ID NF1_MOUSE Reviewed; 2841 AA. AC Q04690; Q61956; Q61957; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 27-MAR-2024, entry version 191. DE RecName: Full=Neurofibromin; DE AltName: Full=Neurofibromatosis-related protein NF-1; GN Name=Nf1; 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 [GENOMIC DNA / MRNA]. RC STRAIN=BALB/cJ; TISSUE=Brain; RX PubMed=8353485; DOI=10.1093/hmg/2.6.645; RA Bernards A., Snijders A.J., Hannigan G.E., Murthy A.E., Gusella J.F.; RT "Mouse neurofibromatosis type 1 cDNA sequence reveals high degree of RT conservation of both coding and non-coding mRNA segments."; RL Hum. Mol. Genet. 2:645-650(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1178-1555, ALTERNATIVE SPLICING (ISOFORMS I; RP II; III AND IV), AND TISSUE SPECIFICITY. RX PubMed=7958951; DOI=10.1016/0378-1119(94)90695-5; RA Mantani A., Makasugi S., Yokota Y., Abe K., Ushio Y., Yamamura K.; RT "A novel isoform of the neurofibromatosis type-1 mRNA and a switch of RT isoforms during murine cell differentiation and proliferation."; RL Gene 148:245-251(1994). RN [3] RP NUCLEOTIDE SEQUENCE OF 1950-2568. RX PubMed=2169593; DOI=10.1038/347291a0; RA Buchberg A.M., Cleveland L.S., Jenkins N.A., Copeland N.G.; RT "Sequence homology shared by neurofibromatosis type-1 gene and IRA-1 and RT IRA-2 negative regulators of the RAS cyclic AMP pathway."; RL Nature 347:291-294(1990). RN [4] RP PROTEIN SEQUENCE OF 1973-1979, AND IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=OF1; TISSUE=Hippocampus; RA Lubec G., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-866; SER-878; SER-2469; RP THR-2516; SER-2517; SER-2525 AND SER-2599, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, 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: Stimulates the GTPase activity of Ras. NF1 shows greater CC affinity for Ras GAP, but lower specific activity. May be a regulator CC of Ras activity. CC -!- SUBUNIT: Interacts with HTR6. Interacts with SPRED2. CC {ECO:0000250|UniProtKB:P21359}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P21359}. Nucleus, CC nucleolus {ECO:0000250|UniProtKB:P21359}. Cell membrane CC {ECO:0000250|UniProtKB:P21359}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=II {ECO:0000303|PubMed:7958951}; CC IsoId=Q04690-1; Sequence=Displayed; CC Name=I {ECO:0000303|PubMed:7958951}; CC IsoId=Q04690-2; Sequence=VSP_001633; CC Name=III {ECO:0000303|PubMed:7958951}; CC IsoId=Q04690-3; Sequence=VSP_001634, VSP_001635; CC Name=IV {ECO:0000303|Ref.4}; CC IsoId=Q04690-4; Sequence=VSP_001633, VSP_001634, VSP_001635; CC -!- TISSUE SPECIFICITY: [Isoform I]: Expressed predominantly in brain, CC spinal cord and testis. {ECO:0000269|PubMed:7958951}. CC -!- TISSUE SPECIFICITY: [Isoform II]: Expressed predominantly in adrenal CC gland, kidney, ovary and lung. {ECO:0000269|PubMed:7958951}. CC -!- TISSUE SPECIFICITY: [Isoform III]: Widely and more weakly expressed. CC Predominantly expressed in adrenal gland. {ECO:0000269|PubMed:7958951}. CC -!- TISSUE SPECIFICITY: [Isoform IV]: Widely and more weakly expressed. CC Expressed mainly in testis. {ECO:0000269|PubMed:7958951}. CC -!