CI_DROME
ID CI_DROME Reviewed; 1397 AA.
AC P19538; O18525; Q8T6T1; Q9V4A8;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Transcriptional activator cubitus interruptus;
DE Short=Transcriptional activator ci;
DE AltName: Full=ci form of 155 kDa;
DE Short=ci-155;
DE AltName: Full=ci full-length protein;
DE Short=ciFL;
DE Contains:
DE RecName: Full=Transcriptional repressor cubitus interruptus;
DE Short=Transcriptional repressor ci;
DE AltName: Full=ci C-terminally truncated form;
DE AltName: Full=ci form of 75 kDa;
DE Short=ci-75;
GN Name=ci; Synonyms=ci-D; ORFNames=CG2125;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC STRAIN=Oregon-R; TISSUE=Embryo;
RX PubMed=2166702; DOI=10.1101/gad.4.6.1053;
RA Orenic T.V., Slusarski D.C., Kroll K.L., Holmgren R.A.;
RT "Cloning and characterization of the segment polarity gene cubitus
RT interruptus Dominant of Drosophila.";
RL Genes Dev. 4:1053-1067(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Oregon-R; TISSUE=Embryo;
RX PubMed=1686006; DOI=10.1093/genetics/129.4.1111;
RA Berry A.J., Ajioka J.W., Kreitman M.;
RT "Lack of polymorphism on the Drosophila fourth chromosome resulting from
RT selection.";
RL Genetics 129:1111-1117(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Embryo;
RX PubMed=9332387; DOI=10.1016/s0378-1119(97)00285-0;
RA Ahmed A., Podemski L.;
RT "Use of ordered deletions in genome sequencing.";
RL Gene 197:367-373(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
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 [5]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-5.
RX PubMed=7600980; DOI=10.1242/dev.121.6.1625;
RA Schwartz C., Locke J., Nishida C., Kornberg T.B.;
RT "Analysis of cubitus interruptus regulation in Drosophila embryos and
RT imaginal disks.";
RL Development 121:1625-1635(1995).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 521-769.
RC STRAIN=253.27;
RX PubMed=11778050; DOI=10.1126/science.1064521;
RA Wang W., Thornton K., Berry A., Long M.;
RT "Nucleotide variation along the Drosophila melanogaster fourth
RT chromosome.";
RL Science 295:134-137(2002).
RN [8]
RP INTERACTION WITH COS.
RX PubMed=9244298; DOI=10.1016/s0092-8674(00)80332-3;
RA Sisson J.C., Ho K.S., Suyama K., Scott M.P.;
RT "Costal2, a novel kinesin-related protein in the Hedgehog signaling
RT pathway.";
RL Cell 90:235-245(1997).
RN [9]
RP PHOSPHORYLATION, PROTEOLYTIC PROCESSING, AND INTERACTION WITH COS.
RX PubMed=15691767; DOI=10.1016/j.devcel.2005.01.001;
RA Zhang W., Zhao Y., Tong C., Wang G., Wang B., Jia J., Jiang J.;
RT "Hedgehog-regulated Costal2-kinase complexes control phosphorylation and
RT proteolytic processing of Cubitus interruptus.";
RL Dev. Cell 8:267-278(2005).
RN [10]
RP INTERACTION WITH SLMB, AND PHOSPHORYLATION.
RX PubMed=16326393; DOI=10.1016/j.devcel.2005.10.006;
RA Jia J., Zhang L., Zhang Q., Tong C., Wang B., Hou F., Amanai K., Jiang J.;
RT "Phosphorylation by double-time/CKIepsilon and CKIalpha targets cubitus
RT interruptus for Slimb/beta-TRCP-mediated proteolytic processing.";
RL Dev. Cell 9:819-830(2005).
RN [11]
RP INTERACTION WITH RDX, AND UBIQUITINATION.
RX PubMed=16740475; DOI=10.1016/j.devcel.2006.05.004;
RA Zhang Q., Zhang L., Wang B., Ou C.-Y., Chien C.-T., Jiang J.;
RT "A hedgehog-induced BTB protein modulates hedgehog signaling by degrading
RT Ci/Gli transcription factor.";
RL Dev. Cell 10:719-729(2006).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25639794; DOI=10.1016/j.chom.2014.12.012;
RA Lee K.A., Kim B., Bhin J., Kim D.H., You H., Kim E.K., Kim S.H., Ryu J.H.,
RA Hwang D., Lee W.J.;
RT "Bacterial uracil modulates Drosophila DUOX-dependent gut immunity via
RT Hedgehog-induced signaling endosomes.";
RL Cell Host Microbe 17:191-204(2015).
