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DIAP1_MOUSE
ID   DIAP1_MOUSE             Reviewed;        1255 AA.
AC   O08808;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 196.
DE   RecName: Full=Protein diaphanous homolog 1;
DE   AltName: Full=Diaphanous-related formin-1;
DE            Short=DRF1;
DE   AltName: Full=p140mDIA;
DE            Short=mDIA1 {ECO:0000303|PubMed:23558171};
GN   Name=Diaph1; Synonyms=Diap1;
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 [MRNA], FUNCTION, INTERACTION WITH RHOA, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=9214622; DOI=10.1093/emboj/16.11.3044;
RA   Watanabe N., Madaule P., Reid T., Ishizaki T., Watanabe G., Kakizuka A.,
RA   Saito Y., Nakao K., Jockusch B.M., Narumiya S.;
RT   "p140mDia, a mammalian homolog of Drosophila diaphanous, is a target
RT   protein for Rho small GTPase and is a ligand for profilin.";
RL   EMBO J. 16:3044-3056(1997).
RN   [2]
RP   INTERACTION WITH BAIAP2.
RX   PubMed=10814512; DOI=10.1006/bbrc.2000.2671;
RA   Fujiwara T., Mammoto A., Kim Y., Takai Y.;
RT   "Rho small G-protein-dependent binding of mDia to an Src homology 3 domain-
RT   containing IRSp53/BAIAP2.";
RL   Biochem. Biophys. Res. Commun. 271:626-629(2000).
RN   [3]
RP   FUNCTION.
RX   PubMed=10678165; DOI=10.1016/s1097-2765(00)80399-8;
RA   Tominaga T., Sahai E., Chardin P., McCormick F., Courtneidge S.A.,
RA   Alberts A.S.;
RT   "Diaphanous-related formins bridge Rho GTPase and Src tyrosine kinase
RT   signaling.";
RL   Mol. Cell 5:13-25(2000).
RN   [4]
RP   FUNCTION, AND INTERACTION WITH APC AND MAPRE1.
RX   PubMed=15311282; DOI=10.1038/ncb1160;
RA   Wen Y., Eng C.H., Schmoranzer J., Cabrera-Poch N., Morris E.J.S., Chen M.,
RA   Wallar B.J., Alberts A.S., Gundersen G.G.;
RT   "EB1 and APC bind to mDia to stabilize microtubules downstream of Rho and
RT   promote cell migration.";
RL   Nat. Cell Biol. 6:820-830(2004).
RN   [5]
RP   FUNCTION, AND INTERACTION WITH ACTIN.
RX   PubMed=15044801; DOI=10.1126/science.1093923;
RA   Higashida C., Miyoshi T., Fujita A., Oceguera-Yanez F., Monypenny J.,
RA   Andou Y., Narumiya S., Watanabe N.;
RT   "Actin polymerization-driven molecular movement of mDia1 in living cells.";
RL   Science 303:2007-2010(2004).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1104, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Mast cell;
RX   PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [8]
RP   FUNCTION, AND INTERACTION WITH NCDN.
RX   PubMed=18572016; DOI=10.1016/j.bbrc.2008.06.042;
RA   Schwaibold E.M., Brandt D.T.;
RT   "Identification of Neurochondrin as a new interaction partner of the FH3
RT   domain of the Diaphanous-related formin Dia1.";
RL   Biochem. Biophys. Res. Commun. 373:366-372(2008).
RN   [9]
RP   INTERACTION WITH SCAI.
RX   PubMed=19350017; DOI=10.1038/ncb1862;
RA   Brandt D.T., Baarlink C., Kitzing T.M., Kremmer E., Ivaska J., Nollau P.,
RA   Grosse R.;
RT   "SCAI acts as a suppressor of cancer cell invasion through the
RT   transcriptional control of beta1-integrin.";
RL   Nat. Cell Biol. 11:557-568(2009).
RN   [10]
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).
RN   [11]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=23558171; DOI=10.1126/science.1235038;
RA   Baarlink C., Wang H., Grosse R.;
RT   "Nuclear actin network assembly by formins regulates the SRF coactivator
RT   MAL.";
RL   Science 340:864-867(2013).
