FARP2_MOUSE
ID FARP2_MOUSE Reviewed; 1065 AA.
AC Q91VS8; E9QJS4; Q3TAP2; Q69ZZ0;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=FERM, ARHGEF and pleckstrin domain-containing protein 2;
DE AltName: Full=FERM domain including RhoGEF;
DE Short=FIR;
DE AltName: Full=FERM, RhoGEF and pleckstrin domain-containing protein 2;
GN Name=Farp2; Synonyms=Kiaa0793;
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=NOD; TISSUE=Spleen;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 880-1065.
RC TISSUE=Pancreatic islet;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [5]
RP FUNCTION, INTERACTION WITH RAC1, AND TISSUE SPECIFICITY.
RX PubMed=12351724; DOI=10.1523/jneurosci.22-19-08504.2002;
RA Kubo T., Yamashita T., Yamaguchi A., Sumimoto H., Hosokawa K., Tohyama M.;
RT "A novel FERM domain including guanine nucleotide exchange factor is
RT involved in Rac signaling and regulates neurite remodeling.";
RL J. Neurosci. 22:8504-8513(2002).
RN [6]
RP FUNCTION, AND INTERACTION WITH PLXNA1 AND PIP5K1C.
RX PubMed=16286926; DOI=10.1038/nn1596;
RA Toyofuku T., Yoshida J., Sugimoto T., Zhang H., Kumanogoh A., Hori M.,
RA Kikutani H.;
RT "FARP2 triggers signals for Sema3A-mediated axonal repulsion.";
RL Nat. Neurosci. 8:1712-1719(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-863, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-863 AND SER-880, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Liver, Lung, and Pancreas;
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 [9]
RP FUNCTION, AND INDUCTION.
RX PubMed=20702777; DOI=10.1096/fj.10-158212;
RA Takegahara N., Kang S., Nojima S., Takamatsu H., Okuno T., Kikutani H.,
RA Toyofuku T., Kumanogoh A.;
RT "Integral roles of a guanine nucleotide exchange factor, FARP2, in
RT osteoclast podosome rearrangements.";
RL FASEB J. 24:4782-4792(2010).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 536-749, FUNCTION, MUTAGENESIS OF
RP LEU-730 AND LEU-733, INTERACTION WITH RAC1, AND DOMAIN.
RX PubMed=23375260; DOI=10.1016/j.str.2013.01.001;
RA He X., Kuo Y.C., Rosche T.J., Zhang X.;
RT "Structural basis for autoinhibition of the guanine nucleotide exchange
RT factor FARP2.";
RL Structure 21:355-364(2013).
CC -!- FUNCTION: Functions as guanine nucleotide exchange factor that
CC activates RAC1. May have relatively low activity (PubMed:23375260 and
CC PubMed:20702777). Plays a role in the response to class 3 semaphorins
CC and remodeling of the actin cytoskeleton. Plays a role in TNFSF11-
CC mediated osteoclast differentiation, especially in podosome
CC rearrangement and reorganization of the actin cytoskeleton. Regulates
CC the activation of ITGB3, integrin signaling and cell adhesion.
CC {ECO:0000269|PubMed:12351724, ECO:0000269|PubMed:16286926,
CC ECO:0000269|PubMed:20702777, ECO:0000269|PubMed:23375260}.
CC -!- SUBUNIT: Interacts with PLXNA1. Interaction with PLXNA1 or PIP5K1C
CC lowers its guanine nucleotide exchange activity. Dissociates from
CC PLXNA1 when SEMA3A binds to the receptor. Interacts with PIP5K1C via
CC its FERM domain. The interaction with PIP5K1C is enhanced by SEMA3A
CC binding. Interacts with RAC1. {ECO:0000269|PubMed:12351724,
CC ECO:0000269|PubMed:16286926, ECO:0000269|PubMed:23375260}.
CC -!- TISSUE SPECIFICITY: Detected in adult brain, lung and testis. Detected
CC in embryonic hippocampus and brain cortex.
CC {ECO:0000269|PubMed:12351724}.
CC -!- INDUCTION: Up-regulated by TNFSF11. {ECO:0000269|PubMed:20702777}.
CC -!- DOMAIN: Intramolecular interaction between the DH domain and the PH
CC domains can stabilize the protein in an autoinhibited conformation.
CC {ECO:0000269|PubMed:23375260}.
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; AK171713; BAE42626.1; -; mRNA.
DR EMBL; AC108412; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC131316; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC009153; AAH09153.1; -; mRNA.
