q99K70; protein.
DR Bgee; ENSMUSG00000028646; Expressed in secondary oocyte and 260 other tissues.
DR Genevisible; Q99K70; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:HGNC.
DR GO; GO:1990131; C:Gtr1-Gtr2 GTPase complex; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:HGNC.
DR GO; GO:0019003; F:GDP binding; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; ISS:HGNC.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0051020; F:GTPase binding; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0034198; P:cellular response to amino acid starvation; ISO:MGI.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IBA:GO_Central.
DR GO; GO:0009267; P:cellular response to starvation; IBA:GO_Central.
DR GO; GO:0032008; P:positive regulation of TOR signaling; ISS:UniProtKB.
DR GO; GO:0010506; P:regulation of autophagy; IBA:GO_Central.
DR GO; GO:0032006; P:regulation of TOR signaling; ISO:MGI.
DR GO; GO:1903432; P:regulation of TORC1 signaling; ISO:MGI.
DR GO; GO:0043200; P:response to amino acid; ISO:MGI.
DR CDD; cd11385; RagC_like; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR006762; Gtr1_RagA.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039400; RagC/D.
DR PANTHER; PTHR11259; PTHR11259; 1.
DR Pfam; PF04670; Gtr1_RagA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; GTP-binding;
KW Hydrolase; Lysosome; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9HB90"
FT CHAIN 2..398
FT /note="Ras-related GTP-binding protein C"
FT /id="PRO_0000239952"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 67..74
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P53290"
FT BINDING 115..119
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q00582"
FT BINDING 177..180
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P53290"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HB90"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HB90"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HB90"
FT MOD_RES 95
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT VAR_SEQ 147..182
FT /note="DDYMEALTRLHITVSKAYKVNPDMNFEVFIHKVDGL -> VVRHDGVCTSLV
FT AKRQRKGGKLFVSFVMCLKLLSFQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10660099,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_052076"
FT VAR_SEQ 183..398
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10660099,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_052077"
FT CONFLICT 19..20
FT /note="AD -> R (in Ref. 1; BAA75671)"
FT /evidence="ECO:0000305"
FT CONFLICT 55
FT /note="G -> R (in Ref. 1; BAA75671)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="A -> DA (in Ref. 1; BAA75671)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="S -> H (in Ref. 1; BAA75671)"
FT /evidence="ECO:0000305"
FT CONFLICT 376..398
FT /note="CSHQTSAPSLKALAHNGTPRNAI -> TSCR (in Ref. 2;
FT BAE38923)"
FT /evidence="ECO:0000305"
FT CONFLICT 386
FT /note="K -> R (in Ref. 1; BAA75671)"
FT /evidence="ECO:0000305"
FT HELIX 239..253
FT /evidence="ECO:0007829|PDB:5X6V"
FT STRAND 256..262
FT /evidence="ECO:0007829|PDB:5X6V"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:5X6V"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:5X6V"
FT HELIX 278..298
FT /evidence="ECO:0007829|PDB:5X6V"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:5X6V"
FT STRAND 314..319
FT /evidence="ECO:0007829|PDB:5X6V"
FT STRAND 322..341
FT /evidence="ECO:0007829|PDB:5X6V"
FT HELIX 344..347
FT /evidence="ECO:0007829|PDB:5X6V"
FT HELIX 348..368
FT /evidence="ECO:0007829|PDB:5X6V"
SQ SEQUENCE 398 AA; 44121 MW; 094F670E44B37A25 CRC64;
MSLQYGAEET PLAGSYGAAD SFPKDFGYGV EEEEEEAAAG GGGGAGAGGG CGPGGADSSK
PRILLMGLRR SGKSSIQKVV FHKMSPNETL FLESTNKIYK DDISNSSFVN FQIWDFPGQM
DFFDPTFDYE MIFRGTGALI YVIDAQDDYM EALTRLHITV SKAYKVNPDM NFEVFIHKVD
GLSDDHKIET QRDIHQRAND DLADAGLEKL HLSFYLTSIY DHSIFEAFSK VVQKLIPQLP
TLENLLNIFI SNSGIEKAFL FDVVSKIYIA TDSSPVDMQS YELCCDMIDV VIDVSCIYGL
KEDGSGSAYD KESMAIIKLN NTTVLYLKEV TKFLALVCIL REESFERKGL IDYNFHCFRK
AIHEVFEVGV TSHRSCSHQT SAPSLKALAH NGTPRNAI
