CSKP_DROME
ID CSKP_DROME Reviewed; 898 AA.
AC Q24210; B5X553; Q24272; Q86P03; Q86P17; Q8SX09; Q9VD77; Q9VD78; Q9VD79;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2003, sequence version 4.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Peripheral plasma membrane protein CASK;
DE Short=dCASK;
DE EC=2.7.11.17;
DE AltName: Full=Calcium/calmodulin-dependent protein kinase;
DE Short=CAKI;
DE Short=Camguk;
GN Name=CASK; Synonyms=Caki, cmg; ORFNames=CG6703;
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).
RC STRAIN=Oregon-R;
RX PubMed=9178262; DOI=10.1016/s0925-4773(97)00668-0;
RA Dimitratos S.D., Woods D.F., Bryant P.J.;
RT "Camguk, Lin-2, and CASK: novel membrane-associated guanylate kinase
RT homologs that also contain CaM kinase domains.";
RL Mech. Dev. 63:127-130(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), AND TISSUE SPECIFICITY.
RC TISSUE=Embryo;
RX PubMed=8617233; DOI=10.1002/j.1460-2075.1996.tb00537.x;
RA Martin J.-R., Ollo R.;
RT "A new Drosophila Ca2+/calmodulin-dependent protein kinase (Caki) is
RT localized in the central nervous system and implicated in walking speed.";
RL EMBO J. 15:1865-1876(1996).
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, and Head;
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 B).
RC STRAIN=Berkeley; TISSUE=Embryo, and Head;
RA Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, AND INTERACTION WITH CAMKII.
RX PubMed=14687552; DOI=10.1016/s0896-6273(03)00786-4;
RA Lu C.S., Hodge J.J., Mehren J., Sun X.X., Griffith L.C.;
RT "Regulation of the Ca2+/CaM-responsive pool of CaMKII by scaffold-dependent
RT autophosphorylation.";
RL Neuron 40:1185-1197(2003).
RN [8]
RP FUNCTION, INTERACTION WITH EAG, AND SUBCELLULAR LOCATION.
RX PubMed=15901771; DOI=10.1523/jneurosci.4566-04.2005;
RA Marble D.D., Hegle A.P., Snyder E.D. II, Dimitratos S., Bryant P.J.,
RA Wilson G.F.;
RT "Camguk/CASK enhances Ether-a-go-go potassium current by a phosphorylation-
RT dependent mechanism.";
RL J. Neurosci. 25:4898-4907(2005).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16880127; DOI=10.1016/j.neuron.2006.06.020;
RA Hodge J.J., Mullasseril P., Griffith L.C.;
RT "Activity-dependent gating of CaMKII autonomous activity by Drosophila
RT CASK.";
RL Neuron 51:327-337(2006).
CC -!- FUNCTION: May regulate transmembrane proteins that bind calcium,
CC calmodulin, or nucleotides. Functionally modulates eag potassium
CC channels; increases eag current and whole-cell conductance. Also
CC regulates autophosphorylation of CaMKII. {ECO:0000269|PubMed:14687552,
CC ECO:0000269|PubMed:15901771, ECO:0000269|PubMed:16880127}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.17;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.17;
CC -!- SUBUNIT: Interacts with eag. Interacts with CaMKII.
CC {ECO:0000269|PubMed:14687552, ECO:0000269|PubMed:15901771}.
