FERM2_MOUSE
ID FERM2_MOUSE Reviewed; 680 AA.
AC Q8CIB5; Q8C542; Q8K035;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Fermitin family homolog 2;
DE AltName: Full=Kindlin-2;
DE AltName: Full=Pleckstrin homology domain-containing family C member 1;
GN Name=Fermt2; Synonyms=Plekhc1;
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 [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-149.
RC STRAIN=C57BL/6J; TISSUE=Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=18174465; DOI=10.1161/circresaha.107.161489;
RA Dowling J.J., Gibbs E., Russell M., Goldman D., Minarcik J., Golden J.A.,
RA Feldman E.L.;
RT "Kindlin-2 is an essential component of intercalated discs and is required
RT for vertebrate cardiac structure and function.";
RL Circ. Res. 102:423-431(2008).
RN [4]
RP DISRUPTION PHENOTYPE, FUNCTION, INTERACTION WITH ILK; ITGB1 AND ITGB3, AND
RP MUTAGENESIS OF 614-GLN-TRP-615.
RX PubMed=18483218; DOI=10.1101/gad.469408;
RA Montanez E., Ussar S., Schifferer M., Bosl M., Zent R., Moser M.,
RA Fassler R.;
RT "Kindlin-2 controls bidirectional signaling of integrins.";
RL Genes Dev. 22:1325-1330(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159 AND SER-666, AND
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 [6]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=21378273; DOI=10.1182/blood-2010-11-321182;
RA Pluskota E., Dowling J.J., Gordon N., Golden J.A., Szpak D., West X.Z.,
RA Nestor C., Ma Y.Q., Bialkowska K., Byzova T., Plow E.F.;
RT "The integrin coactivator kindlin-2 plays a critical role in angiogenesis
RT in mice and zebrafish.";
RL Blood 117:4978-4987(2011).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=21768292; DOI=10.1083/jcb.201007108;
RA Brunner M., Millon-Fremillon A., Chevalier G., Nakchbandi I.A., Mosher D.,
RA Block M.R., Albiges-Rizo C., Bouvard D.;
RT "Osteoblast mineralization requires beta1 integrin/ICAP-1-dependent
RT fibronectin deposition.";
RL J. Cell Biol. 194:307-322(2011).
CC -!- FUNCTION: Scaffolding protein that enhances integrin activation
CC mediated by TLN1 and/or TLN2, but activates integrins only weakly by
CC itself. Binds to membranes enriched in phosphoinositides. Enhances
CC integrin-mediated cell adhesion onto the extracellular matrix and cell
CC spreading; this requires both its ability to interact with integrins
CC and with phospholipid membranes. Required for the assembly of focal
CC adhesions. Participates in the connection between extracellular matrix
CC adhesion sites and the actin cytoskeleton and also in the orchestration
CC of actin assembly and cell shape modulation. Recruits FBLIM1 to focal
CC adhesions. Plays a role in the TGFB1 and integrin signaling pathways.
CC Stabilizes active CTNNB1 and plays a role in the regulation of
CC transcription mediated by CTNNB1 and TCF7L2/TCF4 and in Wnt signaling.
CC {ECO:0000269|PubMed:18174465, ECO:0000269|PubMed:18483218,
CC ECO:0000269|PubMed:21378273}.
CC -!- SUBUNIT: Interacts with ITGB1; the interaction is inhibited in presence
CC of ITGB1BP1. Interacts with FBLIM1. Interacts with active,
CC unphosphorylated CTNNB1. Identified in a complex with CTNNB1 and
CC TCF7L2/TCF4 (By similarity). Interacts with ILK, ITGB1 and ITGB3.
CC {ECO:0000250, ECO:0000269|PubMed:18483218}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cell cortex
CC {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm,
CC cytoskeleton, stress fiber {ECO:0000250}. Cell junction, focal adhesion
CC {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell projection,
CC lamellipodium membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus {ECO:0000250}.
CC Cytoplasm, myofibril, sarcomere, I band. Cell surface. Note=Colocalizes
CC with actin stress fibers at cell-ECM focal adhesion sites. Colocalizes
CC with ITGB3 at lamellipodia at the leading edge of spreading cells.
CC Binds to membranes that contain phosphatidylinositides (By similarity).
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in adult heart muscle (at protein level).
