SRC64_DROME
ID SRC64_DROME Reviewed; 552 AA.
AC P00528; A4V1H7; O18372; Q9VZA2;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 3.
DT 03-AUG-2022, entry version 227.
DE RecName: Full=Tyrosine-protein kinase Src64B;
DE Short=Dsrc64;
DE EC=2.7.10.2;
GN Name=Src64B; Synonyms=Src1; ORFNames=CG7524;
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], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=2996778; DOI=10.1016/0092-8674(85)90279-x;
RA Simon M.A., Drees B., Kornberg T., Bishop J.M.;
RT "The nucleotide sequence and the tissue-specific expression of Drosophila
RT c-src.";
RL Cell 42:831-840(1985).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 249-552.
RX PubMed=6317185; DOI=10.1016/0092-8674(83)90172-1;
RA Hoffmann F.M., Fresco L.D., Hoffman-Falk H., Shilo B.-Z.;
RT "Nucleotide sequences of the Drosophila src and abl homologs: conservation
RT and variability in the src family oncogenes.";
RL Cell 35:393-401(1983).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 410-461.
RX PubMed=9731193; DOI=10.1006/bbrc.1998.9003;
RA Oates A.C., Wollberg P., Achen M.G., Wilks A.F.;
RT "Sampling the genomic pool of protein tyrosine kinase genes using the
RT polymerase chain reaction with genomic DNA.";
RL Biochem. Biophys. Res. Commun. 249:660-667(1998).
RN [7]
RP INTERACTION WITH HZG, AND PHOSPHORYLATION.
RX PubMed=31491385; DOI=10.1016/j.cell.2019.08.019;
RA Nil Z., Hervas R., Gerbich T., Leal P., Yu Z., Saraf A., Sardiu M.,
RA Lange J.J., Yi K., Unruh J., Slaughter B., Si K.;
RT "Amyloid-like Assembly Activates a Phosphatase in the Developing Drosophila
RT Embryo.";
RL Cell 178:1403-1420.E21(2019).
CC -!- FUNCTION: May play a role in the development of neural tissue and
CC smooth muscle. {ECO:0000269|PubMed:2996778}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC -!- SUBUNIT: Interacts with hzg. {ECO:0000269|PubMed:31491385}.
CC -!- INTERACTION:
CC P00528; P11346: Raf; NbExp=3; IntAct=EBI-87092, EBI-664624;
CC P00528; Q03720: slo; NbExp=3; IntAct=EBI-87092, EBI-426805;
CC -!- TISSUE SPECIFICITY: After the first 8 hours of development, accumulates
CC almost exclusively in neural tissues such as the brain, ventral nerve
CC chord, and eye-antennal disks, and in differentiating smooth muscle.
CC {ECO:0000269|PubMed:2996778}.
CC -!- DEVELOPMENTAL STAGE: Abundant in embryos and pupae, rare in larvae and
CC adults. {ECO:0000269|PubMed:2996778}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:31491385}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. SRC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; M11917; AAA28913.1; -; mRNA.
DR EMBL; AE014296; AAF47922.1; -; Genomic_DNA.
DR EMBL; AE014296; AAX52734.1; -; Genomic_DNA.
DR EMBL; AE014296; AAX52735.1; -; Genomic_DNA.
DR EMBL; AE014296; AAX52736.1; -; Genomic_DNA.
DR EMBL; AE014296; AAX52737.1; -; Genomic_DNA.
DR EMBL; AY051781; AAK93205.1; -; mRNA.
DR EMBL; K01043; AAA28489.1; -; Genomic_DNA.
DR EMBL; AJ002919; CAA05754.1; -; Genomic_DNA.
DR RefSeq; NP_001014561.1; NM_001014561.2.
DR RefSeq; NP_001014562.1; NM_001014562.3.
DR RefSeq; NP_001014563.1; NM_001014563.3.
DR RefSeq; NP_001014564.1; NM_001014564.3.