CC -!- FUNCTION: Has a dual function as a transcriptional activator and a
CC repressor of the hedgehog (Hh) pathway. The full-length ci form (ciFL),
CC acts as an activator (ciA) while ciR, its C-terminally truncated form,
CC acts as a repressor. Involved in segment polarity. Required for the
CC normal development of the posterior half of each embryonic segment.
CC Engrailed protein directly represses ci expression in posterior
CC compartment cells. Essential component of a hh-signaling pathway which
CC regulates the Duox-dependent gut immune response to bacterial uracil;
CC required to activate Cad99C-dependent endosome formation, norpA-
CC dependent Ca2+ mobilization and p38 MAPK, which are essential steps in
CC the Duox-dependent production of reactive oxygen species (ROS) in
CC response to intestinal bacterial infection (PubMed:25639794).
CC -!- SUBUNIT: Interacts with RDX (PubMed:16740475). Interacts with cos
CC (PubMed:9244298, PubMed:15691767). Interacts with slmb; the interaction
CC is enhanced by phosphorylation by CkIalpha and dco (PubMed:16326393).
CC {ECO:0000269|PubMed:15691767, ECO:0000269|PubMed:16326393,
CC ECO:0000269|PubMed:16740475, ECO:0000269|PubMed:9244298}.
CC -!- INTERACTION:
CC P19538; P19538: ci; NbExp=6; IntAct=EBI-94976, EBI-94976;
CC P19538; O16844: cos; NbExp=12; IntAct=EBI-94976, EBI-102069;
CC P19538; P23647: fu; NbExp=8; IntAct=EBI-94976, EBI-165536;
CC P19538; O01368: nej; NbExp=3; IntAct=EBI-94976, EBI-868028;
CC P19538; Q9VFP2-2: rdx; NbExp=8; IntAct=EBI-94976, EBI-15659276;
CC P19538; Q9VG38: Su(fu); NbExp=5; IntAct=EBI-94976, EBI-110605;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- DEVELOPMENTAL STAGE: In embryos, expressed uniformly throughout the
CC blastoderm stage and gastrulation (from stage 5). During stage 10, ci
CC is eliminated from the posterior compartment of each segment forming 15
CC segmentally repeating stripes at the end of the short phase of germ-
CC band extension. {ECO:0000269|PubMed:2166702}.
CC -!- PTM: Polyubiquitinated by RDX in the presence of CUL3, which results in
CC proteasomal degradation. {ECO:0000269|PubMed:16740475}.
CC -!- PTM: Phosphorylated on multiple sites by protein kinase A (PKA) and
CC phosphorylation by PKA primes further phosphorylation by CK1 and GSK3.
CC Phosphorylation is essential for its proteolytic processing. cos
CC recruits multiple kinases to promote efficient phosphorylation of ci
CC while Hh signaling inhibits phosphorylation by restricting the
CC accessibility of ci to the kinases (PubMed:15691767). Phosphorylation
CC by CkIalpha and dco enhances binding to Slmb, the F-box recognition
CC component of the SCF(slmb) E3 ubiquitin-protein ligase required for ci
CC processing (PubMed:16326393). {ECO:0000269|PubMed:15691767,
CC ECO:0000269|PubMed:16326393}.
CC -!- PTM: Transcriptional repressor ciR, a C-terminally truncated form, is
CC generated from the full-length ci (ciFL/ci-155) through proteolytic
CC processing. Hh suppresses the formation of ci75 and promotes the
CC conversion of ci155 into a transcriptional activator (ci155A).
CC {ECO:0000269|PubMed:15691767}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown severely reduces adult
CC survival following the ingestion of E.carotovora. Abolishes Cad99C-
CC dependent formation of endosomes and DUOX-dependent up-regulation of
CC reactive oxygen species (ROS) in the intestines of adults fed bacteria-
CC derived uracil. {ECO:0000269|PubMed:25639794}.
CC -!- SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; X54360; CAA38244.1; -; mRNA.
DR EMBL; U66884; AAC47752.1; -; Genomic_DNA.
DR EMBL; AE014135; AAF59373.2; -; Genomic_DNA.
DR EMBL; AH003430; AAG15271.1; -; Genomic_DNA.
DR EMBL; AF433680; AAM17953.1; -; Genomic_DNA.
DR PIR; A38926; A38926.
DR RefSeq; NP_524617.3; NM_079878.5.
