NBEA_DROME
ID NBEA_DROME Reviewed; 3466 AA.
AC Q9W4E2; O16024; Q8IRR9; Q961G8; Q9GP69; Q9GP70;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-MAR-2016, sequence version 4.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Neurobeachin;
DE AltName: Full=A-kinase anchor protein 550;
DE Short=AKAP 550;
DE AltName: Full=Protein rugose;
DE AltName: Full=dAKAP550;
GN Name=rg; Synonyms=Akap550; ORFNames=CG44835;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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 [2] {ECO:0000305}
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537572};
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 [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 197-3466 (ISOFORM N), FUNCTION, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Head {ECO:0000269|PubMed:11102458};
RX PubMed=11102458; DOI=10.1523/jneurosci.20-23-08551.2000;
RA Wang X., Herberg F.W., Laue M.M., Wullner C., Hu B., Petrasch-Parwez E.,
RA Kilimann M.W.;
RT "Neurobeachin: a protein kinase A-anchoring, beige/Chediak-Higashi protein
RT homolog implicated in neuronal membrane traffic.";
RL J. Neurosci. 20:8551-8565(2000).
RN [4] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 197-2271 (ISOFORM N), FUNCTION, SUBUNIT,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Canton-S {ECO:0000269|PubMed:9334242};
RC TISSUE=Embryo {ECO:0000269|PubMed:9334242};
RX PubMed=9334242; DOI=10.1074/jbc.272.42.26611;
RA Han J.-D., Baker N.E., Rubin C.S.;
RT "Molecular characterization of a novel A kinase anchor protein from
RT Drosophila melanogaster.";
RL J. Biol. Chem. 272:26611-26619(1997).
RN [5] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2478-3466 (ISOFORMS N/R).
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Head {ECO:0000269|PubMed:12537569};
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, SUBUNIT, AND TISSUE SPECIFICITY.
RX PubMed=12072466; DOI=10.1093/genetics/161.2.693;
RA Shamloula H.K., Mbogho M.P., Pimentel A.C., Chrzanowska-Lightowlers Z.M.,
RA Hyatt V., Okano H., Venkatesh T.R.;
RT "rugose (rg), a Drosophila A kinase anchor protein, is required for retinal
RT pattern formation and interacts genetically with multiple signaling
RT pathways.";
RL Genetics 161:693-710(2002).
RN [7] {ECO:0000305}
RP INTERACTION WITH NOTCH-MEDIATED SIGNALING PATHWAY.
RX PubMed=12124948; DOI=10.1002/gene.10102;
RA Schreiber S.L., Preiss A., Nagel A.C., Wech I., Maier D.;
RT "Genetic screen for modifiers of the rough eye phenotype resulting from
RT overexpression of the Notch antagonist hairless in Drosophila.";
RL Genesis 33:141-152(2002).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=23100440; DOI=10.1523/jneurosci.6424-11.2012;
RA Volders K., Scholz S., Slabbaert J.R., Nagel A.C., Verstreken P.,
RA Creemers J.W., Callaerts P., Schwarzel M.;
RT "Drosophila rugose is a functional homolog of mammalian Neurobeachin and
RT affects synaptic architecture, brain morphology, and associative
RT learning.";
RL J. Neurosci. 32:15193-15204(2012).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23790035; DOI=10.1111/gbb.12056;
RA Zhao J., Lu Y., Zhao X., Yao X., Shuai Y., Huang C., Wang L., Jeong S.H.,
RA Zhong Y.;
RT "Dissociation of rugose-dependent short-term memory component from memory
RT consolidation in Drosophila.";
RL Genes Brain Behav. 12:626-632(2013).
CC -!- FUNCTION: Binds to type II regulatory subunits of protein kinase A and
CC anchors/targets them to the membrane. May anchor the kinase to
CC cytoskeletal and/or organelle-associated proteins. Required for correct
CC retinal pattern formation and may function in cell fate determination
CC through its interactions with the EGFR and Notch signaling pathways.
CC Required for associative odor learning and short-term memory. Involved
CC in development of the neuromuscular junction and the mushroom body.
CC {ECO:0000269|PubMed:11102458, ECO:0000269|PubMed:12072466,
CC ECO:0000269|PubMed:23100440, ECO:0000269|PubMed:23790035,
CC ECO:0000269|PubMed:9334242}.
CC -!- SUBUNIT: Interacts with RII subunit of PKA and components of the EGFR-
CC mediated and Notch-mediated signaling pathways.
