CRAG_DROME
ID CRAG_DROME Reviewed; 1671 AA.
AC Q9W3D3; O96957; Q8T3K8; Q9W3D2;
DT 12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 3.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=DENN domain-containing protein Crag {ECO:0000303|PubMed:18331716};
DE AltName: Full=Calmodulin-binding protein related to a Rab3 GDP/GTP exchange protein {ECO:0000312|FlyBase:FBgn0025864};
GN Name=Crag {ECO:0000303|PubMed:18331716, ECO:0000312|FlyBase:FBgn0025864};
GN ORFNames=CG12737 {ECO:0000312|FlyBase:FBgn0025864};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|EMBL:CAA76938.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Retina {ECO:0000312|EMBL:CAA76938.1};
RX PubMed=9813038; DOI=10.1074/jbc.273.47.31297;
RA Xu X.-Z.S., Wes P.D., Chen H., Li H.-S., Yu M., Morgan S., Liu Y.,
RA Montell C.;
RT "Retinal targets for calmodulin include proteins implicated in synaptic
RT transmission.";
RL J. Biol. Chem. 273:31297-31307(1998).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4] {ECO:0000312|EMBL:ABV82388.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC STRAIN=Berkeley {ECO:0000312|EMBL:ABV82388.1};
RA Stapleton M., Carlson J., Frise E., Kapadia B., Park S., Wan K., Yu C.,
RA Celniker S.;
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000312|EMBL:AAM11315.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 386-1644 (ISOFORM B).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAM11315.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAM11315.1};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6] {ECO:0000305}
RP FUNCTION, INTERACTION WITH CAM, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP AND MUTAGENESIS OF 161-GLN--PRO-1671; 367-GLN--PRO-1671 AND
RP 659-ARG--PRO-1671.
RX PubMed=18331716; DOI=10.1016/j.devcel.2007.12.012;
RA Denef N., Chen Y., Weeks S.D., Barcelo G., Schuepbach T.;
RT "Crag regulates epithelial architecture and polarized deposition of
RT basement membrane proteins in Drosophila.";
RL Dev. Cell 14:354-364(2008).
RN [7] {ECO:0000305}
RP FUNCTION, INTERACTION WITH RAB11, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP 798-ARG--PRO-1671 AND CYS-1372.
RX PubMed=23226104; DOI=10.1371/journal.pbio.1001438;
RA Xiong B., Bayat V., Jaiswal M., Zhang K., Sandoval H., Charng W.L., Li T.,
RA David G., Duraine L., Lin Y.Q., Neely G.G., Yamamoto S., Bellen H.J.;
RT "Crag is a GEF for Rab11 required for rhodopsin trafficking and maintenance
RT of adult photoreceptor cells.";
RL PLoS Biol. 10:E1001438-E1001438(2012).
RN [8] {ECO:0000305}
RP FUNCTION, INTERACTION WITH RAB10, AND SUBCELLULAR LOCATION.
RX PubMed=23369713; DOI=10.1016/j.devcel.2012.12.005;
RA Lerner D.W., McCoy D., Isabella A.J., Mahowald A.P., Gerlach G.F.,
RA Chaudhry T.A., Horne-Badovinac S.;
RT "A Rab10-dependent mechanism for polarized basement membrane secretion
RT during organ morphogenesis.";
RL Dev. Cell 24:159-168(2013).
RN [9] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF 367-GLN--PRO-1671.
RX PubMed=24828534; DOI=10.1073/pnas.1407351111;
RA Devergne O., Tsung K., Barcelo G., Schuepbach T.;
RT "Polarized deposition of basement membrane proteins depends on
RT Phosphatidylinositol synthase and the levels of Phosphatidylinositol 4,5-
RT bisphosphate.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:7689-7694(2014).
RN [10] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF 367-GLN--PRO-1671.
