TSC2_MOUSE
ID TSC2_MOUSE Reviewed; 1814 AA.
AC Q61037; P97723; P97724; P97725; P97727; Q61007; Q61008; Q9WUF6;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Tuberin;
DE AltName: Full=Tuberous sclerosis 2 protein homolog;
GN Name=Tsc2;
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 (ISOFORMS A; B; C; D; E; F AND G).
RC TISSUE=Heart;
RX PubMed=8777431;
RA Kim K.K., Pajak L., Wang H., Field L.J.;
RT "Cloning, developmental expression, and evidence for alternative splicing
RT of the murine tuberous sclerosis (TSC2) gene product.";
RL Cell. Mol. Biol. Res. 41:515-526(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RX PubMed=8833243; DOI=10.1007/s003359900057;
RA Olsson P.G., Schofield J.N., Edwards Y.H., Frischauf A.M.;
RT "Expression and differential splicing of the mouse TSC2 homolog.";
RL Mamm. Genome 7:212-215(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE OF 1-199.
RC STRAIN=BALB/cJ; TISSUE=Leukocyte;
RX PubMed=9743625; DOI=10.1006/jmbi.1998.2042;
RA Sarker A.H., Ikeda S., Nakano H., Terato H., Ide H., Imai K., Akiyama K.,
RA Tsutsui K., Bo Z., Kubo K., Yamamoto K., Yasui A., Yoshida M.C., Seki S.;
RT "Cloning and characterization of a mouse homologue (mNthl1) of Escherichia
RT coli endonuclease III.";
RL J. Mol. Biol. 282:761-774(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 119-1805.
RX PubMed=10584558; DOI=10.1017/s0016672399003985;
RA Kleymenova E.V., Declue J.E., Walker C.L.;
RT "Genetic variants of the tuberous sclerosis 2 tumour suppressor gene in
RT mouse t haplotypes.";
RL Genet. Res. 74:139-144(1999).
RN [5]
RP FUNCTION.
RX PubMed=16707451; DOI=10.1158/0008-5472.can-05-4510;
RA Jiang X., Yeung R.S.;
RT "Regulation of microtubule-dependent protein transport by the
RT TSC2/mammalian target of rapamycin pathway.";
RL Cancer Res. 66:5258-5269(2006).
RN [6]
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1132 AND SER-1772, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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).
CC -!- FUNCTION: In complex with TSC1, this tumor suppressor inhibits the
CC nutrient-mediated or growth factor-stimulated phosphorylation of S6K1
CC and EIF4EBP1 by negatively regulating mTORC1 signaling (By similarity).
CC Acts as a GTPase-activating protein (GAP) for the small GTPase RHEB, a
CC direct activator of the protein kinase activity of mTORC1 (By
CC similarity). May also play a role in microtubule-mediated protein
CC transport (PubMed:16707451). Also stimulates the intrinsic GTPase
CC activity of the Ras-related proteins RAP1A and RAB5 (By similarity).
CC {ECO:0000250|UniProtKB:P49815, ECO:0000250|UniProtKB:P49816,
CC ECO:0000269|PubMed:16707451}.
CC -!- SUBUNIT: Probably forms a complex composed of chaperones HSP90 and
CC HSP70, co-chaperones STIP1/HOP, CDC37, PPP5C, PTGES3/p23, TSC1 and
CC client protein TSC2 (By similarity). Probably forms a complex composed
CC of chaperones HSP90 and HSP70, co-chaperones CDC37, PPP5C, TSC1 and
CC client protein TSC2, CDK4, AKT, RAF1 and NR3C1; this complex does not
CC contain co-chaperones STIP1/HOP and PTGES3/p23 (By similarity). Forms a
CC complex containing HSP90AA1, TSC1 and TSC2; TSC1 is required to recruit
CC TCS2 to the complex thereby stabilizing TSC2 (By similarity). Interacts
CC with TSC1 and HERC1; the interaction with TSC1 stabilizes TSC2 and
CC prevents the interaction with HERC1 (By similarity). May also interact
CC with the adapter molecule RABEP1 (By similarity). The final complex may
CC contain TSC2 and RABEP1 linked to RAB5 (By similarity). Interacts with
CC HSPA1 and HSPA8 (By similarity). Interacts with DAPK1 (By similarity).
