ID   RHG04_HUMAN             Reviewed;         946 AA.
AC   P98171; Q14144; Q86UY3;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 2.
DT   27-MAR-2024, entry version 205.
DE   RecName: Full=Rho GTPase-activating protein 4 {ECO:0000305};
DE   AltName: Full=Rho-GAP hematopoietic protein C1;
DE   AltName: Full=Rho-type GTPase-activating protein 4;
DE   AltName: Full=p115;
GN   Name=ARHGAP4 {ECO:0000312|HGNC:HGNC:674};
GN   Synonyms=KIAA0131, RGC1, RHOGAP4;
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] (ISOFORM 1).
RC   TISSUE=Embryo;
RX   PubMed=8570618; DOI=10.1073/pnas.93.2.695;
RA   Tribioli C., Droetto S., Bione S., Cesareni G., Torrisi M.R., Lotti L.V.,
RA   Lanfrancone L., Toniolo D., Pelicci P.-G.;
RT   "An X chromosome-linked gene encoding a protein with characteristics of a
RT   rhoGAP predominantly expressed in hematopoietic cells.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:695-699(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA   Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA   Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA   Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA   Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA   Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA   Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA   Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA   Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA   Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA   Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA   Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA   Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA   Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA   Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA   Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA   Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA   Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA   Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA   Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA   Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA   Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA   Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA   Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA   Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA   Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA   Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA   Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA   Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA   Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA   Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA   Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA   d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA   Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA   Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA   Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA   Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA   Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA   Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA   Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton 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] (ISOFORM 2).
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-946 (ISOFORM 1).
RC   TISSUE=Bone marrow;
RX   PubMed=8590280; DOI=10.1093/dnares/2.4.167;
RA   Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.;
RT   "Prediction of the coding sequences of unidentified human genes. IV. The
RT   coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of
RT   cDNA clones from human cell line KG-1.";
RL   DNA Res. 2:167-174(1995).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-103 (ISOFORM 1).
RC   TISSUE=Embryo;
RX   PubMed=7981673; DOI=10.1093/hmg/3.7.1061;
RA   Tribioli C., Mancini M., Plassart E., Bione S., Rivella S., Sala C.,
RA   Torri G., Toniolo D.;
RT   "Isolation of new genes in distal Xq28: transcriptional map and
RT   identification of a human homologue of the ARD1 N-acetyl transferase of
RT   Saccharomyces cerevisiae.";
RL   Hum. Mol. Genet. 3:1061-1068(1994).
RN   [7]
RP   INTERACTION WITH NCKAP1L.
RX   PubMed=16417406; DOI=10.1371/journal.pbio.0040038;
RA   Weiner O.D., Rentel M.C., Ott A., Brown G.E., Jedrychowski M., Yaffe M.B.,
RA   Gygi S.P., Cantley L.C., Bourne H.R., Kirschner M.W.;
RT   "Hem-1 complexes are essential for Rac activation, actin polymerization,
RT   and myosin regulation during neutrophil chemotaxis.";
RL   PLoS Biol. 4:E38-E38(2006).
RN   [8]
RP   IDENTIFICATION BY 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   [9]
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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-860; SER-901 AND SER-906, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=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   [11]
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   [12]
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   [13]
RP   STRUCTURE BY NMR OF 746-814.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of SH3 domain in Rho-GTPase-activating protein 4.";
RL   Submitted (OCT-2007) to the PDB data bank.
CC   -!- FUNCTION: Inhibitory effect on stress fiber organization. May down-
CC       regulate Rho-like GTPase in hematopoietic cells.
CC   -!- SUBUNIT: Interacts with NCKAP1L. {ECO:0000269|PubMed:16417406}.
CC   -!- INTERACTION:
CC       P98171-1; P98171-1: ARHGAP4; NbExp=3; IntAct=EBI-16177615, EBI-16177615;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Just below the plasma membrane.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P98171-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P98171-2; Sequence=VSP_042902;
CC   -!- TISSUE SPECIFICITY: Predominantly in hematopoietic cells (spleen,
CC       thymus and leukocytes); low levels in placenta, lung and various fetal
CC       tissues.
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DR   EMBL; X78817; CAA55394.1; -; mRNA.
DR   EMBL; U52112; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471172; EAW72778.1; -; Genomic_DNA.
DR   EMBL; BC052303; AAH52303.1; -; mRNA.
DR   EMBL; D50921; BAA09480.1; -; mRNA.
DR   CCDS; CCDS14736.1; -. [P98171-1]
DR   CCDS; CCDS55540.1; -. [P98171-2]
DR   PIR; I38100; I38100.