RX PubMed=28228250; DOI=10.1016/j.celrep.2017.02.002;
RA Devergne O., Sun G.H., Schuepbach T.;
RT "Stratum, a Homolog of the Human GEF Mss4, Partnered with Rab8, Controls
RT the Basal Restriction of Basement Membrane Proteins in Epithelial Cells.";
RL Cell Rep. 18:1831-1839(2017).
CC -!- FUNCTION: Calmodulin-binding protein that acts as a guanine exchange
CC factor for Rab10 and Rab11 (PubMed:9813038, PubMed:23369713,
CC PubMed:23226104). Essential for maintenance of adult photoreceptor
CC cells (PubMed:23226104). Upon light stimulation, required for
CC trafficking of newly synthesized ninaE (Rh1) from the trans-Golgi
CC network to rhabdomere membranes via Rab11-dependent vesicular transport
CC (PubMed:23226104). During egg development, essential for establishing
CC and maintaining epithelial cell polarity by regulating the correct
CC polarized deposition of basal membrane (BM) proteins in follicular
CC epithelial (FE) cells (PubMed:18331716, PubMed:23369713,
CC PubMed:24828534). Functions by targeting Rab10 to the basal cytoplasm,
CC where it restricts the secretion of BM proteins such as trol/Pcan and
CC vkg/Coll IV to the basal surface (PubMed:18331716, PubMed:23369713,
CC PubMed:24828534). Appears to be involved in regulating the levels and
CC distribution of the guanine nucleotide exchange factor strat, however
CC the two proteins appear to have independent roles in regulating
CC polarized BM protein secretion in the FE (PubMed:28228250).
CC {ECO:0000269|PubMed:18331716, ECO:0000269|PubMed:23226104,
CC ECO:0000269|PubMed:23369713, ECO:0000269|PubMed:24828534,
CC ECO:0000269|PubMed:28228250, ECO:0000269|PubMed:9813038}.
CC -!- SUBUNIT: Interacts with Cam (PubMed:18331716, PubMed:9813038).
CC Interacts with Rab10 (PubMed:23369713). Interacts (via the DENN
CC domains) with Rab11 (PubMed:23226104). {ECO:0000269|PubMed:18331716,
CC ECO:0000269|PubMed:23226104, ECO:0000269|PubMed:23369713,
CC ECO:0000269|PubMed:9813038}.
CC -!- INTERACTION:
CC Q9W3D3; O18335: Rab11; NbExp=2; IntAct=EBI-868608, EBI-148897;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:18331716, ECO:0000269|PubMed:23369713}. Early
CC endosome {ECO:0000269|PubMed:18331716}. Recycling endosome
CC {ECO:0000269|PubMed:18331716}. Cytoplasmic granule
CC {ECO:0000269|PubMed:23226104}. Note=In follicle cells (FC), accumulates
CC at the plasma membrane and in both early and recycling endosomes. In
CC FCs, detected at the lateral and apical cell cortex during early stages
CC of oogenesis. At later stages, mostly expressed at the lateral cortex
CC but some expression is still detected at the apical surface
CC (PubMed:18331716). Colocalizes with Rab10 near the FC basal surface
CC (PubMed:23369713). In photoreceptor cells, colocalizes with Rab11 in
CC punctate structures (PubMed:23226104). {ECO:0000269|PubMed:18331716,
CC ECO:0000269|PubMed:23226104, ECO:0000269|PubMed:23369713}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A {ECO:0000303|PubMed:18331716, ECO:0000312|FlyBase:FBgn0025864};
CC Synonyms=D {ECO:0000312|FlyBase:FBgn0025864};
CC IsoId=Q9W3D3-1; Sequence=Displayed;
CC Name=B {ECO:0000303|PubMed:18331716, ECO:0000312|FlyBase:FBgn0025864};
CC IsoId=Q9W3D3-2; Sequence=VSP_059814, VSP_059815;
CC -!- TISSUE SPECIFICITY: Expressed in the adult head and body.
