BTKL_DROME
ID BTKL_DROME Reviewed; 786 AA.
AC P08630; A4V0F3; A4V0F4; O45032; O76132; O76133; P11361; Q6NNV0; Q8T0A0;
AC Q9VLQ2; Q9VLQ3;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 229.
DE RecName: Full=Tyrosine-protein kinase Btk29A;
DE EC=2.7.10.2;
DE AltName: Full=Dsrc28C;
DE AltName: Full=Dsrc29a;
GN Name=Btk29A; Synonyms=Src2, Src29A, Tec29; ORFNames=CG8049;
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 A), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=3110602; DOI=10.1128/mcb.7.6.2119-2127.1987;
RA Gregory R.J., Kammermeyer K.L., Vincent W.S. III, Wadsworth S.G.;
RT "Primary sequence and developmental expression of a novel Drosophila
RT melanogaster src gene.";
RL Mol. Cell. Biol. 7:2119-2127(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), FUNCTION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RC STRAIN=Canton-S, and Oregon-R; TISSUE=Head;
RX PubMed=10330180; DOI=10.1128/mcb.19.6.4405;
RA Baba K., Takeshita A., Majima K., Ueda R., Kondo S., Juni N., Yamamoto D.;
RT "The Drosophila Bruton's tyrosine kinase (Btk) homolog is required for
RT adult survival and male genital formation.";
RL Mol. Cell. Biol. 19:4405-4413(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 [LARGE SCALE MRNA] (ISOFORMS A AND B).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 199-786 (ISOFORM A).
RC TISSUE=Eye-antennal disk;
RX PubMed=9660966; DOI=10.1016/s1097-2765(00)80082-9;
RA Guarnieri D.J., Dodson G.S., Simon M.A.;
RT "SRC64 regulates the localization of a Tec-family kinase required for
RT Drosophila ring canal growth.";
RL Mol. Cell 1:831-840(1998).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 552-684.
RX PubMed=3923437; DOI=10.1093/nar/13.6.2153;
RA Wadsworth S.C., Madhavan K., Bilodeau-Wentworth D.;
RT "Maternal inheritance of transcripts from three Drosophila src-related
RT genes.";
RL Nucleic Acids Res. 13:2153-2170(1985).
RN [9]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=9655810; DOI=10.1242/dev.125.15.2883;
RA Dodson G.S., Guarnieri D.J., Simon M.A.;
RT "Src64 is required for ovarian ring canal morphogenesis during Drosophila
RT oogenesis.";
RL Development 125:2883-2892(1998).
RN [10]
RP SIMILARITY TO BTK SUBFAMILY.
RA Sjolander K.;
RL Unpublished observations (JUL-1997).
CC -!- FUNCTION: Required for proper ring canal development. Also required for
CC the development of male genitalia and for adult survival.
CC {ECO:0000269|PubMed:10330180, ECO:0000269|PubMed:9655810}.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Note=Ring canals.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B; Synonyms=D, E, Type 2;
CC IsoId=P08630-1; Sequence=Displayed;
CC Name=A; Synonyms=C, F, Type 1;
CC IsoId=P08630-2; Sequence=VSP_004964, VSP_004965;
CC -!- TISSUE SPECIFICITY: Ring canals in the egg chambers and imaginal disks
CC of third-instar larvae. {ECO:0000269|PubMed:10330180,
CC ECO:0000269|PubMed:3110602, ECO:0000269|PubMed:9655810}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Predominantly in early to middle embryogenesis, in larvae and adult
CC females. {ECO:0000269|PubMed:10330180, ECO:0000269|PubMed:3110602}.
CC -!- DISRUPTION PHENOTYPE: Flies exhibit shortened copulatory duration (due
CC to incomplete fusion of the left and right halves of the apodeme that
CC holds the penis during copulation) and reduced adult-stage life span.
CC {ECO:0000269|PubMed:10330180}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. TEC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA28912.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M16599; AAA28912.1; ALT_FRAME; mRNA.
DR EMBL; AB009840; BAA24063.1; -; mRNA.
DR EMBL; AB009841; BAA24064.1; -; mRNA.
DR EMBL; AE014134; AAF52631.3; -; Genomic_DNA.
DR EMBL; AE014134; AAF52632.2; -; Genomic_DNA.
DR EMBL; AE014134; AAN11161.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN11162.1; -; Genomic_DNA.
DR EMBL; AE014134; ABV53648.1; -; Genomic_DNA.
DR EMBL; AE014134; ABV53649.1; -; Genomic_DNA.
DR EMBL; AY069457; AAL39602.1; -; mRNA.
DR EMBL; AY128441; AAM75034.1; -; mRNA.
DR EMBL; BT011183; AAR88544.1; -; mRNA.
DR EMBL; AF044337; AAB99858.1; -; mRNA.
