GDIR1_MOUSE
ID GDIR1_MOUSE Reviewed; 204 AA.
AC Q99PT1; Q5M9P6; Q8BPI0; Q99KC4;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Rho GDP-dissociation inhibitor 1;
DE Short=Rho GDI 1;
DE AltName: Full=GDI-1;
DE AltName: Full=Rho-GDI alpha;
GN Name=Arhgdia; Synonyms=C87222, Gdi1;
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].
RA Minamitani T., Matsumoto K.;
RT "Mouse cDNA sequence for RhoGDI-1.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Pituitary, and 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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 34-49; 59-98 AND 153-167, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34, 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 [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=19029984; DOI=10.1038/nm.1879;
RA Shibata S., Nagase M., Yoshida S., Kawarazaki W., Kurihara H., Tanaka H.,
RA Miyoshi J., Takai Y., Fujita T.;
RT "Modification of mineralocorticoid receptor function by Rac1 GTPase:
RT implication in proteinuric kidney disease.";
RL Nat. Med. 14:1370-1376(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34, AND IDENTIFICATION BY
RP 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 [9]
RP INTERACTION WITH PLXNB3.
RX PubMed=20696765; DOI=10.1074/jbc.m110.120451;
RA Li X., Lee A.Y.;
RT "Semaphorin 5A and plexin-B3 inhibit human glioma cell motility through
RT RhoGDIalpha-mediated inactivation of Rac1 GTPase.";
RL J. Biol. Chem. 285:32436-32445(2010).
RN [10]
RP FUNCTION, INTERACTION WITH RHOA; RAC1 AND CDC42, TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-185.
RX PubMed=23434736; DOI=10.1136/jmedgenet-2012-101442;
RA Gupta I.R., Baldwin C., Auguste D., Ha K.C., El Andalousi J.,
RA Fahiminiya S., Bitzan M., Bernard C., Akbari M.R., Narod S.A.,
RA Rosenblatt D.S., Majewski J., Takano T.;
RT "ARHGDIA: a novel gene implicated in nephrotic syndrome.";
RL J. Med. Genet. 50:330-338(2013).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-43 AND LYS-141, SUCCINYLATION
RP [LARGE SCALE ANALYSIS] AT LYS-141, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 2-204 IN COMPLEX WITH PRENYLATED
RP RHOA, FUNCTION, AND SUBUNIT.
RX PubMed=22628549; DOI=10.1074/jbc.m112.371294;
RA Tnimov Z., Guo Z., Gambin Y., Nguyen U.T., Wu Y.W., Abankwa D., Stigter A.,
RA Collins B.M., Waldmann H., Goody R.S., Alexandrov K.;
RT "Quantitative analysis of prenylated RhoA interaction with its chaperone,
RT RhoGDI.";
RL J. Biol. Chem. 287:26549-26562(2012).
CC -!- FUNCTION: Controls Rho proteins homeostasis. Regulates the GDP/GTP
CC exchange reaction of the Rho proteins by inhibiting the dissociation of
CC GDP from them, and the subsequent binding of GTP to them. Retains Rho
CC proteins such as CDC42, RAC1 and RHOA in an inactive cytosolic pool,
CC regulating their stability and protecting them from degradation.
CC Actively involved in the recycling and distribution of activated Rho
CC GTPases in the cell, mediates extraction from membranes of both
CC inactive and activated molecules due its exceptionally high affinity
CC for prenylated forms. Through the modulation of Rho proteins, may play
CC a role in cell motility regulation. In glioma cells, inhibits cell
CC migration and invasion by mediating the signals of SEMA5A and PLXNB3
CC that lead to inactivation of RAC1. {ECO:0000269|PubMed:19029984,
CC ECO:0000269|PubMed:22628549, ECO:0000269|PubMed:23434736}.
CC -!- SUBUNIT: Monomer (PubMed:22628549). Interacts with FER (By similarity).
CC Interacts with PLXNB3 (PubMed:20696765). Forms a heterodimer with RAC1
CC (PubMed:23434736). Interacts with RHOA, the affinity is increased by
CC three orders of magnitude when RHOA is prenylated (PubMed:23434736).