DR RefSeq; NP_001189051.1; NM_001202122.1.
DR RefSeq; NP_001246628.1; NM_001259699.2.
DR RefSeq; NP_001246629.1; NM_001259700.2.
DR RefSeq; NP_524934.2; NM_080195.4.
DR AlphaFoldDB; P00528; -.
DR SMR; P00528; -.
DR BioGRID; 71867; 69.
DR DIP; DIP-17438N; -.
DR IntAct; P00528; 9.
DR STRING; 7227.FBpp0293527; -.
DR iPTMnet; P00528; -.
DR PaxDb; P00528; -.
DR DNASU; 48973; -.
DR EnsemblMetazoa; FBtr0073321; FBpp0073177; FBgn0262733.
DR EnsemblMetazoa; FBtr0100504; FBpp0099944; FBgn0262733.
DR EnsemblMetazoa; FBtr0100505; FBpp0099946; FBgn0262733.
DR EnsemblMetazoa; FBtr0100507; FBpp0099947; FBgn0262733.
DR EnsemblMetazoa; FBtr0100508; FBpp0099948; FBgn0262733.
DR EnsemblMetazoa; FBtr0302594; FBpp0291750; FBgn0262733.
DR EnsemblMetazoa; FBtr0304989; FBpp0293526; FBgn0262733.
DR EnsemblMetazoa; FBtr0304990; FBpp0293527; FBgn0262733.
DR GeneID; 48973; -.
DR KEGG; dme:Dmel_CG7524; -.
DR CTD; 48973; -.
DR FlyBase; FBgn0262733; Src64B.
DR VEuPathDB; VectorBase:FBgn0262733; -.
DR eggNOG; KOG0197; Eukaryota.
DR GeneTree; ENSGT00940000164033; -.
DR InParanoid; P00528; -.
DR OMA; NNIAKIC; -.
DR OrthoDB; 539311at2759; -.
DR PhylomeDB; P00528; -.
DR BRENDA; 2.7.10.2; 1994.
DR Reactome; R-DME-1251985; Nuclear signaling by ERBB4.
DR Reactome; R-DME-1253288; Downregulation of ERBB4 signaling.
DR Reactome; R-DME-1257604; PIP3 activates AKT signaling.
DR Reactome; R-DME-1295596; Spry regulation of FGF signaling.
DR Reactome; R-DME-186763; Downstream signal transduction.
DR Reactome; R-DME-2454202; Fc epsilon receptor (FCERI) signaling.
DR Reactome; R-DME-354192; Integrin signaling.
DR Reactome; R-DME-375165; NCAM signaling for neurite out-growth.
DR Reactome; R-DME-3928662; EPHB-mediated forward signaling.
DR Reactome; R-DME-3928663; EPHA-mediated growth cone collapse.
DR Reactome; R-DME-3928664; Ephrin signaling.
DR Reactome; R-DME-3928665; EPH-ephrin mediated repulsion of cells.
DR Reactome; R-DME-399954; Sema3A PAK dependent Axon repulsion.
DR Reactome; R-DME-399955; SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
DR Reactome; R-DME-399956; CRMPs in Sema3A signaling.
DR Reactome; R-DME-418592; ADP signalling through P2Y purinoceptor 1.
DR Reactome; R-DME-418594; G alpha (i) signalling events.
DR Reactome; R-DME-418885; DCC mediated attractive signaling.
DR Reactome; R-DME-430116; GP1b-IX-V activation signalling.
DR Reactome; R-DME-432142; Platelet sensitization by LDL.
DR Reactome; R-DME-456926; Thrombin signalling through proteinase activated receptors (PARs).
DR Reactome; R-DME-5621575; CD209 (DC-SIGN) signaling.
DR Reactome; R-DME-5663220; RHO GTPases Activate Formins.
DR Reactome; R-DME-5673000; RAF activation.
DR Reactome; R-DME-5673001; RAF/MAP kinase cascade.