CC Interacts with FBXW5 (By similarity). Interacts with NAA10 (via C-
CC terminal domain) (By similarity). Interacts with RRAGA
CC (polyubiquitinated) (By similarity). Interacts with WDR45B (By
CC similarity). Interacts with RPAP3 and URI1 (By similarity). Interacts
CC with YWHAG (By similarity). {ECO:0000250|UniProtKB:P49815}.
CC -!- INTERACTION:
CC Q61037; Q9EP53: Tsc1; NbExp=6; IntAct=EBI-7924402, EBI-1202690;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Note=At steady state found
CC in association with membranes. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=G;
CC IsoId=Q61037-1; Sequence=Displayed;
CC Name=A;
CC IsoId=Q61037-2; Sequence=VSP_004473;
CC Name=B;
CC IsoId=Q61037-3; Sequence=VSP_004474;
CC Name=C;
CC IsoId=Q61037-4; Sequence=VSP_004476;
CC Name=D;
CC IsoId=Q61037-5; Sequence=VSP_004478;
CC Name=E;
CC IsoId=Q61037-6; Sequence=VSP_004477, VSP_004478, VSP_004479;
CC Name=F;
CC IsoId=Q61037-7; Sequence=VSP_004475, VSP_004477, VSP_004478,
CC VSP_004479, VSP_004480;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- PTM: Phosphorylation at Ser-1388, Ser-1419 or Ser-1421 does not affect
CC interaction with TSC1. Phosphorylation at Ser-939 and Thr-1465 by
CC PKB/AKT1 is induced by growth factor stimulation. Phosphorylation by
CC AMPK activates it and leads to negative regulation of the mTORC1
CC complex. Phosphorylated at Ser-1805 by RPS6KA1; phosphorylation
CC inhibits TSC2 ability to suppress mTORC1 signaling. Phosphorylated by
CC DAPK1. {ECO:0000250|UniProtKB:P49815}.
CC -!- PTM: Ubiquitinated by the DCX(FBXW5) E3 ubiquitin-protein ligase
CC complex, leading to its subsequent degradation. Ubiquitinated by MYCBP2
CC independently of its phosphorylation status leading to subsequent
CC degradation; association with TSC1 protects from ubiquitination.
CC {ECO:0000250|UniProtKB:P49815}.
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DR EMBL; U37775; AAA86902.1; -; mRNA.
DR EMBL; U37775; AAA86901.1; -; mRNA.
DR EMBL; U39818; AAB18754.1; -; mRNA.
DR EMBL; AB009371; BAA28845.1; -; Genomic_DNA.
DR EMBL; AF132986; AAD27867.1; -; mRNA.
DR AlphaFoldDB; Q61037; -.
DR SMR; Q61037; -.
DR IntAct; Q61037; 20.
DR MINT; Q61037; -.
DR STRING; 10090.ENSMUSP00000094986; -.
DR iPTMnet; Q61037; -.
DR PhosphoSitePlus; Q61037; -.
DR jPOST; Q61037; -.
DR MaxQB; Q61037; -.
DR PeptideAtlas; Q61037; -.
DR PRIDE; Q61037; -.
DR ProteomicsDB; 300036; -. [Q61037-1]
DR ProteomicsDB; 300037; -. [Q61037-2]
DR ProteomicsDB; 300038; -. [Q61037-3]
DR ProteomicsDB; 300039; -. [Q61037-4]
DR ProteomicsDB; 300040; -. [Q61037-5]
DR ProteomicsDB; 300041; -. [Q61037-6]
DR ProteomicsDB; 300042; -. [Q61037-7]
DR MGI; MGI:102548; Tsc2.
DR eggNOG; KOG3687; Eukaryota.
DR InParanoid; Q61037; -.
DR PhylomeDB; Q61037; -.
DR Reactome; R-MMU-1632852; Macroautophagy.
DR Reactome; R-MMU-165181; Inhibition of TSC complex formation by PKB.
DR Reactome; R-MMU-198323; AKT phosphorylates targets in the cytosol.
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-8854214; TBC/RABGAPs.
DR ChiTaRS; Tsc2; mouse.
DR PRO; PR:Q61037; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q61037; protein.
DR GO; GO:0005901; C:caveola; ISO:MGI.
DR GO; GO:0042995; C:cell projection; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005856; C:cytoskeleton; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0030426; C:growth cone; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005764; C:lysosome; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0033596; C:TSC1-TSC2 complex; ISO:MGI.
DR GO; GO:0071889; F:14-3-3 protein binding; IDA:MGI.