RN   [12]
RP   DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX   PubMed=24781755; DOI=10.1038/ejhg.2014.82;
RA   Ercan-Sencicek A.G., Jambi S., Franjic D., Nishimura S., Li M.,
RA   El-Fishawy P., Morgan T.M., Sanders S.J., Bilguvar K., Suri M.,
RA   Johnson M.H., Gupta A.R., Yuksel Z., Mane S., Grigorenko E., Picciotto M.,
RA   Alberts A.S., Gunel M., Sestan N., State M.W.;
RT   "Homozygous loss of DIAPH1 is a novel cause of microcephaly in humans.";
RL   Eur. J. Hum. Genet. 23:165-172(2015).
RN   [13]
RP   TISSUE SPECIFICITY.
RX   PubMed=27808407; DOI=10.1111/cge.12915;
RA   Neuhaus C., Lang-Roth R., Zimmermann U., Heller R., Eisenberger T.,
RA   Weikert M., Markus S., Knipper M., Bolz H.J.;
RT   "Extension of the clinical and molecular phenotype of DIAPH1-associated
RT   autosomal dominant hearing loss (DFNA1).";
RL   Clin. Genet. 91:892-901(2017).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 826-1163, OLIGOMERIZATION, AND
RP   INTERACTION WITH ACTIN.
RX   PubMed=14992721; DOI=10.1016/s1097-2765(04)00059-0;
RA   Shimada A., Nyitrai M., Vetter I.R., Kuehlmann D., Bugyi B., Narumiya S.,
RA   Geeves M.A., Wittinghofer A.;
RT   "The core FH2 domain of diaphanous-related formins is an elongated actin
RT   binding protein that inhibits polymerization.";
RL   Mol. Cell 13:511-522(2004).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 135-451 AND 1145-1200, DOMAIN DAD,
RP   AND AUTOINHIBITION.
RX   PubMed=16292343; DOI=10.1038/sj.emboj.7600879;
RA   Lammers M., Rose R., Scrima A., Wittinghofer A.;
RT   "The regulation of mDia1 by autoinhibition and its release by Rho*GTP.";
RL   EMBO J. 24:4176-4187(2005).
RN   [16]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 69-451 IN COMPLEX WITH RHOC, AND
RP   HOMODIMERIZATION.
RX   PubMed=15864301; DOI=10.1038/nature03604;
RA   Rose R., Weyand M., Lammers M., Ishizaki T., Ahmadian M.R.,
RA   Wittinghofer A.;
RT   "Structural and mechanistic insights into the interaction between Rho and
RT   mammalian Dia.";
RL   Nature 435:513-518(2005).
CC   -!- FUNCTION: Actin nucleation and elongation factor required for the
CC       assembly of F-actin structures, such as actin cables and stress fibers
CC       (PubMed:10678165, PubMed:15044801, PubMed:18572016, PubMed:23558171).
CC       Binds to the barbed end of the actin filament and slows down actin
CC       polymerization and depolymerization (PubMed:10678165, PubMed:15044801,
CC       PubMed:18572016). Required for cytokinesis, and transcriptional
CC       activation of the serum response factor (PubMed:10678165,
CC       PubMed:15044801, PubMed:18572016). DFR proteins couple Rho and Src
CC       tyrosine kinase during signaling and the regulation of actin dynamics
CC       (PubMed:10678165, PubMed:15044801, PubMed:18572016). Functions as a
CC       scaffold protein for MAPRE1 and APC to stabilize microtubules and
CC       promote cell migration (PubMed:15311282). Has neurite outgrowth
CC       promoting activity (PubMed:10678165, PubMed:15044801, PubMed:18572016).
CC       Acts in a Rho-dependent manner to recruit PFY1 to the membrane
CC       (PubMed:9214622). The MEMO1-RHOA-DIAPH1 signaling pathway plays an
CC       important role in ERBB2-dependent stabilization of microtubules at the
CC       cell cortex (By similarity). It controls the localization of APC and
CC       CLASP2 to the cell membrane, via the regulation of GSK3B activity (By
CC       similarity). In turn, membrane-bound APC allows the localization of the
CC       MACF1 to the cell membrane, which is required for microtubule capture
CC       and stabilization (By similarity). Plays a role in the regulation of
CC       cell morphology and cytoskeletal organization (By similarity). Required
CC       in the control of cell shape (By similarity). Also acts as an actin
CC       nucleation and elongation factor in the nucleus by promoting nuclear
CC       actin polymerization inside the nucleus to drive serum-dependent SRF-
CC       MRTFA activity (PubMed:23558171). {ECO:0000250|UniProtKB:O60610,
CC       ECO:0000269|PubMed:10678165, ECO:0000269|PubMed:15044801,
CC       ECO:0000269|PubMed:15311282, ECO:0000269|PubMed:18572016,
CC       ECO:0000269|PubMed:23558171, ECO:0000269|PubMed:9214622}.
