ITPR_DROME
ID ITPR_DROME Reviewed; 2838 AA.
AC P29993; Q24309; Q9U981; Q9VNC8;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 3.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Inositol 1,4,5-trisphosphate receptor {ECO:0000305};
DE AltName: Full=InsP3 receptor {ECO:0000305};
DE Short=IP3R {ECO:0000305};
DE Short=InsP3R {ECO:0000305};
GN Name=Itpr {ECO:0000312|FlyBase:FBgn0010051};
GN Synonyms=dip, InsP3R, Itp-r83A;
GN ORFNames=CG1063 {ECO:0000312|FlyBase:FBgn0010051};
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] (ISOFORM B), FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Oregon-R; TISSUE=Head;
RX PubMed=1322910; DOI=10.1016/s0021-9258(18)42047-9;
RA Yoshikawa S., Tanimura T., Miyawaki A., Nakamura M., Yuzaki M.,
RA Furuichi T., Mikoshiba K.;
RT "Molecular cloning and characterization of the inositol 1,4,5-trisphosphate
RT receptor in Drosophila melanogaster.";
RL J. Biol. Chem. 267:16613-16619(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
RC TISSUE=Embryo;
RX PubMed=10375644; DOI=10.1016/s0378-1119(99)00158-4;
RA Sinha M., Hasan G.;
RT "Sequencing and exon mapping of the inositol 1,4,5-trisphosphate receptor
RT cDNA from Drosophila embryos suggests the presence of differentially
RT regulated forms of RNA and protein.";
RL Gene 233:271-276(1999).
RN [3]
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 [4]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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 [5]
RP NUCLEOTIDE SEQUENCE OF 2370-2837, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC TISSUE=Brain;
RX PubMed=1338312; DOI=10.1242/dev.116.4.967;
RA Hasan G., Rosbash M.;
RT "Drosophila homologs of two mammalian intracellular Ca(2+)-release
RT channels: identification and expression patterns of the inositol 1,4,5-
RT triphosphate and the ryanodine receptor genes.";
RL Development 116:967-975(1992).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28726639; DOI=10.1074/jbc.m116.765578;
RA Choi S., Quan X., Bang S., Yoo H., Kim J., Park J., Park K.S., Chung J.;
RT "Mitochondrial calcium uniporter in Drosophila transfers calcium between
RT the endoplasmic reticulum and mitochondria in oxidative stress-induced cell
RT death.";
RL J. Biol. Chem. 292:14473-14485(2017).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=29444420; DOI=10.1016/j.celrep.2018.01.049;
RA Parkhurst S.J., Adhikari P., Navarrete J.S., Legendre A., Manansala M.,
RA Wolf F.W.;
RT "Perineurial Barrier Glia Physically Respond to Alcohol in an Akap200-
RT Dependent Manner to Promote Tolerance.";
RL Cell Rep. 22:1647-1656(2018).
CC -!- FUNCTION: Receptor for inositol 1,4,5-trisphosphate, a second messenger
CC that mediates the release of intracellular calcium (PubMed:1322910).
CC Together with MCU, has a role in oxidative stress-induced ER-
CC mitochondria calcium transfer (PubMed:28726639). May be involved in
CC visual and olfactory transduction, and myoblast proliferation
CC (PubMed:1322910). May be involved in ethanol tolerance
CC (PubMed:29444420). {ECO:0000269|PubMed:1322910,
CC ECO:0000269|PubMed:28726639, ECO:0000269|PubMed:29444420}.
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B; Synonyms=Head;
CC IsoId=P29993-1; Sequence=Displayed;
CC Name=A; Synonyms=Embryo;
CC IsoId=P29993-2; Sequence=VSP_002703;
CC -!- TISSUE SPECIFICITY: Segmental expression of isoform B is first detected
CC in stage 13 embryos in lateral and posterior epidermis. Expression
CC extends to head region during stages 13-17: gnathal buds, clypeolabrum,
CC procephalic lobe, labial organ and anterior sense organs. Adults
CC exhibit high expression in antenna and lower expression in retina,
CC head, legs and thorax. {ECO:0000269|PubMed:1322910,
CC ECO:0000269|PubMed:1338312}.
