位置:首页 > 蛋白库 > NF1_MOUSE
NF1_MOUSE
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   03-AUG-2022, entry version 182.
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, 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).
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 (By similarity).
CC       {ECO:0000250|UniProtKB:P21359}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, nucleolus
CC       {ECO:0000250}.
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; 20.
DR   IntAct; Q04690; 11.
DR   MINT; Q04690; -.
DR   STRING; 10090.ENSMUSP00000071289; -.
DR   ChEMBL; CHEMBL2176807; -.
DR   iPTMnet; Q04690; -.
DR   PhosphoSitePlus; Q04690; -.
DR   SwissPalm; Q04690; -.
DR   EPD; Q04690; -.
DR   jPOST; Q04690; -.
DR   MaxQB; Q04690; -.
DR   PaxDb; Q04690; -.
DR   PeptideAtlas; Q04690; -.
DR   PRIDE; Q04690; -.
DR   ProteomicsDB; 252826; -. [Q04690-1]
DR   ProteomicsDB; 252827; -. [Q04690-2]
DR   ProteomicsDB; 252828; -. [Q04690-3]
DR   ProteomicsDB; 252829; -. [Q04690-4]
DR   Antibodypedia; 3471; 487 antibodies from 39 providers.
DR   DNASU; 18015; -.
DR   Ensembl; ENSMUST00000071325; ENSMUSP00000071289; ENSMUSG00000020716. [Q04690-1]
DR   Ensembl; ENSMUST00000108251; ENSMUSP00000103886; ENSMUSG00000020716. [Q04690-2]
DR   GeneID; 18015; -.
DR   KEGG; mmu:18015; -.
DR   UCSC; uc007kkl.1; mouse. [Q04690-1]
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; WSIDMEA; -.
DR   OrthoDB; 9686at2759; -.
DR   PhylomeDB; Q04690; -.
DR   TreeFam; TF300302; -.
DR   Reactome; R-MMU-5658442; Regulation of RAS by GAPs.
DR   BioGRID-ORCS; 18015; 17 hits in 82 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 178 other tissues.
DR   ExpressionAtlas; Q04690; baseline and differential.
DR   Genevisible; Q04690; MM.
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:0016020; C:membrane; ISO:MGI.
DR   GO; GO:0043005; C:neuron projection; ISO:MGI.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0014069; C:postsynaptic density; 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: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:0043407; P:negative regulation of MAP kinase activity; IMP: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:0006469; P:negative regulation of protein kinase activity; 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:0014065; P:phosphatidylinositol 3-kinase signaling; IMP:MGI.
DR   GO; GO:0043473; P:pigmentation; IMP:MGI.
DR   GO; GO:0045762; P:positive regulation of adenylate cyclase activity; 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:0043547; P:positive regulation of GTPase activity; 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: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:0010468; P:regulation of gene expression; IGI:MGI.
DR   GO; GO:0045685; P:regulation of glial cell differentiation; IMP:MGI.
DR   GO; GO:0043087; P:regulation of GTPase activity; ISO: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:0045664; P:regulation of neuron differentiation; ISO:MGI.
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; cd00170; SEC14; 1.
DR   Gene3D; 1.10.506.10; -; 5.
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; Alternative splicing; Direct protein sequencing;
KW   GTPase activation; Lipid-binding; Nucleus; Phosphoprotein;
KW   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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024