CC   -!- SUBUNIT: Homodimer (PubMed:14992721, PubMed:15864301). Interacts with
CC       the GTP-bound form of RHOA (PubMed:9214622). Interacts with RHOC, PFY1,
CC       MAPRE1, BAIAP2 and APC (PubMed:10814512, PubMed:15311282,
CC       PubMed:15864301). Interacts with SCAI (PubMed:19350017). Interacts with
CC       DCAF7, via FH2 domain (By similarity). Interacts with NCDN
CC       (PubMed:18572016). Interacts with OSBPL10, OSBPL2, VIM, TUBB and DYN1
CC       (By similarity). {ECO:0000250|UniProtKB:O60610,
CC       ECO:0000269|PubMed:10814512, ECO:0000269|PubMed:14992721,
CC       ECO:0000269|PubMed:15311282, ECO:0000269|PubMed:15864301,
CC       ECO:0000269|PubMed:18572016, ECO:0000269|PubMed:19350017,
CC       ECO:0000269|PubMed:9214622}.
CC   -!- INTERACTION:
CC       O08808; Q8BKX1: Baiap2; NbExp=3; IntAct=EBI-1026445, EBI-771498;
CC       O08808; O08808: Diaph1; NbExp=9; IntAct=EBI-1026445, EBI-1026445;
CC       O08808; P46940: IQGAP1; Xeno; NbExp=8; IntAct=EBI-1026445, EBI-297509;
CC       O08808; P61586: RHOA; Xeno; NbExp=3; IntAct=EBI-1026445, EBI-446668;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9214622}. Cell
CC       projection, ruffle membrane {ECO:0000269|PubMed:9214622}. Cytoplasm,
CC       cytoskeleton {ECO:0000269|PubMed:9214622}. Cytoplasm, cytoskeleton,
CC       microtubule organizing center, centrosome
CC       {ECO:0000250|UniProtKB:O60610}. Cytoplasm, cytoskeleton, spindle
CC       {ECO:0000250|UniProtKB:O60610}. Cytoplasm
CC       {ECO:0000269|PubMed:23558171}. Nucleus {ECO:0000269|PubMed:23558171}.
CC       Note=Membrane ruffles, especially at the tip of ruffles, of motile
CC       cells. {ECO:0000269|PubMed:9214622}.
CC   -!- TISSUE SPECIFICITY: Widely expressed. In the organ of Corti, it is
CC       expressed at the outer and inner hair cell layers. Expression at the
CC       inner hair cell layer is restricted to inner pillar cells. Detected in
CC       cochlear spiral ganglion neurons (PubMed:27808407).
CC       {ECO:0000269|PubMed:27808407}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the ventricular and subventricular
CC       zone progenitor cells of the dorsal and ventral forebrain and the
CC       brainstem, at 12.5 dpc, 14.5 dpc, and 17.5 dpc. At later embryonic age,
CC       it is observed in neurons of the cortex and hippocampus. During
CC       postnatal development, expression is detected in the cerebral cortex,
CC       basal ganglia, hippocampus, thalamus, and external granular layer of
CC       the cerebellum. {ECO:0000269|PubMed:24781755}.
CC   -!- DOMAIN: The DAD domain regulates activation via by an autoinhibitory
CC       interaction with the GBD/FH3 domain. This autoinhibition is released
CC       upon competitive binding of an activated GTPase. The release of DAD
CC       allows the FH2 domain to then nucleate and elongate nonbranched actin
CC       filaments. {ECO:0000269|PubMed:16292343}.
CC   -!- PTM: Phosphorylation at Thr-751 is stimulated by cAMP and regulates
CC       stability, complex formation and mitochondrial movement (By
CC       similarity). {ECO:0000250|UniProtKB:O60610}.
CC   -!- DISRUPTION PHENOTYPE: Knockout mice show normal organization of the
CC       cerebral cortex with no significant differences in cortical white
CC       matter or callosal thickness (PubMed:24781755). Histological analysis
CC       of coronal brain sections at early and postnatal stages shows
CC       unilateral ventricular enlargement (PubMed:24781755).
