ZASP_DROME
ID ZASP_DROME Reviewed; 2194 AA.
AC A1ZA47; A1ZA48; A1ZA49; A8DYF3; B0EW00; Q4V6Y5; Q6NNA6; Q86NZ1; Q8IGJ7;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=PDZ and LIM domain protein Zasp;
DE AltName: Full=Z band alternatively spliced PDZ-motif protein {ECO:0000303|PubMed:18166658};
GN Name=Zasp52; Synonyms=Zasp {ECO:0000312|EMBL:AAZ52806.2}; ORFNames=CG30084;
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] {ECO:0000305, ECO:0000312|EMBL:ABQ18241.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS E AND I), FUNCTION, INTERACTION WITH
RP ACTN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=18166658; DOI=10.1083/jcb.200707045;
RA Jani K., Schock F.;
RT "Zasp is required for the assembly of functional integrin adhesion sites.";
RL J. Cell Biol. 179:1583-1597(2007).
RN [2] {ECO:0000312|EMBL:AAZ52806.2}
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] {ECO:0000305, ECO:0000312|EMBL:AAZ52806.2}
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 [4] {ECO:0000305, ECO:0000312|EMBL:AAN71507.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM E).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAN71507.1};
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 [5] {ECO:0000305, ECO:0000312|EMBL:AAY51565.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM G), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 548-2194 (ISOFORMS C/E/G).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAO39569.1}; TISSUE=Larva, and Pupae;
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 (MAY-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulator of cell matrix adhesion having two related
CC functions, one upstream of Actn organizing the Z line and the other
CC downstream of integrins regulating assembly of integrin adhesion sites.
CC Also required for the formation of myotendinous junctions in muscles.
CC {ECO:0000269|PubMed:18166658}.
CC -!- SUBUNIT: Interacts with alpha-actinin (Actn).
CC {ECO:0000269|PubMed:18166658}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:18166658}. Note=Regulates or strengthens the link
CC of integrins to the actin cytoskeleton. {ECO:0000269|PubMed:18166658}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=F {ECO:0000312|FlyBase:FBgn0265991};
CC IsoId=A1ZA47-1; Sequence=Displayed;
CC Name=C {ECO:0000312|FlyBase:FBgn0265991};
CC IsoId=A1ZA47-3; Sequence=VSP_040045, VSP_040050, VSP_040052;
CC Name=E {ECO:0000312|FlyBase:FBgn0265991}; Synonyms=Enigma
CC {ECO:0000303|PubMed:18166658};
CC IsoId=A1ZA47-4; Sequence=VSP_040043, VSP_040046, VSP_040050,
CC VSP_040052;
CC Name=G {ECO:0000312|FlyBase:FBgn0265991};
CC IsoId=A1ZA47-5; Sequence=VSP_040043, VSP_040050, VSP_040052;
CC Name=I {ECO:0000312|EMBL:ABQ18241.1}; Synonyms=Alp
CC {ECO:0000303|PubMed:18166658};
CC IsoId=A1ZA47-7; Sequence=VSP_040046, VSP_040048, VSP_040051;
CC -!- TISSUE SPECIFICITY: Expression is first detected in the proctodeum and
CC the midgut primordium. In stage 11 embryos, expression is predominant
CC in the leading edge of epidermal cells adjacent to the amnioserosa.
CC Stage 12 embryos exhibit expression in the midgut and the leading edge.
CC Expressed in several rows of germ band cells next to the leading edge
CC at stage 14. Strong expression is visible in the midgut and pharyngeal
CC muscles of stage 17 embryos. Also expressed in somatic muscles and
CC visceral mesoderm. Colocalizes with mys (beta PS integrin) in
CC myotendinous junctions and with Actn in muscle Z lines.
CC {ECO:0000269|PubMed:18166658}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:18166658}.
CC -!- DISRUPTION PHENOTYPE: Fails to form the muscle Z line. At the
CC myotendinous junction, muscles detach with the onset of contractility.
CC {ECO:0000269|PubMed:18166658}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO39569.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; EF221635; ABQ18241.1; -; mRNA.
DR EMBL; AE013599; AAF58107.5; -; Genomic_DNA.
DR EMBL; AE013599; AAM70963.2; -; Genomic_DNA.
DR EMBL; AE013599; AAZ52805.1; -; Genomic_DNA.