CC {ECO:0000269|PubMed:11102458, ECO:0000269|PubMed:12072466,
CC ECO:0000269|PubMed:12124948, ECO:0000269|PubMed:9334242}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein.
CC Perikaryon. Note=Found in the cortical region of perikarya with no
CC expression in neuropil regions. Located at or near the Golgi network in
CC perikarya of the dorsal medial cluster neurons.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=N {ECO:0000312|FlyBase:FBgn0266098};
CC IsoId=Q9W4E2-5; Sequence=Displayed;
CC Name=R {ECO:0000312|FlyBase:FBgn0266098};
CC IsoId=Q9W4E2-6; Sequence=VSP_058161, VSP_058162, VSP_058163,
CC VSP_058164;
CC -!- TISSUE SPECIFICITY: In early embryos, ubiquitous expression with
CC elevated levels in ventral furrow and flanking mesectodermal cells,
CC neuroblasts and mesoderm. Late embryos show reduced expression in
CC epidermis and skeletal muscle and elevated in nervous system, gut
CC endothelium, tracheal system and salivary gland. Larvae show expression
CC in imaginal disks and many neural cells. Developing eye imaginal disk
CC shows expression throughout the disk and in the region of the
CC morphogenetic furrow. Ubiquitous expression in adults with higher
CC levels in head region. Expressed in larval neurons but not in larval
CC glia. {ECO:0000269|PubMed:12072466, ECO:0000269|PubMed:23100440,
CC ECO:0000269|PubMed:9334242}.
CC -!- DEVELOPMENTAL STAGE: All stages of development.
CC {ECO:0000269|PubMed:9334242}.
CC -!- DOMAIN: RII-alpha binding site, predicted to form an amphipathic helix,
CC could participate in protein-protein interactions with a complementary
CC surface on the R-subunit dimer. {ECO:0000303|PubMed:11102458}.
CC -!- DISRUPTION PHENOTYPE: Mutants are viable and fertile but display a
CC rough eye surface phenotype, impaired short-term memory, aberrant
CC associative odor learning, aberrant neuromuscular junction morphology
CC with increased numbers of synaptic boutons, and defective axonal
CC morphology of the Kenyon cells, the neurons of the mushroom body.
CC {ECO:0000269|PubMed:23100440, ECO:0000269|PubMed:23790035}.
CC -!- SIMILARITY: Belongs to the WD repeat neurobeachin family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB83959.1; Type=Miscellaneous discrepancy; Note=Intron retention. In addition to the intron retained at the N-terminus, there are other discrepancies towards the C-terminus.; Evidence={ECO:0000305};
CC Sequence=AAK93020.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAC18799.1; Type=Miscellaneous discrepancy; Note=Intron retention. In addition, there are retained or missing exons which cannot be reconciled with any described isoform.; Evidence={ECO:0000305};
CC Sequence=CAC18800.1; Type=Miscellaneous discrepancy; Note=Intron retention. In addition, there are retained or missing exons which cannot be reconciled with any described isoform.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE014298; AAF46011.4; -; Genomic_DNA.
DR EMBL; AE014298; AAN09135.1; -; Genomic_DNA.
DR EMBL; Y18278; CAC18799.1; ALT_SEQ; mRNA.
DR EMBL; Y18278; CAC18800.1; ALT_SEQ; mRNA.
DR EMBL; AF003622; AAB83959.1; ALT_SEQ; mRNA.
DR EMBL; AY051596; AAK93020.1; ALT_INIT; mRNA.
DR PIR; T03094; T03094.
DR RefSeq; NP_001138158.2; NM_001144686.2. [Q9W4E2-5]
DR RefSeq; NP_726978.2; NM_167028.3. [Q9W4E2-6]
DR SMR; Q9W4E2; -.
DR BioGRID; 69112; 13.
DR DIP; DIP-17945N; -.
DR IntAct; Q9W4E2; 2.
DR STRING; 7227.FBpp0288527; -.
DR PaxDb; Q9W4E2; -.
DR EnsemblMetazoa; FBtr0344649; FBpp0310996; FBgn0266098. [Q9W4E2-5]
DR EnsemblMetazoa; FBtr0344668; FBpp0311009; FBgn0266098. [Q9W4E2-6]
DR GeneID; 44531; -.
DR KEGG; dme:Dmel_CG44835; -.
DR CTD; 44531; -.
DR FlyBase; FBgn0266098; rg.
DR VEuPathDB; VectorBase:FBgn0266098; -.