CC       {ECO:0000269|PubMed:24781755}.
CC   -!- SIMILARITY: Belongs to the formin homology family. Diaphanous
CC       subfamily. {ECO:0000305}.
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DR   EMBL; U96963; AAC53280.1; -; mRNA.
DR   CCDS; CCDS57121.1; -.
DR   PIR; T31065; T31065.
DR   RefSeq; NP_031884.1; NM_007858.4.
DR   PDB; 1V9D; X-ray; 2.60 A; A/B/C/D=826-1163.
DR   PDB; 1Z2C; X-ray; 3.00 A; B/D=69-451.
DR   PDB; 2BAP; X-ray; 3.30 A; A/B=135-451, C/D=1145-1200.
DR   PDB; 2BNX; X-ray; 2.40 A; A/B=131-516.
DR   PDB; 2F31; X-ray; 2.10 A; A=135-367, B=1177-1196.
DR   PDB; 2V8F; X-ray; 1.10 A; C=635-655.
DR   PDB; 3EG5; X-ray; 2.70 A; B/D=69-451.
DR   PDB; 3O4X; X-ray; 3.20 A; A/B/C/D=131-458, E/F/G/H=736-1200.
DR   PDB; 3OBV; X-ray; 2.75 A; A/B/C/D=131-457, E/F/G/H=753-1209.
DR   PDB; 4UWX; X-ray; 1.65 A; A/B=135-369.
DR   PDBsum; 1V9D; -.
DR   PDBsum; 1Z2C; -.
DR   PDBsum; 2BAP; -.
DR   PDBsum; 2BNX; -.
DR   PDBsum; 2F31; -.
DR   PDBsum; 2V8F; -.
DR   PDBsum; 3EG5; -.
DR   PDBsum; 3O4X; -.
DR   PDBsum; 3OBV; -.
DR   PDBsum; 4UWX; -.
DR   AlphaFoldDB; O08808; -.
DR   SMR; O08808; -.
DR   BioGRID; 199221; 19.
DR   CORUM; O08808; -.
DR   DIP; DIP-29028N; -.
DR   IntAct; O08808; 16.
DR   STRING; 10090.ENSMUSP00000025337; -.
DR   iPTMnet; O08808; -.
DR   PhosphoSitePlus; O08808; -.
DR   EPD; O08808; -.
DR   jPOST; O08808; -.
DR   MaxQB; O08808; -.
DR   PaxDb; O08808; -.
DR   PRIDE; O08808; -.
DR   ProteomicsDB; 279658; -.
DR   Antibodypedia; 7674; 376 antibodies from 41 providers.
DR   DNASU; 13367; -.
DR   Ensembl; ENSMUST00000115634; ENSMUSP00000111297; ENSMUSG00000024456.
DR   GeneID; 13367; -.
DR   KEGG; mmu:13367; -.
DR   UCSC; uc033hgk.1; mouse.
DR   CTD; 1729; -.
DR   MGI; MGI:1194490; Diaph1.
DR   VEuPathDB; HostDB:ENSMUSG00000024456; -.
DR   eggNOG; KOG1924; Eukaryota.
DR   GeneTree; ENSGT00940000159910; -.
DR   InParanoid; O08808; -.
DR   PhylomeDB; O08808; -.
DR   Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR   Reactome; R-MMU-6785631; ERBB2 Regulates Cell Motility.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR   Reactome; R-MMU-9013026; RHOB GTPase cycle.
DR   Reactome; R-MMU-9013106; RHOC GTPase cycle.
DR   Reactome; R-MMU-9013405; RHOD GTPase cycle.
DR   Reactome; R-MMU-9035034; RHOF GTPase cycle.
DR   BioGRID-ORCS; 13367; 6 hits in 42 CRISPR screens.
DR   ChiTaRS; Diaph1; mouse.
DR   EvolutionaryTrace; O08808; -.
DR   PRO; PR:O08808; -.
DR   Proteomes; UP000000589; Chromosome 18.
DR   RNAct; O08808; protein.
DR   Bgee; ENSMUSG00000024456; Expressed in granulocyte and 255 other tissues.
DR   ExpressionAtlas; O08808; baseline and differential.
