ID   RHG26_HUMAN             Reviewed;         814 AA.
AC   Q9UNA1; O75117; Q5D035; Q9BYS6; Q9BYS7; Q9UJ00;
DT   11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   24-JAN-2024, entry version 211.
DE   RecName: Full=Rho GTPase-activating protein 26;
DE   AltName: Full=GTPase regulator associated with focal adhesion kinase;
DE            Short=GRAF1 {ECO:0000303|PubMed:32344433};
DE   AltName: Full=Oligophrenin-1-like protein;
DE   AltName: Full=Rho-type GTPase-activating protein 26;
GN   Name=ARHGAP26; Synonyms=GRAF, KIAA0621, OPHN1L;
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=Heart, Liver, and Placenta;
RA   Xia J.H., Tang X.X., Yu K.P., Pan Q., Dai H.P.;
RT   "Molecular cloning of human oligophrenin-1 like (OPHN1L) gene, complete
RT   CDS.";
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2), DISEASE, AND VARIANT JMML
RP   SER-417.
RX   PubMed=10908648; DOI=10.1073/pnas.150079597;
RA   Borkhardt A., Bojesen S., Haas O.A., Fuchs U., Bartelheimer D.,
RA   Loncarevic I.F., Bohle R.M., Harbott J., Repp R., Jaeger U., Viehmann S.,
RA   Henn T., Korth P., Scharr D., Lampert F.;
RT   "The human GRAF gene is fused to MLL in a unique t(5;11)(q31;q23) and both
RT   alleles are disrupted in three cases of myelodysplastic syndrome/acute
RT   myeloid leukemia with a deletion 5q.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:9168-9173(2000).
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] (ISOFORM 2).
RC   TISSUE=Placenta;
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 [GENOMIC DNA] OF 53-785.
RA   Bojesen S.E., Link C., Borkhardt A.;
RT   "Genomic structure of the human GRAF gene.";
RL   Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 62-814 (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA   Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA   Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. X. The
RT   complete sequences of 100 new cDNA clones from brain which can code for
RT   large proteins in vitro.";
RL   DNA Res. 5:169-176(1998).
RN   [7]
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   [8]
RP   FUNCTION, INTERACTION WITH WDR44 AND MICAL1, SUBCELLULAR LOCATION, AND
RP   DOMAIN.
RX   PubMed=32344433; DOI=10.1083/jcb.201811014;
RA   Lucken-Ardjomande Haesler S., Vallis Y., Pasche M., McMahon H.T.;
RT   "GRAF2, WDR44, and MICAL1 mediate Rab8/10/11-dependent export of E-
RT   cadherin, MMP14, and CFTR DeltaF508.";
RL   J. Cell Biol. 219:0-0(2020).
RN   [9]
RP   STRUCTURE BY NMR OF 754-814.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the SH3 domain of human oligophrenin-1-like protein
RT   (KIAA0621).";
RL   Submitted (DEC-2003) to the PDB data bank.
CC   -!- FUNCTION: GTPase-activating protein for RHOA and CDC42.
CC       {ECO:0000250|UniProtKB:Q5ZMW5}.
CC   -!- FUNCTION: [Isoform 2]: Associates with MICAL1 on the endosomal membrane
CC       to promote Rab8-Rab10-dependent tubule extension. After dissociation of
CC       MICAL1, recruits WDR44 which connects the endoplasmic reticulum (ER)
CC       with the endosomal tubule, thereby participating in the export of a
CC       subset of neosynthesized proteins. {ECO:0000269|PubMed:32344433}.
CC   -!- SUBUNIT: [Isoform 2]: Interacts with NYAP1, NYAP2 and MYO16 (By
CC       similarity). Interacts with MICAL1 and WDR44 (PubMed:32344433). Binds
CC       to the C-terminus of PTK2/FAK1 (By similarity).
CC       {ECO:0000250|UniProtKB:Q5ZMW5, ECO:0000250|UniProtKB:Q6ZQ82,
CC       ECO:0000269|PubMed:32344433}.
