NF1_RAT
ID NF1_RAT Reviewed; 2820 AA.
AC P97526;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 29-SEP-2021, entry version 161.
DE RecName: Full=Neurofibromin;
DE AltName: Full=Neurofibromatosis-related protein NF-1;
GN Name=Nf1;
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]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Brain;
RA Kyritsis A.P., Lee P.S., Mochizuki H., Nishi T., Levin V.A., Saya H.;
RT "Differential splicing of the neurofibromatosis type 1 (NF1) gene in rats:
RT homologous splice variants in human are expressed in rat cells.";
RL Int. J. Oncol. 1:149-152(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=8982875; DOI=10.1093/oxfordjournals.jbchem.a021498;
RA Suzuki H., Takahashi K., Yasumoto K., Fuse N., Shibahara S.;
RT "Differential tissue-specific expression of neurofibromin isoform mRNAs in
RT rat.";
RL J. Biochem. 120:1048-1054(1996).
RN [3]
RP PROTEIN SEQUENCE OF 2-24; 51-63; 78-92; 104-111; 207-218; 249-262; 298-305;
RP 355-366; 462-469; 491-498; 767-785; 792-798; 972-999; 1003-1014; 1179-1209;
RP 1244-1252; 1266-1278; 1293-1327; 1340-1364; 1394-1410; 1426-1438;
RP 1451-1457; 1491-1507; 1550-1556; 1570-1592; 1619-1634; 1707-1726;
RP 1738-1750; 1810-1825; 1830-1851; 1952-1976; 1998-2025; 2132-2150;
RP 2153-2160; 2167-2175; 2206-2228; 2262-2281; 2331-2345; 2468-2498;
RP 2502-2516; 2596-2618 AND 2702-2714, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Pheochromocytoma;
RA Bienvenut W.V., von Kriegsheim A.F., Kolch W.;
RL Submitted (MAR-2007) to UniProtKB.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-866; SER-2169; SER-2504 AND
RP SER-2524, AND IDENTIFICATION BY 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: 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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with HTR6 (By similarity).
CC {ECO:0000250|UniProtKB:P21359}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, nucleolus
CC {ECO:0000250}.
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}.
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DR EMBL; D45201; BAA08141.1; -; mRNA.
DR PIR; JC5196; JC5196.
DR RefSeq; NP_036741.1; NM_012609.1.
DR SMR; P97526; -.
DR BioGRID; 246735; 7.
DR IntAct; P97526; 4.
DR MINT; P97526; -.
DR STRING; 10116.ENSRNOP00000050393; -.
DR CarbonylDB; P97526; -.
DR iPTMnet; P97526; -.
DR PhosphoSitePlus; P97526; -.
DR PaxDb; P97526; -.
DR PRIDE; P97526; -.
DR GeneID; 24592; -.
DR KEGG; rno:24592; -.
DR CTD; 4763; -.
DR RGD; 3168; Nf1.
DR eggNOG; KOG1826; Eukaryota.
DR InParanoid; P97526; -.
DR OrthoDB; 9686at2759; -.
DR PhylomeDB; P97526; -.
DR Reactome; R-RNO-5658442; Regulation of RAS by GAPs.
DR ChiTaRS; Nf1; rat.
DR PRO; PR:P97526; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030424; C:axon; IDA:HGNC-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:HGNC-UCL.
DR GO; GO:0030425; C:dendrite; IDA:HGNC-UCL.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:HGNC-UCL.
DR GO; GO:0014069; C:postsynaptic density; IDA:RGD.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0005096; F:GTPase activator activity; ISS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IDA: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; IPI:RGD.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISS:HGNC-UCL.
DR GO; GO:0030325; P:adrenal gland development; ISS:HGNC-UCL.
DR GO; GO:0021764; P:amygdala development; ISO:RGD.
DR GO; GO:0048844; P:artery morphogenesis; ISS:HGNC-UCL.
DR GO; GO:0007420; P:brain development; ISS:HGNC-UCL.
DR GO; GO:0048593; P:camera-type eye morphogenesis; ISS:HGNC-UCL.
DR GO; GO:0007154; P:cell communication; ISS:HGNC-UCL.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEP:RGD.
DR GO; GO:0034605; P:cellular response to heat; ISO:RGD.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEP:RGD.