DR EMBL; AK173028; BAD32306.1; -; mRNA.
DR CCDS; CCDS15191.1; -.
DR RefSeq; NP_663494.2; NM_145519.2.
DR PDB; 4GYV; X-ray; 2.90 A; A/B/C/D/E/F/G/H/I=536-749.
DR PDB; 4GZU; X-ray; 3.20 A; A/B=536-1032.
DR PDB; 6D2K; X-ray; 1.55 A; A=38-324.
DR PDBsum; 4GYV; -.
DR PDBsum; 4GZU; -.
DR PDBsum; 6D2K; -.
DR AlphaFoldDB; Q91VS8; -.
DR SMR; Q91VS8; -.
DR BioGRID; 230620; 10.
DR IntAct; Q91VS8; 2.
DR MINT; Q91VS8; -.
DR STRING; 10090.ENSMUSP00000112725; -.
DR iPTMnet; Q91VS8; -.
DR PhosphoSitePlus; Q91VS8; -.
DR jPOST; Q91VS8; -.
DR MaxQB; Q91VS8; -.
DR PaxDb; Q91VS8; -.
DR PeptideAtlas; Q91VS8; -.
DR PRIDE; Q91VS8; -.
DR ProteomicsDB; 267572; -.
DR Antibodypedia; 34561; 157 antibodies from 23 providers.
DR DNASU; 227377; -.
DR Ensembl; ENSMUST00000120301; ENSMUSP00000112725; ENSMUSG00000034066.
DR GeneID; 227377; -.
DR KEGG; mmu:227377; -.
DR UCSC; uc007cec.2; mouse.
DR CTD; 9855; -.
DR MGI; MGI:2385126; Farp2.
DR VEuPathDB; HostDB:ENSMUSG00000034066; -.
DR eggNOG; KOG3531; Eukaryota.
DR GeneTree; ENSGT00940000158642; -.
DR HOGENOM; CLU_012301_0_0_1; -.
DR InParanoid; Q91VS8; -.
DR OMA; RMDNQEE; -.
DR OrthoDB; 476668at2759; -.
DR PhylomeDB; Q91VS8; -.
DR TreeFam; TF351276; -.
DR Reactome; R-MMU-399955; SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR BioGRID-ORCS; 227377; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Farp2; mouse.
DR PRO; PR:Q91VS8; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q91VS8; protein.
DR Bgee; ENSMUSG00000034066; Expressed in bone fossa and 219 other tissues.
DR ExpressionAtlas; Q91VS8; baseline and differential.
DR Genevisible; Q91VS8; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IMP:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IMP:UniProtKB.
DR GO; GO:0022405; P:hair cycle process; IMP:MGI.
DR GO; GO:0016322; P:neuron remodeling; ISO:MGI.
DR GO; GO:0030316; P:osteoclast differentiation; IMP:UniProtKB.
DR GO; GO:0071800; P:podosome assembly; IMP:UniProtKB.
DR GO; GO:0016601; P:Rac protein signal transduction; ISO:MGI.
DR GO; GO:0033623; P:regulation of integrin activation; IMP:UniProtKB.
DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; IMP:UniProtKB.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13193; FERM_C_FARP1-like; 1.
DR CDD; cd00160; RhoGEF; 1.
DR DisProt; DP02896; -.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 3.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR000798; Ez/rad/moesin-like.
DR InterPro; IPR041788; FARP1/FARP2/FRMD7_FERM_C.
DR InterPro; IPR014847; FERM-adjacent.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR019747; FERM_CS.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR018979; FERM_N.
DR InterPro; IPR018980; FERM_PH-like_C.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF08736; FA; 1.
DR Pfam; PF09380; FERM_C; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF09379; FERM_N; 1.
DR Pfam; PF00169; PH; 2.
DR Pfam; PF00621; RhoGEF; 1.
DR PRINTS; PR00935; BAND41.
DR PRINTS; PR00661; ERMFAMILY.
DR SMART; SM00295; B41; 1.
DR SMART; SM01195; FA; 1.
DR SMART; SM01196; FERM_C; 1.
DR SMART; SM00233; PH; 2.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF47031; SSF47031; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS00660; FERM_1; 1.
DR PROSITE; PS50057; FERM_3; 1.