CC   -!- INTERACTION:
CC       Q9UNA1; O14613: CDC42EP2; NbExp=3; IntAct=EBI-1390913, EBI-3438291;
CC       Q9UNA1; Q6P5Z2: PKN3; NbExp=5; IntAct=EBI-1390913, EBI-1384335;
CC       Q9UNA1-2; O14613: CDC42EP2; NbExp=3; IntAct=EBI-16430964, EBI-3438291;
CC   -!- SUBCELLULAR LOCATION: [Isoform 2]: Endosome membrane
CC       {ECO:0000269|PubMed:32344433}. Note=Colocalized with RAB8A, RAB8B and
CC       RAB10 on endosomal tubules. {ECO:0000269|PubMed:32344433}.
CC   -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000250}.
CC       Cytoplasm, cytoskeleton {ECO:0000250}. Note=Colocalizes with actin
CC       stress fibers and cortical actin structures. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9UNA1-1; Sequence=Displayed;
CC       Name=2; Synonyms=GRAF1b {ECO:0000303|PubMed:32344433};
CC         IsoId=Q9UNA1-2; Sequence=VSP_001659;
CC   -!- DOMAIN: The BAR domain is important to associate RAB8A (or RAB8B) and
CC       RAB10 to endosomal membrane to promote tubule extension. The BAR domain
CC       is also important to recruit WDR44 to endosomal tubules.
CC       {ECO:0000269|PubMed:32344433}.
CC   -!- DISEASE: Leukemia, juvenile myelomonocytic (JMML) [MIM:607785]: An
CC       aggressive pediatric myelodysplastic syndrome/myeloproliferative
CC       disorder characterized by malignant transformation in the hematopoietic
CC       stem cell compartment with proliferation of differentiated progeny.
CC       Patients have splenomegaly, enlarged lymph nodes, rashes, and
CC       hemorrhages. Note=The gene represented in this entry is involved in
CC       disease pathogenesis. A chromosomal translocation t(5;11)(q31;q23) with
CC       KMT2A/MLL1 has been found in leukemic cells from JMML patients, also
CC       carrying inactivating mutations on the second allele (PubMed:10908648).
CC       {ECO:0000269|PubMed:10908648}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="https://atlasgeneticsoncology.org/gene/291/GRAF";
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Graf1 entry;
CC       URL="https://en.wikipedia.org/wiki/Graf1";
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DR   EMBL; AF141884; AAD39482.1; -; mRNA.
DR   EMBL; Y10388; CAA71414.2; -; Genomic_DNA.
DR   EMBL; CH471062; EAW61876.1; -; Genomic_DNA.
DR   EMBL; BC068555; AAH68555.1; -; mRNA.
DR   EMBL; AJ309466; CAC29145.2; -; Genomic_DNA.
DR   EMBL; AJ309467; CAC29145.2; JOINED; Genomic_DNA.
DR   EMBL; AJ309468; CAC29145.2; JOINED; Genomic_DNA.
DR   EMBL; AJ309469; CAC29145.2; JOINED; Genomic_DNA.
DR   EMBL; AJ309470; CAC29145.2; JOINED; Genomic_DNA.
DR   EMBL; AJ309471; CAC29145.2; JOINED; Genomic_DNA.
DR   EMBL; AJ309472; CAC29145.2; JOINED; Genomic_DNA.
DR   EMBL; AJ309473; CAC29145.2; JOINED; Genomic_DNA.
DR   EMBL; AJ309474; CAC29145.2; JOINED; Genomic_DNA.
DR   EMBL; AJ309475; CAC29145.2; JOINED; Genomic_DNA.
DR   EMBL; AJ309476; CAC29145.2; JOINED; Genomic_DNA.
DR   EMBL; AJ309477; CAC29145.2; JOINED; Genomic_DNA.
DR   EMBL; AJ309478; CAC29145.2; JOINED; Genomic_DNA.
DR   EMBL; AJ309479; CAC29145.2; JOINED; Genomic_DNA.
DR   EMBL; AJ309480; CAC29145.2; JOINED; Genomic_DNA.