- DOMAIN: Binds phospholipids via a region that includes the CRAL-TRIO CC domain. Binds primarily glycerophospholipids with monounsaturated C18:1 CC and/or C16:1 fatty acid moieties and a phosphatidylethanolamine or CC phosphatidylcholine headgroup. Has lesser affinity for lipids CC containing phosphatidylserine and phosphatidylinositol (By similarity). CC {ECO:0000250}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L10369; AAA39806.1; -; Genomic_DNA. DR EMBL; L10367; AAA39806.1; JOINED; Genomic_DNA. DR EMBL; L10368; AAA39806.1; JOINED; Genomic_DNA. DR EMBL; L10370; AAA68132.1; -; mRNA. DR EMBL; X54924; CAA38690.1; -; mRNA. DR EMBL; D30730; BAA06395.1; -; mRNA. DR EMBL; D30731; BAA06396.1; -; mRNA. DR CCDS; CCDS25119.1; -. [Q04690-1] DR PIR; I53855; I53855. DR PIR; I54352; I54352. DR PIR; I67934; I67934. DR PIR; I68623; I68623. DR RefSeq; NP_035027.1; NM_010897.2. [Q04690-1] DR RefSeq; XP_006532504.1; XM_006532441.3. [Q04690-2] DR SMR; Q04690; -. DR BioGRID; 201736; 21. DR IntAct; Q04690; 11. DR MINT; Q04690; -. DR STRING; 10090.ENSMUSP00000071289; -. DR ChEMBL; CHEMBL2176807; -. DR GlyGen; Q04690; 4 sites, 1 O-linked glycan (4 sites). DR iPTMnet; Q04690; -. DR PhosphoSitePlus; Q04690; -. DR SwissPalm; Q04690; -. DR EPD; Q04690; -. DR jPOST; Q04690; -. DR MaxQB; Q04690; -. DR PaxDb; 10090-ENSMUSP00000071289; -. DR PeptideAtlas; Q04690; -. DR ProteomicsDB; 252826; -. [Q04690-1] DR ProteomicsDB; 252827; -. [Q04690-2] DR ProteomicsDB; 252828; -. [Q04690-3] DR ProteomicsDB; 252829; -. [Q04690-4] DR Pumba; Q04690; -. DR Antibodypedia; 3471; 583 antibodies from 39 providers. DR DNASU; 18015; -. DR Ensembl; ENSMUST00000071325.9; ENSMUSP00000071289.3; ENSMUSG00000020716.17. [Q04690-1] DR Ensembl; ENSMUST00000108251.9; ENSMUSP00000103886.3; ENSMUSG00000020716.17. [Q04690-2] DR GeneID; 18015; -. DR KEGG; mmu:18015; -. DR UCSC; uc007kkl.1; mouse. [Q04690-1] DR AGR; MGI:97306; -. DR CTD; 4763; -. DR MGI; MGI:97306; Nf1. DR VEuPathDB; HostDB:ENSMUSG00000020716; -. DR eggNOG; KOG1826; Eukaryota. DR GeneTree; ENSGT00550000074797; -. DR HOGENOM; CLU_000249_0_0_1; -. DR InParanoid; Q04690; -. DR OMA; TKEPYMF; -. DR OrthoDB; 1356198at2759; -. DR PhylomeDB; Q04690; -. DR TreeFam; TF300302; -. DR Reactome; R-MMU-5658442; Regulation of RAS by GAPs. DR BioGRID-ORCS; 18015; 17 hits in 87 CRISPR screens. DR ChiTaRS; Nf1; mouse. DR PRO; PR:Q04690; -. DR Proteomes; UP000000589; Chromosome 11. DR RNAct; Q04690; Protein. DR Bgee; ENSMUSG00000020716; Expressed in spermatocyte and 179 other cell types or tissues. DR ExpressionAtlas; Q04690; baseline and differential. DR GO; GO:0030424; C:axon; ISO:MGI. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0030425; C:dendrite; ISO:MGI. DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO. DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; ISO:MGI. DR GO; GO:0005886; C:plasma membrane; ISO:MGI. DR GO; GO:0098793; C:presynapse; IEA:GOC. DR GO; GO:0032991; C:protein-containing complex; ISO:MGI. DR GO; GO:0005096; F:GTPase activator activity; IMP:MGI. DR GO; GO:0008017; F:microtubule binding; ISO:MGI. DR GO; GO:0031210; F:phosphatidylcholine binding; ISS:UniProtKB. DR GO; GO:0008429; F:phosphatidylethanolamine binding; ISS:UniProtKB. DR GO; GO:0045545; F:syndecan binding; ISO:MGI. DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:MGI. DR GO; GO:0030325; P:adrenal gland development; IMP:MGI. DR GO; GO:0021764; P:amygdala development; IGI:MGI. DR