DR PROSITE; PS50003; PH_DOMAIN; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Guanine-nucleotide releasing factor; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..1065
FT /note="FERM, ARHGEF and pleckstrin domain-containing
FT protein 2"
FT /id="PRO_0000232756"
FT DOMAIN 44..324
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT DOMAIN 538..729
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 758..855
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 930..1027
FT /note="PH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 406..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 874..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 880..894
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94887"
FT MOD_RES 440
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94887"
FT MOD_RES 863
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 880
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MUTAGEN 730
FT /note="L->R: Increases guanyl-nucleotide exchange factor
FT activity with RAC1; when associated with Q-733."
FT /evidence="ECO:0000269|PubMed:23375260"
FT MUTAGEN 733
FT /note="L->Q: Increases guanyl-nucleotide exchange factor
FT activity with RAC1; when associated with R-730."
FT /evidence="ECO:0000269|PubMed:23375260"
FT CONFLICT 234
FT /note="H -> R (in Ref. 1; BAE42626)"
FT /evidence="ECO:0000305"
FT CONFLICT 821
FT /note="P -> L (in Ref. 1; BAE42626 and 3; AAH09153)"
FT /evidence="ECO:0000305"
FT CONFLICT 1019
FT /note="M -> I (in Ref. 4; BAD32306)"
FT /evidence="ECO:0000305"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:6D2K"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:6D2K"
FT HELIX 66..77
FT /evidence="ECO:0007829|PDB:6D2K"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:6D2K"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:6D2K"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:6D2K"
FT HELIX 105..109
FT /evidence="ECO:0007829|PDB:6D2K"
FT STRAND 115..121
FT /evidence="ECO:0007829|PDB:6D2K"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:6D2K"
FT HELIX 134..149
FT /evidence="ECO:0007829|PDB:6D2K"
FT HELIX 157..172
FT /evidence="ECO:0007829|PDB:6D2K"
FT HELIX 177..186
FT /evidence="ECO:0007829|PDB:6D2K"
FT HELIX 193..196
FT /evidence="ECO:0007829|PDB:6D2K"
FT HELIX 197..204
FT /evidence="ECO:0007829|PDB:6D2K"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:6D2K"
FT HELIX 212..223
FT /evidence="ECO:0007829|PDB:6D2K"
FT TURN 227..230
FT /evidence="ECO:0007829|PDB:6D2K"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:6D2K"
FT STRAND 243..249
FT /evidence="ECO:0007829|PDB:6D2K"
FT STRAND 252..257
FT /evidence="ECO:0007829|PDB:6D2K"
FT STRAND 260..266
FT /evidence="ECO:0007829|PDB:6D2K"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:6D2K"
FT STRAND 272..276
FT /evidence="ECO:0007829|PDB:6D2K"
FT STRAND 279..283
FT /evidence="ECO:0007829|PDB:6D2K"
FT STRAND 288..291
FT /evidence="ECO:0007829|PDB:6D2K"
FT STRAND 295..302
FT /evidence="ECO:0007829|PDB:6D2K"
FT HELIX 303..320
FT /evidence="ECO:0007829|PDB:6D2K"
FT HELIX 538..561
FT /evidence="ECO:0007829|PDB:4GYV"
FT HELIX 563..570
FT /evidence="ECO:0007829|PDB:4GYV"
FT HELIX 576..583