DR   EMBL; AJ309481; CAC29145.2; JOINED; Genomic_DNA.
DR   EMBL; AJ309482; CAC29145.2; JOINED; Genomic_DNA.
DR   EMBL; AJ309483; CAC29145.2; JOINED; Genomic_DNA.
DR   EMBL; AJ309484; CAC29145.2; JOINED; Genomic_DNA.
DR   EMBL; AJ309485; CAC29145.2; JOINED; Genomic_DNA.
DR   EMBL; AJ309486; CAC29145.2; JOINED; Genomic_DNA.
DR   EMBL; AJ309487; CAC29145.2; JOINED; Genomic_DNA.
DR   EMBL; AJ309466; CAC29146.2; -; Genomic_DNA.
DR   EMBL; AJ309467; CAC29146.2; JOINED; Genomic_DNA.
DR   EMBL; AJ309468; CAC29146.2; JOINED; Genomic_DNA.
DR   EMBL; AJ309469; CAC29146.2; JOINED; Genomic_DNA.
DR   EMBL; AJ309470; CAC29146.2; JOINED; Genomic_DNA.
DR   EMBL; AJ309471; CAC29146.2; JOINED; Genomic_DNA.
DR   EMBL; AJ309472; CAC29146.2; JOINED; Genomic_DNA.
DR   EMBL; AJ309473; CAC29146.2; JOINED; Genomic_DNA.
DR   EMBL; AJ309474; CAC29146.2; JOINED; Genomic_DNA.
DR   EMBL; AJ309475; CAC29146.2; JOINED; Genomic_DNA.
DR   EMBL; AJ309476; CAC29146.2; JOINED; Genomic_DNA.
DR   EMBL; AJ309477; CAC29146.2; JOINED; Genomic_DNA.
DR   EMBL; AJ309478; CAC29146.2; JOINED; Genomic_DNA.
DR   EMBL; AJ309479; CAC29146.2; JOINED; Genomic_DNA.
DR   EMBL; AJ309480; CAC29146.2; JOINED; Genomic_DNA.
DR   EMBL; AJ309481; CAC29146.2; JOINED; Genomic_DNA.
DR   EMBL; AJ309482; CAC29146.2; JOINED; Genomic_DNA.
DR   EMBL; AJ309483; CAC29146.2; JOINED; Genomic_DNA.
DR   EMBL; AJ309484; CAC29146.2; JOINED; Genomic_DNA.
DR   EMBL; AJ309485; CAC29146.2; JOINED; Genomic_DNA.
DR   EMBL; AJ309487; CAC29146.2; JOINED; Genomic_DNA.
DR   EMBL; AB014521; BAA31596.1; -; mRNA.
DR   CCDS; CCDS4277.1; -. [Q9UNA1-1]
DR   CCDS; CCDS47297.1; -. [Q9UNA1-2]
DR   PIR; F59430; F59430.
DR   RefSeq; NP_001129080.1; NM_001135608.1. [Q9UNA1-2]
DR   RefSeq; NP_055886.1; NM_015071.4. [Q9UNA1-1]
DR   PDB; 1UGV; NMR; -; A=756-814.
DR   PDBsum; 1UGV; -.
DR   AlphaFoldDB; Q9UNA1; -.
DR   BMRB; Q9UNA1; -.
DR   SMR; Q9UNA1; -.
DR   BioGRID; 116720; 62.
DR   IntAct; Q9UNA1; 31.
DR   MINT; Q9UNA1; -.
DR   STRING; 9606.ENSP00000274498; -.
DR   iPTMnet; Q9UNA1; -.
DR   PhosphoSitePlus; Q9UNA1; -.
DR   SwissPalm; Q9UNA1; -.
DR   BioMuta; ARHGAP26; -.
DR   DMDM; 21759332; -.
DR   EPD; Q9UNA1; -.
DR   jPOST; Q9UNA1; -.
DR   MassIVE; Q9UNA1; -.
DR   MaxQB; Q9UNA1; -.
DR   PaxDb; 9606-ENSP00000274498; -.