GO; GO:0001525; P:angiogenesis; IGI:MGI. DR GO; GO:0006915; P:apoptotic process; IMP:MGI. DR GO; GO:0048844; P:artery morphogenesis; IMP:MGI. DR GO; GO:0048708; P:astrocyte differentiation; IMP:MGI. DR GO; GO:0007420; P:brain development; IMP:MGI. DR GO; GO:0048593; P:camera-type eye morphogenesis; IMP:MGI. DR GO; GO:0007154; P:cell communication; IMP:MGI. DR GO; GO:0016477; P:cell migration; IMP:MGI. DR GO; GO:0008283; P:cell population proliferation; IMP:MGI. DR GO; GO:0034605; P:cellular response to heat; IDA:MGI. DR GO; GO:0021987; P:cerebral cortex development; IMP:MGI. DR GO; GO:0050890; P:cognition; ISO:MGI. DR GO; GO:0030199; P:collagen fibril organization; IMP:MGI. DR GO; GO:0001935; P:endothelial cell proliferation; IMP:MGI. DR GO; GO:0030198; P:extracellular matrix organization; IMP:MGI. DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IMP:MGI. DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IMP:MGI. DR GO; GO:0048144; P:fibroblast proliferation; IMP:MGI. DR GO; GO:0021897; P:forebrain astrocyte development; IMP:MGI. DR GO; GO:0048853; P:forebrain morphogenesis; IMP:MGI. DR GO; GO:0061534; P:gamma-aminobutyric acid secretion, neurotransmission; IGI:MGI. DR GO; GO:0014009; P:glial cell proliferation; IMP:MGI. DR GO; GO:0061535; P:glutamate secretion, neurotransmission; IGI:MGI. DR GO; GO:0048820; P:hair follicle maturation; IMP:MGI. DR GO; GO:0007507; P:heart development; IMP:MGI. DR GO; GO:0071887; P:leukocyte apoptotic process; IMP:MGI. DR GO; GO:0001889; P:liver development; IMP:MGI. DR GO; GO:0060291; P:long-term synaptic potentiation; IMP:MGI. DR GO; GO:0000165; P:MAPK cascade; IMP:MGI. DR GO; GO:0033024; P:mast cell apoptotic process; IGI:MGI. DR GO; GO:0070662; P:mast cell proliferation; IGI:MGI. DR GO; GO:0001656; P:metanephros development; IMP:MGI. DR GO; GO:0022011; P:myelination in peripheral nervous system; IMP:MGI. DR GO; GO:0033028; P:myeloid cell apoptotic process; IMP:MGI. DR GO; GO:0097529; P:myeloid leukocyte migration; IGI:MGI. DR GO; GO:0016525; P:negative regulation of angiogenesis; IGI:MGI. DR GO; GO:0048712; P:negative regulation of astrocyte differentiation; IMP:MGI. DR GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:MGI. DR GO; GO:0001953; P:negative regulation of cell-matrix adhesion; IGI:MGI. DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IMP:MGI. DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; IMP:BHF-UCL. DR GO; GO:0060253; P:negative regulation of glial cell proliferation; IMP:MGI. DR GO; GO:0002686; P:negative regulation of leukocyte migration; IGI:MGI. DR GO; GO:0043409; P:negative regulation of MAPK cascade; IMP:MGI. DR GO; GO:0070667; P:negative regulation of mast cell proliferation; IGI:MGI. DR GO; GO:0007406; P:negative regulation of neuroblast proliferation; IMP:MGI. DR GO; GO:0046929; P:negative regulation of neurotransmitter secretion; IMP:MGI. DR GO; GO:0048715; P:negative regulation of oligodendrocyte differentiation; IMP:MGI. DR GO; GO:0045671; P:negative regulation of osteoclast differentiation; IGI:MGI. DR GO; GO:0042308; P:negative regulation of protein import into nucleus; IMP:MGI. DR GO; GO:0035021; P:negative regulation of Rac protein signal transduction; IGI:MGI. DR GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IMP:MGI. DR GO; GO:1900148; P:negative