FT /evidence="ECO:0007829|PDB:4GYV"
FT TURN 584..586
FT /evidence="ECO:0007829|PDB:4GYV"
FT HELIX 587..608
FT /evidence="ECO:0007829|PDB:4GYV"
FT HELIX 613..619
FT /evidence="ECO:0007829|PDB:4GYV"
FT HELIX 623..633
FT /evidence="ECO:0007829|PDB:4GYV"
FT HELIX 634..636
FT /evidence="ECO:0007829|PDB:4GYV"
FT HELIX 637..641
FT /evidence="ECO:0007829|PDB:4GYV"
FT HELIX 643..655
FT /evidence="ECO:0007829|PDB:4GYV"
FT HELIX 658..668
FT /evidence="ECO:0007829|PDB:4GYV"
FT HELIX 677..680
FT /evidence="ECO:0007829|PDB:4GYV"
FT HELIX 683..701
FT /evidence="ECO:0007829|PDB:4GYV"
FT HELIX 709..725
FT /evidence="ECO:0007829|PDB:4GYV"
FT HELIX 727..743
FT /evidence="ECO:0007829|PDB:4GYV"
FT STRAND 746..748
FT /evidence="ECO:0007829|PDB:4GZU"
FT STRAND 759..768
FT /evidence="ECO:0007829|PDB:4GZU"
FT STRAND 773..781
FT /evidence="ECO:0007829|PDB:4GZU"
FT STRAND 784..788
FT /evidence="ECO:0007829|PDB:4GZU"
FT STRAND 799..806
FT /evidence="ECO:0007829|PDB:4GZU"
FT STRAND 810..813
FT /evidence="ECO:0007829|PDB:4GZU"
FT TURN 817..822
FT /evidence="ECO:0007829|PDB:4GZU"
FT STRAND 823..827
FT /evidence="ECO:0007829|PDB:4GZU"
FT STRAND 832..836
FT /evidence="ECO:0007829|PDB:4GZU"
FT HELIX 840..856
FT /evidence="ECO:0007829|PDB:4GZU"
FT HELIX 909..914
FT /evidence="ECO:0007829|PDB:4GZU"
FT TURN 915..917
FT /evidence="ECO:0007829|PDB:4GZU"
FT STRAND 919..921
FT /evidence="ECO:0007829|PDB:4GZU"
FT HELIX 922..928
FT /evidence="ECO:0007829|PDB:4GZU"
FT STRAND 933..939
FT /evidence="ECO:0007829|PDB:4GZU"
FT STRAND 948..955
FT /evidence="ECO:0007829|PDB:4GZU"
FT STRAND 958..964
FT /evidence="ECO:0007829|PDB:4GZU"
FT STRAND 971..975
FT /evidence="ECO:0007829|PDB:4GZU"
FT STRAND 980..982
FT /evidence="ECO:0007829|PDB:4GZU"
FT STRAND 994..1000
FT /evidence="ECO:0007829|PDB:4GZU"
FT STRAND 1003..1008
FT /evidence="ECO:0007829|PDB:4GZU"
FT STRAND 1010..1012
FT /evidence="ECO:0007829|PDB:4GZU"
FT HELIX 1013..1023
FT /evidence="ECO:0007829|PDB:4GZU"
SQ SEQUENCE 1065 AA; 121281 MW; 452F3BB652BE99D9 CRC64;
MGEIEGTYRA LPTSGTRLGG QTAIGVSTLE PEQSLSPRMQ EKHMRIRVKL LDSTVELFDI
EPKCDGQVLL TQVWKHLNLI ECDYFGLEFK NVQSYWIWLE PMKPIIRQVR KPKNAVLRLA
VKFFPPDPGQ LQEEYTRYLF ALQLKRDLLE ERLTCTANTA ALLISHLLQS EIGDYDETLD
REHLKANEYL PNQEKSLEKI LDFHQRHTGQ TPAESDFQVL EIARKLEMYG IRFHMASDRE
GTKINLAVSH MGVLVFQGTT KINTFNWSKV RKLSFKRKRF LIKLHPEVHG PYQDTLEFLL
GSRDECKNFW KICVEYHTFF RLSDQPKPKA KAVFFSRGSS FRYSGRTQKQ LVDYVKDGGM
KRIPYERRHS KTRTSLHALT VDLPKQSVSF TDGLRTSASL SSANVSFYPP PSSSLSPPGL
PNLKDSSSSL VDPQAPVIKS TAAERSSGPS SSDGPSTQSA HLPGPPVLRP GPGFSMDSPQ
PSPSSLKSHL SLCPELQAAL STAEQGASPV LSPVLSGAGT ARMDNQEEQK HKHMPEDEAY
FIAKEILATE RTYLKDLEVI TVWFRSVLIK EEAMPAALMA LLFSNIDPVY EFHRGFLHEV
EQRLALWEGP SSAHLKGDHQ RIGDILLRNM RQLKEFTSYF QRHDEVLTEL EKATKHCKKL
EAVYKEFELQ KVCYLPLNTF LLKPVQRLVH YRLLLSRLCA HYSPGHRDYA DCHEALKAIT
EVTTELQQSL TRLENLQKLT ELQRDLVGVE NLIAPGREFI REGCLHKLTK KGLQQRMFFL
FSDMLLYTSK SVTGASHFRI RGFLPLRGML VEESENEWSV PHCFTIYAAQ KTIVVAASTR
LEKEKWMQDL NAAIQAAKTI GDSPPVLLGG PVYTRTPRSS DEVSLEESED GRGNRGSLEG
NSQHRANTTM HVCWYRNTSV SRADHSAAVE NQLSGYLLRK FKNSNGWQKL WVVFTNFCLF
FYKTHQDDYP LASLPLLGYS VSLPREADSI HKDYVFKLQF KSHVYFFRAE SKYTFERWMD
VIKRASSSPG RPPSFTQDCS HHSPGLEAEI REKEACPSPC LDKNL