CC {ECO:0000269|PubMed:9813038}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the follicle epithelial cells
CC throughout their development (PubMed:18331716). Not detected until the
CC adult stage (PubMed:9813038). {ECO:0000269|PubMed:18331716,
CC ECO:0000269|PubMed:9813038}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA76938.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Y17918; CAA76938.1; ALT_FRAME; mRNA.
DR EMBL; AE014298; AAF46397.3; -; Genomic_DNA.
DR EMBL; AE014298; AAF46398.3; -; Genomic_DNA.
DR EMBL; AE014298; ACZ95245.2; -; Genomic_DNA.
DR EMBL; BT031006; ABV82388.1; -; mRNA.
DR EMBL; AY094962; AAM11315.1; -; mRNA.
DR PIR; T13717; T13717.
DR RefSeq; NP_001162710.2; NM_001169239.2. [Q9W3D3-1]
DR RefSeq; NP_525080.3; NM_080341.4. [Q9W3D3-1]
DR RefSeq; NP_727281.2; NM_167164.4.
DR AlphaFoldDB; Q9W3D3; -.
DR SMR; Q9W3D3; -.
DR DIP; DIP-59994N; -.
DR IntAct; Q9W3D3; 2.
DR STRING; 7227.FBpp0071165; -.
DR PaxDb; Q9W3D3; -.
DR PRIDE; Q9W3D3; -.
DR DNASU; 31800; -.
DR EnsemblMetazoa; FBtr0071219; FBpp0071165; FBgn0025864. [Q9W3D3-1]
DR EnsemblMetazoa; FBtr0071220; FBpp0089320; FBgn0025864.
DR EnsemblMetazoa; FBtr0343356; FBpp0310013; FBgn0025864. [Q9W3D3-1]
DR GeneID; 31800; -.
DR KEGG; dme:Dmel_CG12737; -.
DR UCSC; CG12737-RA; d. melanogaster. [Q9W3D3-1]
DR UCSC; CG12737-RB; d. melanogaster.
DR CTD; 31800; -.
DR FlyBase; FBgn0025864; Crag.
DR VEuPathDB; VectorBase:FBgn0025864; -.
DR eggNOG; KOG2127; Eukaryota.
DR GeneTree; ENSGT00940000168597; -.
DR HOGENOM; CLU_003074_0_0_1; -.
DR InParanoid; Q9W3D3; -.
DR OrthoDB; 75304at2759; -.
DR PhylomeDB; Q9W3D3; -.
DR Reactome; R-DME-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR BioGRID-ORCS; 31800; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Crag; fly.
DR GenomeRNAi; 31800; -.
DR PRO; PR:Q9W3D3; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0025864; Expressed in cleaving embryo and 27 other tissues.
DR ExpressionAtlas; Q9W3D3; baseline and differential.
DR GO; GO:0045179; C:apical cortex; IDA:FlyBase.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:FlyBase.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0097575; C:lateral cell cortex; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0055037; C:recycling endosome; IDA:FlyBase.
DR GO; GO:0005516; F:calmodulin binding; IDA:FlyBase.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:FlyBase.
DR GO; GO:0031267; F:small GTPase binding; IPI:FlyBase.
DR GO; GO:0090630; P:activation of GTPase activity; IDA:FlyBase.
DR GO; GO:0045175; P:basal protein localization; IMP:FlyBase.
DR GO; GO:0070831; P:basement membrane assembly; IMP:FlyBase.
DR GO; GO:0061864; P:basement membrane constituent secretion; IMP:FlyBase.
DR GO; GO:0110010; P:basolateral protein secretion; IMP:FlyBase.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; HMP:FlyBase.
DR GO; GO:0042998; P:positive regulation of Golgi to plasma membrane protein transport; IMP:FlyBase.
DR GO; GO:0045089; P:positive regulation of innate immune response; HMP:FlyBase.
DR GO; GO:0110011; P:regulation of basement membrane organization; IMP:FlyBase.
