RAB21_HUMAN
ID RAB21_HUMAN Reviewed; 225 AA.
AC Q9UL25; Q14466; Q569H3;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Ras-related protein Rab-21;
DE Flags: Precursor;
GN Name=RAB21 {ECO:0000312|HGNC:HGNC:18263}; Synonyms=KIAA0118;
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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Colon carcinoma;
RX PubMed=10887961; DOI=10.1078/s0171-9335(04)70034-5;
RA Opdam F.J.M., Kamps G., Croes H., van Bokhoven H., Ginsel L.A.,
RA Fransen J.A.M.;
RT "Expression of Rab small GTPases in epithelial Caco-2 cells: Rab21 is an
RT apically located GTP-binding protein in polarised intestinal epithelial
RT cells.";
RL Eur. J. Cell Biol. 79:308-316(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph, and 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 [3]
RP PROTEIN SEQUENCE OF 2-16; 48-59; 91-109 AND 141-157, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (JUN-2005) to UniProtKB.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 65-225.
RC TISSUE=Bone marrow;
RX PubMed=7788527; DOI=10.1093/dnares/2.1.37;
RA Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S.,
RA Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. III. The
RT coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 2:37-43(1995).
RN [5]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF THR-33 AND GLN-78.
RX PubMed=15561770; DOI=10.1242/jcs.01560;
RA Simpson J.C., Griffiths G., Wessling-Resnick M., Fransen J.A.M.,
RA Bennett H., Jones A.T.;
RT "A role for the small GTPase Rab21 in the early endocytic pathway.";
RL J. Cell Sci. 117:6297-6311(2004).
RN [6]
RP INTERACTION WITH ANKRD27, AND SUBCELLULAR LOCATION.
RX PubMed=16525121; DOI=10.1242/jcs.02810;
RA Zhang X., He X., Fu X.-Y., Chang Z.;
RT "Varp is a Rab21 guanine nucleotide exchange factor and regulates endosome
RT dynamics.";
RL J. Cell Sci. 119:1053-1062(2006).
RN [7]
RP INTERACTION WITH ANKRD27.
RX PubMed=18477474; DOI=10.1016/j.bbrc.2008.05.017;
RA Wang F., Zhang H., Zhang X., Wang Y., Ren F., Zhang X., Zhai Y., Chang Z.;
RT "Varp interacts with Rab38 and functions as its potential effector.";
RL Biochem. Biophys. Res. Commun. 372:162-167(2008).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18804435; DOI=10.1016/j.devcel.2008.08.001;
RA Pellinen T., Tuomi S., Arjonen A., Wolf M., Edgren H., Meyer H., Grosse R.,
RA Kitzing T., Rantala J.K., Kallioniemi O., Faessler R., Kallio M.,
RA Ivaska J.;
RT "Integrin trafficking regulated by Rab21 is necessary for cytokinesis.";
RL Dev. Cell 15:371-385(2008).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [10]
RP SUBCELLULAR LOCATION.
RX PubMed=19745841; DOI=10.1038/embor.2009.186;
RA Burgo A., Sotirakis E., Simmler M.C., Verraes A., Chamot C., Simpson J.C.,
RA Lanzetti L., Proux-Gillardeaux V., Galli T.;
RT "Role of Varp, a Rab21 exchange factor and TI-VAMP/VAMP7 partner, in
RT neurite growth.";
RL EMBO Rep. 10:1117-1124(2009).
RN [11]
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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [13]
RP FUNCTION, INTERACTION WITH VAMP7 AND VAMP8, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF THR-33 AND GLN-78.
RX PubMed=25648148; DOI=10.15252/embr.201439464;
RA Jean S., Cox S., Nassari S., Kiger A.A.;
RT "Starvation-induced MTMR13 and RAB21 activity regulates VAMP8 to promote
RT autophagosome-lysosome fusion.";
RL EMBO Rep. 16:297-311(2015).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [15]
RP FUNCTION, INTERACTION WITH TMED10, AND MUTAGENESIS OF THR-33 AND GLN-78.
RX PubMed=31455601; DOI=10.1242/bio.045336;
RA Del Olmo T., Lacarriere-Keita C., Normandin C., Jean D., Boisvert F.M.,
RA Jean S.;
RT "RAB21 interacts with TMED10 and modulates its localization and
RT abundance.";
RL Biol. Open 8:0-0(2019).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 16-183 IN COMPLEX WITH GTP ANALOG
RP AND GDP.