regulation of Schwann cell migration; IMP:MGI. DR GO; GO:0010626; P:negative regulation of Schwann cell proliferation; IMP:MGI. DR GO; GO:2000647; P:negative regulation of stem cell proliferation; IGI:MGI. DR GO; GO:1904753; P:negative regulation of vascular associated smooth muscle cell migration; IGI:MGI. DR GO; GO:0021915; P:neural tube development; IGI:MGI. DR GO; GO:0007405; P:neuroblast proliferation; IMP:MGI. DR GO; GO:0051402; P:neuron apoptotic process; IMP:MGI. DR GO; GO:0007269; P:neurotransmitter secretion; IMP:MGI. DR GO; GO:0098597; P:observational learning; IGI:MGI. DR GO; GO:0048709; P:oligodendrocyte differentiation; IMP:MGI. DR GO; GO:0001649; P:osteoblast differentiation; IMP:MGI. DR GO; GO:0030316; P:osteoclast differentiation; IGI:MGI. DR GO; GO:0007422; P:peripheral nervous system development; IMP:MGI. DR GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; IMP:MGI. DR GO; GO:0043473; P:pigmentation; IMP:MGI. DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:MGI. DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IGI:MGI. DR GO; GO:2001241; P:positive regulation of extrinsic apoptotic signaling pathway in absence of ligand; IMP:MGI. DR GO; GO:2000108; P:positive regulation of leukocyte apoptotic process; IMP:MGI. DR GO; GO:0033027; P:positive regulation of mast cell apoptotic process; IGI:MGI. DR GO; GO:0033034; P:positive regulation of myeloid cell apoptotic process; IMP:MGI. DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:MGI. DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI. DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; IGI:MGI. DR GO; GO:0098926; P:postsynaptic signal transduction; ISO:MGI. DR GO; GO:0006606; P:protein import into nucleus; IMP:MGI. DR GO; GO:0016601; P:Rac protein signal transduction; IGI:MGI. DR GO; GO:0007265; P:Ras protein signal transduction; IMP:MGI. DR GO; GO:0045765; P:regulation of angiogenesis; IMP:MGI. DR GO; GO:0043535; P:regulation of blood vessel endothelial cell migration; ISO:MGI. DR GO; GO:0045124; P:regulation of bone resorption; IMP:MGI. DR GO; GO:0042127; P:regulation of cell population proliferation; IGI:MGI. DR GO; GO:0001952; P:regulation of cell-matrix adhesion; IMP:MGI. DR GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; IMP:MGI. DR GO; GO:0010468; P:regulation of gene expression; IGI:MGI. DR GO; GO:0045685; P:regulation of glial cell differentiation; IMP:MGI. DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IMP:MGI. DR GO; GO:1900271; P:regulation of long-term synaptic potentiation; IGI:MGI. DR GO; GO:0043408; P:regulation of MAPK cascade; IGI:MGI. DR GO; GO:0099159; P:regulation of modification of postsynaptic structure; ISO:MGI. DR GO; GO:0045664; P:regulation of neuron differentiation; ISO:MGI. DR GO; GO:0099175; P:regulation of postsynapse organization; IDA:SynGO. DR GO; GO:0032228; P:regulation of synaptic transmission, GABAergic; IGI:MGI. DR GO; GO:0001666; P:response to hypoxia; IMP:MGI. DR GO; GO:0014044; P:Schwann cell development; IMP:MGI. DR GO; GO:0036135; P:Schwann cell migration; IMP:MGI. DR GO; GO:0014010; P:Schwann cell proliferation; IMP:MGI. DR GO; GO:0007519; P:skeletal muscle tissue development; IMP:MGI. DR GO; GO:0048745; P:smooth muscle tissue development; IMP:MGI. DR GO; GO:0021510; P:spinal cord