DR eggNOG; KOG1787; Eukaryota.
DR InParanoid; Q9W4E2; -.
DR BioGRID-ORCS; 44531; 0 hits in 3 CRISPR screens.
DR ChiTaRS; rg; fly.
DR GenomeRNAi; 44531; -.
DR PRO; PR:Q9W4E2; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0266098; Expressed in brain and 25 other tissues.
DR ExpressionAtlas; Q9W4E2; baseline and differential.
DR Genevisible; Q9W4E2; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IDA:FlyBase.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0051018; F:protein kinase A binding; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0042675; P:compound eye cone cell differentiation; IMP:FlyBase.
DR GO; GO:0042462; P:eye photoreceptor cell development; IMP:UniProtKB.
DR GO; GO:0016319; P:mushroom body development; IMP:FlyBase.
DR GO; GO:0007528; P:neuromuscular junction development; IMP:FlyBase.
DR GO; GO:0008355; P:olfactory learning; IMP:FlyBase.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0007614; P:short-term memory; IMP:FlyBase.
DR CDD; cd06071; Beach; 1.
DR CDD; cd01201; PH_BEACH; 1.
DR Gene3D; 1.10.1540.10; -; 1.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000409; BEACH_dom.
DR InterPro; IPR036372; BEACH_dom_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR010508; NBEA-like_DUF1088.
DR InterPro; IPR031570; NBEA/BDCP_DUF4704.
DR InterPro; IPR023362; PH-BEACH_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF02138; Beach; 1.
DR Pfam; PF06469; DUF1088; 1.
DR Pfam; PF15787; DUF4704; 1.
DR Pfam; PF14844; PH_BEACH; 1.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM01026; Beach; 1.
DR SMART; SM00320; WD40; 4.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF81837; SSF81837; 1.
DR PROSITE; PS50197; BEACH; 1.
DR PROSITE; PS51783; PH_BEACH; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Membrane; Reference proteome; Repeat;
KW WD repeat.
FT CHAIN 1..3466
FT /note="Neurobeachin"
FT /id="PRO_0000051093"
FT REPEAT 1846..1888
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT DOMAIN 2666..2774
FT /note="BEACH-type PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01119"
FT DOMAIN 2793..3082
FT /note="BEACH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00026"
FT REPEAT 3241..3284
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 3298..3338
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 3380..3419
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 3422..3461
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REGION 523..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1363..1382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1393..1465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1545..1583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1601..1695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1716..1767
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1794..1848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2105..2130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2198..2257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2284..2365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1393..1441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1558..1574