CC -!- DEVELOPMENTAL STAGE: Isoform A is expressed only in early embryos.
CC Isoform B is expressed from mid-late embryos to adults. Predominant
CC expression is in the adult. {ECO:0000269|PubMed:1338312}.
CC -!- DOMAIN: The receptor contains a calcium channel in its C-terminal
CC extremity. Its large N-terminal cytoplasmic region has the ligand-
CC binding site in the N-terminus and modulatory sites in the middle
CC portion immediately upstream of the channel region.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in the perineurial glia
CC results in decreased ethanol tolerance following repeated ethanol
CC exposure (PubMed:29444420). RNAi-mediated knockdown in muscle reduces
CC mitochondrial calcium uptake (PubMed:28726639).
CC {ECO:0000269|PubMed:28726639, ECO:0000269|PubMed:29444420}.
CC -!- SIMILARITY: Belongs to the InsP3 receptor family. {ECO:0000305}.
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DR EMBL; D90403; BAA14399.1; -; mRNA.
DR EMBL; AJ238949; CAB51853.1; -; mRNA.
DR EMBL; AE014297; AAF52015.2; -; Genomic_DNA.
DR EMBL; AE014297; AAN13240.1; -; Genomic_DNA.
DR EMBL; Z18535; CAA79220.1; -; mRNA.
DR PIR; A43360; A43360.
DR RefSeq; NP_001287180.1; NM_001300251.1.
DR RefSeq; NP_730941.1; NM_169060.2.
DR RefSeq; NP_730942.1; NM_169061.2.
DR SMR; P29993; -.
DR BioGRID; 65871; 21.
DR IntAct; P29993; 5.
DR STRING; 7227.FBpp0078336; -.
DR TCDB; 1.A.3.2.2; the ryanodine-inositol 1,4,5-triphosphate receptor ca(2+) channel (rir-cac) family.
DR PaxDb; P29993; -.
DR PRIDE; P29993; -.
DR GeneID; 40664; -.
DR KEGG; dme:Dmel_CG1063; -.
DR CTD; 40664; -.
DR FlyBase; FBgn0010051; Itpr.
DR VEuPathDB; VectorBase:FBgn0010051; -.
DR eggNOG; KOG3533; Eukaryota.
DR InParanoid; P29993; -.
DR PhylomeDB; P29993; -.
DR Reactome; R-DME-114508; Effects of PIP2 hydrolysis.
DR Reactome; R-DME-139853; Elevation of cytosolic Ca2+ levels.
DR Reactome; R-DME-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR Reactome; R-DME-5578775; Ion homeostasis.
DR Reactome; R-DME-9717207; Sensory perception of sweet, bitter, and umami (glutamate) taste.
DR Reactome; R-DME-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR SignaLink; P29993; -.
DR BioGRID-ORCS; 40664; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Itp-r83A; fly.
DR GenomeRNAi; 40664; -.
DR PRO; PR:P29993; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR ExpressionAtlas; P29993; baseline and differential.
DR Genevisible; P29993; DM.
DR GO; GO:0044295; C:axonal growth cone; IDA:FlyBase.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:FlyBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0030667; C:secretory granule membrane; IBA:GO_Central.
DR GO; GO:0005790; C:smooth endoplasmic reticulum; IDA:FlyBase.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; IBA:GO_Central.
DR GO; GO:0005220; F:inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity; IDA:FlyBase.
DR GO; GO:0035091; F:phosphatidylinositol binding; IBA:GO_Central.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IMP:UniProtKB.
DR GO; GO:0006816; P:calcium ion transport; IGI:UniProtKB.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:FlyBase.
DR GO; GO:0071361; P:cellular response to ethanol; IMP:UniProtKB.
DR GO; GO:0009267; P:cellular response to starvation; IMP:FlyBase.
DR GO; GO:0055089; P:fatty acid homeostasis; IMP:FlyBase.
DR GO; GO:0007629; P:flight behavior; IMP:FlyBase.
DR GO; GO:0030536; P:larval feeding behavior; IMP:FlyBase.
DR GO; GO:0055088; P:lipid homeostasis; IMP:FlyBase.
DR GO; GO:0007591; P:molting cycle, chitin-based cuticle; IGI:FlyBase.