CC -!- INTERACTION:
CC Q24210; Q00168: CaMKII; NbExp=5; IntAct=EBI-214423, EBI-124595;
CC Q24210; Q9W2A3: Dmel\CG13501; NbExp=4; IntAct=EBI-214423, EBI-96532;
CC Q24210; Q02280: eag; NbExp=10; IntAct=EBI-214423, EBI-85304;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15901771};
CC Peripheral membrane protein {ECO:0000269|PubMed:15901771}. Note=Eag
CC recruits CASK to the plasma membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=B;
CC IsoId=Q24210-3; Sequence=Displayed;
CC Name=A;
CC IsoId=Q24210-2; Sequence=VSP_008088, VSP_008089, VSP_008090;
CC Name=G;
CC IsoId=Q24210-4; Sequence=VSP_008088, VSP_008089, VSP_008090,
CC VSP_041854;
CC -!- TISSUE SPECIFICITY: During embryogenesis, larval and pupal life, found
CC almost exclusively in the central nervous system. In the adult head
CC found in the lamina, the neuropil of the medulla, lobula, lobula plate
CC and in the central brain. {ECO:0000269|PubMed:8617233}.
CC -!- DISRUPTION PHENOTYPE: Increases synapse-specific, activity-dependent
CC autophosphorylation of CaMKII Thr-287. {ECO:0000269|PubMed:16880127}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the protein kinase
CC superfamily. CAMK Ser/Thr protein kinase family. CaMK subfamily.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM11269.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC Sequence=AAO39536.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA63940.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U53190; AAC80169.1; -; mRNA.
DR EMBL; X94264; CAA63940.1; ALT_FRAME; mRNA.
DR EMBL; AE014297; AAF55920.3; -; Genomic_DNA.
DR EMBL; AE014297; AAF55921.2; -; Genomic_DNA.
DR EMBL; AE014297; AAF55922.2; -; Genomic_DNA.
DR EMBL; AY094916; AAM11269.1; ALT_SEQ; mRNA.
DR EMBL; BT003532; AAO39536.1; ALT_FRAME; mRNA.
DR EMBL; BT003550; AAO39554.1; -; mRNA.
DR EMBL; BT046172; ACI49771.1; -; mRNA.
DR PIR; S69210; S69210.
DR RefSeq; NP_001097862.1; NM_001104392.3. [Q24210-2]
DR RefSeq; NP_524441.2; NM_079717.4. [Q24210-3]
DR RefSeq; NP_732661.1; NM_169970.2. [Q24210-2]
DR RefSeq; NP_732662.2; NM_169971.3. [Q24210-4]
DR AlphaFoldDB; Q24210; -.
DR SMR; Q24210; -.
DR BioGRID; 67530; 14.
DR DIP; DIP-19769N; -.
DR IntAct; Q24210; 23.
DR STRING; 7227.FBpp0290542; -.
DR TCDB; 8.A.24.1.11; the ezrin/radixin/moesin-binding phosphoprotein 50 (ebp50) family.
DR PaxDb; Q24210; -.
DR PRIDE; Q24210; -.
DR DNASU; 42567; -.
DR EnsemblMetazoa; FBtr0084161; FBpp0083559; FBgn0013759. [Q24210-3]
DR EnsemblMetazoa; FBtr0084162; FBpp0083560; FBgn0013759. [Q24210-2]
DR EnsemblMetazoa; FBtr0112872; FBpp0111785; FBgn0013759. [Q24210-2]
DR EnsemblMetazoa; FBtr0301328; FBpp0290543; FBgn0013759. [Q24210-4]
DR GeneID; 42567; -.
DR KEGG; dme:Dmel_CG6703; -.
DR CTD; 8573; -.
DR FlyBase; FBgn0013759; CASK.
DR VEuPathDB; VectorBase:FBgn0013759; -.
DR eggNOG; KOG0033; Eukaryota.
DR eggNOG; KOG0609; Eukaryota.
DR GeneTree; ENSGT00940000169045; -.
DR HOGENOM; CLU_001715_5_3_1; -.
DR InParanoid; Q24210; -.
DR PhylomeDB; Q24210; -.
DR BRENDA; 2.7.11.17; 1994.
DR Reactome; R-DME-212676; Dopamine Neurotransmitter Release Cycle.
DR Reactome; R-DME-6794361; Neurexins and neuroligins.
DR SignaLink; Q24210; -.
DR BioGRID-ORCS; 42567; 0 hits in 3 CRISPR screens.
