RHGBA_HUMAN
ID RHGBA_HUMAN Reviewed; 1023 AA.
AC Q6P4F7; B4DZN9; Q6PI96; Q9Y3S6;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Rho GTPase-activating protein 11A {ECO:0000305};
DE AltName: Full=Rho-type GTPase-activating protein 11A {ECO:0000305};
GN Name=ARHGAP11A {ECO:0000303|PubMed:27957544, ECO:0000312|HGNC:HGNC:15783};
GN Synonyms=KIAA0013 {ECO:0000303|PubMed:7584026};
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=7584026; DOI=10.1093/dnares/1.1.27;
RA Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S.,
RA Nagase T., Seki N., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. I. The
RT coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of
RT randomly sampled cDNA clones from human immature myeloid cell line KG-1.";
RL DNA Res. 1:27-35(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Eye, and Uterus;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285, 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285; SER-339; SER-340;
RP SER-484; THR-508; SER-582; SER-585 AND SER-675, AND IDENTIFICATION BY MASS
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285; SER-318 AND THR-323, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316; SER-318; THR-323;
RP SER-484; THR-508; SER-582; SER-585; SER-638; SER-675; SER-847; THR-866 AND
RP SER-868, AND IDENTIFICATION BY 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285; THR-306; SER-318;
RP THR-323; SER-484; THR-508; SER-585; SER-675; SER-847 AND SER-868, 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 [10]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-253.
RG Structural genomics consortium (SGC);
RT "Crystal structure of the Rho-GAP domain of ARHGAP11A.";
RL Submitted (FEB-2009) to the PDB data bank.
RN [11]
RP VARIANT [LARGE SCALE ANALYSIS] LYS-605.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [12]
RP FUNCTION.
RX PubMed=27957544; DOI=10.1126/sciadv.1601941;
RA Florio M., Namba T., Paeaebo S., Hiller M., Huttner W.B.;
RT "A single splice site mutation in human-specific ARHGAP11B causes basal
RT progenitor amplification.";
RL Sci. Adv. 2:e1601941-e1601941(2016).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=31883789; DOI=10.1016/j.neuron.2019.11.027;
RA Namba T., Doczi J., Pinson A., Xing L., Kalebic N., Wilsch-Braeuninger M.,
RA Long K.R., Vaid S., Lauer J., Bogdanova A., Borgonovo B., Shevchenko A.,
RA Keller P., Drechsel D., Kurzchalia T., Wimberger P., Chinopoulos C.,
RA Huttner W.B.;
RT "Human-specific ARHGAP11B acts in mitochondria to expand neocortical
RT progenitors by glutaminolysis.";
RL Neuron 105:867-881(2020).
CC -!- FUNCTION: GTPase activator for the Rho-type GTPases by converting them
CC to an inactive GDP-bound state. {ECO:0000269|PubMed:27957544}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:31883789}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6P4F7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P4F7-2; Sequence=VSP_054102, VSP_054103;
CC Name=3;
CC IsoId=Q6P4F7-3; Sequence=VSP_055370;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13442.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D87717; BAA13442.2; ALT_INIT; mRNA.
DR EMBL; AK303025; BAG64151.1; -; mRNA.
DR EMBL; AK316437; BAH14808.1; -; mRNA.
DR EMBL; AC123768; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC039563; AAH39563.1; -; mRNA.
DR EMBL; BC063444; AAH63444.1; -; mRNA.
DR CCDS; CCDS10028.1; -. [Q6P4F7-1]
DR CCDS; CCDS58349.1; -. [Q6P4F7-2]
DR CCDS; CCDS66730.1; -. [Q6P4F7-3]
DR PIR; A59431; A59431.
DR RefSeq; NP_001273408.1; NM_001286479.2. [Q6P4F7-3]
DR RefSeq; NP_001273409.1; NM_001286480.2. [Q6P4F7-3]
DR RefSeq; NP_055598.1; NM_014783.5. [Q6P4F7-1]
DR RefSeq; NP_955389.1; NM_199357.2. [Q6P4F7-2]
DR PDB; 3EAP; X-ray; 2.30 A; A/B/C/D=1-253.