RX PubMed=16034420; DOI=10.1038/nature03798;
RA Eathiraj S., Pan X., Ritacco C., Lambright D.G.;
RT "Structural basis of family-wide Rab GTPase recognition by rabenosyn-5.";
RL Nature 436:415-419(2005).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 16-183 IN COMPLEX WITH RABGEF1.
RX PubMed=17450153; DOI=10.1038/nsmb1232;
RA Delprato A., Lambright D.G.;
RT "Structural basis for Rab GTPase activation by VPS9 domain exchange
RT factors.";
RL Nat. Struct. Mol. Biol. 14:406-412(2007).
CC -!- FUNCTION: Small GTPase involved in membrane trafficking control
CC (PubMed:18804435, PubMed:25648148). During the mitosis of adherent
CC cells, controls the endosomal trafficking of integrins which is
CC required for the successful completion of cytokinesis
CC (PubMed:18804435). Regulates integrin internalization and recycling,
CC but does not influence the traffic of endosomally translocated
CC receptors in general (By similarity). As a result, may regulate cell
CC adhesion and migration (By similarity). Involved in neurite growth (By
CC similarity). Following SBF2/MTMT13-mediated activation in response to
CC starvation-induced autophagy, binds to and regulates SNARE protein
CC VAMP8 endolysosomal transport required for SNARE-mediated
CC autophagosome-lysosome fusion (PubMed:25648148). Modulates protein
CC levels of the cargo receptors TMED2 and TMED10, and required for
CC appropriate Golgi localization of TMED10 (PubMed:31455601).
CC {ECO:0000250|UniProtKB:P35282, ECO:0000250|UniProtKB:Q6AXT5,
CC ECO:0000269|PubMed:18804435, ECO:0000269|PubMed:25648148,
CC ECO:0000269|PubMed:31455601}.
CC -!- SUBUNIT: Interacts with the cytoplasmic tail of integrins ITGA1, ITGA2,
CC ITGA5, ITGA6, ITGA11 and ITGB1 (By similarity). Interacts with RABGEF1
CC (via VPS9 domain) (PubMed:17450153). Interacts with ANKRD27
CC (PubMed:16525121, PubMed:18477474). Interacts with VAMP7
CC (PubMed:25648148). Interacts (in GTP-bound form) with VAMP8 in response
CC to starvation; the interaction probably regulates VAMP8 endolysosomal
CC trafficking (PubMed:25648148). Interacts (active GTP-bound form) with
CC TMED10; the interaction is indirect and regulates TMED10 abundance and
CC localization at the Golgi (PubMed:31455601).
CC {ECO:0000250|UniProtKB:P35282, ECO:0000269|PubMed:16525121,
CC ECO:0000269|PubMed:17450153, ECO:0000269|PubMed:18477474,
CC ECO:0000269|PubMed:25648148, ECO:0000269|PubMed:31455601}.
CC -!- INTERACTION:
CC Q9UL25; Q9UKG1: APPL1; NbExp=10; IntAct=EBI-1056039, EBI-741243;
CC Q9UL25; Q9UJ41-2: RABGEF1; NbExp=2; IntAct=EBI-1056039, EBI-6448458;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:10887961}; Lipid-anchor {ECO:0000305}. Golgi
CC apparatus, trans-Golgi network {ECO:0000269|PubMed:19745841}. Golgi
CC apparatus membrane {ECO:0000305}. Early endosome membrane
CC {ECO:0000269|PubMed:16525121, ECO:0000269|PubMed:25648148}. Cytoplasmic
CC vesicle membrane {ECO:0000269|PubMed:10887961}. Cleavage furrow
CC {ECO:0000269|PubMed:18804435}. Cell projection, neuron projection
CC {ECO:0000250|UniProtKB:P35282}. Note=Colocalizes with ANKRD27 and VAMP7
CC in neurites (By similarity). In nonpolarized epithelial Caco-2 cells,
CC found in the endoplasmic reticulum; in polarized cells, observed in
CC vesicles in the apical cytoplasm (PubMed:10887961). During mitosis, in
CC mid-telophase, localized in the ingressing cleavage furrow
CC (PubMed:18804435). In late telophase, detected at the opposite poles of
CC the daughter cells, in vesicles at the base of lamellipodia formed by
CC the separating daughter cells (PubMed:18804435).