CC Interacts with PSMD10; the interaction increases ARHGDIA association
CC with RHOA, leading to ARHGDIA-mediated inactivation of RHOA and ROCK
CC and prolonged AKT activation (By similarity). Interacts with KANK2; the
CC interaction is direct and may regulate the interaction of ARHGDIA with
CC RHOA, RAC1 and CDC42 (By similarity). Interacts with RHOC (By
CC similarity). Interacts with CDC42 (PubMed:23434736). Interacts with
CC NGFR (via death domain); NGFR binding decreases the affinity for RHOA
CC (By similarity). {ECO:0000250|UniProtKB:P52565,
CC ECO:0000269|PubMed:20696765, ECO:0000269|PubMed:22628549,
CC ECO:0000269|PubMed:23434736}.
CC -!- INTERACTION:
CC Q99PT1; P60764: Rac3; NbExp=3; IntAct=EBI-494354, EBI-644949;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23434736}.
CC -!- TISSUE SPECIFICITY: In kidney glomerulus, expressed in podocytes and
CC mesangial cells. {ECO:0000269|PubMed:19029984,
CC ECO:0000269|PubMed:23434736}.
CC -!- DISRUPTION PHENOTYPE: From 1 week to 12 weeks of age, progressive
CC deterioration from mild to massive albuminuria as consequence of renal
CC abnormalities. In kidney, severe podocyte damage, glomerular lesions
CC with focal and segmental sclerosis, along with prominent intratubular
CC casts and luminal dilatation. Tubular epithelial cells show
CC degenerative changes with basement membrane thickening. Increase of
CC apoptotic cells in kidney glomeruli and tubulointerstitium.
CC {ECO:0000269|PubMed:19029984}.
CC -!- SIMILARITY: Belongs to the Rho GDI family. {ECO:0000305}.
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DR EMBL; AB055070; BAB21527.1; -; mRNA.
DR EMBL; AK075656; BAC35881.1; -; mRNA.
DR EMBL; AK077343; BAC36761.1; -; mRNA.
DR EMBL; AK143516; BAE25410.1; -; mRNA.
DR EMBL; AK156819; BAE33865.1; -; mRNA.
DR EMBL; AK165241; BAE38098.1; -; mRNA.
DR EMBL; AK170553; BAE41876.1; -; mRNA.
DR EMBL; AK170718; BAE41976.1; -; mRNA.
DR EMBL; AK172140; BAE42844.1; -; mRNA.
DR EMBL; AL663030; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004732; AAH04732.1; -; mRNA.
DR EMBL; BC086755; AAH86755.1; -; mRNA.
DR CCDS; CCDS25743.1; -.
DR RefSeq; NP_598557.3; NM_133796.7.
DR RefSeq; XP_006532612.1; XM_006532549.3.
DR PDB; 4F38; X-ray; 2.80 A; B=2-204.
DR PDBsum; 4F38; -.
DR AlphaFoldDB; Q99PT1; -.
DR SMR; Q99PT1; -.
DR BioGRID; 228703; 18.
DR IntAct; Q99PT1; 3.
DR MINT; Q99PT1; -.
DR STRING; 10090.ENSMUSP00000063714; -.
DR iPTMnet; Q99PT1; -.
DR PhosphoSitePlus; Q99PT1; -.
DR SwissPalm; Q99PT1; -.
DR REPRODUCTION-2DPAGE; IPI00322312; -.
DR REPRODUCTION-2DPAGE; Q99PT1; -.
DR UCD-2DPAGE; Q99PT1; -.
DR EPD; Q99PT1; -.
DR jPOST; Q99PT1; -.
DR MaxQB; Q99PT1; -.
DR PaxDb; Q99PT1; -.
DR PeptideAtlas; Q99PT1; -.
DR PRIDE; Q99PT1; -.
DR ProteomicsDB; 267790; -.
DR TopDownProteomics; Q99PT1; -.
DR Antibodypedia; 3880; 580 antibodies from 39 providers.
DR DNASU; 192662; -.
DR Ensembl; ENSMUST00000067936; ENSMUSP00000063714; ENSMUSG00000025132.
DR Ensembl; ENSMUST00000106197; ENSMUSP00000101803; ENSMUSG00000025132.
DR GeneID; 192662; -.
DR KEGG; mmu:192662; -.
DR UCSC; uc007mtj.1; mouse.
DR CTD; 396; -.
DR MGI; MGI:2178103; Arhgdia.
DR VEuPathDB; HostDB:ENSMUSG00000025132; -.
DR eggNOG; KOG3205; Eukaryota.
DR GeneTree; ENSGT00390000006233; -.
DR HOGENOM; CLU_076228_1_1_1; -.
DR InParanoid; Q99PT1; -.