DR EMBL; AE013599; AAZ52806.2; -; Genomic_DNA.
DR EMBL; AE013599; ABI31098.1; -; Genomic_DNA.
DR EMBL; BT001752; AAN71507.1; -; mRNA.
DR EMBL; BT003565; AAO39569.1; ALT_SEQ; mRNA.
DR EMBL; BT011386; AAR96178.1; -; mRNA.
DR EMBL; BT022171; AAY51565.1; -; mRNA.
DR RefSeq; NP_001027420.2; NM_001032249.4. [A1ZA47-1]
DR RefSeq; NP_001027421.1; NM_001032250.3. [A1ZA47-4]
DR RefSeq; NP_001036551.1; NM_001043086.3. [A1ZA47-5]
DR RefSeq; NP_611058.4; NM_137214.5.
DR RefSeq; NP_665700.2; NM_145757.3. [A1ZA47-3]
DR AlphaFoldDB; A1ZA47; -.
DR BioGRID; 62468; 39.
DR IntAct; A1ZA47; 5.
DR STRING; 7227.FBpp0099801; -.
DR PaxDb; A1ZA47; -.
DR PRIDE; A1ZA47; -.
DR DNASU; 36740; -.
DR EnsemblMetazoa; FBtr0087315; FBpp0086449; FBgn0265991. [A1ZA47-3]
DR EnsemblMetazoa; FBtr0100387; FBpp0099800; FBgn0265991. [A1ZA47-4]
DR EnsemblMetazoa; FBtr0100388; FBpp0099801; FBgn0265991. [A1ZA47-1]
DR EnsemblMetazoa; FBtr0111048; FBpp0110340; FBgn0265991. [A1ZA47-5]
DR GeneID; 36740; -.
DR KEGG; dme:Dmel_CG30084; -.
DR UCSC; CG30084-RA; d. melanogaster.
DR UCSC; CG30084-RC; d. melanogaster.
DR UCSC; CG30084-RE; d. melanogaster.
DR UCSC; CG30084-RF; d. melanogaster. [A1ZA47-1]
DR UCSC; CG30084-RG; d. melanogaster.
DR UCSC; CG30084-RH; d. melanogaster.
DR CTD; 36740; -.
DR FlyBase; FBgn0265991; Zasp52.
DR VEuPathDB; VectorBase:FBgn0265991; -.
DR eggNOG; KOG1703; Eukaryota.
DR GeneTree; ENSGT00940000168514; -.
DR InParanoid; A1ZA47; -.
DR OMA; HVAFNDE; -.
DR PhylomeDB; A1ZA47; -.
DR SignaLink; A1ZA47; -.
DR BioGRID-ORCS; 36740; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Zasp52; fly.
DR GenomeRNAi; 36740; -.
DR PRO; PR:A1ZA47; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0265991; Expressed in crop (Drosophila) and 40 other tissues.
DR ExpressionAtlas; A1ZA47; baseline and differential.
DR Genevisible; A1ZA47; DM.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0045177; C:apical part of cell; IDA:FlyBase.
DR GO; GO:0045178; C:basal part of cell; IDA:FlyBase.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:FlyBase.
DR GO; GO:0031252; C:cell leading edge; IDA:FlyBase.
DR GO; GO:0031941; C:filamentous actin; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; IDA:FlyBase.
DR GO; GO:0005927; C:muscle tendon junction; IDA:FlyBase.
DR GO; GO:0001725; C:stress fiber; IDA:FlyBase.
DR GO; GO:0030018; C:Z disc; IDA:FlyBase.
DR GO; GO:0005915; C:zonula adherens; IDA:FlyBase.
DR GO; GO:0003779; F:actin binding; IPI:UniProtKB.
DR GO; GO:0042805; F:actinin binding; IPI:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051371; F:muscle alpha-actinin binding; IMP:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0061061; P:muscle structure development; IMP:FlyBase.
DR GO; GO:0030239; P:myofibril assembly; IMP:FlyBase.
DR GO; GO:0001952; P:regulation of cell-matrix adhesion; IMP:UniProtKB.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR031847; DUF4749.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR006643; Zasp-like_motif.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF15936; DUF4749; 1.