development; IMP:MGI. DR GO; GO:0072089; P:stem cell proliferation; IGI:MGI. DR GO; GO:0048485; P:sympathetic nervous system development; IMP:MGI. DR GO; GO:1904738; P:vascular associated smooth muscle cell migration; IGI:MGI. DR GO; GO:1990874; P:vascular associated smooth muscle cell proliferation; IGI:MGI. DR GO; GO:0008542; P:visual learning; IMP:MGI. DR GO; GO:0042060; P:wound healing; IMP:MGI. DR CDD; cd13313; PH_NF1; 1. DR CDD; cd05130; RasGAP_Neurofibromin; 1. DR CDD; cd00170; SEC14; 1. DR Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR001251; CRAL-TRIO_dom. DR InterPro; IPR036865; CRAL-TRIO_dom_sf. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR039360; Ras_GTPase. DR InterPro; IPR023152; RasGAP_CS. DR InterPro; IPR001936; RasGAP_dom. DR InterPro; IPR008936; Rho_GTPase_activation_prot. DR PANTHER; PTHR10194:SF142; NEUROFIBROMIN; 1. DR PANTHER; PTHR10194; RAS GTPASE-ACTIVATING PROTEINS; 1. DR Pfam; PF13716; CRAL_TRIO_2; 1. DR Pfam; PF00616; RasGAP; 1. DR SMART; SM00323; RasGAP; 1. DR SMART; SM00516; SEC14; 1. DR SUPFAM; SSF48371; ARM repeat; 1. DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1. DR PROSITE; PS50191; CRAL_TRIO; 1. DR PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1. DR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1. DR Genevisible; Q04690; MM. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Cell membrane; KW Direct protein sequencing; GTPase activation; Lipid-binding; Membrane; KW Nucleus; Phosphoprotein; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P97526" FT CHAIN 2..2841 FT /note="Neurofibromin" FT /id="PRO_0000056666" FT DOMAIN 1237..1453 FT /note="Ras-GAP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00167" FT DOMAIN 1582..1740 FT /note="CRAL-TRIO" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056" FT REGION 1582..1839 FT /note="Lipid binding" FT /evidence="ECO:0000250" FT REGION 2786..2841 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 2557..2573 FT /note="Bipartite nuclear localization signal" FT /evidence="ECO:0000250" FT COMPBIAS 2805..2833 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:P97526" FT MOD_RES 866 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 878 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 2190 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P21359" FT MOD_RES 2469 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 2516 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 2517 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 2523 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P21359" FT MOD_RES 2525 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 2545 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P21359" FT MOD_RES 2567 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P21359" FT MOD_RES 2599 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 2804 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P21359" FT MOD_RES 2819 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P21359" FT VAR_SEQ 1373..1393 FT /note="Missing (in isoform I and isoform IV)" FT /evidence="ECO:0000305" FT /id="VSP_001633" FT VAR_SEQ 1394..1406 FT /note="VVSQRFPQNSIGA -> VPKSSCFSCLNNRWLASASLRTASVP (in FT isoform III and isoform IV)" FT /evidence="ECO:0000305" FT /id="VSP_001634" FT VAR_SEQ 