DR GO; GO:0032483; P:regulation of Rab protein signal transduction; IDA:FlyBase.
DR Gene3D; 3.40.50.11500; -; 1.
DR InterPro; IPR001194; cDENN_dom.
DR InterPro; IPR005112; dDENN_dom.
DR InterPro; IPR043153; DENN_C.
DR InterPro; IPR023341; MABP.
DR InterPro; IPR037516; Tripartite_DENN.
DR InterPro; IPR005113; uDENN_dom.
DR Pfam; PF03455; dDENN; 1.
DR Pfam; PF02141; DENN; 1.
DR Pfam; PF03456; uDENN; 1.
DR SMART; SM00801; dDENN; 1.
DR SMART; SM00799; DENN; 1.
DR SMART; SM00800; uDENN; 1.
DR PROSITE; PS50211; DENN; 1.
DR PROSITE; PS51498; MABP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calmodulin-binding; Cytoplasm; Endosome;
KW Guanine-nucleotide releasing factor; Reference proteome.
FT CHAIN 1..1671
FT /note="DENN domain-containing protein Crag"
FT /id="PRO_0000445077"
FT DOMAIN 39..195
FT /note="MABP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00831"
FT DOMAIN 187..364
FT /note="uDENN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT DOMAIN 385..521
FT /note="cDENN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT DOMAIN 523..632
FT /note="dDENN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT REGION 997..1160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1245..1311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1415..1435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1046..1061
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1070..1125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1137..1160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1256..1276
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1277..1309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1180..1206
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000305"
FT /id="VSP_059814"
FT VAR_SEQ 1431..1435
FT /note="IANGN -> TANGT (in isoform B)"
FT /id="VSP_059815"
FT MUTAGEN 161..1671
FT /note="Missing: In GG43; larvae lethal."
FT /evidence="ECO:0000269|PubMed:18331716"
FT MUTAGEN 367..1671
FT /note="Missing: In CJ101; larvae lethal. In egg chambers,
FT follicle cells (FC) display abnormal localization of
FT various apical, junctional and basolateral proteins, and
FT loss of epithelial integrity. In follicle epithelium (FE)
FT cells, the basal membrane proteins, trol, Lam and vkg
FT display abnormal localization; accumulating on the apical
FT side of the cell in addition to the normal basal
FT accumulation. Expression of strat in the FE is reduced. In
FT egg chambers, trol also shows abnormal apical localization
FT at the posterior pole. Many FCs appear irregularly shaped
FT at the poles, form multiple layers and are often found in
FT the germline cluster. FCs on the lateral side however,
FT appear normal."
FT /evidence="ECO:0000269|PubMed:18331716,
FT ECO:0000269|PubMed:24828534, ECO:0000269|PubMed:28228250"
FT MUTAGEN 659..1671
FT /note="Missing: In CZ085; larvae lethal."
FT /evidence="ECO:0000269|PubMed:18331716"
FT MUTAGEN 798..1671
FT /note="Missing: Larvae lethal at the L2 stage. In
FT photoreceptor cells, light-induced accumulation of newly
FT synthesized ninaE (Rh1) post-Golgi vesicles leads to a
FT reduction in membrane stack volume, and eventually,
FT photoreceptor cell degeneration. Disruption of
FT photoreceptor cell function is light- and age-dependent."
FT /evidence="ECO:0000269|PubMed:23226104"
FT MUTAGEN 1372
FT /note="C->S: Larvae lethal at the L2 stage. Adult flies
FT display subtle defects in ommatidial organization."