DR EMBL; X02305; CAA26170.1; -; Genomic_DNA.
DR PIR; A23051; A23051.
DR PIR; A27807; TVFFDS.
DR RefSeq; NP_001097120.1; NM_001103650.2. [P08630-2]
DR RefSeq; NP_001097121.1; NM_001103651.3. [P08630-1]
DR RefSeq; NP_476745.1; NM_057397.6. [P08630-1]
DR RefSeq; NP_476746.1; NM_057398.4. [P08630-2]
DR RefSeq; NP_723369.1; NM_164804.2. [P08630-1]
DR RefSeq; NP_723370.1; NM_164805.2. [P08630-2]
DR AlphaFoldDB; P08630; -.
DR SMR; P08630; -.
DR BioGRID; 60259; 26.
DR DIP; DIP-23748N; -.
DR IntAct; P08630; 1.
DR STRING; 7227.FBpp0079237; -.
DR iPTMnet; P08630; -.
DR PaxDb; P08630; -.
DR PRIDE; P08630; -.
DR DNASU; 34132; -.
DR EnsemblMetazoa; FBtr0079615; FBpp0079235; FBgn0003502. [P08630-2]
DR EnsemblMetazoa; FBtr0079616; FBpp0079236; FBgn0003502. [P08630-1]
DR EnsemblMetazoa; FBtr0079617; FBpp0079237; FBgn0003502. [P08630-1]
DR EnsemblMetazoa; FBtr0079618; FBpp0079238; FBgn0003502. [P08630-2]
DR EnsemblMetazoa; FBtr0112835; FBpp0111748; FBgn0003502. [P08630-2]
DR EnsemblMetazoa; FBtr0112836; FBpp0111749; FBgn0003502. [P08630-1]
DR GeneID; 34132; -.
DR KEGG; dme:Dmel_CG8049; -.
DR CTD; 34132; -.
DR FlyBase; FBgn0003502; Btk29A.
DR VEuPathDB; VectorBase:FBgn0003502; -.
DR eggNOG; KOG0197; Eukaryota.
DR GeneTree; ENSGT00940000170881; -.
DR InParanoid; P08630; -.
DR PhylomeDB; P08630; -.
DR Reactome; R-DME-111465; Apoptotic cleavage of cellular proteins.
DR Reactome; R-DME-2424491; DAP12 signaling.
DR Reactome; R-DME-2871809; FCERI mediated Ca+2 mobilization.
DR Reactome; R-DME-416476; G alpha (q) signalling events.
DR Reactome; R-DME-416482; G alpha (12/13) signalling events.
DR Reactome; R-DME-512988; Interleukin-3, Interleukin-5 and GM-CSF signaling.
DR Reactome; R-DME-8964315; G beta:gamma signalling through BTK.
DR SignaLink; P08630; -.
DR BioGRID-ORCS; 34132; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Btk29A; fly.
DR GenomeRNAi; 34132; -.
DR PRO; PR:P08630; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0003502; Expressed in cleaving embryo and 83 other tissues.
DR ExpressionAtlas; P08630; baseline and differential.
DR Genevisible; P08630; DM.
DR GO; GO:0045177; C:apical part of cell; IDA:FlyBase.
DR GO; GO:0071944; C:cell periphery; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0045172; C:germline ring canal; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA:FlyBase.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:FlyBase.
DR GO; GO:0007349; P:cellularization; IMP:FlyBase.
DR GO; GO:0007619; P:courtship behavior; NAS:FlyBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:UniProtKB.
DR GO; GO:0042023; P:DNA endoreduplication; IMP:FlyBase.
DR GO; GO:0007391; P:dorsal closure; TAS:FlyBase.
DR GO; GO:0007301; P:female germline ring canal formation; IDA:UniProtKB.
DR GO; GO:0008258; P:head involution; IMP:FlyBase.
DR GO; GO:0007485; P:imaginal disc-derived male genitalia development; IMP:UniProtKB.
DR GO; GO:0007254; P:JNK cascade; TAS: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:0018108; P:peptidyl-tyrosine phosphorylation; IDA:FlyBase.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IMP:FlyBase.
DR GO; GO:0007435; P:salivary gland morphogenesis; IMP:FlyBase.
DR GO; GO:0046960; P:sensitization; IMP:FlyBase.
DR GO; GO:0035277; P:spiracle morphogenesis, open tracheal system; IMP:FlyBase.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
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 InterPro; IPR001562; Znf_Btk_motif.
DR Pfam; PF00779; BTK; 1.
DR Pfam; PF00169; PH; 1.
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; PR00109; TYRKINASE.
DR SMART; SM00233; PH; 1.
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; PS50003; PH_DOMAIN; 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.