DR ChiTaRS; CASK; fly.
DR GenomeRNAi; 42567; -.
DR PRO; PR:Q24210; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0013759; Expressed in brain and 40 other tissues.
DR ExpressionAtlas; Q24210; baseline and differential.
DR Genevisible; Q24210; DM.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0031594; C:neuromuscular junction; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0061174; C:type I terminal bouton; IDA:BHF-UCL.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0042043; F:neurexin family protein binding; IPI:BHF-UCL.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:FlyBase.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0008344; P:adult locomotory behavior; IMP:FlyBase.
DR GO; GO:0007628; P:adult walking behavior; IMP:FlyBase.
DR GO; GO:0007615; P:anesthesia-resistant memory; IMP:FlyBase.
DR GO; GO:0048149; P:behavioral response to ethanol; IMP:FlyBase.
DR GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
DR GO; GO:0040011; P:locomotion; IMP:BHF-UCL.
DR GO; GO:0007616; P:long-term memory; IMP:FlyBase.
DR GO; GO:0008049; P:male courtship behavior; IMP:FlyBase.
DR GO; GO:0072375; P:medium-term memory; IMP:FlyBase.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:BHF-UCL.
DR GO; GO:0007269; P:neurotransmitter secretion; NAS:FlyBase.
DR GO; GO:1900244; P:positive regulation of synaptic vesicle endocytosis; IMP:FlyBase.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0040012; P:regulation of locomotion; IMP:FlyBase.
DR GO; GO:1900073; P:regulation of neuromuscular synaptic transmission; IMP:FlyBase.
DR GO; GO:0046928; P:regulation of neurotransmitter secretion; IDA:FlyBase.
DR GO; GO:0008582; P:regulation of synaptic assembly at neuromuscular junction; IMP:FlyBase.
DR GO; GO:2000331; P:regulation of terminal button organization; IMP:BHF-UCL.
DR GO; GO:0016081; P:synaptic vesicle docking; NAS:FlyBase.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IMP:BHF-UCL.
DR GO; GO:0016080; P:synaptic vesicle targeting; NAS:FlyBase.
DR CDD; cd12081; SH3_CASK; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR035473; CASK_SH3.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR020590; Guanylate_kinase_CS.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR014775; L27_C.
DR InterPro; IPR004172; L27_dom.
DR InterPro; IPR036892; L27_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF02828; L27; 2.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00569; L27; 2.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF101288; SSF101288; 2.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR PROSITE; PS51022; L27; 2.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Calmodulin-binding; Cell membrane;
KW Kinase; Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Repeat; Serine/threonine-protein kinase; SH3 domain; Transferase.
FT CHAIN 1..898
FT /note="Peripheral plasma membrane protein CASK"
FT /id="PRO_0000094571"
FT DOMAIN 12..278
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 343..397
FT /note="L27 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365"
FT DOMAIN 402..461
FT /note="L27 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365"