1407..2841 FT /note="Missing (in isoform III and isoform IV)" FT /evidence="ECO:0000305" FT /id="VSP_001635" SQ SEQUENCE 2841 AA; 319596 MW; 06650BDCDC531002 CRC64; MAAHRPVEWV QAVVSRFDEQ LPIKTGQQNT HTKVSTEHNK ECLINISKYK FSLVISGLTT ILKNVNNMRI FGEAAEKNLY LSQLIILDTL EKCLAGQPKD TMRLDETMLV KQLLPEICHF LHTCREGNQH AAELRNSASG VLFSLSCNNF NAVFSRISTR LQELTVCSED NVDVHDIELL QYINVDCAKL KRLLKETAFK FKALKKVAQL AVINSLEKAF WNWVENYPDE FTKLYQIPQT DMAECAEKLF DLVDGFAEST KRKAAVWPLQ IILLILCPEI IQDISKDVVD ESNINKKLFL DSLRKALAGH GGSRQLTESA AIACVKLCKA STYINWEDNS VIFLLVQSMV VDLKNLLFNP SKPFSRGSQP ADVDLMIDCL VSCFRISPHN NQHFKICLAQ NSPSTFHYVL VNSLHRIITN SALDWWPKID AVYCHSVELR NMFGETLHKA VQGCGAHPAI RMAPSLTFKE KVTSLKFKEK PTDLETRSYK CLLLSMVKLI HADPKLLLCN PRKQGPETQS STAELITGLV QLVPQSHMPE VAQEAMEALL VLHQLDSIDL WNPDAPVETF WEISSQMLFY ICKKLTSHQM LSSTEILKWL REILICRNKF LLKNKQADRS SCHSLYLYGV GCEMSATGNT TQMSVDHDEF LRACTPGASL RKGRGNSSMD STAGCSGTPP ICRQAQTKLE VALYMFLWNP DTEAVLVAMS CFRHLCEEAD IRCGVDEVSV HNFLPNYNTF MEFASVSNMM STGRAALQKR VMALLRRIEH PTAGNIEAWE DTHAKWEQAT KLILNYPKAK MEDGQAAESL HKTIVKRRMS HVSGGGSIDL SDTDSLQEWI NMTGFLCALG GVCLQQRSSS GLATYSPPMG AVSERKGSMI SVMSSEGNID SPVSRFMDRL LSLMVCNHEK VGLQIRTNVK DLVGLELSPA LYPMLFNKLK NTISKFFDSQ GQVLLSDSNT QFVEQTIAIM KNLLDNHTEG SSEHLGQASI ETMMLNLVRY VRVLGNMVHA IQIKTKLCQL VEVMMARRDD LSFCQEMKFR NKMVEYLTDW VMGTSNQAAD DDIKCLTRDL DQASMEAVVS LLAGLPLQPE EGDGVELMEA KSQLFLKYFT LFMNLLNDCS EVEDENAQTG GRKRGMSRRL ASLRHCTVLA MSNLLNANVD SGLMHSIGLG YHKDLQTRAT FMEVLTKILQ QGTEFDTLAE TVLADRFERL VELVTMMGDQ GELPIAMALA NVVPCSQWDE LARVLVTLFD SRHLLYQLLW NMFSKEVELA DSMQTLFRGN SLASKIMTFC FKVYGATYLQ KLLDPLLRVI ITSSDWQHVS FEVDPTRLEP SESLEENQRN LLQMTEKFFH AIISSSSEFP SQLRSVCHCL YQATCHSLLN KATVKERKEN KKSVVSQRFP QNSIGAVGSA MFLRFINPAI VSPYEAGILD KKPPPRIERG LKLMSKVLQS IANHVLFTKE EHMRPFNDFV KSNFDLARRF FLDIASDCPT SDAVNHSLSF ISDGNVLALH RLLWNNQEKI GQYLSSNRDH KAVGRRPFDK MATLLAYLGP PEHKPVADTH WSSLNLTSSK FEEFMTRHQV HEKEEFKALK TLSIFYQAGT SKAGNPIFYY VARRFKTGQI NGDLLIYHVL LTLKPYYAKP YEIVVDLTHT GPSNRFKTDF LSKWFVVFPG FAYDNVSAVY IYNCNSWVRE YTKYHERLLT GLKGSKRLIF IDCPGKLAEH IEHEQQKLPA ATLALEEDLK VFHNALKLAH KDTKVSIKVG STAVQVTSAE RTKVLGQSVF LNDIYYASEI EEICLVDENQ FTLTIANQGT PLTFMHQECE AIVQSIIHIR TRWELSQPDS IPQHTKIRPK DVPGTLLNIA LLNLGSSDPS LRSAAYNLLC ALTCTFNLKI EGQLLETSGL CIPANNTLFI VSISKTLAAN EPHLTLEFLE ECISGFSKSS IELKHLCLEY MTPWLSNLVR FCKHNDDAKR QRVTAILDKL ITMTINEKQM YPSIQAKIWG SLGQITDLLD VVLDSFIKTS ATGGLGSIKA EVMADTAVAL ASGNVKLVSS KVIGRMCKII DKTCLSPTPT LEQHLMWDDI AILARYMLML SFNNSLDVAA HLPYLFHVVT FLVATGPLSL RASTHGLLIN IIHSLCTCSQ LHFSEETKQV LRLSLTEFSL PKFYLLFGIS KVKSAAVIAF RSSYRDRSFS PGSYERETFA LTSLETVTEA LLEIMEACMR DIPTCKWLDQ WTELAQRFAF QYNPSLQPRA LVVFGCISKR VSHGQIKQII RILSKALESC LKGPDTYNSQ VLIESTVIAL TKLQPLLNKD SPLHKALFWV AVAVLQLDEV NLYSAGTALL EQNLHTLDSL RIFNDKSPEE VFMAIRNPLE WHCKQMDHFV GLNFNSNFNF ALVGHLLKGY RHPSPAIVAR TVRILHTLLT LVNKHRNCDK FEVNTQSVAY LAALLTVSEE VRSRCSLKHR KSLLLTDISM ENVPMDTYPI HHGDPSYRTL KETQPWSSPK GSEGYLAATY PAVGQTSPRA RKSMSLDMGQ PSQANTKKLL GTRKSFDHLI SDTKAPKRQE MESGITTPPK MRRVAETDYE METQRIPSSQ QHPHLRKVSV SESNVLLDEE VLTDPKIQAL LLTVLATLVK YTTDEFDQRI LYEYLAEASV VFPKVFPVVH NLLDSKINTL LSLCQDPNLL NPIHGIVQSV VYHEESPPQY QTSYLQSFGF NGLWRFAGPF SKQTQIPDYA ELIVKFLDAL IDTYLPGIDE ETSEESLLTP TSPYPPALQS QLSITANLNL SNSMTSLATS QHSPGLDKEN VELSPTAGHC NSGRTRHGSA SQVQKQRSAG SFKRNSIKKI V //