FHOD1_HUMAN
ID FHOD1_HUMAN Reviewed; 1164 AA.
AC Q9Y613; Q59F76; Q6Y1F2; Q76MS8; Q8N521;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=FH1/FH2 domain-containing protein 1;
DE AltName: Full=Formin homolog overexpressed in spleen 1;
DE Short=FHOS;
DE AltName: Full=Formin homology 2 domain-containing protein 1;
GN Name=FHOD1; Synonyms=FHOS, FHOS1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10352228; DOI=10.1016/s0378-1119(99)00127-4;
RA Westendorf J.J., Mernaugh R., Hiebert S.W.;
RT "Identification and characterization of a protein containing formin
RT homology (FH1/FH2) domains.";
RL Gene 232:173-182(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBUNIT.
RX PubMed=14576350; DOI=10.1242/jcs.00769;
RA Takeya R., Sumimoto H.;
RT "Fhos, a mammalian formin, directly binds to F-actin via a region N-
RT terminal to the FH1 domain and forms a homotypic complex via the FH2 domain
RT to promote actin fiber formation.";
RL J. Cell Sci. 116:4567-4575(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBUNIT.
RX PubMed=15138285; DOI=10.1242/jcs.01113;
RA Gill M.B., Roecklein-Canfield J., Sage D.R., Zambela-Soediono M.,
RA Longtine N., Uknis M., Fingeroth J.D.;
RT "EBV attachment stimulates FHOS/FHOD1 redistribution and co-aggregation
RT with CD21: formin interactions with the cytoplasmic domain of human CD21.";
RL J. Cell Sci. 117:2709-2720(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 2-19.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 148-1164.
RC TISSUE=Spleen;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, AUTOINHIBITION, AND SUBCELLULAR LOCATION.
RX PubMed=15878344; DOI=10.1016/j.yexcr.2005.02.006;
RA Gasteier J.E., Schroeder S., Muranyi W., Madrid R., Benichou S.,
RA Fackler O.T.;
RT "FHOD1 coordinates actin filament and microtubule alignment to mediate cell
RT elongation.";
RL Exp. Cell Res. 306:192-202(2005).
RN [8]
RP DOMAIN DAD, AND AUTOINHIBITION.
RX PubMed=16361249; DOI=10.1074/jbc.m509226200;
RA Schonichen A., Alexander M., Gasteier J.E., Cuesta F.E., Fackler O.T.,
RA Geyer M.;
RT "Biochemical characterization of the diaphanous autoregulatory interaction
RT in the formin homology protein FHOD1.";
RL J. Biol. Chem. 281:5084-5093(2006).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ROCK1, AND
RP PHOSPHORYLATION.
RX PubMed=18694941; DOI=10.1074/jbc.m801800200;
RA Hannemann S., Madrid R., Stastna J., Kitzing T., Gasteier J.,
RA Schoenichen A., Bouchet J., Jimenez A., Geyer M., Grosse R., Benichou S.,
RA Fackler O.T.;
RT "The diaphanous-related formin FHOD1 associates with ROCK1 and promotes
RT Src-dependent plasma membrane blebbing.";
RL J. Biol. Chem. 283:27891-27903(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-498, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367; THR-495; SER-498 AND
RP SER-523, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367; SER-486; SER-523 AND
RP SER-573, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523 AND THR-690, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-486; SER-498; SER-523 AND
RP THR-690, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-573, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Required for the assembly of F-actin structures, such as
CC stress fibers. Depends on the Rho-ROCK cascade for its activity.
CC Contributes to the coordination of microtubules with actin fibers and
CC plays a role in cell elongation. Acts synergistically with ROCK1 to
CC promote SRC-dependent non-apoptotic plasma membrane blebbing.
CC {ECO:0000269|PubMed:14576350, ECO:0000269|PubMed:15878344,
CC ECO:0000269|PubMed:18694941}.
CC -!- SUBUNIT: Self-associates via the FH2 domain. Binds to F-actin via its
CC N-terminus. Binds to the cytoplasmic domain of CD21 via its C-terminus.
CC Interacts with ROCK1 in a Src-dependent manner.
CC {ECO:0000269|PubMed:14576350, ECO:0000269|PubMed:15138285,
CC ECO:0000269|PubMed:18694941}.