DR GO; GO:0021987; P:cerebral cortex development; ISS:HGNC-UCL.
DR GO; GO:0050890; P:cognition; ISO:RGD.
DR GO; GO:0030199; P:collagen fibril organization; ISS:HGNC-UCL.
DR GO; GO:0030198; P:extracellular matrix organization; ISS:HGNC-UCL.
DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; ISO:RGD.
DR GO; GO:0021897; P:forebrain astrocyte development; ISS:HGNC-UCL.
DR GO; GO:0048853; P:forebrain morphogenesis; ISS:HGNC-UCL.
DR GO; GO:0061534; P:gamma-aminobutyric acid secretion, neurotransmission; ISO:RGD.
DR GO; GO:0061535; P:glutamate secretion, neurotransmission; ISO:RGD.
DR GO; GO:0048820; P:hair follicle maturation; ISO:RGD.
DR GO; GO:0007507; P:heart development; ISS:HGNC-UCL.
DR GO; GO:0001889; P:liver development; ISS:HGNC-UCL.
DR GO; GO:0000165; P:MAPK cascade; ISS:HGNC-UCL.
DR GO; GO:0001656; P:metanephros development; ISS:HGNC-UCL.
DR GO; GO:0022011; P:myelination in peripheral nervous system; ISS:HGNC-UCL.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISO:RGD.
DR GO; GO:0048712; P:negative regulation of astrocyte differentiation; ISO:RGD.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0001953; P:negative regulation of cell-matrix adhesion; ISO:RGD.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; ISO:RGD.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; ISS:UniProtKB.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; ISS:HGNC-UCL.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; ISS:HGNC-UCL.
DR GO; GO:0007406; P:negative regulation of neuroblast proliferation; ISS:HGNC-UCL.
DR GO; GO:0046929; P:negative regulation of neurotransmitter secretion; ISO:RGD.
DR GO; GO:0048715; P:negative regulation of oligodendrocyte differentiation; ISS:HGNC-UCL.
DR GO; GO:0045671; P:negative regulation of osteoclast differentiation; ISO:RGD.
DR GO; GO:0042308; P:negative regulation of protein import into nucleus; ISO:RGD.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; ISS:HGNC-UCL.
DR GO; GO:0035021; P:negative regulation of Rac protein signal transduction; ISO:RGD.
DR GO; GO:0046580; P:negative regulation of Ras protein signal transduction; ISO:RGD.
DR GO; GO:0021915; P:neural tube development; ISO:RGD.
DR GO; GO:0098597; P:observational learning; ISO:RGD.
DR GO; GO:0001649; P:osteoblast differentiation; ISS:HGNC-UCL.
DR GO; GO:0007422; P:peripheral nervous system development; ISS:HGNC-UCL.
DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; ISS:HGNC-UCL.
DR GO; GO:0043473; P:pigmentation; ISS:HGNC-UCL.
DR GO; GO:0045762; P:positive regulation of adenylate cyclase activity; ISS:HGNC-UCL.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:HGNC-UCL.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISO:RGD.
DR GO; GO:2001241; P:positive regulation of extrinsic apoptotic signaling pathway in absence of ligand; ISO:RGD.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISS:HGNC-UCL.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:RGD.
DR GO; GO:0007265; P:Ras protein signal transduction; ISS:HGNC-UCL.
DR GO; GO:0045765; P:regulation of angiogenesis; ISS:HGNC-UCL.
DR GO; GO:0043535; P:regulation of blood vessel endothelial cell migration; ISO:RGD.
DR GO; GO:0045124; P:regulation of bone resorption; ISS:HGNC-UCL.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0001952; P:regulation of cell-matrix adhesion; ISS:HGNC-UCL.
DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR GO; GO:0045685; P:regulation of glial cell differentiation; ISS:HGNC-UCL.
DR GO; GO:0043087; P:regulation of GTPase activity; IMP:HGNC-UCL.
DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; ISO:RGD.
DR GO; GO:1900271; P:regulation of long-term synaptic potentiation; ISO:RGD.
DR GO; GO:0043408; P:regulation of MAPK cascade; ISO:RGD.
DR GO; GO:0045664; P:regulation of neuron differentiation; IMP:RGD.
DR GO; GO:0032228; P:regulation of synaptic transmission, GABAergic; ISO:RGD.