DR   RefSeq; NP_001158213.1; NM_001164741.1. [P98171-2]
DR   RefSeq; NP_001657.3; NM_001666.4. [P98171-1]
DR   PDB; 2EPD; NMR; -; A=746-814.
DR   PDBsum; 2EPD; -.
DR   AlphaFoldDB; P98171; -.
DR   BMRB; P98171; -.
DR   SMR; P98171; -.
DR   BioGRID; 106886; 31.
DR   DIP; DIP-41592N; -.
DR   IntAct; P98171; 9.
DR   MINT; P98171; -.
DR   STRING; 9606.ENSP00000359045; -.
DR   GlyCosmos; P98171; 6 sites, 2 glycans.
DR   GlyGen; P98171; 8 sites, 2 O-linked glycans (8 sites).
DR   iPTMnet; P98171; -.
DR   PhosphoSitePlus; P98171; -.
DR   BioMuta; ARHGAP4; -.
DR   EPD; P98171; -.
DR   jPOST; P98171; -.
DR   MassIVE; P98171; -.
DR   MaxQB; P98171; -.
DR   PaxDb; 9606-ENSP00000359045; -.
DR   PeptideAtlas; P98171; -.
DR   ProteomicsDB; 57804; -. [P98171-1]
DR   ProteomicsDB; 57805; -. [P98171-2]
DR   Pumba; P98171; -.
DR   Antibodypedia; 360; 150 antibodies from 30 providers.
DR   DNASU; 393; -.
DR   Ensembl; ENST00000350060.10; ENSP00000203786.8; ENSG00000089820.17. [P98171-1]
DR   Ensembl; ENST00000370028.7; ENSP00000359045.3; ENSG00000089820.17. [P98171-2]
DR   GeneID; 393; -.
DR   KEGG; hsa:393; -.
DR   MANE-Select; ENST00000350060.10; ENSP00000203786.8; NM_001666.5; NP_001657.3.
DR   UCSC; uc004fjk.3; human. [P98171-1]
DR   AGR; HGNC:674; -.
DR   CTD; 393; -.
DR   DisGeNET; 393; -.
DR   GeneCards; ARHGAP4; -.
DR   HGNC; HGNC:674; ARHGAP4.
DR   HPA; ENSG00000089820; Tissue enhanced (bone marrow, lymphoid tissue).
DR   MIM; 300023; gene.
DR   neXtProt; NX_P98171; -.
DR   OpenTargets; ENSG00000089820; -.
DR   PharmGKB; PA24958; -.
DR   VEuPathDB; HostDB:ENSG00000089820; -.
DR   eggNOG; KOG3565; Eukaryota.
DR   GeneTree; ENSGT00950000182824; -.
DR   HOGENOM; CLU_005715_1_1_1; -.
DR   InParanoid; P98171; -.
DR   OMA; ECAGARG; -.
DR   OrthoDB; 2904755at2759; -.
DR   PhylomeDB; P98171; -.
DR   TreeFam; TF315892; -.
DR   PathwayCommons; P98171; -.
DR   Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR   Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR   Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR   SignaLink; P98171; -.
DR   SIGNOR; P98171; -.
DR   BioGRID-ORCS; 393; 10 hits in 771 CRISPR screens.
DR   ChiTaRS; ARHGAP4; human.
DR   EvolutionaryTrace; P98171; -.
DR   GeneWiki; ARHGAP4; -.
DR   GenomeRNAi; 393; -.
DR   Pharos; P98171; Tbio.
DR   PRO; PR:P98171; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; P98171; Protein.
DR   Bgee; ENSG00000089820; Expressed in granulocyte and 160 other cell types or tissues.
DR   ExpressionAtlas; P98171; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0030426; C:growth cone; IEA:Ensembl.
DR   GO; GO:0005874; C:microtubule; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005096; F:GTPase activator activity; TAS:Reactome.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0007010; P:cytoskeleton organization; TAS:ProtInc.
DR   GO; GO:0030517; P:negative regulation of axon extension; IEA:Ensembl.
DR   GO; GO:0030336; P:negative regulation of cell migration; IBA:GO_Central.
DR   GO; GO:0010764; P:negative regulation of fibroblast migration; IEA:Ensembl.
DR   GO; GO:0007399; P:nervous system development; IEA:Ensembl.
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   CDD; cd07656; F-BAR_srGAP; 1.
DR   CDD; cd11956; SH3_srGAP4; 1.
DR   Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR031160; F_BAR.