DR GO; GO:0005096; F:GTPase activator activity; ISO:MGI.
DR GO; GO:0051879; F:Hsp90 protein binding; ISO:MGI.
DR GO; GO:0019902; F:phosphatase binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0007568; P:aging; ISO:MGI.
DR GO; GO:0043276; P:anoikis; IMP:ParkinsonsUK-UCL.
DR GO; GO:0042100; P:B cell proliferation; IGI:MGI.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0030030; P:cell projection organization; ISO:MGI.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IMP:MGI.
DR GO; GO:0030010; P:establishment of cell polarity; ISO:MGI.
DR GO; GO:0045184; P:establishment of protein localization; ISO:MGI.
DR GO; GO:0098976; P:excitatory chemical synaptic transmission; IMP:MGI.
DR GO; GO:0046323; P:glucose import; IMP:MGI.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0098977; P:inhibitory chemical synaptic transmission; IMP:MGI.
DR GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; IMP:MGI.
DR GO; GO:0050771; P:negative regulation of axonogenesis; ISO:MGI.
DR GO; GO:0030889; P:negative regulation of B cell proliferation; IGI:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:MGI.
DR GO; GO:0045792; P:negative regulation of cell size; ISO:MGI.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISO:MGI.
DR GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; ISO:MGI.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; ISO:MGI.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0016242; P:negative regulation of macroautophagy; ISO:MGI.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; ISO:MGI.
DR GO; GO:0014067; P:negative regulation of phosphatidylinositol 3-kinase signaling; IMP:MGI.
DR GO; GO:0048550; P:negative regulation of pinocytosis; ISO:MGI.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IMP:MGI.
DR GO; GO:0051898; P:negative regulation of protein kinase B signaling; IMP:MGI.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0042130; P:negative regulation of T cell proliferation; IGI:MGI.
DR GO; GO:0032007; P:negative regulation of TOR signaling; IMP:MGI.
DR GO; GO:1904262; P:negative regulation of TORC1 signaling; IMP:ParkinsonsUK-UCL.
DR GO; GO:1905563; P:negative regulation of vascular endothelial cell proliferation; ISO:MGI.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; ISO:MGI.
DR GO; GO:0001843; P:neural tube closure; IMP:MGI.
DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IMP:MGI.
DR GO; GO:0050918; P:positive chemotaxis; IMP:MGI.
DR GO; GO:0010508; P:positive regulation of autophagy; IMP:ParkinsonsUK-UCL.
DR GO; GO:0045785; P:positive regulation of cell adhesion; ISO:MGI.
DR GO; GO:0060999; P:positive regulation of dendritic spine development; ISO:MGI.
DR GO; GO:0010763; P:positive regulation of fibroblast migration; ISO:MGI.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:InterPro.
DR GO; GO:0016239; P:positive regulation of macroautophagy; IMP:ParkinsonsUK-UCL.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0006606; P:protein import into nucleus; IMP:MGI.
DR GO; GO:0043491; P:protein kinase B signaling; IMP:MGI.
DR GO; GO:0008104; P:protein localization; IDA:MGI.
DR GO; GO:0034394; P:protein localization to cell surface; ISO:MGI.
DR GO; GO:0044861; P:protein transport into plasma membrane raft; IMP:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central.
DR GO; GO:0030100; P:regulation of endocytosis; IMP:MGI.
DR GO; GO:0046626; P:regulation of insulin receptor signaling pathway; IMP:MGI.
DR GO; GO:0099175; P:regulation of postsynapse organization; ISO:MGI.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
DR GO; GO:0001666; P:response to hypoxia; IMP:MGI.
DR GO; GO:0007165; P:signal transduction; ISO:MGI.
DR GO; GO:0035176; P:social behavior; ISO:MGI.
DR GO; GO:0042098; P:T cell proliferation; IGI:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IMP:MGI.
DR Gene3D; 3.40.50.11210; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR035974; Rap/Ran-GAP_sf.
DR InterPro; IPR000331; Rap/Ran_GAP_dom.
DR InterPro; IPR003913; Tuberin.
DR InterPro; IPR018515; Tuberin-type_domain.
DR InterPro; IPR027107; Tuberin/Ral-act_asu.
DR InterPro; IPR024584; Tuberin_N.
DR PANTHER; PTHR10063; PTHR10063; 3.
DR Pfam; PF11864; DUF3384; 1.