DR PROSITE; PS51113; ZF_BTK; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Kinase; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Proto-oncogene; Reference proteome;
KW SH2 domain; SH3 domain; Transferase; Tyrosine-protein kinase; Zinc;
KW Zinc-finger.
FT CHAIN 1..786
FT /note="Tyrosine-protein kinase Btk29A"
FT /id="PRO_0000088068"
FT DOMAIN 41..184
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 342..402
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 410..503
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 526..779
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ZN_FING 187..223
FT /note="Btk-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 647
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT BINDING 206
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT BINDING 217
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT BINDING 532..540
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 554
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 677
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..183
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000303|PubMed:10330180,
FT ECO:0000303|PubMed:12537569, ECO:0000303|PubMed:3110602,
FT ECO:0000303|PubMed:9660966, ECO:0000303|Ref.6"
FT /id="VSP_004964"
FT VAR_SEQ 184..231
FT /note="EDSNTPKSYRYHPGLWSGKKWSCCKGLSRTTFGCRAAAHWREANNNPS ->
FT MIPCVSLAETSVIGNMKERVKEMKVFGCRLNFWNHIGHSLTSSKTKEG (in
FT isoform A)"
FT /evidence="ECO:0000303|PubMed:10330180,
FT ECO:0000303|PubMed:12537569, ECO:0000303|PubMed:3110602,
FT ECO:0000303|PubMed:9660966, ECO:0000303|Ref.6"
FT /id="VSP_004965"
FT CONFLICT 243
FT /note="S -> A (in Ref. 1; AAA28912)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="T -> N (in Ref. 1; AAA28912 and 2; BAA24063/
FT BAA24064)"
FT /evidence="ECO:0000305"
FT CONFLICT 352..353
FT /note="PF -> LG (in Ref. 1; AAA28912)"
FT /evidence="ECO:0000305"
FT CONFLICT 363
FT /note="L -> VG (in Ref. 1; AAA28912)"
FT /evidence="ECO:0000305"
FT CONFLICT 398..400
FT /note="KPK -> QAE (in Ref. 1; AAA28912)"
FT /evidence="ECO:0000305"
FT CONFLICT 414
FT /note="D -> Y (in Ref. 1; AAA28912)"
FT /evidence="ECO:0000305"
FT CONFLICT 524..525
FT /note="ME -> IQ (in Ref. 1; AAA28912)"
FT /evidence="ECO:0000305"
FT CONFLICT 589
FT /note="S -> T (in Ref. 1; AAA28912 and 7; CAA26170)"
FT /evidence="ECO:0000305"
FT CONFLICT 657
FT /note="S -> F (in Ref. 7; CAA26170)"
FT /evidence="ECO:0000305"
FT CONFLICT 681..684
FT /note="GGTK -> AEPS (in Ref. 7; CAA26170)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 786 AA; 87392 MW; E2BCE122E6AAA0AA CRC64;
MMGTKHRNSH VNGSIKSSSS LRSSSKSFQA KMDLMSERLY DVVKSGSMVK RAQNKKRFTP
VNYKHRWFEL TKRTFSYFDV ENVERRRERG RIHLKGVRLV EEATVSGEGG DPFAPDGYPF
QVGYCEISAS ANSHQLENGN GGGSGVGIEG QQSGRAVPQY TLYVIANSEK ERSEWIRAIR
QVCEDSNTPK SYRYHPGLWS GKKWSCCKGL SRTTFGCRAA AHWREANNNP SNGSSPAQNS
TRSISPNSST TNSQFSLQHN SSGSLGGGVG GGLGGGGSLG LGGGGGGGGS CTPTSLQPQS
SLTTFKQSPT LLNGNGTLLD ANMPGGIPTP GTPNSKAKDN SHFVKLVVAL YPFKAIEGGD
LSLEKNAEYE VIDDSQEHWW KVKDALGNVG YIPSNYVKPK ALLGLERYEW YVGDMSRQRA
ESLLKQGDKE GCFVVRKSST KGLYTLSLHT KVPQSHVKHY HIKQNARCEY YLSEKHCCET
IPDLINYHRH NSGGLACRLK SSPCDRPVPP TAGLSHDKWE IHPMELMLME ELGSGQFGVV
RRGKWRGSID TAVKMMKEGT MSEDDFIEEA KVMTKLQHPN LVQLYGVCSK HRPIYIVTEY
MKHGSLLNYL RRHEKTLIGN MGLLLDMCIQ VSKGMTYLER HNYIHRDLAA RNCLVGSENV
VKVADFGLAR YVLDDQYTSS GGTKFPIKWA PPEVLNYTRF SSKSDVWAYG VLMWEIFTCG
KMPYGRLKNT EVVERVQRGI ILEKPKSCAK EIYDVMKLCW SHGPEERPAF RVLMDQLALV
AQTLTD
