ID RHG01_HUMAN Reviewed; 439 AA.
AC Q07960; D3DQQ6;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 225.
DE RecName: Full=Rho GTPase-activating protein 1;
DE AltName: Full=CDC42 GTPase-activating protein;
DE AltName: Full=GTPase-activating protein rhoGAP;
DE AltName: Full=Rho-related small GTPase protein activator;
DE AltName: Full=Rho-type GTPase-activating protein 1;
DE AltName: Full=p50-RhoGAP;
GN Name=ARHGAP1; Synonyms=CDC42GAP, RHOGAP1;
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].
RC TISSUE=Platelet;
RX PubMed=8253717; DOI=10.1016/s0021-9258(19)74277-x;
RA Barfod E.T., Zheng Y., Kuang W.-J., Hart M.J., Evans T., Cerione R.A.,
RA Ashkenazi A.;
RT "Cloning and expression of a human CDC42 GTPase-activating protein reveals
RT a functional SH3-binding domain.";
RL J. Biol. Chem. 268:26059-26062(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fibrosarcoma;
RX PubMed=8288572; DOI=10.1016/s0021-9258(17)42232-0;
RA Lancaster C.A., Taylor-Harris P.M., Self A.J., Brill S., van Erp H.E.,
RA Hall A.;
RT "Characterization of rhoGAP. A GTPase-activating protein for rho-related
RT small GTPases.";
RL J. Biol. Chem. 269:1137-1142(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
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 213-227.
RC TISSUE=Spleen;
RX PubMed=1905930; DOI=10.1042/bj2760833;
RA Garrett M.D., Major G.N., Totty N., Hall A.;
RT "Purification and N-terminal sequence of the p21rho GTPase-activating
RT protein, rho GAP.";
RL Biochem. J. 276:833-836(1991).
RN [6]
RP PROTEIN SEQUENCE OF 386-416.
RX PubMed=1903516; DOI=10.1038/351400a0;
RA Diekmann D., Brill S., Garrett M.D., Totty N., Hsuan J., Monfries C.,
RA Hall C., Lim L., Hall A.;
RT "Bcr encodes a GTPase-activating protein for p21rac.";
RL Nature 351:400-402(1991).
RN [7]
RP INTERACTION WITH BNIPL.
RX PubMed=12901880; DOI=10.1016/s0006-291x(03)01387-1;
RA Qin W., Hu J., Guo M., Xu J., Li J., Yao G., Zhou X., Jiang H., Zhang P.,
RA Shen L., Wan D., Gu J.;
RT "BNIPL-2, a novel homologue of BNIP-2, interacts with Bcl-2 and Cdc42GAP in
RT apoptosis.";
RL Biochem. Biophys. Res. Commun. 308:379-385(2003).
RN [8]
RP IDENTIFICATION IN A COMPLEX WITH XPO7; EIF4A1; VPS26A; VPS29; VPS35 AND
RP SFN.
RX PubMed=15282546; DOI=10.1038/sj.emboj.7600338;
RA Mingot J.-M., Bohnsack M.T., Jaekle U., Goerlich D.;
RT "Exportin 7 defines a novel general nuclear export pathway.";
RL EMBO J. 23:3227-3236(2004).
RN [9]
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND IDENTIFICATION BY
RP 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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-80, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-50 AND SER-51, AND
RP 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 [18]
RP IDENTIFICATION BY 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 [19]
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).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 198-439.
RX PubMed=9009196; DOI=10.1038/385458a0;
RA Barrett T., Xiao B., Dodson E.J., Dodson G., Ludbrook S.B., Nurmahomed K.,
RA Gamblin S.J., Musacchio A., Smerdon S.J., Eccleston J.F.;
RT "The structure of the GTPase-activating domain from p50rhoGAP.";
RL Nature 385:458-461(1997).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 233-431 IN COMPLEX WITH CDC42.
RX PubMed=9262406; DOI=10.1038/41805;
RA Rittinger K., Walker P.A., Eccleston J.F., Nurmahomed K., Owen D., Laue E.,
RA Gamblin S.J., Smerdon S.J.;
RT "Crystal structure of a small G protein in complex with the GTPase-
RT activating protein rhoGAP.";
RL Nature 388:693-697(1997).
CC -!- FUNCTION: GTPase activator for the Rho, Rac and Cdc42 proteins,
CC converting them to the putatively inactive GDP-bound state. Cdc42 seems
CC to be the preferred substrate.
CC -!- SUBUNIT: Found in a complex with XPO7, EIF4A1, ARHGAP1, VPS26A, VPS29,
CC VPS35 and SFN. Interacts with BNIPL. {ECO:0000269|PubMed:12901880,
CC ECO:0000269|PubMed:15282546, ECO:0000269|PubMed:9262406}.
CC -!- INTERACTION:
CC Q07960; P60953-2: CDC42; NbExp=3; IntAct=EBI-602762, EBI-287394;
CC Q07960; P61586: RHOA; NbExp=3; IntAct=EBI-602762, EBI-446668;
CC Q07960; Q99961: SH3GL1; NbExp=3; IntAct=EBI-602762, EBI-697911;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA16142.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U02570; AAA16142.1; ALT_INIT; mRNA.