FT DOMAIN 495..576
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 582..651
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 711..883
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT REGION 306..316
FT /note="Calmodulin-binding"
FT ACT_SITE 141
FT /evidence="ECO:0000250"
FT BINDING 18..26
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 292
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..317
FT /note="Missing (in isoform A and isoform G)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_008088"
FT VAR_SEQ 318..443
FT /note="MDPLYATDADMPITGATDEWADEEAGIEAVQRILDCLDDIYSLQDAHVDADV
FT LRDMLRDNRLHQFLQLFDRIAATVVTSNGRAPAAEAVGRCRDVLEQLSSTSGGNSLGGK
FT YAKEELMRLLAAPHM -> MCQHHGLTSQSLMSGGSHISLLGSSGSSGMSGSGVGSSGQ
FT SVPQCPAAVAAADAAMMGSNAGGHCRSLSGLSSISIPPPPPALFNPCSSALSLQQAAVT
FT RWGPRTSCPVHSPFRVRVPNGSICSGH (in isoform A and isoform G)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_008089"
FT VAR_SEQ 584
FT /note="E -> ELFRIRPAPVL (in isoform A and isoform G)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_008090"
FT VAR_SEQ 663
FT /note="Q -> QGEPGAGCSAHADGCDGSA (in isoform G)"
FT /evidence="ECO:0000305"
FT /id="VSP_041854"
FT CONFLICT 7
FT /note="L -> V (in Ref. 1; AAC80169)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="D -> E (in Ref. 1; AAC80169)"
FT /evidence="ECO:0000305"
FT CONFLICT 463
FT /note="L -> A (in Ref. 1; AAC80169)"
FT /evidence="ECO:0000305"
FT CONFLICT 465..477
FT /note="VTPPPMVPYLNGD -> HPAPDGALPQWR (in Ref. 1; AAC80169)"
FT /evidence="ECO:0000305"
FT CONFLICT 497
FT /note="Q -> H (in Ref. 1; AAC80169)"
FT /evidence="ECO:0000305"
FT CONFLICT 523
FT /note="I -> L (in Ref. 1; AAC80169)"
FT /evidence="ECO:0000305"
FT CONFLICT 632
FT /note="D -> G (in Ref. 1; AAC80169)"
FT /evidence="ECO:0000305"
FT CONFLICT 740
FT /note="A -> V (in Ref. 1; AAC80169)"
FT /evidence="ECO:0000305"
FT CONFLICT 759
FT /note="S -> N (in Ref. 5; AAO39554)"
FT /evidence="ECO:0000305"
FT CONFLICT 886..892
FT /note="HTTPQWV -> DIPPRSGC (in Ref. 2; CAA63940)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 898 AA; 100911 MW; 5B16014EC66E0E9B CRC64;
MTEDEILFDD VYELCEVIGK GPFSIVRRCI HRESNQQFAV KIVDVAKFTA SPGLSTADLK
REATICHMLK HPHIVELLET YSSEGMLYMV FEFMEGSDLC FEVVRRAVAG FVYSEAVACH
YMRQILEALR YCHENDILHR DVRPACALLA TVDNSAPVKL GGFGSAIQLP GTRETIETHG
RVGCPHYMAP EVVTRRLYGK GCDVWGAGVM LHVLLSGRLP FLGSGVRLQQ SVARGRLSFE
APEWKSISAN AKDLVMKMLA ANPHHRLSIT EVLDHPWIRD RDKLQRTHLA DTVEELKRYN
ARRKLKGAVQ AIAGGTNMDP LYATDADMPI TGATDEWADE EAGIEAVQRI LDCLDDIYSL
QDAHVDADVL RDMLRDNRLH QFLQLFDRIA ATVVTSNGRA PAAEAVGRCR DVLEQLSSTS
GGNSLGGKYA KEELMRLLAA PHMQALLHSH DVVARDVYGE EALRVTPPPM VPYLNGDELD
NVEGGELQHV TRVRLVQFQK NTDEPMGITL KMTEDGRCIV ARIMHGGMIH RQATLHVGDE
IREINGQPVQ HQSVGQLQRM LREARGSVTF KIVPSYRSAP PPCEIFVRAQ FDYNPLDDEL
IPCAQAGISF QVGDILQIIS KDDHHWWQAR LDTVGGSAGL IPSPELQEWR IACQTVDKTK
QEQVNCSIFG RKKKQCRDKY LAKHNAIFDT LDVVTYEEVV KVPVGDPNFQ RKTLVLLGAH
GVGRRHIKNT LISKYPDKYA YPIPHTTRPA KPEEENGRSY YFVSHDEMMA DIGANEYLEY
GTHEDAMYGT KLDTIRRIHT EGKMAILDVE PQALKILRTA EFTPYVVFIA APSLQNIADY
DGSLERLAKE SEMLRQLYGH FFDLTIVNND ISETIATLET AIDRVHTTPQ WVPVSWLY