CC -!- INTERACTION:
CC Q9Y613; Q9Y613: FHOD1; NbExp=9; IntAct=EBI-348433, EBI-348433;
CC Q9Y613; Q8WXH0: SYNE2; NbExp=4; IntAct=EBI-348433, EBI-2372294;
CC Q9Y613; P19474: TRIM21; NbExp=3; IntAct=EBI-348433, EBI-81290;
CC Q9Y613; Q6ZWQ0-1: Syne2; Xeno; NbExp=2; IntAct=EBI-348433, EBI-16108623;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Cell
CC projection, bleb. Note=Predominantly cytoplasmic.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in spleen.
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:16361249}.
CC -!- PTM: Phosphorylated by ROCK1. {ECO:0000269|PubMed:18694941}.
CC -!- SIMILARITY: Belongs to the formin homology family. {ECO:0000305}.
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; AF113615; AAD39906.1; -; mRNA.
DR EMBL; AB041046; BAD06250.1; -; mRNA.
DR EMBL; AY192154; AAO38757.1; -; mRNA.
DR EMBL; BC033084; AAH33084.1; -; mRNA.
DR EMBL; AB209584; BAD92821.1; -; mRNA.
DR CCDS; CCDS10834.1; -.
DR RefSeq; NP_037373.2; NM_013241.2.
DR PDB; 3DAD; X-ray; 2.30 A; A/B=1-339.
DR PDB; 6XF1; X-ray; 2.80 A; B/D=14-334.
DR PDB; 6XF2; X-ray; 7.11 A; B/D=14-334.
DR PDBsum; 3DAD; -.
DR PDBsum; 6XF1; -.
DR PDBsum; 6XF2; -.
DR AlphaFoldDB; Q9Y613; -.
DR SMR; Q9Y613; -.
DR BioGRID; 118877; 52.
DR DIP; DIP-31134N; -.
DR IntAct; Q9Y613; 31.
DR MINT; Q9Y613; -.
DR STRING; 9606.ENSP00000258201; -.
DR GlyGen; Q9Y613; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y613; -.
DR MetOSite; Q9Y613; -.
DR PhosphoSitePlus; Q9Y613; -.
DR BioMuta; FHOD1; -.
DR DMDM; 62512187; -.
DR EPD; Q9Y613; -.
DR jPOST; Q9Y613; -.
DR MassIVE; Q9Y613; -.
DR MaxQB; Q9Y613; -.
DR PaxDb; Q9Y613; -.
DR PeptideAtlas; Q9Y613; -.
DR PRIDE; Q9Y613; -.
DR ProteomicsDB; 86575; -.
DR Antibodypedia; 15694; 163 antibodies from 26 providers.
DR DNASU; 29109; -.
DR Ensembl; ENST00000258201.9; ENSP00000258201.4; ENSG00000135723.14.
DR GeneID; 29109; -.
DR KEGG; hsa:29109; -.
DR MANE-Select; ENST00000258201.9; ENSP00000258201.4; NM_013241.3; NP_037373.2.
DR UCSC; uc002esl.4; human.
DR CTD; 29109; -.
DR DisGeNET; 29109; -.
DR GeneCards; FHOD1; -.
DR HGNC; HGNC:17905; FHOD1.
DR HPA; ENSG00000135723; Tissue enhanced (lymphoid tissue, skeletal muscle).
DR MIM; 606881; gene.
DR neXtProt; NX_Q9Y613; -.
DR OpenTargets; ENSG00000135723; -.
DR PharmGKB; PA28143; -.
DR VEuPathDB; HostDB:ENSG00000135723; -.
DR eggNOG; KOG1925; Eukaryota.
DR GeneTree; ENSGT00940000160212; -.
DR HOGENOM; CLU_000814_0_0_1; -.
DR InParanoid; Q9Y613; -.
DR OMA; TSPNCSC; -.
DR PhylomeDB; Q9Y613; -.
DR TreeFam; TF316268; -.
DR PathwayCommons; Q9Y613; -.
DR SignaLink; Q9Y613; -.
DR SIGNOR; Q9Y613; -.
DR BioGRID-ORCS; 29109; 8 hits in 1083 CRISPR screens.
DR ChiTaRS; FHOD1; human.
DR EvolutionaryTrace; Q9Y613; -.
DR GeneWiki; FHOD1; -.
DR GenomeRNAi; 29109; -.