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1605..1691
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1716..1739
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1747..1767
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1794..1840
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2218..2236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2240..2254
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2297..2316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 2..53
FT /note="ADIMRPPYSEIKRPDEIVRMTTADNLKFAVLIGLIEVGQVTNREVVNTVLHL
FT -> DSLERLMRAAPLPRMLTSGVVATAAAAASAAAGKGMVSVGGGATAIAAGGGQQRAL
FT VHASLAAATVGRKGRHLTGTFCLTGDTMEGIIQCLVFLKAFS (in isoform R)"
FT /id="VSP_058161"
FT VAR_SEQ 388..594
FT /note="Missing (in isoform R)"
FT /id="VSP_058162"
FT VAR_SEQ 759..768
FT /note="Missing (in isoform R)"
FT /id="VSP_058163"
FT VAR_SEQ 2159..2214
FT /note="Missing (in isoform R)"
FT /id="VSP_058164"
FT CONFLICT 218
FT /note="F -> C (in Ref. 3; CAC18799/CAC18800 and 4;
FT AAB83959)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="C -> S (in Ref. 3; CAC18799/CAC18800 and 4;
FT AAB83959)"
FT /evidence="ECO:0000305"
FT CONFLICT 411
FT /note="T -> A (in Ref. 3; CAC18799 and 4; AAB83959)"
FT /evidence="ECO:0000305"
FT CONFLICT 415
FT /note="T -> S (in Ref. 3; CAC18799 and 4; AAB83959)"
FT /evidence="ECO:0000305"
FT CONFLICT 552
FT /note="H -> D (in Ref. 3; CAC18799 and 4; AAB83959)"
FT /evidence="ECO:0000305"
FT CONFLICT 590
FT /note="N -> D (in Ref. 3; CAC18799 and 4; AAB83959)"
FT /evidence="ECO:0000305"
FT CONFLICT 1702
FT /note="N -> T (in Ref. 3; CAC18799/CAC18800 and 4;
FT AAB83959)"
FT /evidence="ECO:0000305"
FT CONFLICT 2230..2239
FT /note="ENEVPEVESS -> GKTKCPRWSHP (in Ref. 3; CAC18799/
FT CAC18800 and 4; AAB83959)"
FT /evidence="ECO:0000305"
FT CONFLICT 2576
FT /note="V -> G (in Ref. 3; CAC18799/CAC18800)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3466 AA; 384513 MW; 152AEB5152C8F37C CRC64;
MADIMRPPYS EIKRPDEIVR MTTADNLKFA VLIGLIEVGQ VTNREVVNTV LHLLVGGEFD
MELNFVIQDA QNIKHMLELL DHCPPNLQAE IWSVFIAILR KSVRNLQACT DVGLIEHVLV
RLQRSETVVA DLLIEMLGVL ASYSITVKEL KLLFGTMKAT NGKWPRHSAK LLNVLRQMPH
RNGPDVFFSF PGRKGSAMVL PPLAKWPYEN GFTFTTWFRL DPINSVNIER EKPYLYCFKT
SKGVGYTAHF VGNCLVLTSM KVKGKGFQHC VKYEFQPRKW YMIAIVYIYN RWTKSEIKCL
VNGQLASSTE MAWFVSTNDP FDKCYIGATP ELDEERVFCG QMSAIYLFSE ALTTQQICAM
HRLGPGYKSQ FRFDNECYLN LPDNHKRVSH FQLLPATLGA SALSGGSGSG TGSGTGNDAS
AAAAAAVAAG QQQQLQLQFQ ILAAEQEARA IDWSDEKLDL NAAFVKIRAV LTARNAVTLA
GSSSTGTTAV ATAAAAAAAA GAGAGTTAAA TSAAAAAAAT QNENDAAVGQ QQHATHHHAT
AATGSADDPL GHLPTGNASS SSSSFEQLRR MSSVSSLNSM VGSADTEEVN QLKAVLYDGK
LSNAIVFMYN PVATDGQLCL QSSPKGNVSY FVHTPHALML QDVKAVVTHS IHCTLNSIGG
IQVLFPLFSQ LDMAHEGLGD IKRDPTLCSK LLGFICELVE TSQTVQQHMI QNRGFLVISF
MLQRSSREHL TLEVLGSFLN LTKYLVTCLS ANSDLLLKQL FCFSFLTWQL LDHVLFNPAL