DR Pfam; PF00412; LIM; 4.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM00132; LIM; 4.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00735; ZM; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR PROSITE; PS50023; LIM_DOMAIN_2; 4.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoskeleton; LIM domain; Metal-binding;
KW Reference proteome; Repeat; Zinc.
FT CHAIN 1..2194
FT /note="PDZ and LIM domain protein Zasp"
FT /id="PRO_0000401106"
FT DOMAIN 8..90
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 280..339
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 2018..2078
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 2079..2138
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 2139..2194
FT /note="LIM zinc-binding 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 211..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 511..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 580..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 896..940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1223..1260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1297..1322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1550..1632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1646..1738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1815..1837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..549
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..692
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1559..1573
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1585..1632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1646..1671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1672..1690
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1691..1738
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1817..1837
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 217..290
FT /note="AFGNSHYEHDAPQQLQQPQQQYNQHQQHYHQQQQQQQSSTTRHVSAPVNSPK
FT PPSTGGLPTGQNICTECERLIT -> EPHSPANFYWTQSHAIGGNERRTPLHHQHQQPQ
FT QDERIGVPLQSNTLAPEATHRPSLPVAPKDNEEQARQDQQEQPDPRIIVLPICPGLQGP
FT EYKAEMEAAAAALATDQDGRPRPLAASGHPACQLCGVGIV (in isoform E and
FT isoform G)"
FT /evidence="ECO:0000303|PubMed:10731132,
FT ECO:0000303|PubMed:12537569, ECO:0000303|PubMed:18166658,
FT ECO:0000303|Ref.5"
FT /id="VSP_040043"
FT VAR_SEQ 391
FT /note="P -> PPESESSQELPLPPPPSPTQLLQYEAEQQVLPEPHMSTIQQPQQQQK
FT LEHTRTHSSLSSISSGSSSSGVGGSGSGSGSGSGVGQSQQSYSSTLSLDRFGSPLHSRQ
FT TSGSSTSLEVALAAPGAGQGDNYTMTPPSPPPPPPPQAQSVTNYRLQAAQNENDMNTQN
FT KSPNAYNQLLKEYSNKLQQQHHHNTTQHTTATTAPSLKHNNTAKPFAVAATSTPQQHLP
FT HQQHQQQPLVAALTATLANQLKFNPHQ (in isoform C)"
FT /evidence="ECO:0000303|PubMed:10731132"
FT /id="VSP_040045"
FT VAR_SEQ 393..502
FT /note="Missing (in isoform I and isoform E)"
FT /evidence="ECO:0000303|PubMed:10731132,
FT ECO:0000303|PubMed:12537569, ECO:0000303|PubMed:18166658"
FT /id="VSP_040046"
FT VAR_SEQ 552..560