DR   Genevisible; O08808; MM.
DR   GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR   GO; GO:0005903; C:brush border; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   GO; GO:0072686; C:mitotic spindle; ISO:MGI.
DR   GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0032587; C:ruffle membrane; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; IDA:MGI.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0005522; F:profilin binding; IDA:MGI.
DR   GO; GO:0031267; F:small GTPase binding; IDA:MGI.
DR   GO; GO:0044325; F:transmembrane transporter binding; IPI:BHF-UCL.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IDA:UniProtKB.
DR   GO; GO:0030041; P:actin filament polymerization; IDA:UniProtKB.
DR   GO; GO:0007420; P:brain development; IMP:UniProtKB.
DR   GO; GO:0071420; P:cellular response to histamine; ISO:MGI.
DR   GO; GO:0007010; P:cytoskeleton organization; IDA:UniProtKB.
DR   GO; GO:0031175; P:neuron projection development; IDA:UniProtKB.
DR   GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR   GO; GO:0035372; P:protein localization to microtubule; ISO:MGI.
DR   GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR   GO; GO:0051493; P:regulation of cytoskeleton organization; ISO:MGI.
DR   GO; GO:0032886; P:regulation of microtubule-based process; ISS:UniProtKB.
DR   GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; ISO:MGI.
DR   GO; GO:0007605; P:sensory perception of sound; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.20.40; -; 1.
DR   Gene3D; 1.20.58.2220; -; 1.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR014767; DAD_dom.
DR   InterPro; IPR044933; DIA_GBD_sf.
DR   InterPro; IPR015425; FH2_Formin.
DR   InterPro; IPR042201; FH2_Formin_sf.
DR   InterPro; IPR010472; FH3_dom.
DR   InterPro; IPR027653; Formin_Diaph1.
DR   InterPro; IPR014768; GBD/FH3_dom.
DR   InterPro; IPR010473; GTPase-bd.
DR   PANTHER; PTHR45691:SF4; PTHR45691:SF4; 2.
DR   Pfam; PF06367; Drf_FH3; 1.
DR   Pfam; PF06371; Drf_GBD; 1.
DR   Pfam; PF02181; FH2; 1.
DR   SMART; SM01139; Drf_FH3; 1.
DR   SMART; SM01140; Drf_GBD; 1.
DR   SMART; SM00498; FH2; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   PROSITE; PS51231; DAD; 1.
DR   PROSITE; PS51444; FH2; 1.
DR   PROSITE; PS51232; GBD_FH3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Actin-binding; Cell membrane; Cell projection;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Hearing; Membrane; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..1255
FT                   /note="Protein diaphanous homolog 1"
FT                   /id="PRO_0000194894"
FT   DOMAIN          75..440
FT                   /note="GBD/FH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00579"
FT   DOMAIN          586..747
FT                   /note="FH1"
FT   DOMAIN          752..1154
FT                   /note="FH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT   DOMAIN          1177..1205
FT                   /note="DAD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00577"
FT   REGION          1..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          567..737
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          460..562
FT                   /evidence="ECO:0000255"
FT   COILED          1027..1179
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        12..58
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..73
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        569..737
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:O60610"
FT   MOD_RES         22
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O60610"
FT   MOD_RES         751
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O60610"