DR GO; GO:0016319; P:mushroom body development; IMP:FlyBase.
DR GO; GO:0010888; P:negative regulation of lipid storage; IMP:FlyBase.
DR GO; GO:0000280; P:nuclear division; IDA:FlyBase.
DR GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; IMP:FlyBase.
DR GO; GO:0046000; P:positive regulation of ecdysteroid secretion; IMP:FlyBase.
DR GO; GO:0060259; P:regulation of feeding behavior; IMP:FlyBase.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IMP:FlyBase.
DR GO; GO:0006979; P:response to oxidative stress; IMP:UniProtKB.
DR GO; GO:0042594; P:response to starvation; IMP:FlyBase.
DR GO; GO:0035071; P:salivary gland cell autophagic cell death; IMP:FlyBase.
DR GO; GO:0007608; P:sensory perception of smell; IEA:UniProtKB-KW.
DR GO; GO:0050909; P:sensory perception of taste; IDA:FlyBase.
DR GO; GO:0030322; P:stabilization of membrane potential; IGI:FlyBase.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR InterPro; IPR014821; Ins145_P3_rcpt.
DR InterPro; IPR000493; InsP3_rcpt.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR036300; MIR_dom_sf.
DR InterPro; IPR016093; MIR_motif.
DR InterPro; IPR013662; RIH_assoc-dom.
DR InterPro; IPR000699; RIH_dom.
DR InterPro; IPR035910; RyR/IP3R_RIH_dom_sf.
DR Pfam; PF08709; Ins145_P3_rec; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF02815; MIR; 1.
DR Pfam; PF08454; RIH_assoc; 1.
DR Pfam; PF01365; RYDR_ITPR; 2.
DR PRINTS; PR00779; INSP3RECEPTR.
DR SMART; SM00472; MIR; 4.
DR SUPFAM; SSF100909; SSF100909; 2.
DR SUPFAM; SSF82109; SSF82109; 2.
DR PROSITE; PS50919; MIR; 5.
PE 2: Evidence at transcript level;
KW Alternative splicing; Calcium; Calcium channel; Calcium transport;
KW Developmental protein; Endoplasmic reticulum; Ion channel; Ion transport;
KW Ligand-gated ion channel; Membrane; Olfaction; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Sensory transduction; Transmembrane;
KW Transmembrane helix; Transport; Vision.
FT CHAIN 1..2838
FT /note="Inositol 1,4,5-trisphosphate receptor"
FT /id="PRO_0000153931"
FT TOPO_DOM 1..2366
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2367..2387
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2388..2398
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2399..2419
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2420..2434
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2435..2455
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2456..2487
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2488..2508
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2509..2531
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2532..2552
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2553..2659
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2660..2680
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2681..2838
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 115..170
FT /note="MIR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 177..229