CC Detected in heart, skeletal muscle and testis.
CC {ECO:0000269|PubMed:18174465}.
CC -!- DOMAIN: The FERM domain is not correctly detected by PROSITE or Pfam
CC techniques because it contains the insertion of a PH domain.
CC -!- DOMAIN: The PH domain binds phospholipids. Binds preferentially
CC phosphatidylinositol-3,4,5-trisphosphate, and has lower affinity for
CC phosphatidylinositol-4,5-bisphosphate (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The N-terminal region displays a ubiquitin-type fold and
CC mediates interaction with membranes containing negatively charged
CC phosphatidylinositol phosphate via a surface enriched in positively
CC charged residues. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Complete embryonic lethality at peri-implantation
CC stage, due to severe detachment of the endoderm and epiblast from the
CC basement membrane. Heterozygous mice lacking one copy of Fermt2 show no
CC visible phenotype, but show decreased tumor angiogenesis upon
CC transplantation of tumor cells, and their blood vessels are abnormally
CC leaky. {ECO:0000269|PubMed:18174465, ECO:0000269|PubMed:18483218,
CC ECO:0000269|PubMed:21378273}.
CC -!- SIMILARITY: Belongs to the kindlin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH34168.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC033436; AAH33436.1; -; mRNA.
DR EMBL; BC034168; AAH34168.1; ALT_INIT; mRNA.
DR EMBL; AK079588; BAC37692.1; -; mRNA.
DR CCDS; CCDS26977.1; -.
DR RefSeq; NP_666166.2; NM_146054.2.
DR PDB; 5XPY; X-ray; 2.10 A; A=15-680.
DR PDB; 5XPZ; X-ray; 2.60 A; A/B=1-680.
DR PDB; 5XQ0; X-ray; 2.75 A; A/B=1-680.
DR PDB; 5XQ1; X-ray; 2.95 A; A/B=1-680.
DR PDBsum; 5XPY; -.
DR PDBsum; 5XPZ; -.
DR PDBsum; 5XQ0; -.
DR PDBsum; 5XQ1; -.
DR AlphaFoldDB; Q8CIB5; -.
DR BMRB; Q8CIB5; -.
DR SMR; Q8CIB5; -.
DR BioGRID; 230085; 21.
DR IntAct; Q8CIB5; 3.
DR STRING; 10090.ENSMUSP00000044554; -.
DR iPTMnet; Q8CIB5; -.
DR PhosphoSitePlus; Q8CIB5; -.
DR SwissPalm; Q8CIB5; -.
DR EPD; Q8CIB5; -.
DR jPOST; Q8CIB5; -.
DR MaxQB; Q8CIB5; -.
DR PaxDb; Q8CIB5; -.
DR PRIDE; Q8CIB5; -.
DR ProteomicsDB; 271741; -.
DR Antibodypedia; 23904; 326 antibodies from 31 providers.
DR DNASU; 218952; -.
DR Ensembl; ENSMUST00000045905; ENSMUSP00000044554; ENSMUSG00000037712.
DR GeneID; 218952; -.
DR KEGG; mmu:218952; -.
DR UCSC; uc007tgq.1; mouse.
DR CTD; 10979; -.
DR MGI; MGI:2385001; Fermt2.
DR VEuPathDB; HostDB:ENSMUSG00000037712; -.
DR eggNOG; KOG3727; Eukaryota.
DR GeneTree; ENSGT00390000013444; -.
DR HOGENOM; CLU_011611_1_0_1; -.
DR InParanoid; Q8CIB5; -.
DR OMA; YWVRCEN; -.
DR OrthoDB; 1485238at2759; -.
DR PhylomeDB; Q8CIB5; -.
DR TreeFam; TF314677; -.
DR Reactome; R-MMU-446353; Cell-extracellular matrix interactions.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR BioGRID-ORCS; 218952; 14 hits in 72 CRISPR screens.
DR ChiTaRS; Fermt2; mouse.
DR PRO; PR:Q8CIB5; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q8CIB5; protein.
DR Bgee; ENSMUSG00000037712; Expressed in ureter smooth muscle and 260 other tissues.
DR ExpressionAtlas; Q8CIB5; baseline and differential.
DR Genevisible; Q8CIB5; MM.