CC {ECO:0000250|UniProtKB:P35282, ECO:0000269|PubMed:10887961,
CC ECO:0000269|PubMed:18804435}.
CC -!- TISSUE SPECIFICITY: Widely expressed. In jejunal tissue, predominantly
CC expressed in the apical region of the epithelial cell layer of the
CC villi, weak expression, if any, in the crypt epithelium. Capillary
CC endothelium and some cell types in the lamina propria also show
CC expression. {ECO:0000269|PubMed:10887961}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AF091035; AAF00048.1; -; mRNA.
DR EMBL; BC021901; AAH21901.1; -; mRNA.
DR EMBL; BC092475; AAH92475.1; -; mRNA.
DR EMBL; D42087; BAA07682.1; -; mRNA.
DR CCDS; CCDS9003.1; -.
DR RefSeq; NP_055814.1; NM_014999.3.
DR PDB; 1YZT; X-ray; 2.05 A; A/B=16-183.
DR PDB; 1YZU; X-ray; 2.50 A; A/B=16-183.
DR PDB; 1Z08; X-ray; 1.80 A; A/B/C/D=16-183.
DR PDB; 1Z0I; X-ray; 2.33 A; A=16-183.
DR PDB; 2OT3; X-ray; 2.10 A; B=16-183.
DR PDBsum; 1YZT; -.
DR PDBsum; 1YZU; -.
DR PDBsum; 1Z08; -.
DR PDBsum; 1Z0I; -.
DR PDBsum; 2OT3; -.
DR AlphaFoldDB; Q9UL25; -.
DR SMR; Q9UL25; -.
DR BioGRID; 116653; 98.
DR DIP; DIP-29349N; -.
DR IntAct; Q9UL25; 30.
DR MINT; Q9UL25; -.
DR STRING; 9606.ENSP00000261263; -.
DR CarbonylDB; Q9UL25; -.
DR GlyGen; Q9UL25; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UL25; -.
DR PhosphoSitePlus; Q9UL25; -.
DR SwissPalm; Q9UL25; -.
DR BioMuta; RAB21; -.
DR DMDM; 13633613; -.
DR EPD; Q9UL25; -.
DR jPOST; Q9UL25; -.
DR MassIVE; Q9UL25; -.
DR MaxQB; Q9UL25; -.
DR PaxDb; Q9UL25; -.
DR PeptideAtlas; Q9UL25; -.
DR PRIDE; Q9UL25; -.
DR ProteomicsDB; 84934; -.
DR Antibodypedia; 1484; 426 antibodies from 30 providers.
DR DNASU; 23011; -.
DR Ensembl; ENST00000261263.5; ENSP00000261263.3; ENSG00000080371.6.
DR GeneID; 23011; -.
DR KEGG; hsa:23011; -.
DR MANE-Select; ENST00000261263.5; ENSP00000261263.3; NM_014999.4; NP_055814.1.
DR UCSC; uc001swt.4; human.
DR CTD; 23011; -.
DR DisGeNET; 23011; -.
DR GeneCards; RAB21; -.
DR HGNC; HGNC:18263; RAB21.
DR HPA; ENSG00000080371; Low tissue specificity.
DR MIM; 612398; gene.
DR neXtProt; NX_Q9UL25; -.
DR OpenTargets; ENSG00000080371; -.
DR PharmGKB; PA34111; -.
DR VEuPathDB; HostDB:ENSG00000080371; -.
DR eggNOG; KOG0088; Eukaryota.
DR GeneTree; ENSGT00940000156786; -.
DR HOGENOM; CLU_041217_10_2_1; -.
DR InParanoid; Q9UL25; -.
DR OMA; DICLCIA; -.
DR OrthoDB; 1226895at2759; -.
DR PhylomeDB; Q9UL25; -.
DR TreeFam; TF300199; -.
DR BRENDA; 3.6.5.2; 2681.
DR PathwayCommons; Q9UL25; -.
DR Reactome; R-HSA-8873719; RAB geranylgeranylation.
DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR SignaLink; Q9UL25; -.
DR SIGNOR; Q9UL25; -.
DR BioGRID-ORCS; 23011; 32 hits in 1087 CRISPR screens.
DR ChiTaRS; RAB21; human.
DR EvolutionaryTrace; Q9UL25; -.
DR GeneWiki; RAB21; -.
DR GenomeRNAi; 23011; -.
DR Pharos; Q9UL25; Tbio.
DR PRO; PR:Q9UL25; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9UL25; protein.