DR   InterPro; IPR001060; FCH_dom.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR035678; srGAP4_SH3.
DR   PANTHER; PTHR14166:SF16; RHO GTPASE-ACTIVATING PROTEIN 4; 1.
DR   PANTHER; PTHR14166; SLIT-ROBO RHO GTPASE ACTIVATING PROTEIN; 1.
DR   Pfam; PF00611; FCH; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   Pfam; PF14604; SH3_9; 1.
DR   SMART; SM00055; FCH; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS51741; F_BAR; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
DR   PROSITE; PS50002; SH3; 1.
DR   Genevisible; P98171; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Coiled coil; Cytoplasm;
KW   GTPase activation; Phosphoprotein; Reference proteome; SH3 domain.
FT   CHAIN           1..946
FT                   /note="Rho GTPase-activating protein 4"
FT                   /id="PRO_0000056701"
FT   DOMAIN          19..317
FT                   /note="F-BAR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT   DOMAIN          507..695
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT   DOMAIN          746..805
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          187..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          402..435
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          885..946
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          128..195
FT                   /evidence="ECO:0000255"
FT   MOD_RES         860
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         901
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         906
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         227
FT                   /note="K -> KLWPPQRPVAASSCAPVCWLQAGFLVHPPWWGAMCAPSTHQ (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_042902"
FT   VARIANT         104
FT                   /note="A -> V (in dbSNP:rs5987182)"
FT                   /id="VAR_028413"
FT   CONFLICT        609
FT                   /note="A -> D (in Ref. 1; CAA55394)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        731
FT                   /note="E -> D (in Ref. 1; CAA55394)"
FT                   /evidence="ECO:0000305"
FT   STRAND          749..755
FT                   /evidence="ECO:0007829|PDB:2EPD"
FT   STRAND          772..780
FT                   /evidence="ECO:0007829|PDB:2EPD"
FT   STRAND          783..788
FT                   /evidence="ECO:0007829|PDB:2EPD"
FT   STRAND          791..801
FT                   /evidence="ECO:0007829|PDB:2EPD"
SQ   SEQUENCE   946 AA;  105026 MW;  ED3D48C5DAA24969 CRC64;
     MAAHGKLRRE RGLQAEYETQ VKEMRWQLSE QLRCLELQGE LRRELLQELA EFMRRRAEVE
     LEYSRGLEKL AERFSSRGGR LGSSREHQSF RKEPSLLSPL HCWAVLLQHT RQQSRESAAL
     SEVLAGPLAQ RLSHIAEDVG RLVKKSRDLE QQLQDELLEV VSELQTAKKT YQAYHMESVN
     AEAKLREAER QEEKRAGRSV PTTTAGATEA GPLRKSSLKK GGRLVEKRQA KFMEHKLKCT
     KARNEYLLSL ASVNAAVSNY YLHDVLDLMD CCDTGFHLAL GQVLRSYTAA ESRTQASQVQ
     GLGSLEEAVE ALDPPGDKAK VLEVHATVFC PPLRFDYHPH DGDEVAEICV EMELRDEILP
     RAQNIQSRLD RQTIETEEVN KTLKATLQAL LEVVASDDGD VLDSFQTSPS TESLKSTSSD
     PGSRQAGRRR GQQQETETFY LTKLQEYLSG RSILAKLQAK HEKLQEALQR GDKEEQEVSW
     TQYTQRKFQK SRQPRPSSQY NQRLFGGDME KFIQSSGQPV PLVVESCIRF INLNGLQHEG
     IFRVSGAQLR VSEIRDAFER GEDPLVEGCT AHDLDSVAGV LKLYFRSLEP PLFPPDLFGE
     LLASSELEAT AERVEHVSRL LWRLPAPVLV VLRYLFTFLN HLAQYSDENM MDPYNLAVCF
     GPTLLPVPAG QDPVALQGRV NQLVQTLIVQ PDRVFPPLTS LPGPVYEKCM APPSASCLGD
     AQLESLGADN EPELEAEMPA QEDDLEGVVE AVACFAYTGR TAQELSFRRG DVLRLHERAS
     SDWWRGEHNG MRGLIPHKYI TLPAGTEKQV VGAGLQTAGE SGSSPEGLLA SELVHRPEPC
     TSPEAMGPSG HRRRCLVPAS PEQHVEVDKA VAQNMDSVFK ELLGKTSVRQ GLGPASTTSP
     SPGPRSPKAP PSSRLGRNKG FSRGPGAPAS PSASHPQGLD TTPKPH
//