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Protein diaphanous homolog 1 (Diaphanous-related formin-1) (DRF1) (p140mDIA) (mDIA1)

 DIAP1_MOUSE             Reviewed;        1255 AA.
O08808;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
01-JUL-1997, sequence version 1.
05-DEC-2018, entry version 176.
RecName: Full=Protein diaphanous homolog 1;
AltName: Full=Diaphanous-related formin-1;
Short=DRF1;
AltName: Full=p140mDIA;
Short=mDIA1 {ECO:0000303|PubMed:23558171};
Name=Diaph1; Synonyms=Diap1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH RHOA, AND
SUBCELLULAR LOCATION.
PubMed=9214622; DOI=10.1093/emboj/16.11.3044;
Watanabe N., Madaule P., Reid T., Ishizaki T., Watanabe G.,
Kakizuka A., Saito Y., Nakao K., Jockusch B.M., Narumiya S.;
"p140mDia, a mammalian homolog of Drosophila diaphanous, is a target
protein for Rho small GTPase and is a ligand for profilin.";
EMBO J. 16:3044-3056(1997).
[2]
INTERACTION WITH BAIAP2.
PubMed=10814512; DOI=10.1006/bbrc.2000.2671;
Fujiwara T., Mammoto A., Kim Y., Takai Y.;
"Rho small G-protein-dependent binding of mDia to an Src homology 3
domain-containing IRSp53/BAIAP2.";
Biochem. Biophys. Res. Commun. 271:626-629(2000).
[3]
FUNCTION.
PubMed=10678165; DOI=10.1016/S1097-2765(00)80399-8;
Tominaga T., Sahai E., Chardin P., McCormick F., Courtneidge S.A.,
Alberts A.S.;
"Diaphanous-related formins bridge Rho GTPase and Src tyrosine kinase
signaling.";
Mol. Cell 5:13-25(2000).
[4]
FUNCTION, AND INTERACTION WITH APC AND MAPRE1.
PubMed=15311282; DOI=10.1038/ncb1160;
Wen Y., Eng C.H., Schmoranzer J., Cabrera-Poch N., Morris E.J.S.,
Chen M., Wallar B.J., Alberts A.S., Gundersen G.G.;
"EB1 and APC bind to mDia to stabilize microtubules downstream of Rho
and promote cell migration.";
Nat. Cell Biol. 6:820-830(2004).
[5]
FUNCTION, AND INTERACTION WITH ACTIN.
PubMed=15044801; DOI=10.1126/science.1093923;
Higashida C., Miyoshi T., Fujita A., Oceguera-Yanez F., Monypenny J.,
Andou Y., Narumiya S., Watanabe N.;
"Actin polymerization-driven molecular movement of mDia1 in living
cells.";
Science 303:2007-2010(2004).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic
density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1104, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Mast cell;
PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
Kawakami T., Salomon A.R.;
"Quantitative time-resolved phosphoproteomic analysis of mast cell
signaling.";
J. Immunol. 179:5864-5876(2007).
[8]
FUNCTION, AND INTERACTION WITH NCDN.
PubMed=18572016; DOI=10.1016/j.bbrc.2008.06.042;
Schwaibold E.M., Brandt D.T.;
"Identification of Neurochondrin as a new interaction partner of the
FH3 domain of the Diaphanous-related formin Dia1.";
Biochem. Biophys. Res. Commun. 373:366-372(2008).
[9]
INTERACTION WITH SCAI.
PubMed=19350017; DOI=10.1038/ncb1862;
Brandt D.T., Baarlink C., Kitzing T.M., Kremmer E., Ivaska J.,
Nollau P., Grosse R.;
"SCAI acts as a suppressor of cancer cell invasion through the
transcriptional control of beta1-integrin.";
Nat. Cell Biol. 11:557-568(2009).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[11]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=23558171; DOI=10.1126/science.1235038;
Baarlink C., Wang H., Grosse R.;
"Nuclear actin network assembly by formins regulates the SRF
coactivator MAL.";
Science 340:864-867(2013).