DR EMBL; Z23024; CAA80560.1; -; mRNA.
DR EMBL; CH471064; EAW67983.1; -; Genomic_DNA.
DR EMBL; CH471064; EAW67984.1; -; Genomic_DNA.
DR EMBL; BC018118; AAH18118.1; -; mRNA.
DR CCDS; CCDS7922.1; -.
DR PIR; A49678; A49678.
DR RefSeq; NP_004299.1; NM_004308.3.
DR RefSeq; XP_011518397.1; XM_011520095.1.
DR PDB; 1AM4; X-ray; 2.70 A; A/B/C=233-431.
DR PDB; 1GRN; X-ray; 2.10 A; B=237-439.
DR PDB; 1OW3; X-ray; 1.80 A; A=198-439.
DR PDB; 1RGP; X-ray; 2.00 A; A=198-439.
DR PDB; 1TX4; X-ray; 1.65 A; A=234-431.
DR PDB; 2NGR; X-ray; 1.90 A; B=206-439.
DR PDB; 5M6X; X-ray; 2.40 A; A/H=198-437.
DR PDB; 5M70; X-ray; 2.20 A; A/F=198-437.
DR PDB; 6R3V; X-ray; 1.75 A; A=1-439.
DR PDB; 7QSC; X-ray; 1.91 A; A/C=198-439.
DR PDB; 7QTM; X-ray; 2.25 A; A/H=198-439.
DR PDBsum; 1AM4; -.
DR PDBsum; 1GRN; -.
DR PDBsum; 1OW3; -.
DR PDBsum; 1RGP; -.
DR PDBsum; 1TX4; -.
DR PDBsum; 2NGR; -.
DR PDBsum; 5M6X; -.
DR PDBsum; 5M70; -.
DR PDBsum; 6R3V; -.
DR PDBsum; 7QSC; -.
DR PDBsum; 7QTM; -.
DR AlphaFoldDB; Q07960; -.
DR SMR; Q07960; -.
DR BioGRID; 106885; 245.
DR DIP; DIP-6081N; -.
DR IntAct; Q07960; 51.
DR MINT; Q07960; -.
DR STRING; 9606.ENSP00000310491; -.
DR iPTMnet; Q07960; -.
DR MetOSite; Q07960; -.
DR PhosphoSitePlus; Q07960; -.
DR SwissPalm; Q07960; -.
DR BioMuta; ARHGAP1; -.
DR DMDM; 3024550; -.
DR OGP; Q07960; -.
DR EPD; Q07960; -.
DR jPOST; Q07960; -.
DR MassIVE; Q07960; -.
DR MaxQB; Q07960; -.
DR PaxDb; 9606-ENSP00000310491; -.
DR PeptideAtlas; Q07960; -.
DR PRIDE; Q07960; -.
DR ProteomicsDB; 58563; -.
DR Pumba; Q07960; -.
DR Antibodypedia; 1399; 265 antibodies from 30 providers.
DR DNASU; 392; -.
DR Ensembl; ENST00000311956.9; ENSP00000310491.4; ENSG00000175220.12.
DR GeneID; 392; -.
DR KEGG; hsa:392; -.
DR MANE-Select; ENST00000311956.9; ENSP00000310491.4; NM_004308.5; NP_004299.1.
DR UCSC; uc001ndd.5; human.
DR AGR; HGNC:673; -.
DR CTD; 392; -.
DR DisGeNET; 392; -.
DR GeneCards; ARHGAP1; -.
DR HGNC; HGNC:673; ARHGAP1.
DR HPA; ENSG00000175220; Low tissue specificity.
DR MIM; 602732; gene.
DR neXtProt; NX_Q07960; -.
DR OpenTargets; ENSG00000175220; -.
DR PharmGKB; PA24956; -.
DR VEuPathDB; HostDB:ENSG00000175220; -.
DR eggNOG; KOG4406; Eukaryota.
DR GeneTree; ENSGT00940000160630; -.
DR HOGENOM; CLU_030214_1_0_1; -.
DR InParanoid; Q07960; -.
DR OMA; PTRVREY; -.
DR OrthoDB; 3030820at2759; -.
DR PhylomeDB; Q07960; -.
DR TreeFam; TF324164; -.
DR PathwayCommons; Q07960; -.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013026; RHOB GTPase cycle.
DR Reactome; R-HSA-9013106; RHOC GTPase cycle.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013404; RAC2 GTPase cycle.
DR Reactome; R-HSA-9013405; RHOD GTPase cycle.
DR Reactome; R-HSA-9013406; RHOQ GTPase cycle.
DR Reactome; R-HSA-9013408; RHOG GTPase cycle.
DR Reactome; R-HSA-9013409; RHOJ GTPase cycle.
DR Reactome; R-HSA-9013423; RAC3 GTPase cycle.
DR Reactome; R-HSA-9035034; RHOF GTPase cycle.