DR OMA; DDDKRCH; -.
DR OrthoDB; 1265661at2759; -.
DR PhylomeDB; Q99PT1; -.
DR TreeFam; TF105387; -.
DR Reactome; R-MMU-193634; Axonal growth inhibition (RHOA activation).
DR Reactome; R-MMU-209563; Axonal growth stimulation.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013106; RHOC GTPase cycle.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR Reactome; R-MMU-9013407; RHOH GTPase cycle.
DR Reactome; R-MMU-9013408; RHOG GTPase cycle.
DR BioGRID-ORCS; 192662; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Arhgdia; mouse.
DR PRO; PR:Q99PT1; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q99PT1; protein.
DR Bgee; ENSMUSG00000025132; Expressed in embryonic post-anal tail and 271 other tissues.
DR Genevisible; Q99PT1; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0001772; C:immunological synapse; IDA:MGI.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0005504; F:fatty acid binding; ISO:MGI.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0051879; F:Hsp90 protein binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0005094; F:Rho GDP-dissociation inhibitor activity; IDA:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; ISO:MGI.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
DR GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; ISO:MGI.
DR GO; GO:0008360; P:regulation of cell shape; ISO:MGI.
DR GO; GO:0032880; P:regulation of protein localization; IDA:MGI.
DR GO; GO:0035023; P:regulation of Rho protein signal transduction; ISO:MGI.
DR GO; GO:0007266; P:Rho protein signal transduction; IDA:MGI.
DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; IMP:UniProtKB.
DR Gene3D; 2.70.50.30; -; 1.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR000406; Rho_GDI.
DR InterPro; IPR024792; RhoGDI_dom_sf.
DR PANTHER; PTHR10980; PTHR10980; 1.
DR Pfam; PF02115; Rho_GDI; 1.
DR PRINTS; PR00492; RHOGDI.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW GTPase activation; Isopeptide bond; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P52565"
FT CHAIN 2..204
FT /note="Rho GDP-dissociation inhibitor 1"
FT /id="PRO_0000219014"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P52565"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 43
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52565"
FT MOD_RES 105
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52565"
FT MOD_RES 127
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52565"
FT MOD_RES 141
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 141
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 178
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52565"
FT CROSSLNK 138
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P52565"
FT CROSSLNK 138
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P52565"
FT CROSSLNK 141
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P52565"
FT CROSSLNK 141
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P52565"
FT MUTAGEN 185
FT /note="Missing: Loss of interaction with CDC42, RHOA and
FT RAC1."
FT /evidence="ECO:0000269|PubMed:23434736"
FT CONFLICT 55
FT /note="L -> P (in Ref. 4; AAH04732)"
FT /evidence="ECO:0000305"
FT HELIX 11..14
FT /evidence="ECO:0007829|PDB:4F38"
FT HELIX 35..40
FT /evidence="ECO:0007829|PDB:4F38"
FT TURN 41..44
FT /evidence="ECO:0007829|PDB:4F38"
FT HELIX 46..56
FT /evidence="ECO:0007829|PDB:4F38"
FT STRAND 69..78
FT /evidence="ECO:0007829|PDB:4F38"
FT STRAND 86..92
FT /evidence="ECO:0007829|PDB:4F38"
FT HELIX 94..99
FT /evidence="ECO:0007829|PDB:4F38"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:4F38"
FT STRAND 109..118
FT /evidence="ECO:0007829|PDB:4F38"
FT STRAND 123..134
FT /evidence="ECO:0007829|PDB:4F38"
FT STRAND 137..149
FT /evidence="ECO:0007829|PDB:4F38"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:4F38"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:4F38"
FT STRAND 173..182
FT /evidence="ECO:0007829|PDB:4F38"
FT STRAND 190..201
FT /evidence="ECO:0007829|PDB:4F38"
SQ SEQUENCE 204 AA; 23407 MW; 8ACE6F4456D842D8 CRC64;
MAEQEPTAEQ LAQIAAENEE DEHSVNYKPP AQKSIQEIQE LDKDDESLRK YKEALLGRVA
VSADPNVPNV IVTRLTLVCS TAPGPLELDL TGDLESFKKQ SFVLKEGVEY RIKISFRVNR
EIVSGMKYIQ HTYRKGVKID KTDYMVGSYG PRAEEYEFLT PMEEAPKGML ARGSYNIKSR
FTDDDKTDHL SWEWNLTIKK EWKD