DR PDB; 3HQM; X-ray; 1.74 A; C/D=1356-1367.
DR PDBsum; 3HQM; -.
DR AlphaFoldDB; P19538; -.
DR SMR; P19538; -.
DR BioGRID; 68605; 192.
DR DIP; DIP-121N; -.
DR ELM; P19538; -.
DR IntAct; P19538; 8.
DR STRING; 7227.FBpp0088245; -.
DR iPTMnet; P19538; -.
DR PaxDb; P19538; -.
DR PRIDE; P19538; -.
DR EnsemblMetazoa; FBtr0089178; FBpp0088245; FBgn0004859.
DR GeneID; 43767; -.
DR KEGG; dme:Dmel_CG2125; -.
DR CTD; 12679; -.
DR FlyBase; FBgn0004859; ci.
DR VEuPathDB; VectorBase:FBgn0004859; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000169506; -.
DR HOGENOM; CLU_004194_1_0_1; -.
DR InParanoid; P19538; -.
DR PhylomeDB; P19538; -.
DR Reactome; R-DME-209159; Assembly of the CI containing complexes.
DR Reactome; R-DME-209190; Phosphorylation of CI.
DR Reactome; R-DME-209214; Phosphorylation of SMO.
DR Reactome; R-DME-209338; Assembly of the 'signalling complexes'.
DR Reactome; R-DME-209360; Ubiquitination and proteolysis of phosphorylated CI.
DR Reactome; R-DME-209446; N-HH ligand not bound to PTC receptor complex.
DR Reactome; R-DME-216119; Activation of CI.
DR Reactome; R-DME-216167; Nuclear CI is degraded.
DR Reactome; R-DME-216217; Activation of SMO.
DR Reactome; R-DME-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-DME-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-DME-5610787; Hedgehog 'off' state.
DR Reactome; R-DME-5632684; Hedgehog 'on' state.
DR SignaLink; P19538; -.
DR BioGRID-ORCS; 43767; 0 hits in 3 CRISPR screens.
DR EvolutionaryTrace; P19538; -.
DR GenomeRNAi; 43767; -.
DR PRO; PR:P19538; -.
DR Proteomes; UP000000803; Chromosome 4.
DR Bgee; FBgn0004859; Expressed in wing disc and 61 other tissues.
DR ExpressionAtlas; P19538; baseline and differential.
DR Genevisible; P19538; DM.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0035301; C:Hedgehog signaling complex; IPI:FlyBase.
DR GO; GO:0016020; C:membrane; IDA:FlyBase.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0032991; C:protein-containing complex; IPI:FlyBase.
DR GO; GO:0008140; F:cAMP response element binding protein binding; IPI:FlyBase.
DR GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IMP:FlyBase.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:FlyBase.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:FlyBase.
DR GO; GO:0019901; F:protein kinase binding; IDA:FlyBase.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:FlyBase.
DR GO; GO:0001745; P:compound eye morphogenesis; IMP:FlyBase.
DR GO; GO:0035017; P:cuticle pattern formation; IMP:FlyBase.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
DR GO; GO:0035224; P:genital disc anterior/posterior pattern formation; IEP:FlyBase.
DR GO; GO:0060914; P:heart formation; IMP:FlyBase.
DR GO; GO:0035217; P:labial disc development; IMP:FlyBase.
DR GO; GO:0002385; P:mucosal immune response; IMP:FlyBase.
DR GO; GO:0035331; P:negative regulation of hippo signaling; IGI:FlyBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR GO; GO:0030858; P:positive regulation of epithelial cell differentiation; IMP:FlyBase.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IMP:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:FlyBase.
DR GO; GO:2000495; P:regulation of cell proliferation involved in compound eye morphogenesis; IMP:FlyBase.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
DR GO; GO:0007367; P:segment polarity determination; IMP:UniProtKB.
DR GO; GO:0007224; P:smoothened signaling pathway; IDA:FlyBase.
DR GO; GO:0035277; P:spiracle morphogenesis, open tracheal system; IMP:FlyBase.
DR GO; GO:0048100; P:wing disc anterior/posterior pattern formation; IMP:FlyBase.
DR InterPro; IPR043359; GLI-like.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR45718; PTHR45718; 1.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Developmental protein; DNA-binding; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor;
KW Segmentation polarity protein; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1397
FT /note="Transcriptional activator cubitus interruptus"
FT /id="PRO_0000046917"
FT CHAIN 1..?