DR GO; GO:0001666; P:response to hypoxia; ISS:HGNC-UCL.
DR GO; GO:0014044; P:Schwann cell development; ISS:HGNC-UCL.
DR GO; GO:0014037; P:Schwann cell differentiation; IEP:RGD.
DR GO; GO:0007519; P:skeletal muscle tissue development; ISO:RGD.
DR GO; GO:0048745; P:smooth muscle tissue development; ISS:HGNC-UCL.
DR GO; GO:0021510; P:spinal cord development; ISS:HGNC-UCL.
DR GO; GO:0048485; P:sympathetic nervous system development; ISS:HGNC-UCL.
DR GO; GO:0008542; P:visual learning; ISS:HGNC-UCL.
DR GO; GO:0042060; P:wound healing; ISS:HGNC-UCL.
DR CDD; cd00170; SEC14; 1.
DR Gene3D; 1.10.506.10; -; 2.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.40.525.10; -; 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; PTHR10194; 2.
DR Pfam; PF13716; CRAL_TRIO_2; 1.
DR Pfam; PF00616; RasGAP; 1.
DR SMART; SM00323; RasGAP; 1.
DR SMART; SM00516; SEC14; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
DR PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; GTPase activation; Lipid-binding;
KW Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.3"
FT CHAIN 2..2820
FT /note="Neurofibromin"
FT /id="PRO_0000056667"
FT DOMAIN 1237..1432
FT /note="Ras-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00167"
FT DOMAIN 1561..1719
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT REGION 1561..1818
FT /note="Lipid binding"
FT /evidence="ECO:0000250"
FT REGION 2457..2482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2768..2820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 2536..2552
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 2783..2812
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.3"
FT MOD_RES 866
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 878
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21359"
FT MOD_RES 2169
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2448
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04690"
FT MOD_RES 2495
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q04690"
FT MOD_RES 2496
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21359"
FT MOD_RES 2502
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21359"
FT MOD_RES 2504
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2524
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2546
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P21359"
FT MOD_RES 2578
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21359"
FT MOD_RES 2783
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21359"
FT MOD_RES 2798
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21359"
SQ SEQUENCE 2820 AA; 317083 MW; FC108487E86DA89F 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
DMAECAGKLF DLVDGFAEST KRKAAVWPLQ IILLILCPEI IQDISRDVVD ENNTNKKLFL