DR Pharos; Q9Y613; Tbio.
DR PRO; PR:Q9Y613; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9Y613; protein.
DR Bgee; ENSG00000135723; Expressed in spleen and 131 other tissues.
DR ExpressionAtlas; Q9Y613; baseline and differential.
DR Genevisible; Q9Y613; HS.
DR GO; GO:0032059; C:bleb; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0014704; C:intercalated disc; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0043621; F:protein self-association; IMP:CAFA.
DR GO; GO:0051639; P:actin filament network formation; IBA:GO_Central.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0051660; P:establishment of centrosome localization; IEA:Ensembl.
DR GO; GO:0007097; P:nuclear migration; IEA:Ensembl.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IDA:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0051492; P:regulation of stress fiber assembly; IMP:CAFA.
DR DisProt; DP00448; -.
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; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR InterPro; IPR027647; FHOD1.
DR InterPro; IPR041387; FHOD1_GBD_N.
DR InterPro; IPR014768; GBD/FH3_dom.
DR PANTHER; PTHR45920:SF2; PTHR45920:SF2; 2.
DR Pfam; PF02181; FH2; 1.
DR Pfam; PF18382; Formin_GBD_N; 1.
DR SMART; SM00498; FH2; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS51444; FH2; 1.
DR PROSITE; PS51232; GBD_FH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Cell projection; Coiled coil; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801"
FT CHAIN 2..1164
FT /note="FH1/FH2 domain-containing protein 1"
FT /id="PRO_0000194905"
FT DOMAIN 53..458
FT /note="GBD/FH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00579"
FT DOMAIN 487..615
FT /note="FH1"
FT DOMAIN 616..1013
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT DOMAIN 1053..1133
FT /note="DAD"
FT REGION 340..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 612..807
FT /note="Interaction with ROCK1"
FT /evidence="ECO:0000269|PubMed:18694941"
FT REGION 1020..1143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 884..921
FT /evidence="ECO:0000255"
FT COMPBIAS 340..369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..610
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1070..1120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:18691976"
FT MOD_RES 486
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 495
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18088087"
FT MOD_RES 498
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:23186163"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 573
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 690
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT CONFLICT 249
FT /note="S -> T (in Ref. 1; AAD39906 and 3; AAO38757)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="E -> D (in Ref. 3; AAO38757)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="T -> M (in Ref. 2; BAD06250)"
FT /evidence="ECO:0000305"
FT CONFLICT 307..308
FT /note="EA -> DT (in Ref. 1; AAD39906 and 3; AAO38757)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="E -> D (in Ref. 3; AAO38757)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="S -> T (in Ref. 3; AAO38757)"
FT /evidence="ECO:0000305"
FT CONFLICT 533
FT /note="P -> L (in Ref. 6; BAD92821)"
FT /evidence="ECO:0000305"
FT CONFLICT 633..634
FT /note="EL -> DV (in Ref. 1; AAD39906)"
FT /evidence="ECO:0000305"
FT CONFLICT 689
FT /note="R -> Q (in Ref. 3; AAO38757)"
FT /evidence="ECO:0000305"