DR Pfam; PF02145; Rap_GAP; 1.
DR Pfam; PF03542; Tuberin; 1.
DR PRINTS; PR01431; TUBERIN.
DR SUPFAM; SSF111347; SSF111347; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50085; RAPGAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; GTPase activation; Membrane;
KW Phosphoprotein; Reference proteome; Tumor suppressor; Ubl conjugation.
FT CHAIN 1..1814
FT /note="Tuberin"
FT /id="PRO_0000065655"
FT DOMAIN 1532..1766
FT /note="Rap-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00165"
FT REGION 1078..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1325..1356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1428..1490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1772..1798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1472..1487
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 540
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49815"
FT MOD_RES 664
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49815"
FT MOD_RES 927
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49815"
FT MOD_RES 939
FT /note="Phosphoserine; by PKB/AKT1"
FT /evidence="ECO:0000250|UniProtKB:P49815"
FT MOD_RES 981
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49815"
FT MOD_RES 1132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1155
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49815"
FT MOD_RES 1270
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49815"
FT MOD_RES 1339
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49815"
FT MOD_RES 1340
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49815"
FT MOD_RES 1348
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49815"
FT MOD_RES 1365
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49815"
FT MOD_RES 1388
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49815"
FT MOD_RES 1412
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49815"
FT MOD_RES 1419
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49815"
FT MOD_RES 1421
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49815"
FT MOD_RES 1455
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49815"
FT MOD_RES 1465
FT /note="Phosphothreonine; by PKB/AKT1"
FT /evidence="ECO:0000250|UniProtKB:P49815"
FT MOD_RES 1772
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1805
FT /note="Phosphoserine; by RPS6KA1"
FT /evidence="ECO:0000250|UniProtKB:P49815"
FT MOD_RES 1806
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49815"
FT VAR_SEQ 79..115
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000305"
FT /id="VSP_004473"
FT VAR_SEQ 534..572
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000305"
FT /id="VSP_004474"
FT VAR_SEQ 947..990
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000305"
FT /id="VSP_004476"
FT VAR_SEQ 947..989
FT /note="Missing (in isoform F)"
FT /evidence="ECO:0000305"
FT /id="VSP_004475"
FT VAR_SEQ 1245..1258
FT /note="GHAPVQVIVSATGC -> RDTALYKSLSVPAAG (in isoform E and
FT isoform F)"
FT /evidence="ECO:0000305"
FT /id="VSP_004477"
FT VAR_SEQ 1271..1293
FT /note="Missing (in isoform D, isoform E and isoform F)"
FT /evidence="ECO:0000305"
FT /id="VSP_004478"
FT VAR_SEQ 1693..1728