[12]
DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
PubMed=24781755; DOI=10.1038/ejhg.2014.82;
Ercan-Sencicek A.G., Jambi S., Franjic D., Nishimura S., Li M.,
El-Fishawy P., Morgan T.M., Sanders S.J., Bilguvar K., Suri M.,
Johnson M.H., Gupta A.R., Yuksel Z., Mane S., Grigorenko E.,
Picciotto M., Alberts A.S., Gunel M., Sestan N., State M.W.;
"Homozygous loss of DIAPH1 is a novel cause of microcephaly in
humans.";
Eur. J. Hum. Genet. 23:165-172(2015).
[13]
TISSUE SPECIFICITY.
PubMed=27808407; DOI=10.1111/cge.12915;
Neuhaus C., Lang-Roth R., Zimmermann U., Heller R., Eisenberger T.,
Weikert M., Markus S., Knipper M., Bolz H.J.;
"Extension of the clinical and molecular phenotype of DIAPH1-
associated autosomal dominant hearing loss (DFNA1).";
Clin. Genet. 91:892-901(2017).
[14]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 826-1163, OLIGOMERIZATION,
AND INTERACTION WITH ACTIN.
PubMed=14992721; DOI=10.1016/S1097-2765(04)00059-0;
Shimada A., Nyitrai M., Vetter I.R., Kuehlmann D., Bugyi B.,
Narumiya S., Geeves M.A., Wittinghofer A.;
"The core FH2 domain of diaphanous-related formins is an elongated
actin binding protein that inhibits polymerization.";
Mol. Cell 13:511-522(2004).
[15]
X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 135-451 AND 1145-1200, DOMAIN
DAD, AND AUTOINHIBITION.
PubMed=16292343; DOI=10.1038/sj.emboj.7600879;
Lammers M., Rose R., Scrima A., Wittinghofer A.;
"The regulation of mDia1 by autoinhibition and its release by
Rho*GTP.";
EMBO J. 24:4176-4187(2005).
[16]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 69-451 IN COMPLEX WITH RHOC,
AND HOMODIMERIZATION.
PubMed=15864301; DOI=10.1038/nature03604;
Rose R., Weyand M., Lammers M., Ishizaki T., Ahmadian M.R.,
Wittinghofer A.;
"Structural and mechanistic insights into the interaction between Rho
and mammalian Dia.";
Nature 435:513-518(2005).
-!- FUNCTION: Actin nucleation and elongation factor required for the
assembly of F-actin structures, such as actin cables and stress
fibers (PubMed:10678165, PubMed:15044801, PubMed:18572016,
PubMed:23558171). Binds to the barbed end of the actin filament
and slows down actin polymerization and depolymerization
(PubMed:10678165, PubMed:15044801, PubMed:18572016). Required for
cytokinesis, and transcriptional activation of the serum response
factor (PubMed:10678165, PubMed:15044801, PubMed:18572016). DFR
proteins couple Rho and Src tyrosine kinase during signaling and
the regulation of actin dynamics (PubMed:10678165,
PubMed:15044801, PubMed:18572016). Functions as a scaffold protein
for MAPRE1 and APC to stabilize microtubules and promote cell
migration (PubMed:15311282). Has neurite outgrowth promoting
activity (PubMed:10678165, PubMed:15044801, PubMed:18572016). Acts
in a Rho-dependent manner to recruit PFY1 to the membrane
(PubMed:9214622). The MEMO1-RHOA-DIAPH1 signaling pathway plays an
important role in ERBB2-dependent stabilization of microtubules at
the cell cortex (By similarity). It controls the localization of
APC and CLASP2 to the cell membrane, via the regulation of GSK3B
activity (By similarity). In turn, membrane-bound APC allows the
localization of the MACF1 to the cell membrane, which is required
for microtubule capture and stabilization (By similarity). Plays a
role in the regulation of cell morphology and cytoskeletal
organization (By similarity). Required in the control of cell
shape (By similarity). Also acts as an actin nucleation and
elongation factor in the nucleus by promoting nuclear actin
polymerization inside the nucleus to drive serum-dependent SRF-
MRTFA activity (PubMed:23558171). {ECO:0000250|UniProtKB:O60610,
ECO:0000269|PubMed:10678165, ECO:0000269|PubMed:15044801,
ECO:0000269|PubMed:15311282, ECO:0000269|PubMed:18572016,
ECO:0000269|PubMed:23558171, ECO:0000269|PubMed:9214622}.