FT /evidence="ECO:0000269|PubMed:23226104"
FT CONFLICT 1347..1349
FT /note="LTS -> VTG (in Ref. 1; CAA76938)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1671 AA; 187010 MW; 1C06079C01DCB55B CRC64;
MEEKRIADYF VVAGMPENPQ LLQENSFNDS GRLRAATTIE PITDIGVYFP LLGEEVPEGY
EILSHTPTGL QANLNHGSVR TTDCYIYFRR GKDRPPLVDI GVLYDGHERI MSDAEIVAET
PGGRVANVNN SSAKTFLTYR RARADMPCNE LVVTELCVIV QSKGERAPHA FCLIYKTLNK
GYVGSDVYLC YKKSMYRPKH ISYKPEILLR YPTFDHTDFP LNLCPSVPLF CLPMGASLEA
WPHVNGTEKR KPISPVFSTF VLTVSDGTYK VYGSALTFYE DYDESKLSAE QKELLGWDEE
FGAQHSLHMI KAICLLSHHP FGDTFDKWLK YLHRMVLYDV NIPIPVERYI TQLLDEVPFP
APSIHLQLSS ESNDRILLTQ PEDSPLPRSG AGFHILLQNL GTDNCLHVLL LALTEQKILI
HSLRPATLTA VAEAIVSLLF PFKWQCPYIP LCPLGLAEVL HAPLPYLIGV DSRFFDLYEP
PTDVTCIDLD TNNISLCESQ RHLSPKLLPK RAARLLRQTL TELENAKPIS YDSTNSLDRD
IRKRKRELVL EQRIQEAFLL FMASILRGYR DFLVPISKAP SVGATDPSAL FQLKAFLRSR
DKSHQKFFEL MMKTQMFIRF IEERSFVSDG DHGLSFFDEC AEKVGNYDET PAQLHLVDWD
TGQNSERTKY IFPPDSVTPA GSQPGGGGGG LAYNYENFTL QPELLQSTKK TALSKFLQLQ
LNASLSPGSP IARRTKHEIK LSQKMASRCQ QHPEAWSKYL LATCYSLYFL ILPSMVLDPR
HAGKEPEILR AAYDVLVRAS RLKITCDEFC YRIMMQLCGI HNLPVLAVRL HYLMKRSGVQ
ANALTYGFYN RCVLESQWPQ DSTTISQIRW NRIKNVVLGA AQFRKAGKQR AASKVNKSLS
ASQDQNLSTL ETVDGQSRTS LASSSGDGGG HGLLDFAAFD RLRNKLGSIV RQTVTGGNNE
TMGDAVNNTG LLIPGELSAP NTPTYGGDTE ILAKALQQQQ PRKQIMSIGG GDDDDEDEDE
DEYTAGSPST PQKQLEAGAD DLEYAGGGDY EADEEDEDEV DEHVAAQRAR QRVQSPTKIS
PRTPVTQNDP LGALNEEESA ASATPTQETQ QEQQHSQSQI DSSIYSDKPI LFRGQRSATF
DESTQIGKSM HRSETMPVAS SGVTNSLANI GSSLKFTFGR YSPARLSLKK DLKLPANIIE
NISSISPSLT GKKSNELIQG SLSSIKSAAN SLTKKFDEIK GVISANSTPT KTNNGHHPHG
LHHGHHHPHH HHHHHSQHGN AEQEEHDAAV HEEGKLRRVS SDLDPWGRLS ESRKSSYNNL
VPLGENSSTG ALHMHAFPAV PDNLYSLTSE NAADRDCDVL IQLTTCSQCH NCSVLVYDEE
IMSGWTAEDS NLNTTCHACN KLTVPFLSVQ IERQVEESEQ SDPLQDGKEQ IANGNSHKTS
LTVPYLNPLV LRKELENILT QEGDIALIKP EFVDEHPIIY WNLLWLMERI ESKTHLPELC
LPVPSDKEHI DPLSKVKTVH IQCLWDNLSL HTEASGPPMY LLYRETQPTS PLIKALLTDQ
AQLNKNVIQQ IISAIRCNDF ATPLKRLANE RHKLKSNGVE RSHSFYRDIL FLALTAIGRS
NVDLATFHRE YAAVFDKLTE RECNMYYRNQ DLPPSASTIF CRAYFRPLLL P