DR PDBsum; 3EAP; -.
DR AlphaFoldDB; Q6P4F7; -.
DR SMR; Q6P4F7; -.
DR BioGRID; 115162; 67.
DR IntAct; Q6P4F7; 49.
DR MINT; Q6P4F7; -.
DR STRING; 9606.ENSP00000355090; -.
DR iPTMnet; Q6P4F7; -.
DR PhosphoSitePlus; Q6P4F7; -.
DR BioMuta; ARHGAP11A; -.
DR DMDM; 119361641; -.
DR EPD; Q6P4F7; -.
DR jPOST; Q6P4F7; -.
DR MassIVE; Q6P4F7; -.
DR MaxQB; Q6P4F7; -.
DR PaxDb; Q6P4F7; -.
DR PeptideAtlas; Q6P4F7; -.
DR PRIDE; Q6P4F7; -.
DR ProteomicsDB; 5612; -.
DR ProteomicsDB; 66975; -. [Q6P4F7-1]
DR Antibodypedia; 51650; 90 antibodies from 19 providers.
DR DNASU; 9824; -.
DR Ensembl; ENST00000361627.8; ENSP00000355090.3; ENSG00000198826.11. [Q6P4F7-1]
DR Ensembl; ENST00000543522.5; ENSP00000440073.1; ENSG00000198826.11. [Q6P4F7-3]
DR Ensembl; ENST00000565905.5; ENSP00000455754.1; ENSG00000198826.11. [Q6P4F7-3]
DR Ensembl; ENST00000567348.5; ENSP00000454575.1; ENSG00000198826.11. [Q6P4F7-2]
DR Ensembl; ENST00000611363.1; ENSP00000480085.1; ENSG00000275568.4. [Q6P4F7-3]
DR Ensembl; ENST00000619401.4; ENSP00000479117.1; ENSG00000275568.4. [Q6P4F7-1]
DR Ensembl; ENST00000622253.4; ENSP00000481011.1; ENSG00000275568.4. [Q6P4F7-3]
DR GeneID; 9824; -.
DR KEGG; hsa:9824; -.
DR MANE-Select; ENST00000361627.8; ENSP00000355090.3; NM_014783.6; NP_055598.1.
DR UCSC; uc001zgw.4; human. [Q6P4F7-1]
DR CTD; 9824; -.
DR DisGeNET; 9824; -.
DR GeneCards; ARHGAP11A; -.
DR HGNC; HGNC:15783; ARHGAP11A.
DR HPA; ENSG00000198826; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 610589; gene.
DR neXtProt; NX_Q6P4F7; -.
DR OpenTargets; ENSG00000198826; -.
DR PharmGKB; PA134982615; -.
DR VEuPathDB; HostDB:ENSG00000198826; -.
DR eggNOG; KOG2710; Eukaryota.
DR GeneTree; ENSGT00940000155312; -.
DR HOGENOM; CLU_010134_1_0_1; -.
DR InParanoid; Q6P4F7; -.
DR OMA; RQPIRHK; -.
DR OrthoDB; 213929at2759; -.
DR PhylomeDB; Q6P4F7; -.
DR TreeFam; TF332212; -.
DR PathwayCommons; Q6P4F7; -.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR SignaLink; Q6P4F7; -.
DR SIGNOR; Q6P4F7; -.
DR BioGRID-ORCS; 9824; 186 hits in 1076 CRISPR screens.
DR ChiTaRS; ARHGAP11A; human.
DR EvolutionaryTrace; Q6P4F7; -.
DR GenomeRNAi; 9824; -.
DR Pharos; Q6P4F7; Tbio.
DR PRO; PR:Q6P4F7; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q6P4F7; protein.
DR Bgee; ENSG00000198826; Expressed in ganglionic eminence and 105 other tissues.
DR ExpressionAtlas; Q6P4F7; baseline and differential.
DR Genevisible; Q6P4F7; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.555.10; -; 1.