-!- SUBUNIT: Homodimer (PubMed:14992721, PubMed:15864301). Interacts
with the GTP-bound form of RHOA (PubMed:9214622). Interacts with
RHOC, PFY1, MAPRE1, BAIAP2 and APC (PubMed:10814512,
PubMed:15311282, PubMed:15864301). Interacts with SCAI
(PubMed:19350017). Interacts with DCAF7, via FH2 domain (By
similarity). Interacts with NCDN (PubMed:18572016). Interacts with
OSBPL10, OSBPL2, VIM, TUBB and DYN1 (By similarity).
{ECO:0000250|UniProtKB:O60610, ECO:0000269|PubMed:10814512,
ECO:0000269|PubMed:14992721, ECO:0000269|PubMed:15311282,
ECO:0000269|PubMed:15864301, ECO:0000269|PubMed:18572016,
ECO:0000269|PubMed:19350017, ECO:0000269|PubMed:9214622}.
-!- INTERACTION:
Self; NbExp=9; IntAct=EBI-1026445, EBI-1026445;
Q8BKX1:Baiap2; NbExp=3; IntAct=EBI-1026445, EBI-771498;
P46940:IQGAP1 (xeno); NbExp=8; IntAct=EBI-1026445, EBI-297509;
P61586:RHOA (xeno); NbExp=3; IntAct=EBI-1026445, EBI-446668;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9214622}.
Cell projection, ruffle membrane {ECO:0000269|PubMed:9214622}.
Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9214622}. Cytoplasm,
cytoskeleton, microtubule organizing center, centrosome
{ECO:0000250|UniProtKB:O60610}. Cytoplasm, cytoskeleton, spindle
{ECO:0000250|UniProtKB:O60610}. Cytoplasm
{ECO:0000269|PubMed:23558171}. Nucleus
{ECO:0000269|PubMed:23558171}. Note=Membrane ruffles, especially
at the tip of ruffles, of motile cells.
{ECO:0000269|PubMed:9214622}.
-!- TISSUE SPECIFICITY: Widely expressed. In the organ of Corti, it is
expressed at the outer and inner hair cell layers. Expression at
the inner hair cell layer is restricted to inner pillar cells.
Detected in cochlear spiral ganglion neurons (PubMed:27808407).
{ECO:0000269|PubMed:27808407}.
-!- DEVELOPMENTAL STAGE: Expressed in the ventricular and
subventricular zone progenitor cells of the dorsal and ventral
forebrain and the brainstem, at embryonic days E12.5, E14.5, and
E17.5. At later embryonic age, it is observed in neurons of the
cortex and hippocampus. During postnatal development, expression
is detected in the cerebral cortex, basal ganglia, hippocampus,
thalamus, and external granular layer of the cerebellum.
{ECO:0000269|PubMed:24781755}.
-!- DOMAIN: The DAD domain regulates activation via by an
autoinhibitory interaction with the GBD/FH3 domain. This
autoinhibition is released upon competitive binding of an
activated GTPase. The release of DAD allows the FH2 domain to then
nucleate and elongate nonbranched actin filaments.
{ECO:0000269|PubMed:16292343}.
-!- PTM: Phosphorylation at Thr-751 is stimulated by cAMP and
regulates stability, complex formation and mitochondrial movement
(By similarity). {ECO:0000250|UniProtKB:O60610}.
-!- DISRUPTION PHENOTYPE: Knockout mice show normal organization of
the cerebral cortex with no significant differences in cortical
white matter or callosal thickness (PubMed:24781755). Histological
analysis of coronal brain sections at early and postnatal stages
shows unilateral ventricular enlargement (PubMed:24781755).