FT   MOD_RES         1040
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O60610"
FT   MOD_RES         1086
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O60610"
FT   MOD_RES         1104
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:17947660"
FT   MOD_RES         1237
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O60610"
FT   HELIX           85..93
FT                   /evidence="ECO:0007829|PDB:3EG5"
FT   HELIX           98..105
FT                   /evidence="ECO:0007829|PDB:3EG5"
FT   HELIX           109..122
FT                   /evidence="ECO:0007829|PDB:3EG5"
FT   HELIX           135..143
FT                   /evidence="ECO:0007829|PDB:4UWX"
FT   TURN            144..146
FT                   /evidence="ECO:0007829|PDB:4UWX"
FT   HELIX           149..165
FT                   /evidence="ECO:0007829|PDB:4UWX"
FT   HELIX           168..191
FT                   /evidence="ECO:0007829|PDB:4UWX"
FT   TURN            194..196
FT                   /evidence="ECO:0007829|PDB:2BNX"
FT   HELIX           201..215
FT                   /evidence="ECO:0007829|PDB:4UWX"
FT   HELIX           219..226
FT                   /evidence="ECO:0007829|PDB:4UWX"
FT   STRAND          228..230
FT                   /evidence="ECO:0007829|PDB:4UWX"
FT   HELIX           231..237
FT                   /evidence="ECO:0007829|PDB:4UWX"
FT   HELIX           244..258
FT                   /evidence="ECO:0007829|PDB:4UWX"
FT   STRAND          261..264
FT                   /evidence="ECO:0007829|PDB:4UWX"
FT   HELIX           266..281
FT                   /evidence="ECO:0007829|PDB:4UWX"
FT   HELIX           287..292
FT                   /evidence="ECO:0007829|PDB:4UWX"
FT   HELIX           299..313
FT                   /evidence="ECO:0007829|PDB:4UWX"
FT   HELIX           319..332
FT                   /evidence="ECO:0007829|PDB:4UWX"
FT   HELIX           334..342
FT                   /evidence="ECO:0007829|PDB:4UWX"
FT   HELIX           347..367
FT                   /evidence="ECO:0007829|PDB:4UWX"
FT   HELIX           381..392
FT                   /evidence="ECO:0007829|PDB:2BNX"
FT   STRAND          393..395
FT                   /evidence="ECO:0007829|PDB:2BAP"
FT   HELIX           397..408
FT                   /evidence="ECO:0007829|PDB:2BNX"
FT   TURN            415..417
FT                   /evidence="ECO:0007829|PDB:2BNX"
FT   HELIX           418..433
FT                   /evidence="ECO:0007829|PDB:2BNX"
FT   HELIX           436..438
FT                   /evidence="ECO:0007829|PDB:2BNX"
FT   STRAND          447..451
FT                   /evidence="ECO:0007829|PDB:3OBV"
FT   TURN            453..455
FT                   /evidence="ECO:0007829|PDB:2BNX"
FT   HELIX           457..461
FT                   /evidence="ECO:0007829|PDB:2BNX"
FT   HELIX           464..469
FT                   /evidence="ECO:0007829|PDB:2BNX"
FT   TURN            470..472
FT                   /evidence="ECO:0007829|PDB:2BNX"
FT   STRAND          748..750
FT                   /evidence="ECO:0007829|PDB:3O4X"
FT   TURN            772..775
FT                   /evidence="ECO:0007829|PDB:3OBV"
FT   STRAND          777..780
FT                   /evidence="ECO:0007829|PDB:3OBV"
FT   HELIX           781..783
FT                   /evidence="ECO:0007829|PDB:3OBV"
FT   HELIX           786..789
FT                   /evidence="ECO:0007829|PDB:3OBV"
FT   HELIX           794..801
FT                   /evidence="ECO:0007829|PDB:3OBV"
FT   STRAND          833..835
FT                   /evidence="ECO:0007829|PDB:1V9D"
FT   HELIX           837..850
FT                   /evidence="ECO:0007829|PDB:1V9D"
FT   HELIX           854..863