DR   PeptideAtlas; Q9UNA1; -.
DR   ProteomicsDB; 85274; -. [Q9UNA1-1]
DR   ProteomicsDB; 85275; -. [Q9UNA1-2]
DR   Pumba; Q9UNA1; -.
DR   Antibodypedia; 27437; 285 antibodies from 33 providers.
DR   DNASU; 23092; -.
DR   Ensembl; ENST00000274498.9; ENSP00000274498.4; ENSG00000145819.18. [Q9UNA1-1]
DR   Ensembl; ENST00000645722.2; ENSP00000495131.1; ENSG00000145819.18. [Q9UNA1-2]
DR   GeneID; 23092; -.
DR   KEGG; hsa:23092; -.
DR   MANE-Select; ENST00000645722.2; ENSP00000495131.1; NM_001135608.3; NP_001129080.1. [Q9UNA1-2]
DR   UCSC; uc003lmt.4; human. [Q9UNA1-1]
DR   AGR; HGNC:17073; -.
DR   CTD; 23092; -.
DR   DisGeNET; 23092; -.
DR   GeneCards; ARHGAP26; -.
DR   HGNC; HGNC:17073; ARHGAP26.
DR   HPA; ENSG00000145819; Low tissue specificity.
DR   MalaCards; ARHGAP26; -.
DR   MIM; 605370; gene.
DR   MIM; 607785; phenotype.
DR   neXtProt; NX_Q9UNA1; -.
DR   OpenTargets; ENSG00000145819; -.
DR   PharmGKB; PA134946198; -.
DR   VEuPathDB; HostDB:ENSG00000145819; -.
DR   eggNOG; KOG1451; Eukaryota.
DR   GeneTree; ENSGT00940000157254; -.
DR   HOGENOM; CLU_011532_2_0_1; -.
DR   InParanoid; Q9UNA1; -.
DR   OMA; YALITSQ; -.
DR   OrthoDB; 5395569at2759; -.
DR   PhylomeDB; Q9UNA1; -.
DR   TreeFam; TF316851; -.
DR   PathwayCommons; Q9UNA1; -.
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-9013409; RHOJ GTPase cycle.
DR   Reactome; R-HSA-9013423; RAC3 GTPase cycle.
DR   SignaLink; Q9UNA1; -.
DR   SIGNOR; Q9UNA1; -.
DR   BioGRID-ORCS; 23092; 14 hits in 1154 CRISPR screens.
DR   ChiTaRS; ARHGAP26; human.
DR   EvolutionaryTrace; Q9UNA1; -.
DR   GeneWiki; ARHGAP26; -.
DR   GenomeRNAi; 23092; -.
DR   Pharos; Q9UNA1; Tbio.
DR   PRO; PR:Q9UNA1; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; Q9UNA1; Protein.
DR   Bgee; ENSG00000145819; Expressed in sural nerve and 186 other cell types or tissues.
DR   ExpressionAtlas; Q9UNA1; baseline and differential.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR   GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR   GO; GO:0005543; F:phospholipid binding; IDA:FlyBase.
DR   GO; GO:0030036; P:actin cytoskeleton organization; NAS:UniProtKB.
DR   GO; GO:0007399; P:nervous system development; NAS: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   CDD; cd01249; BAR-PH_GRAF_family; 1.
DR   CDD; cd07636; BAR_GRAF; 1.
DR   CDD; cd04374; RhoGAP_Graf; 1.
DR   CDD; cd12064; SH3_GRAF; 1.
DR   Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 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; IPR004148; BAR_dom.
DR   InterPro; IPR035483; GRAF_BAR.
DR   InterPro; IPR047234; GRAF_fam.
DR   InterPro; IPR035481; GRAF_SH3.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR047225; PH_GRAF.
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   PANTHER; PTHR12552; OLIGOPHRENIN 1; 1.
DR   PANTHER; PTHR12552:SF4; RHO GTPASE-ACTIVATING PROTEIN 26; 1.
DR   Pfam; PF16746; BAR_3; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   Pfam; PF14604; SH3_9; 1.