{ECO:0000269|PubMed:24781755}.
-!- SIMILARITY: Belongs to the formin homology family. Diaphanous
subfamily. {ECO:0000305}.
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EMBL; U96963; AAC53280.1; -; mRNA.
CCDS; CCDS57121.1; -.
PIR; T31065; T31065.
RefSeq; NP_031884.1; NM_007858.4.
UniGene; Mm.195916; -.
PDB; 1V9D; X-ray; 2.60 A; A/B/C/D=826-1163.
PDB; 1Z2C; X-ray; 3.00 A; B/D=69-451.
PDB; 2BAP; X-ray; 3.30 A; A/B=135-451, C/D=1145-1200.
PDB; 2BNX; X-ray; 2.40 A; A/B=131-516.
PDB; 2F31; X-ray; 2.10 A; A=135-367, B=1177-1196.
PDB; 2V8F; X-ray; 1.10 A; C=635-655.
PDB; 3EG5; X-ray; 2.70 A; B/D=69-451.
PDB; 3O4X; X-ray; 3.20 A; A/B/C/D=131-458, E/F/G/H=736-1200.
PDB; 3OBV; X-ray; 2.75 A; A/B/C/D=131-457, E/F/G/H=753-1209.
PDB; 4UWX; X-ray; 1.65 A; A/B=135-369.
PDBsum; 1V9D; -.
PDBsum; 1Z2C; -.
PDBsum; 2BAP; -.
PDBsum; 2BNX; -.
PDBsum; 2F31; -.
PDBsum; 2V8F; -.
PDBsum; 3EG5; -.
PDBsum; 3O4X; -.
PDBsum; 3OBV; -.
PDBsum; 4UWX; -.
ProteinModelPortal; O08808; -.
SMR; O08808; -.
BioGrid; 199221; 7.
CORUM; O08808; -.
DIP; DIP-29028N; -.
IntAct; O08808; 17.
MINT; O08808; -.
STRING; 10090.ENSMUSP00000111297; -.
iPTMnet; O08808; -.
PhosphoSitePlus; O08808; -.
EPD; O08808; -.
MaxQB; O08808; -.
PaxDb; O08808; -.
PRIDE; O08808; -.
Ensembl; ENSMUST00000115634; ENSMUSP00000111297; ENSMUSG00000024456.
GeneID; 13367; -.
KEGG; mmu:13367; -.
UCSC; uc033hgk.1; mouse.
CTD; 1729; -.
MGI; MGI:1194490; Diaph1.
eggNOG; KOG1924; Eukaryota.
eggNOG; ENOG410Y29H; LUCA.
GeneTree; ENSGT00940000159910; -.
HOGENOM; HOG000293231; -.
HOVERGEN; HBG051357; -.
InParanoid; O08808; -.
KO; K05740; -.
PhylomeDB; O08808; -.
Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
Reactome; R-MMU-6785631; ERBB2 Regulates Cell Motility.
Reactome; R-MMU-6798695; Neutrophil degranulation.
ChiTaRS; Diaph1; mouse.
EvolutionaryTrace; O08808; -.
PRO; PR:O08808; -.
Proteomes; UP000000589; Chromosome 18.
Bgee; ENSMUSG00000024456; Expressed in 282 organ(s), highest expression level in conjunctival fornix.
CleanEx; MM_DIAP1; -.
ExpressionAtlas; O08808; baseline and differential.
Genevisible; O08808; MM.
GO; GO:0005903; C:brush border; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
GO; GO:0072686; C:mitotic spindle; ISO:MGI.
GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0032587; C:ruffle membrane; IDA:MGI.
GO; GO:0003779; F:actin binding; IDA:MGI.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0044325; F:ion channel binding; IPI:BHF-UCL.
GO; GO:0005522; F:profilin binding; IDA:MGI.
GO; GO:0017048; F:Rho GTPase binding; IDA:MGI.
GO; GO:0030036; P:actin cytoskeleton organization; IDA:UniProtKB.
GO; GO:0030041; P:actin filament polymerization; IDA:UniProtKB.