DR InterPro; IPR042869; ARHGAP11A/B.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR15670; PTHR15670; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; GTPase activation; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1023
FT /note="Rho GTPase-activating protein 11A"
FT /id="PRO_0000267213"
FT DOMAIN 49..239
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 567..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 999..1023
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 306
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 323
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 508
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 582
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 585
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 638
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 675
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 847
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 866
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 868
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..189
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055370"
FT VAR_SEQ 496..501
FT /note="SEKISK -> TFTYYC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054102"
FT VAR_SEQ 502..1023
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054103"
FT VARIANT 605
FT /note="E -> K (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035546"
FT HELIX 4..19
FT /evidence="ECO:0007829|PDB:3EAP"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:3EAP"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:3EAP"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:3EAP"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:3EAP"
FT HELIX 67..76
FT /evidence="ECO:0007829|PDB:3EAP"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:3EAP"
FT HELIX 92..104
FT /evidence="ECO:0007829|PDB:3EAP"
FT HELIX 114..127
FT /evidence="ECO:0007829|PDB:3EAP"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:3EAP"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:3EAP"
FT HELIX 138..144
FT /evidence="ECO:0007829|PDB:3EAP"
FT HELIX 149..160
FT /evidence="ECO:0007829|PDB:3EAP"
FT HELIX 165..183
FT /evidence="ECO:0007829|PDB:3EAP"
FT HELIX 185..188
FT /evidence="ECO:0007829|PDB:3EAP"
FT HELIX 192..204
FT /evidence="ECO:0007829|PDB:3EAP"
FT HELIX 215..233
FT /evidence="ECO:0007829|PDB:3EAP"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:3EAP"
FT HELIX 243..246
FT /evidence="ECO:0007829|PDB:3EAP"
SQ SEQUENCE 1023 AA; 113866 MW; 053C89371B5F614F CRC64;
MWDQRLVRLA LLQHLRAFYG IKVKGVRGQC DRRRHETAAT EIGGKIFGVP FNALPHSAVP
EYGHIPSFLV DACTSLEDHI HTEGLFRKSG SVIRLKALKN KVDHGEGCLS SAPPCDIAGL
LKQFFRELPE PILPADLHEA LLKAQQLGTE EKNKATLLLS CLLADHTVHV LRYFFNFLRN
VSLRSSENKM DSSNLAVIFA PNLLQTSEGH EKMSSNTEKK LRLQAAVVQT LIDYASDIGR
VPDFILEKIP AMLGIDGLCA TPSLEGFEEG EYETPGEYKR KRRQSVGDFV SGALNKFKPN
RTPSITPQEE RIAQLSESPV ILTPNAKRTL PVDSSHGFSS KKRKSIKHNF NFELLPSNLF
NSSSTPVSVH IDTSSEGSSQ SSLSPVLIGG NHLITAGVPR RSKRIAGKKV CRVESGKAGC
FSPKISHKEK VRRSLRLKFN LGKNGREVNG CSGVNRYESV GWRLANQQSL KNRIESVKTG
LLFSPDVDEK LPKKGSEKIS KSEETLLTPE RLVGTNYRMS WTGPNNSSFQ EVDANEASSM
VENLEVENSL EPDIMVEKSP ATSCELTPSN LNNKHNSNIT SSPLSGDENN MTKETLVKVQ
KAFSESGSNL HALMNQRQSS VTNVGKVKLT EPSYLEDSPE ENLFETNDLT IVESKEKYEH
HTGKGEKCFS ERDFSPLQTQ TFNRETTIKC YSTQMKMEHE KDIHSNMPKD YLSKQEFSSD
EEIKKQQSPK DKLNNKLKEN ENMMEGNLPK CAAHSKDEAR SSFSQQSTCV VTNLSKPRPM
RIAKQQSLET CEKTVSESSQ MTEHRKVSDH IQWFNKLSLN EPNRIKVKSP LKFQRTPVRQ
SVRRINSLLE YSRQPTGHKL ASLGDTASPL VKSVSCDGAL SSCIESASKD SSVSCIKSGP
KEQKSMSCEE SNIGAISKSS MELPSKSFLK MRKHPDSVNA SLRSTTVYKQ KILSDGQVKV
PLDDLTNHDI VKPVVNNNMG ISSGINNRVL RRPSERGRAW YKGSPKHPIG KTQLLPTSKP
VDL