FT /note="MIR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 237..293
FT /note="MIR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 300..359
FT /note="MIR 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 398..454
FT /note="MIR 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT REGION 723..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1080..1112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2213..2233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..755
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1081..1110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2213..2228
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 272..276
FT /ligand="1D-myo-inositol 1,4,5-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:203600"
FT /evidence="ECO:0000250"
FT BINDING 530..533
FT /ligand="1D-myo-inositol 1,4,5-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:203600"
FT /evidence="ECO:0000250"
FT BINDING 591..593
FT /ligand="1D-myo-inositol 1,4,5-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:203600"
FT /evidence="ECO:0000250"
FT VAR_SEQ 981..989
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000303|PubMed:10375644"
FT /id="VSP_002703"
FT CONFLICT 183
FT /note="Missing (in Ref. 3; AAF52015/AAN13240)"
FT /evidence="ECO:0000305"
FT CONFLICT 551
FT /note="E -> Q (in Ref. 3; AAF52015/AAN13240)"
FT /evidence="ECO:0000305"
FT CONFLICT 726
FT /note="P -> A (in Ref. 3; AAF52015/AAN13240)"
FT /evidence="ECO:0000305"
FT CONFLICT 1079..1120
FT /note="AASAASNEASQQQSQQQEPQTPGSSNETDPLDSAESVAAGAA -> PLRPLA
FT MRQVSSSRNNRNRRRLAAPMRLIPSTVPSLWPPRC (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 1150..1152
FT /note="SDA -> TP (in Ref. 1; BAA14399)"
FT /evidence="ECO:0000305"
FT CONFLICT 1394..1397
FT /note="VQHF -> GVGHSV (in Ref. 2; CAB51853)"
FT /evidence="ECO:0000305"
FT CONFLICT 1395
FT /note="Missing (in Ref. 1; BAA14399)"
FT /evidence="ECO:0000305"
FT CONFLICT 1419
FT /note="A -> R (in Ref. 3; AAF52015/AAN13240)"
FT /evidence="ECO:0000305"
FT CONFLICT 1466
FT /note="G -> R (in Ref. 3; AAF52015/AAN13240)"
FT /evidence="ECO:0000305"
FT CONFLICT 2108
FT /note="L -> V (in Ref. 3; AAF52015/AAN13240)"
FT /evidence="ECO:0000305"
FT CONFLICT 2333
FT /note="L -> V (in Ref. 3; AAF52015/AAN13240)"
FT /evidence="ECO:0000305"
FT CONFLICT 2452
FT /note="V -> I (in Ref. 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 2483..2497
FT /note="QLLYHCIYIAFCFCG -> STYTALYSVLLLR (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 2511
FT /note="D -> H (in Ref. 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 2802
FT /note="N -> F (in Ref. 1; BAA14399)"
FT /evidence="ECO:0000305"
FT CONFLICT 2807
FT /note="L -> V (in Ref. 5)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2838 AA; 319107 MW; 0718F04D15BE00BB CRC64;
MGDNIIGSAS FLHLGDIVSL YAEGSVCGFL STLGLVDDRT VVCPEAGDLS CPPKKFRDCL
IKICPMNRYS AQKQFWKAAK QSASSNTDPN LLKRLHHAAE IEKKQNETEN KKLLGTSIQY
GRAVVQLLHL KSNKYLTVNK RLPSLLEKNA MRVYLDANGN EGSWFYIKPF YKLRSIGDYV