GO; GO:0007420; P:brain development; IMP:UniProtKB.
GO; GO:0071420; P:cellular response to histamine; ISO:MGI.
GO; GO:0007010; P:cytoskeleton organization; IDA:UniProtKB.
GO; GO:0031175; P:neuron projection development; IDA:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
GO; GO:0035372; P:protein localization to microtubule; ISO:MGI.
GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
GO; GO:0051493; P:regulation of cytoskeleton organization; ISO:MGI.
GO; GO:0032886; P:regulation of microtubule-based process; ISS:UniProtKB.
GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; ISO:MGI.
GO; GO:0007605; P:sensory perception of sound; IEA:UniProtKB-KW.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR014767; DAD_dom.
InterPro; IPR010465; Drf_DAD.
InterPro; IPR015425; FH2_Formin.
InterPro; IPR010472; FH3_dom.
InterPro; IPR027653; Formin_Diaph1.
InterPro; IPR009408; Formin_homology_1.
InterPro; IPR014768; GBD/FH3_dom.
InterPro; IPR010473; GTPase-bd.
PANTHER; PTHR23213:SF17; PTHR23213:SF17; 2.
Pfam; PF06345; Drf_DAD; 1.
Pfam; PF06346; Drf_FH1; 1.
Pfam; PF06367; Drf_FH3; 1.
Pfam; PF06371; Drf_GBD; 1.
Pfam; PF02181; FH2; 1.
SMART; SM01139; Drf_FH3; 1.
SMART; SM01140; Drf_GBD; 1.
SMART; SM00498; FH2; 1.
SUPFAM; SSF48371; SSF48371; 1.
PROSITE; PS51231; DAD; 1.
PROSITE; PS51444; FH2; 1.
PROSITE; PS51232; GBD_FH3; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Actin-binding; Cell membrane;
Cell projection; Coiled coil; Complete proteome; Cytoplasm;
Cytoskeleton; Hearing; Membrane; Nucleus; Phosphoprotein;
Reference proteome; Repeat.
CHAIN 1 1255 Protein diaphanous homolog 1.
/FTId=PRO_0000194894.
DOMAIN 75 440 GBD/FH3. {ECO:0000255|PROSITE-
ProRule:PRU00579}.
DOMAIN 586 747 FH1.
DOMAIN 752 1154 FH2. {ECO:0000255|PROSITE-
ProRule:PRU00774}.
DOMAIN 1177 1205 DAD. {ECO:0000255|PROSITE-
ProRule:PRU00577}.
COILED 460 562 {ECO:0000255}.
COILED 1027 1179 {ECO:0000255}.
COMPBIAS 1196 1199 Arg/Lys-rich (basic).
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:O60610}.
MOD_RES 22 22 Phosphoserine.
{ECO:0000250|UniProtKB:O60610}.
MOD_RES 751 751 Phosphothreonine.
{ECO:0000250|UniProtKB:O60610}.
MOD_RES 1040 1040 N6-acetyllysine.
{ECO:0000250|UniProtKB:O60610}.
MOD_RES 1086 1086 N6-acetyllysine.
{ECO:0000250|UniProtKB:O60610}.
MOD_RES 1104 1104 Phosphotyrosine.
{ECO:0000244|PubMed:17947660}.
MOD_RES 1237 1237 Phosphoserine.
{ECO:0000250|UniProtKB:O60610}.
HELIX 85 93 {ECO:0000244|PDB:3EG5}.
HELIX 98 105 {ECO:0000244|PDB:3EG5}.
HELIX 109 122 {ECO:0000244|PDB:3EG5}.
HELIX 135 143 {ECO:0000244|PDB:4UWX}.
TURN 144 146 {ECO:0000244|PDB:4UWX}.
HELIX 149 165 {ECO:0000244|PDB:4UWX}.
HELIX 168 191 {ECO:0000244|PDB:4UWX}.
TURN 194 196 {ECO:0000244|PDB:2BNX}.
HELIX 201 215 {ECO:0000244|PDB:4UWX}.