DSLRKALAGH GGSRQLTESA AIACVKLCKA STYINWEDNS VIFLLVQSMV VDLKNLLFNP
SKPFSRGSQP ADVDLMIDCL VSCFRISPHN NQHFKICLAQ NSPSTFHYVL VNSLHRIITN
SAWDWWPKID AVYCHSVELR NMFGETLHKA VQGCGAHPAL RMAPSLTFKE KVTSLKFKEK
PTDLEARSYK YLLLSMVKLI HADPKLLLCN PRKQGPETQG STAELITGLV QLVPQSHMPE
VAQEAMEALL VLHQLDSIDL WNPDAPVETF WEISSQMLFY ICKKLTSHQM LSSTEILKWL
REILICRNKF LLKNKQADRS SCHSLYLYGV GCDLPASGNV TQMSVDHEES LRTCAPGASL
RKGRGNSSMD STAGCSGTPP ICRQAQTKLE VALYMFLWSP DTEVVLVAMS CFRHLCEEAD
IRCGVDEVSV HNFLPNYNTF MEFASVSNML STGRAALQKR VMALLRRIEH PTAGNTEAWE
DTHAKWEQAT KLILNYPKAK MEDGQAAESL HKTIVKRRMS HVSGGGSIDL SDTDSLQEWI
NMTGFLCALG GVCLQQRSSS GLATYSPPMG PVSERKGSMI SVMSSEGNVD SPVSRFMDRL
LSLMVCNHEK VGLQIRTNVK DLVGLELSPA LYPMLFNKLK SAISKFFDSQ GQVLLTDSNT
QFVEQTIAIM KNLLDNHTEG SSEHLGQASI ETMMLNLVRY VRVLGNMVHA IQIKTKLCQL
VEVMMARRDD LSFCQEMKFR NKMVEYLTDW VMGTSNQAAD DDVKCLTRDL DQASMEAVVS
LLAGLPLQPE EGDGVELMEA KSQLFLKYFT LFMNLLNDCS EVEDENAQTG GRKRGMSRRL
ASLRHCTVLA MSNLLNANVD SGLMHSIGLG YHKDLQTRAT FMEVLTKILQ QGTEFDTLAE
TVLADRFERL VELVTMMGDQ GELPIAMALA NVVPCSQWDE LARVLVTLFD SRHLLYQLLW
NMFSKEVELA DSMQTLFRGN SLASKIMTFC FKVYGATYLQ KLLDPLLRII ITSSDWQHVS
FEVDPTRLEP SESLEENQRN LLQMTEKFFH AIISSSSEFP SQLRSVCHCL YQVVSQRFPQ
NSIGAVGSAM FLRFINPAIV SPYEAGILDK KPPPRIERGL KLMSKVLQSI ANHVLFTKEE
HMRPFNDFVK SNFDLARRFF LDIASDCPTS DAVNHSLSFI SDGNVLALHR LLWNNQEKIG
QYLSSNRDHK AVGRRPFDKM ATLLAYLGPP EHKPVADTHW SSLNLTSSKF EEFMTRHQVH
EKEEFKALKT LSIFYQAGTS KAGNPIFYYV ARRFKTGQIN GDLLIYHVLL TLKPYYAKPY
EIVVDLTHTG PSNRFKTDFL SKWFVVFPGF AYDNVSAVYI YNCNSWVREY TKYHERLLTG
LKGSKRLIFI DCPGKLAEHI EHEQQKLPAA TLALEEDLKV FHNALKLAHK DTKVSIKVGS
TAVQVTSAER TKVLGQSVFL NDIYYASEIE EICLVDENQF TLTIANQGTP LTFMHQECEA
IVQSIIHIRT RWELSQPDSI PQHTKIRPKD VPGTLLNIAL LNLGSSDPSL RSAAYNLLCA
LTCTFNLKIE GQLLETSGLC IPANNTLFIV SISKTLAANE PHLTLEFLEE CISGFSKSSI
ELKHLCLEYM TPWLSNLVRF CKHNDDAKRQ RVTAILDKLI TMTINEKQMY PSIQAKIWGS
LGQITDLLDV VLDSFIKTSA TGGLGSIKAE VMADTAVALA SGNVKLVSSK VIGRMCKIID
KTCLSPTPTL EQHLMWDDIA ILARYMLMLS FNNSLDVAAH LPYLFHVVTF LVATGPLSLR
ASTHGLVINI IHSLCTCSQL HFSEETKQVL RLSLTEFSLP KFYLLFGISK VKSAAVIAFR
SSYRDRSFSP GSYERETFAL TSLETVTEAL LEIMEACMRD IPTCKWLDQW TELAQRFAFQ
YNPSLQPRAL VVFGCISKRV SHGQIKQIIR ILSKALESCL KGPDTYNSQV LIEATVIALT
KLQPLLNKDS PLHKALFWVA VAVLQLDEVN LYSAGTALLE QNLHTLDSLR IFNDKSPEEV
FMAIRNPLEW HCKQMDHFVG LNFNSNFNFA LVGHLLKGYR HPSPAIVART VRILHTLLTL
VNKHRNCDKF EVNTQSVAYL AALLTVSEEV RSRCSLKHRK SLLLTDISME NVPMDTYPIH
HGDPSSRTLK ETQPWSSPRG SEGYLAATYP AVGQTSPRAR KSMSLDMGQP SQANTKKLLG
TRKSFDHLIS DTKAPKRQEM ESGITTPPKM RRVAETDYEM ETQRISSSQQ HPHLRKVSVS
ESNVLLDEEV LTDPKIQALL LTVLATLVKY TTDEFDQRIL YEYLAEASVV FPKVFPLVHN
LLDSKINTLL SLCQDPNLLN PIHGIVQSVV YHEESPPQYQ TSYLQSFGFN GLWRFAGPFS
KQTQIPDYAE LIVKFLDALI DTYLPGIDEE TSEESLLTPT SPYPPALQSQ LSITANLNLS
NSMTSLATSQ HSPGIDKENV ELSPTTGHCN SGRTRHGSAS QVQKQRSAGS FKRNSIKKIV