FT                   /evidence="ECO:0007829|PDB:1V9D"
FT   TURN            866..868
FT                   /evidence="ECO:0007829|PDB:1V9D"
FT   HELIX           871..880
FT                   /evidence="ECO:0007829|PDB:1V9D"
FT   HELIX           884..891
FT                   /evidence="ECO:0007829|PDB:1V9D"
FT   HELIX           894..899
FT                   /evidence="ECO:0007829|PDB:1V9D"
FT   HELIX           902..911
FT                   /evidence="ECO:0007829|PDB:1V9D"
FT   HELIX           916..934
FT                   /evidence="ECO:0007829|PDB:1V9D"
FT   HELIX           937..951
FT                   /evidence="ECO:0007829|PDB:1V9D"
FT   HELIX           954..958
FT                   /evidence="ECO:0007829|PDB:1V9D"
FT   HELIX           961..968
FT                   /evidence="ECO:0007829|PDB:1V9D"
FT   STRAND          972..974
FT                   /evidence="ECO:0007829|PDB:1V9D"
FT   TURN            975..978
FT                   /evidence="ECO:0007829|PDB:1V9D"
FT   STRAND          980..982
FT                   /evidence="ECO:0007829|PDB:3O4X"
FT   HELIX           984..986
FT                   /evidence="ECO:0007829|PDB:3OBV"
FT   HELIX           987..992
FT                   /evidence="ECO:0007829|PDB:1V9D"
FT   HELIX           1002..1012
FT                   /evidence="ECO:0007829|PDB:1V9D"
FT   HELIX           1015..1019
FT                   /evidence="ECO:0007829|PDB:3OBV"
FT   HELIX           1020..1023
FT                   /evidence="ECO:0007829|PDB:1V9D"
FT   HELIX           1027..1032
FT                   /evidence="ECO:0007829|PDB:1V9D"
FT   HELIX           1035..1057
FT                   /evidence="ECO:0007829|PDB:1V9D"
FT   STRAND          1063..1066
FT                   /evidence="ECO:0007829|PDB:1V9D"
FT   HELIX           1069..1104
FT                   /evidence="ECO:0007829|PDB:1V9D"
FT   TURN            1109..1111
FT                   /evidence="ECO:0007829|PDB:1V9D"
FT   HELIX           1114..1159
FT                   /evidence="ECO:0007829|PDB:1V9D"
FT   HELIX           1181..1191
FT                   /evidence="ECO:0007829|PDB:2F31"
SQ   SEQUENCE   1255 AA;  139343 MW;  09404164873CA7C1 CRC64;
     MEPSGGGLGP GRGTRDKKKG RSPDELPATG GDGGKHKKFL ERFTSMRIKK EKEKPNSAHR
     NSSASYGDDP TAQSLQDISD EQVLVLFEQM LVDMNLNEEK QQPLREKDIV IKREMVSQYL
     HTSKAGMNQK ESSRSAMMYI QELRSGLRDM HLLSCLESLR VSLNNNPVSW VQTFGAEGLA
     SLLDILKRLH DEKEETSGNY DSRNQHEIIR CLKAFMNNKF GIKTMLETEE GILLLVRAMD
     PAVPNMMIDA AKLLSALCIL PQPEDMNERV LEAMTERAEM DEVERFQPLL DGLKSGTSIA
     LKVGCLQLIN ALITPAEELD FRVHIRSELM RLGLHQVLQE LREIENEDMK VQLCVFDEQG
     DEDFFDLKGR LDDIRMEMDD FGEVFQIILN TVKDSKAEPH FLSILQHLLL VRNDYEARPQ
     YYKLIEECVS QIVLHKNGTD PDFKCRHLQI DIERLVDQMI DKTKVEKSEA KATELEKKLD
     SELTARHELQ VEMKKMENDF EQKLQDLQGE KDALDSEKQQ ITAQKQDLEA EVSKLTGEVA
     KLSKELEDAK NEMASLSAVV VAPSVSSSAA VPPAPPLPGD SGTVIPPPPP PPPLPGGVVP
     PSPPLPPGTC IPPPPPLPGG ACIPPPPQLP GSAAIPPPPP LPGVASIPPP PPLPGATAIP
     PPPPLPGATA IPPPPPLPGG TGIPPPPPPL PGSVGVPPPP PLPGGPGLPP PPPPFPGAPG
     IPPPPPGMGV PPPPPFGFGV PAAPVLPFGL TPKKVYKPEV QLRRPNWSKF VAEDLSQDCF
     WTKVKEDRFE NNELFAKLTL AFSAQTKTSK AKKDQEGGEE KKSVQKKKVK ELKVLDSKTA
     QNLSIFLGSF RMPYQEIKNV ILEVNEAVLT ESMIQNLIKQ MPEPEQLKML SELKEEYDDL
     AESEQFGVVM GTVPRLRPRL NAILFKLQFS EQVENIKPEI VSVTAACEEL RKSENFSSLL
     ELTLLVGNYM NAGSRNAGAF GFNISFLCKL RDTKSADQKM TLLHFLAELC ENDHPEVLKF
     PDELAHVEKA SRVSAENLQK SLDQMKKQIA DVERDVQNFP AATDEKDKFV EKMTSFVKDA
     QEQYNKLRMM HSNMETLYKE LGDYFVFDPK KLSVEEFFMD LHNFRNMFLQ AVKENQKRRE
     TEEKMRRAKL AKEKAEKERL EKQQKREQLI DMNAEGDETG VMDSLLEALQ SGAAFRRKRG
     PRQVNRKAGC AVTSLLASEL TKDDAMAPGP VKVPKKSEGV PTILEEAKEL VGRAS
 
 
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