VVVGDKVILS PVNADQQNLH VAANYELPDN PGCKEVNVLN SSTSWKISLF MEHKENQEHI
LKGGDVVRLF HAEQEKFLTM DEYKKQYHVF LRTTGRTSAT AATSSKALWE IEVVQHDSCR
GGAGDWNSLY RFKHLATGHY LAAEAEIDVS AGAMSATSAS GHDLHLGDCS KDSGLSCSTM
NSTINDKPKG KQYRLVSVPY SADIASVFVL DATTMARPDS LVPQSSYVRL QHICSNTWVH
ATSIPIDADD DKPVMSMVCC SPIKEDKEAF ALIPVSPVEV RDLDFANDAC KVLATVTSKL
DNGSISINER RALISLLQDI VYFIAGMENE QNKTKALEFT IKNPIRDRQK LLREQYILKQ
LFKILQGPFQ EHTAGDGPFL RLDELSDPKN SPYKNIFRLC YRILRLSQQD YRKNQEYIAK
HFGLMQKQIG YDILAEDTIT ALLHNNRKLL EKHITAAEIE TFVGLVRKNM HNWDSRFLDY
LSDLCVSNRK AIAVTQELIC KSVLSDKNKD ILIETQVKAL RTGSGPVRCY KGNSEDVCLA
TLAEDPGDDE DRSDVQSTST TTTWDSASLN EDDGTPSTGD KYEIHLKWTG QPTSRSMADL
ASCDGGELEA AILNYYRHQL NLFSNMCLNR QYLALNELSP RLDIDLILKC MSDETMPYEL
RASFCRLMLH LHVDRDPQEP VTPVKYARLW SEIPSKMSIQ DYDGKNQQPD QNKQACRAKF
NTTIAFVENY LCNVATKVWL FTDQEQNKLT FEVVKLARDL IYFGFYSFSD LLRLTKTLLS
ILDCVSDTSS GEFASTDIDS VEEETNAEAE GGVLRSIGDI NTVMTSLALG SVGQAIAAPT
ISLQQRKSVS QLMKEYPLVM DTKLKIIEIL QFILDVRLDY RISCLLSIFK REFDESEVAA
SAASNEASQQ QSQQQEPQTP GSSNETDPLD SAESVAAGAA AAAATTARQK NIDLESIGVQ
AEGIFDCERS DAANLDLDGQ GGRTFLRVLL HLIMHDYAPL VSGALHLLFR HFSQRQEVLQ
AFRQVQLLVS DSDVESYKQI KSDLDILRQS VEKSELWVYK AKATDELGAT DAGGDAVSLE
YNAALSQEQR NEYRKVKEIL IRMNKFCVTA SGPGSVVKPR KHEQRLLRNV GVHTVVLDLL
QNPYDEKDDE LMKELMCLAH EFLQNFCLGN QQNQVLLHNH LDLFLNPGIL EAKTVCAIFK
DNLALCNEVT DKVVQHFVHC IEIHGRHVAY LQFLQTVVAA ENQFIRRCQD MVMQELINSG
EDVLVFYNDK GSFNHFVQMM QQQMLGMEKL SDDSPLKYHV ELVKLLACCT MGKNVYTEIK
CNNLLSLDDI VTIICHPLCM PEVKEAYVDF LNHCYIDTEV EMKEIYASGH MWSLFEKSFL
VDINQLITNP AAASNKTLQA YVLNGVTNLL GSFFASPFSD QSAIVQSRQL IFVQLLQAAH
RITQCRWLSL GDRFNVENCI RTLTESAKMR SIALPPELEQ QVATMSSKTA MLTRQTTKWL
LASKQPKYEA QQAASLMRWD RSIIEGLQDI VSLLEDQLKP VVEAELSLLV DILYRSELLF
PAGTEARKRC ESGGFIRKLI KHTEKLLEEK EERMCVKVLR TLREMMAIDV NYGEKGDALR
QTLLLRYFQT KSTPRLPEDE VPLLAAPLMD PAKQNHLVTH GPGAKYLQRA GKTLHEMQNH
LDREGASDLV VELVIKSVHS PNIFVEAVEL GIALLEGGNP IIQKGMFQKF LSDDLNQAFF
KVFFEKMKDA QQEIKSTVTV NTTDIAAKAH EHKQDTNLEL DKIARKHGLK SNGVVITEEL
KRELHNAGLA TARAYGNARN IHSGEESSAI SVNSPLEDIL AEKLEKHKDS RDQRNQLSNK
VLVMQPILRF LQLLCENHNP DMQNLLRNQN NKTNNNLVSE TLMFLDCICG STTGGLGLLG
LYINEHNLAL INQTLEALTE YCQGPCHENQ NCIATHESNG LDIITALILN NINPLGENRM
DLVLELKNNA SKLLLAIMES RGDSENAERI LYNMNPKQLV EVACKAYHQE ELIDEQDDGD
EPDAGSDDDD ATVSPREVGH NIYILCHQLA QHNKELAGLL KASEDPQSAS FDAKTSQALM
YYATHTAQIE IVRNDRTLEQ IVFPIPEICE YLTTDTKIKI LNTAERDDQG SKLADFFDKA
EEMFNEMKWQ KKLRSQPLLF WISSYMSLWS NILFNCVVVI NMIVAFFYPF DNTVPELSSH
ISLLFWIITI FSLVIVLALP RESGIRTFIG SVILRFIFLL GPESTLCLLG VVTVTLKSVH
IVSIMGNKGT LEKQLIKIIT DFQLLYHCIY IAFCFCGLIF HPFFYSLLLF DVVYREETLV
NVIRSVTRNG RSIVLTAVLA LILVYLFSII GYMFFKDDFL VSVDFEEQDN APPPSVPLTL
SVPVSGDSCS APDDLGNCQA AKEVAPPSAG GGEVKERSCD SLVMCIVTTL NQGLRNGGGI
GDILRAPSSK EGLFVARVIY DLLFFFIVII IVLNLIFGVI IDTFADLRSE KQQKEAILKT
TCFICSLNRS AFDNKTVSFE EHIKSEHNMW HYLYFIVLVK VKDPTEFTGP ESYVYAMVKA
GILEWFPRLR AMSLAAVDAD GEQIELRSMQ AQLLDTQLLI KNLSTQLHEL KDHMTEQRKQ
KQRLGLLNTT ANSLLPFQ