DR Reactome; R-DME-5674135; MAP2K and MAPK activation.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR Reactome; R-DME-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-DME-69231; Cyclin D associated events in G1.
DR Reactome; R-DME-8866376; Reelin signalling pathway.
DR Reactome; R-DME-8934903; Receptor Mediated Mitophagy.
DR Reactome; R-DME-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-DME-9009391; Extra-nuclear estrogen signaling.
DR Reactome; R-DME-9013407; RHOH GTPase cycle.
DR Reactome; R-DME-9027276; Erythropoietin activates Phosphoinositide-3-kinase (PI3K).
DR Reactome; R-DME-9027284; Erythropoietin activates RAS.
DR Reactome; R-DME-912631; Regulation of signaling by CBL.
DR SignaLink; P00528; -.
DR BioGRID-ORCS; 48973; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Src64B; fly.
DR GenomeRNAi; 48973; -.
DR PRO; PR:P00528; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0262733; Expressed in cleaving embryo and 42 other tissues.
DR ExpressionAtlas; P00528; baseline and differential.
DR Genevisible; P00528; DM.
DR GO; GO:0005829; C:cytosol; HDA:FlyBase.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
DR GO; GO:0045172; C:germline ring canal; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; HDA:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IDA:FlyBase.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; IPI:FlyBase.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:FlyBase.
DR GO; GO:0034332; P:adherens junction organization; IMP:FlyBase.
DR GO; GO:0007411; P:axon guidance; IMP:FlyBase.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0007349; P:cellularization; IMP:FlyBase.
DR GO; GO:0090136; P:epithelial cell-cell adhesion; IMP:FlyBase.
DR GO; GO:0007301; P:female germline ring canal formation; IMP:FlyBase.
DR GO; GO:0008302; P:female germline ring canal formation, actin assembly; IMP:FlyBase.
DR GO; GO:0008335; P:female germline ring canal stabilization; IMP:FlyBase.
DR GO; GO:0036058; P:filtration diaphragm assembly; IMP:FlyBase.
DR GO; GO:0007293; P:germarium-derived egg chamber formation; IMP:FlyBase.
DR GO; GO:0030708; P:germarium-derived female germ-line cyst encapsulation; IMP:FlyBase.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0007616; P:long-term memory; IMP:FlyBase.
DR GO; GO:0016319; P:mushroom body development; IMP:FlyBase.
DR GO; GO:0045886; P:negative regulation of synaptic assembly at neuromuscular junction; IGI:FlyBase.
DR GO; GO:0030717; P:oocyte karyosome formation; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:0007424; P:open tracheal system development; IMP:FlyBase.
DR GO; GO:0030723; P:ovarian fusome organization; IMP:FlyBase.
DR GO; GO:0007300; P:ovarian nurse cell to oocyte transport; IMP:FlyBase.
DR GO; GO:0030046; P:parallel actin filament bundle assembly; IMP:FlyBase.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IGI:FlyBase.
DR GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; IGI:FlyBase.
DR GO; GO:0045743; P:positive regulation of fibroblast growth factor receptor signaling pathway; IMP:FlyBase.
DR GO; GO:0035332; P:positive regulation of hippo signaling; IGI:FlyBase.
DR GO; GO:0045874; P:positive regulation of sevenless signaling pathway; IGI:FlyBase.
DR GO; GO:0120176; P:positive regulation of torso signaling pathway; IGI:FlyBase.
DR GO; GO:0008064; P:regulation of actin polymerization or depolymerization; IMP:FlyBase.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IGI:FlyBase.
DR GO; GO:0007435; P:salivary gland morphogenesis; IMP:FlyBase.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00017; SH2; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00452; SH3DOMAIN.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Developmental protein; Kinase; Nucleotide-binding;
KW Phosphoprotein; Proto-oncogene; Reference proteome; SH2 domain; SH3 domain;
KW Transferase; Tyrosine-protein kinase.