FT /note="GPACKCEWWRQPGEIVVWALPVVMELTVTILLCHLQ -> MEGLVDTSVAKI
FT VSDRNLSFVARQMALHAN (in isoform E and isoform F)"
FT /evidence="ECO:0000305"
FT /id="VSP_004479"
FT VAR_SEQ 1776..1814
FT /note="Missing (in isoform F)"
FT /evidence="ECO:0000305"
FT /id="VSP_004480"
FT CONFLICT 161
FT /note="Missing (in Ref. 2; AAA86902/AAA86901)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="G -> S (in Ref. 2; AAA86902/AAA86901)"
FT /evidence="ECO:0000305"
FT CONFLICT 462
FT /note="A -> R (in Ref. 2; AAA86902/AAA86901)"
FT /evidence="ECO:0000305"
FT CONFLICT 476
FT /note="I -> N (in Ref. 2; AAA86902/AAA86901)"
FT /evidence="ECO:0000305"
FT CONFLICT 549
FT /note="D -> N (in Ref. 2; AAA86902/AAA86901)"
FT /evidence="ECO:0000305"
FT CONFLICT 707
FT /note="K -> N (in Ref. 4; AAD27867)"
FT /evidence="ECO:0000305"
FT CONFLICT 861..862
FT /note="VP -> AA (in Ref. 2; AAA86902/AAA86901)"
FT /evidence="ECO:0000305"
FT CONFLICT 1127
FT /note="R -> P (in Ref. 2; AAA86902/AAA86901)"
FT /evidence="ECO:0000305"
FT CONFLICT 1665
FT /note="Missing (in Ref. 2; AAA86902/AAA86901)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1814 AA; 202071 MW; 913AB87194AADA5B CRC64;
MAKPTSKDSG LKEKFKILLG LGTSRPNPRC AEGKQTEFII TSEILRELSG ECGLNNRIRM
IGQICDVAKT KKLEEHAVEA LWKAVSDLLQ PERPPEARHA VLTLLKAIVQ GQGDRLGVLR
ALFFKVIKDY PSNEDLHERL EVFKALTDNG RHITYLEEEL AEFVLQWMDV GLSSEFLLVL
VNLVKFNSCY LDEYIASMVH MICLLCIRTV SSVDIEVSLQ VLDAVVCYNC LPAESLPLFI
ITLCRTINVK ELCEPCWKLM RNLLGTHLGH SAIYNMCRIM EDRSYMEDAP LLRGAVFFVG
MALWGAHRLY SLKNSPTSVL PSFYEAMTCP NEVVSYEIVL SITRLIKKYR KELQAVTWDI
LLDIIERLLQ QLQNLDSPEL KTIVHDLLTT VEELCDQNEF HGSQERYYEL VESYADQRPE
SSLLNLISYR AQSIHPAKDG WIQNLQLLME RFFRNECRSA VAIKVLDVLS FVLLIIRQFY
EEELINSVVI SQLSHIPEDK DHQVRKLATQ LLVDLAEGCH THHFNSLLDI IEKVMARSLS
PPPELEERDL AVHSASLEDV KTAVLGLLVI LQTKLYTLPA SHATRVYESL ISHIQLHYKH
GYSLPIASSI RLQAFDFLLL LRADSLHRLG LPNKDGVVRF SPYCLCDCME LDRASEKKAS
GPLSPPTGPP SPVPMGPAVR LGYLPYSLLF RVLLQCLKQE SDWKVLKLVL SRLPESLRYK
VLIFTSPCSV DQLSSALCSM LSAPKTLERL RGTPEGFSRT DLHLAVVPVL TALISYHNYL
DKTRQREMVY CLEQGLIYRC ASQCVVALAI CSVEMPDIII KALPVLVVKL THISATASMA
IPLLEFLSTL ARLPHLYRNF VPEQYASVFA ISLPYTNPSK FNQYIVCLAH HVIAMWFIRC
RLPFRKDFVP YITKGLRSNV LLSFDDTPEK DSFRARSTSL NERPKSLRIA RAPKQGLNNS
PPVKEFKESC AAEAFRCRSI SVSEHVVRSR IQTSLTSASL GSADENSMAQ ADDNLKNLHL
ELTETCLDMM ARYVFSNFTA VPKRSPVGEF LLAGGRTKTW LVGNKLVTVT TSVGTGTRSL
LGLDSGDLQG GSDSSSDPST HVRQTKEAPA KLESQAGQQV SRGARDRVRS MSGGHGLRVG
VLDTSAPYSP GGSASLGPQT AVAAKPEKPP AGAQLPTAEK TNLAAYVPLL TQGWAEILVR
RPTGNTSWLM SLENPLSPFS SDINNMPLQE LSNALMAAER FKEHGHAPVQ VIVSATGCTA
KPPTLPRSNT VASFSSLYQP SCQGQLHRSV SWADSAMVLE EGSPGETQVP VEPPELEDFE
AALGTDRHCQ RPDTYSRSSS ASSQEEKSHL EELAAGGIPI ERAISSEGAR PAVDLSFQPS
QPLSKSSSSP ELQTLQDILG DLGDKIDIGR LSPEAKVRSQ SGILDGEAAT WSATGEESRI
TVPPEGPLPS SSPRSPSGLR PRGYTISDSA PSRRGKRVER DNFKSRAAAS SAEKVPGINP
SFVFLQLYHS PFFGDESNKP ILLPNESFER SVQLLDQIPS YDTHKIAVLY VGEGQSSSEL
AILSNEHGSY RYTEFLTGLG RLIELKDCQP DKVYLGGLDV CGEDGQFTYC WHDDIMQAVF
HIATLMPTKD VDKHRCDKKR HLGNDFVSII YNDSGEDFKL GTIKQGQFNF VHVIITPLDY
KCNLLTLQCR KDGPACKCEW WRQPGEIVVW ALPVVMELTV TILLCHLQMA SQVHHSRSNP
TDIYPSKWIA RLRHIKRLRQ RIREEVHYSN PSLPLMHPPA HTKAPAQAPE ATPTYETGQR
KRLISSVDDF TEFV