DR Reactome; R-HSA-9696270; RND2 GTPase cycle.
DR SignaLink; Q07960; -.
DR SIGNOR; Q07960; -.
DR BioGRID-ORCS; 392; 29 hits in 1162 CRISPR screens.
DR ChiTaRS; ARHGAP1; human.
DR EvolutionaryTrace; Q07960; -.
DR GeneWiki; ARHGAP1; -.
DR GenomeRNAi; 392; -.
DR Pharos; Q07960; Tbio.
DR PRO; PR:Q07960; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q07960; Protein.
DR Bgee; ENSG00000175220; Expressed in gingival epithelium and 208 other cell types or tissues.
DR ExpressionAtlas; Q07960; baseline and differential.
DR Genevisible; Q07960; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0010008; C:endosome membrane; IDA:CAFA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:CAFA.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0005096; F:GTPase activator activity; IDA:MGI.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; IPI:CAFA.
DR GO; GO:0016197; P:endosomal transport; IMP:CAFA.
DR GO; GO:2001136; P:negative regulation of endocytic recycling; IMP:CAFA.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR GO; GO:0007266; P:Rho protein signal transduction; TAS:ProtInc.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IDA:MGI.
DR GO; GO:0033572; P:transferrin transport; IMP:CAFA.
DR CDD; cd04404; RhoGAP-p50rhoGAP; 1.
DR CDD; cd00170; SEC14; 1.
DR Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR IDEAL; IID00316; -.
DR InterPro; IPR049592; ARHGAP1_RhoGAP.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR45808:SF6; RHO GTPASE-ACTIVATING PROTEIN 1; 1.
DR PANTHER; PTHR45808; RHO GTPASE-ACTIVATING PROTEIN 68F; 1.
DR Pfam; PF13716; CRAL_TRIO_2; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00516; SEC14; 1.
DR SUPFAM; SSF52087; CRAL/TRIO domain; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW GTPase activation; Phosphoprotein; Reference proteome; SH3-binding.
FT CHAIN 1..439
FT /note="Rho GTPase-activating protein 1"
FT /id="PRO_0000056700"
FT DOMAIN 63..218
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT DOMAIN 244..431
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 28..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 228..238
FT /note="SH3-binding"
FT COMPBIAS 30..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 282
FT /note="Involved in G-protein binding to GAPs"
FT /evidence="ECO:0000305"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5FWK3"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 65
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q5FWK3"
FT MOD_RES 80
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VARIANT 369
FT /note="R -> C (in dbSNP:rs11822837)"
FT /id="VAR_049137"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:6R3V"
FT HELIX 246..252
FT /evidence="ECO:0007829|PDB:1TX4"
FT HELIX 261..273
FT /evidence="ECO:0007829|PDB:1TX4"
FT TURN 274..276
FT /evidence="ECO:0007829|PDB:5M6X"
FT TURN 278..282
FT /evidence="ECO:0007829|PDB:1TX4"
FT HELIX 287..298
FT /evidence="ECO:0007829|PDB:1TX4"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:1TX4"
FT HELIX 312..324
FT /evidence="ECO:0007829|PDB:1TX4"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:1TX4"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:1TX4"
FT HELIX 335..339
FT /evidence="ECO:0007829|PDB:1TX4"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:1TX4"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:1TX4"
FT HELIX 349..357
FT /evidence="ECO:0007829|PDB:1TX4"
FT HELIX 362..380
FT /evidence="ECO:0007829|PDB:1TX4"
FT HELIX 382..385
FT /evidence="ECO:0007829|PDB:1TX4"
FT HELIX 389..400
FT /evidence="ECO:0007829|PDB:1TX4"
FT HELIX 406..411
FT /evidence="ECO:0007829|PDB:1TX4"
FT HELIX 413..425
FT /evidence="ECO:0007829|PDB:1TX4"
FT HELIX 427..430
FT /evidence="ECO:0007829|PDB:1TX4"
SQ SEQUENCE 439 AA; 50436 MW; 4DD0CC4419849C35 CRC64;
MDPLSELQDD LTLDDTSEAL NQLKLASIDE KNWPSDEMPD FPKSDDSKSS SPELVTHLKW
DDPYYDIARH QIVEVAGDDK YGRKIIVFSA CRMPPSHQLD HSKLLGYLKH TLDQYVESDY
TLLYLHHGLT SDNKPSLSWL RDAYREFDRK YKKNIKALYI VHPTMFIKTL LILFKPLISF
KFGQKIFYVN YLSELSEHVK LEQLGIPRQV LKYDDFLKST QKSPATAPKP MPPRPPLPNQ
QFGVSLQHLQ EKNPEQEPIP IVLRETVAYL QAHALTTEGI FRRSANTQVV REVQQKYNMG
LPVDFDQYNE LHLPAVILKT FLRELPEPLL TFDLYPHVVG FLNIDESQRV PATLQVLQTL
PEENYQVLRF LTAFLVQISA HSDQNKMTNT NLAVVFGPNL LWAKDAAITL KAINPINTFT
KFLLDHQGEL FPSPDPSGL
//