HELIX 219 226 {ECO:0000244|PDB:4UWX}.
STRAND 228 230 {ECO:0000244|PDB:4UWX}.
HELIX 231 237 {ECO:0000244|PDB:4UWX}.
HELIX 244 258 {ECO:0000244|PDB:4UWX}.
STRAND 261 264 {ECO:0000244|PDB:4UWX}.
HELIX 266 281 {ECO:0000244|PDB:4UWX}.
HELIX 287 292 {ECO:0000244|PDB:4UWX}.
HELIX 299 313 {ECO:0000244|PDB:4UWX}.
HELIX 319 332 {ECO:0000244|PDB:4UWX}.
HELIX 334 342 {ECO:0000244|PDB:4UWX}.
HELIX 347 367 {ECO:0000244|PDB:4UWX}.
HELIX 381 392 {ECO:0000244|PDB:2BNX}.
STRAND 393 395 {ECO:0000244|PDB:2BAP}.
HELIX 397 408 {ECO:0000244|PDB:2BNX}.
TURN 415 417 {ECO:0000244|PDB:2BNX}.
HELIX 418 433 {ECO:0000244|PDB:2BNX}.
HELIX 436 438 {ECO:0000244|PDB:2BNX}.
STRAND 447 451 {ECO:0000244|PDB:3OBV}.
TURN 453 455 {ECO:0000244|PDB:2BNX}.
HELIX 457 461 {ECO:0000244|PDB:2BNX}.
HELIX 464 469 {ECO:0000244|PDB:2BNX}.
TURN 470 472 {ECO:0000244|PDB:2BNX}.
STRAND 748 750 {ECO:0000244|PDB:3O4X}.
TURN 772 775 {ECO:0000244|PDB:3OBV}.
STRAND 777 780 {ECO:0000244|PDB:3OBV}.
HELIX 781 783 {ECO:0000244|PDB:3OBV}.
HELIX 786 789 {ECO:0000244|PDB:3OBV}.
HELIX 794 801 {ECO:0000244|PDB:3OBV}.
STRAND 833 835 {ECO:0000244|PDB:1V9D}.
HELIX 837 850 {ECO:0000244|PDB:1V9D}.
HELIX 854 863 {ECO:0000244|PDB:1V9D}.
TURN 866 868 {ECO:0000244|PDB:1V9D}.
HELIX 871 880 {ECO:0000244|PDB:1V9D}.
HELIX 884 891 {ECO:0000244|PDB:1V9D}.
HELIX 894 899 {ECO:0000244|PDB:1V9D}.
HELIX 902 911 {ECO:0000244|PDB:1V9D}.
HELIX 916 934 {ECO:0000244|PDB:1V9D}.
HELIX 937 951 {ECO:0000244|PDB:1V9D}.
HELIX 954 958 {ECO:0000244|PDB:1V9D}.
HELIX 961 968 {ECO:0000244|PDB:1V9D}.
STRAND 972 974 {ECO:0000244|PDB:1V9D}.
TURN 975 978 {ECO:0000244|PDB:1V9D}.
STRAND 980 982 {ECO:0000244|PDB:3O4X}.
HELIX 984 986 {ECO:0000244|PDB:3OBV}.
HELIX 987 992 {ECO:0000244|PDB:1V9D}.
HELIX 1002 1012 {ECO:0000244|PDB:1V9D}.
HELIX 1015 1019 {ECO:0000244|PDB:3OBV}.
HELIX 1020 1023 {ECO:0000244|PDB:1V9D}.
HELIX 1027 1032 {ECO:0000244|PDB:1V9D}.
HELIX 1035 1057 {ECO:0000244|PDB:1V9D}.
STRAND 1063 1066 {ECO:0000244|PDB:1V9D}.
HELIX 1069 1104 {ECO:0000244|PDB:1V9D}.
TURN 1109 1111 {ECO:0000244|PDB:1V9D}.
HELIX 1114 1159 {ECO:0000244|PDB:1V9D}.
HELIX 1181 1191 {ECO:0000244|PDB:2F31}.
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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