DR Bgee; ENSG00000080371; Expressed in skeletal muscle tissue of rectus abdominis and 213 other tissues.
DR ExpressionAtlas; Q9UL25; baseline and differential.
DR Genevisible; Q9UL25; HS.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0098559; C:cytoplasmic side of early endosome membrane; IDA:UniProtKB.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0031901; C:early endosome membrane; TAS:Reactome.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IDA:LIFEdb.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0032580; C:Golgi cisterna membrane; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0012506; C:vesicle membrane; IDA:UniProtKB.
DR GO; GO:0019003; F:GDP binding; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0008089; P:anterograde axonal transport; IDA:SynGO.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; IEA:Ensembl.
DR GO; GO:2000643; P:positive regulation of early endosome to late endosome transport; IMP:UniProtKB.
DR GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; IMP:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
DR GO; GO:0032482; P:Rab protein signal transduction; IEA:InterPro.
DR GO; GO:0030516; P:regulation of axon extension; IEA:Ensembl.
DR GO; GO:0017157; P:regulation of exocytosis; IDA:UniProtKB.
DR CDD; cd04123; Rab21; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR041833; Rab21.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR020849; Small_GTPase_Ras-type.
DR PANTHER; PTHR24070; PTHR24070; 1.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51419; RAB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell projection; Cytoplasmic vesicle;
KW Direct protein sequencing; Endoplasmic reticulum; Endosome;
KW Golgi apparatus; GTP-binding; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Protein transport; Reference proteome;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
FT CHAIN 2..222
FT /note="Ras-related protein Rab-21"
FT /id="PRO_0000121205"
FT PROPEP 223..225
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000370768"
FT REGION 188..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 48..56
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT COMPBIAS 210..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 26..34
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 74..78
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 132..135
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 162..164
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
FT MOD_RES 222
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 221
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 222
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT MUTAGEN 33
FT /note="T->N: Defects in GTP-binding. Abolishes the
FT interaction with VAMP8 in response to starvation. Abolishes
FT the interaction with TMED10."
FT /evidence="ECO:0000269|PubMed:15561770,
FT ECO:0000269|PubMed:25648148, ECO:0000269|PubMed:31455601"
FT MUTAGEN 78
FT /note="Q->L: Defects in GTP hydrolysis. Does not affect the
FT interaction with VAMP8 in response to starvation. Does not
FT affect the interaction with TMED10."
FT /evidence="ECO:0000269|PubMed:15561770,
FT ECO:0000269|PubMed:31455601"
FT STRAND 18..25
FT /evidence="ECO:0007829|PDB:1Z08"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:2OT3"
FT HELIX 32..41
FT /evidence="ECO:0007829|PDB:1Z08"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:1Z0I"
FT STRAND 55..65
FT /evidence="ECO:0007829|PDB:1Z08"
FT STRAND 67..74
FT /evidence="ECO:0007829|PDB:1Z08"
FT HELIX 79..83
FT /evidence="ECO:0007829|PDB:1Z08"
FT HELIX 85..89
FT /evidence="ECO:0007829|PDB:2OT3"
FT STRAND 93..100
FT /evidence="ECO:0007829|PDB:1Z08"
FT HELIX 104..121
FT /evidence="ECO:0007829|PDB:1Z08"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:1Z08"
FT STRAND 125..132
FT /evidence="ECO:0007829|PDB:1Z08"
FT HELIX 134..139
FT /evidence="ECO:0007829|PDB:1Z08"
FT HELIX 144..153
FT /evidence="ECO:0007829|PDB:1Z08"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:1Z08"
FT TURN 163..166
FT /evidence="ECO:0007829|PDB:1Z08"
FT HELIX 169..181
FT /evidence="ECO:0007829|PDB:1Z08"
SQ SEQUENCE 225 AA; 24348 MW; 73CA2C127F0CBFD6 CRC64;
MAAAGGGGGG AAAAGRAYSF KVVLLGEGCV GKTSLVLRYC ENKFNDKHIT TLQASFLTKK
LNIGGKRVNL AIWDTAGQER FHALGPIYYR DSNGAILVYD ITDEDSFQKV KNWVKELRKM
LGNEICLCIV GNKIDLEKER HVSIQEAESY AESVGAKHYH TSAKQNKGIE ELFLDLCKRM
IETAQVDERA KGNGSSQPGT ARRGVQIIDD EPQAQTSGGG CCSSG