DR GO; GO:0005912; C:adherens junction; ISO:MGI.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0030055; C:cell-substrate junction; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
DR GO; GO:0031674; C:I band; IEA:UniProtKB-SubCell.
DR GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0001725; C:stress fiber; IDA:MGI.
DR GO; GO:0003779; F:actin binding; ISO:MGI.
DR GO; GO:0051015; F:actin filament binding; IDA:MGI.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0046332; F:SMAD binding; ISO:MGI.
DR GO; GO:0034713; F:type I transforming growth factor beta receptor binding; ISO:MGI.
DR GO; GO:0034334; P:adherens junction maintenance; IMP:ARUK-UCL.
DR GO; GO:0007155; P:cell adhesion; ISO:MGI.
DR GO; GO:0007160; P:cell-matrix adhesion; IMP:UniProtKB.
DR GO; GO:0048041; P:focal adhesion assembly; IMP:UniProtKB.
DR GO; GO:0033622; P:integrin activation; IMP:UniProtKB.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0060173; P:limb development; IMP:ARUK-UCL.
DR GO; GO:0060548; P:negative regulation of cell death; ISO:MGI.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; IMP:ARUK-UCL.
DR GO; GO:0043116; P:negative regulation of vascular permeability; IMP:ARUK-UCL.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISO:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; ISO:MGI.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:MGI.
DR GO; GO:0033625; P:positive regulation of integrin activation; ISO:MGI.
DR GO; GO:1902462; P:positive regulation of mesenchymal stem cell proliferation; ISO:MGI.
DR GO; GO:0035505; P:positive regulation of myosin light chain kinase activity; ISO:MGI.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:ARUK-UCL.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:MGI.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; ISO:MGI.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; ISO:MGI.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISO:MGI.
DR GO; GO:1903691; P:positive regulation of wound healing, spreading of epidermal cells; ISO:MGI.
DR GO; GO:1902414; P:protein localization to cell junction; ISO:MGI.
DR GO; GO:0072657; P:protein localization to membrane; IMP:UniProtKB.
DR GO; GO:0022604; P:regulation of cell morphogenesis; ISO:MGI.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IMP:UniProtKB.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; ISS:UniProtKB.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd01237; PH_fermitin; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR037843; Kindlin/fermitin.
DR InterPro; IPR040790; Kindlin_2_N.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR037837; PH_Kindlin/fermitin.
DR PANTHER; PTHR16160; PTHR16160; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF18124; Kindlin_2_N; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00295; B41; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF47031; SSF47031; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Cell junction; Cell membrane; Cell projection;
KW Cell shape; Cytoplasm; Cytoskeleton; Lipid-binding; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Wnt signaling pathway.
FT CHAIN 1..680
FT /note="Fermitin family homolog 2"
FT /id="PRO_0000219457"
FT DOMAIN 189..661
FT /note="FERM"
FT DOMAIN 380..476
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 40..81
FT /note="Interaction with membranes containing
FT phosphatidylinositol phosphate"
FT /evidence="ECO:0000250"
FT REGION 141..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 383
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3,4,5-trisphosphate)"
FT /ligand_id="ChEBI:CHEBI:57836"
FT /evidence="ECO:0000250"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96AC1"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96AC1"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96AC1"
FT MOD_RES 666
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MUTAGEN 614..615
FT /note="QW->AA: Abolishes interaction with integrins ITGB1
FT and ITGB3."