FT CHAIN 1..552
FT /note="Tyrosine-protein kinase Src64B"
FT /id="PRO_0000088140"
FT DOMAIN 95..156
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 162..259
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 284..537
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 404
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 290..298
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 312
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 434
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CONFLICT 102
FT /note="A -> S (in Ref. 1; AAA28913)"
FT /evidence="ECO:0000305"
FT CONFLICT 261..272
FT /note="KPQPQMWDLGPE -> ASLPQTAAPDVGFGPQ (in Ref. 5;
FT AAA28489)"
FT /evidence="ECO:0000305"
FT CONFLICT 286..287
FT /note="LL -> VV (in Ref. 5; AAA28489)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="L -> V (in Ref. 5; AAA28489)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="G -> R (in Ref. 5; AAA28489)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="E -> A (in Ref. 5; AAA28489)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="D -> N (in Ref. 5; AAA28489)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="G -> D (in Ref. 5; AAA28489)"
FT /evidence="ECO:0000305"
FT CONFLICT 384..385
FT /note="IA -> MH (in Ref. 5; AAA28489)"
FT /evidence="ECO:0000305"
FT CONFLICT 389..390
FT /note="AS -> TT (in Ref. 5; AAA28489)"
FT /evidence="ECO:0000305"
FT CONFLICT 393
FT /note="E -> K (in Ref. 5; AAA28489)"
FT /evidence="ECO:0000305"
FT CONFLICT 400
FT /note="L -> V (in Ref. 5; AAA28489)"
FT /evidence="ECO:0000305"
FT CONFLICT 406..407
FT /note="AA -> TT (in Ref. 5; AAA28489)"
FT /evidence="ECO:0000305"
FT CONFLICT 435
FT /note="C -> R (in Ref. 5; AAA28489)"
FT /evidence="ECO:0000305"
FT CONFLICT 460
FT /note="K -> E (in Ref. 6; CAA05754)"
FT /evidence="ECO:0000305"
FT CONFLICT 471
FT /note="M -> T (in Ref. 5; AAA28489)"
FT /evidence="ECO:0000305"
FT CONFLICT 484
FT /note="M -> L (in Ref. 5; AAA28489)"
FT /evidence="ECO:0000305"
FT CONFLICT 507
FT /note="F -> L (in Ref. 5; AAA28489)"
FT /evidence="ECO:0000305"
FT CONFLICT 536
FT /note="F -> L (in Ref. 5; AAA28489)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 552 AA; 63003 MW; 4A63CF4F16562864 CRC64;
MGNKCCSKRQ DQELALAYPT GGYKKSDYTF GQTHINSSGG GNMGGVLGQK HNNGGSLDSR
YTPDPNHRGP LKIGGKGGVD IIRPRTTPTG VPGVVLKRVV VALYDYKSRD ESDLSFMKGD
RMEVIDDTES DWWRVVNLTT RQEGLIPLNF VAEERSVNSE DWFFENVLRK EADKLLLAEE
NPRGTFLVRP SEHNPNGYSL SVKDWEDGRG YHVKHYRIKP LDNGGYYIAT NQTFPSLQAL
VMAYSKNALG LCHILSRPCP KPQPQMWDLG PELRDKYEIP RSEIQLLRKL GRGNFGEVFY
GKWRNSIDVA VKTLREGTMS TAAFLQEAAI MKKFRHNRLV ALYAVCSQEE PIYIVQEYMS
KGSLLDFLRE GDGRYLHFED LIYIATQVAS GMEYLESKQL IHRDLAARNV LIGENNVAKI
CDFGLARVIA DDEYCPKQGS RFPVKWTAPE AIIYGKFSIK SDVWSYGILL MELFTYGQVP
YPGMHSREVI ENIERGFRMP KPTNHYFPDN IYQLLLQCWD AVPEKRPTFE FLNHYFESFS
VTSEVPYREV QD