FT CONFLICT 700
FT /note="S -> T (in Ref. 1; AAD39906)"
FT /evidence="ECO:0000305"
FT CONFLICT 745
FT /note="E -> G (in Ref. 3; AAO38757)"
FT /evidence="ECO:0000305"
FT CONFLICT 751
FT /note="E -> G (in Ref. 1; AAD39906)"
FT /evidence="ECO:0000305"
FT CONFLICT 849
FT /note="E -> D (in Ref. 1; AAD39906)"
FT /evidence="ECO:0000305"
FT CONFLICT 1061
FT /note="P -> L (in Ref. 1; AAD39906 and 3; AAO38757)"
FT /evidence="ECO:0000305"
FT STRAND 15..22
FT /evidence="ECO:0007829|PDB:3DAD"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:6XF1"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:3DAD"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:3DAD"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:3DAD"
FT HELIX 55..61
FT /evidence="ECO:0007829|PDB:3DAD"
FT STRAND 68..75
FT /evidence="ECO:0007829|PDB:3DAD"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:3DAD"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:6XF1"
FT TURN 88..93
FT /evidence="ECO:0007829|PDB:3DAD"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:3DAD"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:3DAD"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:3DAD"
FT HELIX 116..129
FT /evidence="ECO:0007829|PDB:3DAD"
FT HELIX 132..147
FT /evidence="ECO:0007829|PDB:3DAD"
FT HELIX 152..158
FT /evidence="ECO:0007829|PDB:3DAD"
FT HELIX 161..169
FT /evidence="ECO:0007829|PDB:3DAD"
FT HELIX 174..187
FT /evidence="ECO:0007829|PDB:3DAD"
FT HELIX 191..199
FT /evidence="ECO:0007829|PDB:3DAD"
FT HELIX 201..209
FT /evidence="ECO:0007829|PDB:3DAD"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:3DAD"
FT HELIX 216..232
FT /evidence="ECO:0007829|PDB:3DAD"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:3DAD"
FT HELIX 237..251
FT /evidence="ECO:0007829|PDB:3DAD"
FT HELIX 257..263
FT /evidence="ECO:0007829|PDB:3DAD"
FT TURN 264..267
FT /evidence="ECO:0007829|PDB:3DAD"
FT HELIX 271..287
FT /evidence="ECO:0007829|PDB:3DAD"
FT HELIX 291..303
FT /evidence="ECO:0007829|PDB:3DAD"
FT HELIX 306..314
FT /evidence="ECO:0007829|PDB:3DAD"
FT HELIX 321..338
FT /evidence="ECO:0007829|PDB:3DAD"
SQ SEQUENCE 1164 AA; 126551 MW; E6C7AE1FB8DC3FC7 CRC64;
MAGGEDRGDG EPVSVVTVRV QYLEDTDPFA CANFPEPRRA PTCSLDGALP LGAQIPAVHR
LLGAPLKLED CALQVSPSGY YLDTELSLEE QREMLEGFYE EISKGRKPTL ILRTQLSVRV
NAILEKLYSS SGPELRRSLF SLKQIFQEDK DLVPEFVHSE GLSCLIRVGA AADHNYQSYI
LRALGQLMLF VDGMLGVVAH SDTIQWLYTL CASLSRLVVK TALKLLLVFV EYSENNAPLF
IRAVNSVAST TGAPPWANLV SILEEKNGAD PELLVYTVTL INKTLAALPD QDSFYDVTDA
LEQQGMEALV QRHLGTAGTD VDLRTQLVLY ENALKLEDGD IEEAPGAGGR RERRKPSSEE
GKRSRRSLEG GGCPARAPEP GPTGPASPVG PTSSTGPALL TGPASSPVGP PSGLQASVNL
FPTISVAPSA DTSSERSIYK ARFLENVAAA ETEKQVALAQ GRAETLAGAM PNEAGGHPDA
RQLWDSPETA PAARTPQSPA PCVLLRAQRS LAPEPKEPLI PASPKAEPIW ELPTRAPRLS
IGDLDFSDLG EDEDQDMLNV ESVEAGKDIP APSPPLPLLS GVPPPPPLPP PPPIKGPFPP
PPPLPLAAPL PHSVPDSSAL PTKRKTVKLF WRELKLAGGH GVSASRFGPC ATLWASLDPV
SVDTARLEHL FESRAKEVLP SKKAGEGRRT MTTVLDPKRS NAINIGLTTL PPVHVIKAAL
LNFDEFAVSK DGIEKLLTMM PTEEERQKIE EAQLANPDIP LGPAENFLMT LASIGGLAAR
LQLWAFKLDY DSMEREIAEP LFDLKVGMEQ LVQNATFRCI LATLLAVGNF LNGSQSSGFE
LSYLEKVSEV KDTVRRQSLL HHLCSLVLQT RPESSDLYSE IPALTRCAKV DFEQLTENLG
QLERRSRAAE ESLRSLAKHE LAPALRARLT HFLDQCARRV AMLRIVHRRV CNRFHAFLLY
LGYTPQAARE VRIMQFCHTL REFALEYRTC RERVLQQQQK QATYRERNKT RGRMITETEK
FSGVAGEAPS NPSVPVAVSS GPGRGDADSH ASMKSLLTSR PEDTTHNRRS RGMVQSSSPI
MPTVGPSTAS PEEPPGSSLP SDTSDEIMDL LVQSVTKSSP RALAARERKR SRGNRKSLRR
TLKSGLGDDL VQALGLSKGP GLEV