WIYTPANVQA RLYSYLATEF LSDTQIYSNV RRVSTVLQTV HTLKYYYWVV NPRAKSGIIP
KGLDGPRPAQ KDILAIRAYI LLFLKQLIMI GNGVKEDELQ SILNYLTTMH EDENLHDVLQ
MLISLMSEHP SSMVPAFDVK HGVRSIFKLL AAESQLIRLQ ALKLLGFFLS RSTHKRKYDV
MSPHNLYTLL AERLLLYEES LSLPTYNVLY EIMTEHISQQ ILYTRHPEPE SHYRLENPMI
LKVVATLIRQ SKQTESLIDV KKLFLQDMTL LCNSNRENRR TVLQMSVWQE WLIAMAYIHP
KSSEEQKISD MVYSLFRMLL HHAIKHEYGG WRVWVDTLAI VHSKVSYEEF KLQFAQMYEH
YERQRTDNIT DPALRQARPI STISGWEREE LHQQQNGGSA AAVATNQTAA VKGSVSIASL
EDVPPVVEEE VEELELEEVE IQEGPITEET EQKSVIANIS DVYNEQLKTD ATCNGNLEDV
KEEEPVQQQI GDLEKQPEPS TPLGALRETL QLGDDMDVEE LELATAKDAL NAEQHVSRVL
QASEAALNDC KMAVDDVLQE SSSVLKDEEI ELAVNEVVQG VLNNEKKTQS QDNKDNKEQP
GEQDVNVSLL NSKNLLNNNN NNNNNSPSPT PTTATATAET EAETEVNANE IVSSTEAPKA
ETETSVAPEV ETPETAKPSP IVPSPVLATN QKTEDAANKL NNNEKLAEIS ASPEPPIVVE
TPEADLLQLS DSETKPNKET EAEDSVALAV RDIVEQLIDK VIDATEAESA SETKTETNNN
EIPKKEKQTS EEPEDVETAE TLAAAAKEIV QEVVEAALVM VQEESTQEKP EKGANSEEEK
NEIGKEEILL QLEEKPASTE VQETKIEGDL KKPEDPKGHS SVEPKTPNLE EPKPQETEQQ
KSQEVAEELP QKPEEQVVAI VNQVLDTLVD DTVKAVAAEQ TTQTSPAPEE QSPQILAMES
PATSVRVKPT EVDSTTQTTP KNEAGSSLLV EQVQQVLQED DAQQSAGMTI EDEDYSNQQA
AAAVENANSS QLDANHYGPG NPESKQQQQR SKSGSTRPMF SPGPTRPPFR IPEFKWSYIH
QRLLSDVLFS LETDIQVWRS HSTKSVLDFV NSSENAIFVV NTVHLISQLA DNLIIACGGL
LPLLASATSP NSELDVLEPT QGMPLEVAVS FLQRLVNMAD VLIFATSLNF GELEAEKNMS
SGGILRQCLR LVCTCAVRNC LECKERTRYN VGALARDVPG AAHLQALIRG AQASPKNIVE
SITGQLSPVK DPEKLLQDMD VNRLRAVIYR DVEETKQAQF LSLAIVYFIS VLMVSKYRDI
LEPPAEPQIQ RQSPVLQRTA GGGGRQIQDS DYEIIVVDEN NPSVLADNDS HSSGPPSIKA
NQTTTIATTT TTTATTHINN NNTKTTTSNA PTATIKIQQQ PLSPPKPLVP QKLPKSVDSD
VGSLNMNSTE NEVPEVESSS EILIDDHKPS HSNDESWTDV NLNEDAAVQA ASAGIVVGLV
DNRGNVISDK HDPSHHNQQQ QQQAGIIGQQ QQHGSLGHSE RGDKPDSEIS VVRVPDGYGG
AGSGGGVNSG QGQGVPSNQR PRPEELPMKA PALVAQLPLT TPSREASLTQ KLEIALGPVC
PLLREIMVDF APFLSKTLVG SHGQELLMEG KGLTTFKNSH SVVELVMLLC SQEWQNSLQK
HAGLAFIELI NEGRLLSHAM KDHIVRVANE AEFILNRMRA DDVLKHADFE SQCAQTLLER
REEERMCDHL ITAARRRDNV IASRLLEKVR NIMCNRHGAW GDSSSTSSGG AIVGAVQKSP
YWKLDAWEDD ARRRKRMVQN PRGSSHPQAT LKAALENGGP EDAILQTRDE FHTQIAVSRT
HPSGQHNGEL LDDAELLIED RELDLDLTGP VNISTKARLI APGLVAPGTV SITSTEMFFE
VDEEHPEFQK IDGEVLKYCD HLHGKWYFSE VRAIFSRRYL LQNVALEIFL ASRTSILFAF
PDQHTVKKVI KALPRVGVGI KYGIPQTRRA SMMSPRQLMR NSNMTQKWQR REISNFEYLM
FLNTIAGRTY NDLNQYPIFP WVLTNYESKD LDLSLPSNYR DLSKPIGALN PSRRAYFEER
YESWDSDTIP PFHYGTHYST AAFTLNWLVR VEPFTTMFLA LQGGKFDYPD RLFSSVSLSW
KNCQRDTSDV KELIPEWYFL PEMFYNSSGY RLGHREDGAL VDDIELPPWA KSPEEFVRIN
RMALESEFVS CQLHQWIDLI FGYKQRGPEA IRATNVFYYL TYEGSVDLDG VLDPVMREAV
ENQIRNFGQT PSQLLMEPHP PRSSAMHLSP MMFSAMPEDL CQMLKFYQNS PVIHISANTY
PQLSLPSVVT VTAGHQFAVN RWNCNYTASV QSPSYAESPQ SPGSNQPLTI DPVLAVHGTN
NNSNAASRRH LGDNFSQMLK IRSNCFVTTV DSRFLIACGF WDNSFRVFAT ETAKIVQIVF
GHFGVVTCMA RSECNITSDC YIASGSADCT VLLWHWNART QSIVGEGDVP TPRATLTGHE
QAVTSVVISA ELGLVVSGSS NGPVLIHTTF GDLLRSLDPP AEFHSPELIT MSREGFIVIN
YDKGNVAAYT INGKKLRHET HNDNLQCMLL SRDGEYLMTA GDRGIVEVWR TFNLAPLYAF
PACNAGIRSL ALTHDQKYLL AGLSTGSIIV FHIDFNRWHH EYQQRY