FT /evidence="ECO:0000269|PubMed:18483218"
FT CONFLICT 149
FT /note="K -> R (in Ref. 2; BAC37692)"
FT /evidence="ECO:0000305"
FT STRAND 18..24
FT /evidence="ECO:0007829|PDB:5XPY"
FT TURN 25..28
FT /evidence="ECO:0007829|PDB:5XPY"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:5XPY"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:5XPZ"
FT HELIX 41..52
FT /evidence="ECO:0007829|PDB:5XPY"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:5XPY"
FT TURN 66..69
FT /evidence="ECO:0007829|PDB:5XPY"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:5XPY"
FT TURN 79..83
FT /evidence="ECO:0007829|PDB:5XPY"
FT STRAND 89..102
FT /evidence="ECO:0007829|PDB:5XPY"
FT STRAND 108..114
FT /evidence="ECO:0007829|PDB:5XPY"
FT HELIX 119..129
FT /evidence="ECO:0007829|PDB:5XPY"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:5XPY"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:5XPY"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:5XPY"
FT HELIX 230..236
FT /evidence="ECO:0007829|PDB:5XPY"
FT HELIX 242..248
FT /evidence="ECO:0007829|PDB:5XPY"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:5XPY"
FT HELIX 259..262
FT /evidence="ECO:0007829|PDB:5XPY"
FT STRAND 269..274
FT /evidence="ECO:0007829|PDB:5XPY"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:5XPY"
FT HELIX 288..303
FT /evidence="ECO:0007829|PDB:5XPY"
FT HELIX 311..329
FT /evidence="ECO:0007829|PDB:5XPY"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:5XPY"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:5XPY"
FT STRAND 514..516
FT /evidence="ECO:0007829|PDB:5XQ1"
FT HELIX 518..520
FT /evidence="ECO:0007829|PDB:5XPY"
FT HELIX 524..529
FT /evidence="ECO:0007829|PDB:5XPY"
FT HELIX 532..543
FT /evidence="ECO:0007829|PDB:5XPY"
FT TURN 544..548
FT /evidence="ECO:0007829|PDB:5XPY"
FT HELIX 551..563
FT /evidence="ECO:0007829|PDB:5XPY"
FT TURN 566..569
FT /evidence="ECO:0007829|PDB:5XPY"
FT STRAND 571..577
FT /evidence="ECO:0007829|PDB:5XPY"
FT STRAND 584..588
FT /evidence="ECO:0007829|PDB:5XPY"
FT STRAND 590..596
FT /evidence="ECO:0007829|PDB:5XPY"
FT TURN 598..600
FT /evidence="ECO:0007829|PDB:5XPY"
FT STRAND 603..608
FT /evidence="ECO:0007829|PDB:5XPY"
FT HELIX 609..611
FT /evidence="ECO:0007829|PDB:5XPY"
FT STRAND 612..618
FT /evidence="ECO:0007829|PDB:5XPY"
FT TURN 619..622
FT /evidence="ECO:0007829|PDB:5XPY"
FT STRAND 623..628
FT /evidence="ECO:0007829|PDB:5XPY"
FT HELIX 629..631
FT /evidence="ECO:0007829|PDB:5XPY"
FT STRAND 633..637
FT /evidence="ECO:0007829|PDB:5XPY"
FT HELIX 640..656
FT /evidence="ECO:0007829|PDB:5XPY"
FT TURN 657..661
FT /evidence="ECO:0007829|PDB:5XPY"
FT HELIX 669..677
FT /evidence="ECO:0007829|PDB:5XPY"
SQ SEQUENCE 680 AA; 77800 MW; 89767FA0E34B543B CRC64;
MALDGIRMPD GCYADGTWEL SVHVTDLNRD VTLRVTGEVH IGGVMLKLVE KLDVKKDWSD
HALWWEKKRT WLLKTHWTLD KCGIQADAKL QFTPQHKLLR LQLPNMKYVK VKVNFSDRVF
KAVSDICKTF NIRHPEELSL LKKPRDPTKK KKKKLDDQSE DEALELEGPL IMPGSGSIYS
SPGLYSKTMT PTYDAHDGSP LSPTSAWFGD SALSEGNPGI LAVSQPVTSP EILAKMFKPQ
ALLDKAKTNQ GWLDSSRSLM EQDVKENEAL LLRFKYYSFF DLNPKYDAIR INQLYEQAKW
ALLLEEIECT EEEMMMFAAL QYHINKLSIM TSENHLNNSD KEVDEVDAAL SDLEITLEGG
KTSTILGDIT SIPELADYIK VFKPKKLTLK GYKQYWCTFK DTSISCYKSR EESSGTPAHQ
LNLRGCEVTP DVNISGQKFN IKLLIPVAEG MNEIWLRCDN EKQYAHWMAA CRLASKGKTM
ADSSYNLEVQ NILSFLKMQH LNPDPQLIPD QITTDVNPEC LVSPRYLKKY KSKQITARIL
EAHQNVAQMS LIEAKMRFIQ AWQSLPEFGI THFIARFQGG KREELIGIAY NRLIRMDAST
GDAIKTWRFS NMKQWNVNWE IKMVTVEFAD EVRLSFICTE VDCKVVHEFI GGYIFLSTRA
KDQNESLDEE MFYKLTSGWV