FT /note="Transcriptional repressor cubitus interruptus"
FT /id="PRO_0000406217"
FT ZN_FING 451..476
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 484..511
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 517..541
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 547..572
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 578..603
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..440
FT /note="Interaction with RDX"
FT /evidence="ECO:0000269|PubMed:16740475"
FT REGION 193..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 807..877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1161..1397
FT /note="Interaction with RDX"
FT /evidence="ECO:0000269|PubMed:16740475"
FT COMPBIAS 368..383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 403
FT /note="T -> K (in Ref. 3; AAC47752)"
FT /evidence="ECO:0000305"
FT CONFLICT 457
FT /note="S -> R (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 804..805
FT /note="YT -> IS (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 968
FT /note="T -> S (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 1043
FT /note="S -> L (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 1152
FT /note="Missing (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 1155
FT /note="V -> L (in Ref. 3; AAC47752)"
FT /evidence="ECO:0000305"
FT CONFLICT 1378..1397
FT /note="DMTTSLTSLLEENRYLQMMQ -> V (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1397 AA; 153280 MW; C3232A71EF9B8004 CRC64;
MDAYALPTYF PLAYSELQFL ASRRAAAVAA AATVLPGSPC INQHHPTDVS SSVTVPSIIP
TGGTSDSIKT SIQPQICNEN TLLGNAGHQH NHQPQHVHNI NVTGQPHDFH PAYRIPGYME
QLYSLQRTNS ASSFHDPYVN CASAFHLAGL GLGSADFLGS RGLSSLGELH NAAVAAAAAG
SLASTDFHFS VDGNRRLGSP RPPGGSIRAS ISRKRALSSS PYSDSFDINS MIRFSPNSLA
TIMNGSRGSS AASGSYGHIS ATALNPMSHV HSTRLQQIQA HLLRASAGLL NPMTPQQVAA
SGFSIGHMPT SASLRVNDVH PNLSDSHIQI TTSPTVTKDV SQVPAAAFSL KNLDDAREKK
GPFKDVVPEQ PSSTSGGVAQ VEADSASSQL SDRCYNNVVN NITGIPGDVK VNSRLDEYIN
CGSISIPSNE YDCANADTTD IKDEPGDFIE TNCHWRSCRI EFITQDELVK HINNDHIQTN
KKAFVCRWED CTRGEKPFKA QYMLVVHMRR HTGEKPHKCT FEGCFKAYSR LENLKTHLRS
HTGEKPYTCE YPGCSKAFSN ASDRAKHQNR THSNEKPYIC KAPGCTKRYT DPSSLRKHVK
TVHGAEFYAN KKHKGLPLND ANSRLQQNNS RHNLQEHNID SSPCSEDSHL GKMLGTSSPS
IKSESDISSS NHHLVNGVRA SDSLLTYSPD DLAENLNLDD GWNCDDDVDV ADLPIVLRAM
VNIGNGNASA STIGGSVLAR QRFRGRLQTK GINSSTIMLC NIPESNRTFG ISELNQRITE
LKMEPGTDAE IKIPKLPNTT IGGYTEDPLQ NQTSFRNTVS NKQGTVSGSI QGQFRRDSQN
STASTYYGSM QSRRSSQSSQ VSSIPTMRPN PSCNSTASFY DPISPGCSRR SSQMSNGANC
NSFTSTSGLP VLNKESNKSL NACINKPNIG VQGVGIYNSS LPPPPSSHLI ATNLKRLQRK
DSEYHNFTSG RFSVPSYMHS LHIKNNKPVG ENEFDKAIAS NARRQTDPVP NINLDPLTNI
SRFSTTPHSF DINVGKTNNI ASSINKDNLR KDLFTVSIKA DMAMTSDQHP NERINLDEVE
ELILPDEMLQ YLNLVKDDTN HLEKEHQAVP VGSNVSETIA SNHYREQSNI YYTNKQILTP
PSNVDIQPNT TKFTVQDKFA MTAVGGSFSQ RELSTLAVPN EHGHAKCESF HHQSQKYMNT
DIGSKQQSAL PSAHQRQTEK SNYNQIIDSS MTSLPELNVD SIYPRNETEN IFKVHGDHDN
EIQCGIISQS QMSPSTNLNN DGQFSTVNMQ PITTSKLFPP EPQKIVCDTQ ASNTSVMHLD
TYQRTLEYVQ SCQNWMETNN TSTNQIQSLP GMPVNNTLFP DVSSSTHPYH GTNMVINDMT
TSLTSLLEEN RYLQMMQ