DR   SMART; SM00233; PH; 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; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
DR   PROSITE; PS50002; SH3; 1.
DR   Genevisible; Q9UNA1; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell junction;
KW   Chromosomal rearrangement; Cytoplasm; Cytoskeleton; Disease variant;
KW   Endosome; GTPase activation; Membrane; Proto-oncogene; Reference proteome;
KW   SH3 domain.
FT   CHAIN           1..814
FT                   /note="Rho GTPase-activating protein 26"
FT                   /id="PRO_0000056718"
FT   DOMAIN          7..262
FT                   /note="BAR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT   DOMAIN          265..369
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          383..568
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT   DOMAIN          756..814
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          624..696
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        624..651
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        660..682
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         700..754
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_001659"
FT   VARIANT         417
FT                   /note="N -> S (in JMML; somatic mutation;
FT                   dbSNP:rs121918546)"
FT                   /evidence="ECO:0000269|PubMed:10908648"
FT                   /id="VAR_013623"
FT   CONFLICT        355
FT                   /note="E -> G (in Ref. 2; CAA71414 and 3;
FT                   CAC29145/CAC29146)"
FT                   /evidence="ECO:0000305"
FT   STRAND          761..765
FT                   /evidence="ECO:0007829|PDB:1UGV"
FT   STRAND          771..774
FT                   /evidence="ECO:0007829|PDB:1UGV"
FT   STRAND          782..785
FT                   /evidence="ECO:0007829|PDB:1UGV"
FT   STRAND          794..801
FT                   /evidence="ECO:0007829|PDB:1UGV"
FT   STRAND          803..807
FT                   /evidence="ECO:0007829|PDB:1UGV"
FT   HELIX           808..810
FT                   /evidence="ECO:0007829|PDB:1UGV"
FT   STRAND          811..813
FT                   /evidence="ECO:0007829|PDB:1UGV"
SQ   SEQUENCE   814 AA;  92235 MW;  5C81DBDECB32B18A CRC64;
     MGLPALEFSD CCLDSPHFRE TLKSHEAELD KTNKFIKELI KDGKSLISAL KNLSSAKRKF
     ADSLNEFKFQ CIGDAETDDE MCIARSLQEF ATVLRNLEDE RIRMIENASE VLITPLEKFR
     KEQIGAAKEA KKKYDKETEK YCGILEKHLN LSSKKKESQL QEADSQVDLV RQHFYEVSLE
     YVFKVQEVQE RKMFEFVEPL LAFLQGLFTF YHHGYELAKD FGDFKTQLTI SIQNTRNRFE
     GTRSEVESLM KKMKENPLEH KTISPYTMEG YLYVQEKRHF GTSWVKHYCT YQRDSKQITM
     VPFDQKSGGK GGEDESVILK SCTRRKTDSI EKRFCFDVEA VDRPGVITMQ ALSEEDRRLW
     MEAMDGREPV YNSNKDSQSE GTAQLDSIGF SIIRKCIHAV ETRGINEQGL YRIVGVNSRV
     QKLLSVLMDP KTASETETDI CAEWEIKTIT SALKTYLRML PGPLMMYQFQ RSFIKAAKLE
     NQESRVSEIH SLVHRLPEKN RQMLQLLMNH LANVANNHKQ NLMTVANLGV VFGPTLLRPQ
     EETVAAIMDI KFQNIVIEIL IENHEKIFNT VPDMPLTNAQ LHLSRKKSSD SKPPSCSERP
     LTLFHTVQST EKQEQRNSII NSSLESVSSN PNSILNSSSS LQPNMNSSDP DLAVVKPTRP
     NSLPPNPSPT SPLSPSWPMF SAPSSPMPTS STSSDSSPVR SVAGFVWFSV AAVVLSLARS
     SLHAVFSLLV NFVPCHPNLH LLFDRPEEAV HEDSSTPFRK AKALYACKAE HDSELSFTAG
     TVFDNVHPSQ EPGWLEGTLN GKTGLIPENY VEFL
//