FT /note="GGEAVEELQ -> VGYGYPYTY (in isoform I)"
FT /evidence="ECO:0000303|PubMed:10731132,
FT ECO:0000303|PubMed:18166658"
FT /id="VSP_040048"
FT VAR_SEQ 553..622
FT /note="GEAVEELQPEFEEEDCYEMDIEVALAASRQSQRGSSFTWPPPQDDSHLAPTA
FT APLYIPPPETQHVVVSNP -> RNVRYQQQQQQQQQYNNQQKQQYRNSYPMGSNYSTPS
FT QSPYITSNTNNYSSSNSYNNNNYSNYNNNNVYR (in isoform C, isoform E
FT and isoform G)"
FT /evidence="ECO:0000303|PubMed:10731132,
FT ECO:0000303|PubMed:12537569, ECO:0000303|PubMed:18166658,
FT ECO:0000303|Ref.5"
FT /id="VSP_040050"
FT VAR_SEQ 561..2194
FT /note="Missing (in isoform I)"
FT /evidence="ECO:0000303|PubMed:10731132,
FT ECO:0000303|PubMed:18166658"
FT /id="VSP_040051"
FT VAR_SEQ 623..1984
FT /note="Missing (in isoform C, isoform E and isoform G)"
FT /evidence="ECO:0000303|PubMed:10731132,
FT ECO:0000303|PubMed:12537569, ECO:0000303|PubMed:18166658,
FT ECO:0000303|Ref.5"
FT /id="VSP_040052"
SQ SEQUENCE 2194 AA; 238063 MW; 97A349A08DDC7C8E CRC64;
MAQPQLLQIK LSRFDAQPWG FRLQGGTDFA QPLLVQKVNA GSLSEQAGLQ PGDAVVKIND
VDVFNLRHKD AQDIVVRSGN NFVITVQRGG STWRPHVTPT GNVPQPNSPY LQTVTKTSLA
HKQQDSQHIG CGYNNAARPF SNGGDGGVKS IVNKQYNTPV GIYSDESIAE TLSAQAEVLA
GGVLGVNFKK NEKEYQGDRS EVLKFLREEE TGQSTPAFGN SHYEHDAPQQ LQQPQQQYNQ
HQQHYHQQQQ QQQSSTTRHV SAPVNSPKPP STGGLPTGQN ICTECERLIT GVFVRIKDKN
LHVECFKCAT CGTSLKNQGY YNFNNKLYCD IHAKQAAINN PPTGTEGYVP VPIKPNTKLS
ASTISSALNS HGYGGHSNGY SNGNSTPAPA PVASSQATAT VATVAPSAAT AATAAATPQA
ATATDSPAAT ASSSDNMSAY VADEPSSIYG QISAESVALA PPPPQPPTAG GGDQPFEYVT
LTGNVIRSVQ APGKGACPSY KVNQGYARPF GAAAPKSPVS YPPQQQQQSP RPAPGGQNPY
ATLPRSNVGQ QGGEAVEELQ PEFEEEDCYE MDIEVALAAS RQSQRGSSFT WPPPQDDSHL
APTAAPLYIP PPETQHVVVS NPVQQVPPLP PGGATARLDP QPVVGTSANG APQWQSYSAP
QLTTASARQL AEQESSSDSY TSTSTTTTTT SEEYQRMYAA QVQAYQMQEQ SGSEFDYQVD
YASTQDSVQD YPSGRRSAQE CVDSLAVPLS TYKLVDMVRE VTPSPVTTPT QTPAPAAPTT
RRVVFNDEPE IKELPQLPAE LETIPEASEA VEDREGLVIE QRCQILESER KFQPTPEIKI
EIAPVRQIPP TKIPNPMPKE WINPMIRVLT TAPEVPFHLV ECPFPRPCGD DFEAEAAAAE
AAKTQEVPEP LPPQVSAAPP ATVSVEPSPA PLRESPPRGS RLSQAMVTAP EFELKFAPPA
DQGIPLPEET EPYMPPPIDT KPYLREDYRP KSPFVSALTT APDRPFEGHF DKDVPIHMID
LPTPKEHLSM CDALCTAPER GYTPLNPENA MHRVDEEQKQ QELKKREFQV LDHEEELGIR
PEPPQSVEYY ETRRDQPRKS SAFAAMQAFQ PSREPLSSNT VSNAGSVADT PRASIVSALK
EETDLEYQKY LKAQQRNQKR LDYFHQKEEE LSGLQGQQLT QLQRELSNQQ QNLLSQQQLQ
QSKLLQLQQC VQSQELQQQV QHLTQKSQQQ PPQANQQQQQ QQQQRGTQQQ QHSQVTQRTQ
QQQQQVPQQV TQQQQQEHSL LSQTTLAETQ TLQANAQSQS SASYSSKATA CSNSSSTVPP
ANTSTAFAPA PAPAPTSIPV RPSAIAVQSS YCSSQFDVHE LIEETAEELE HSEVLFPPPS
PLSHLTKQGK AVQSGLHKAD SIPKYQRNWT VLPTQSPIRT PEPQELRENV PLAFVDAPKA
PVTSDSSTVH RPIAQVAAPT TVVAPSRERE KERRPQLSVP IIVEDRSGPV TMAFQPLDEL
VRPDQALTPT RPYTPSLTNK PAPIVPFYQT EEKLVFEECS ATHARNYNEL NASPFPDRTR
SPAPGPPPNP LNAIRAPRMK EPETKSNILS VSGGPRLQTG SITTGQSYQG QLLAHSEQSS
QSASQSYNQQ PERITEQRVG NLNIQQREQS SQLQQQAQSQ TQSQTRSQVG NTQIERRRKV
TEEFERTQSA KTIEIRTGSQ SVSQSKAQSQ SISQAQTQAQ SQSQNQSDTE RRSSYGKTGF
VASQAKRLSC MEEEISSLTS QSQAISARAS ALGEGCFPNL RSPTFDSKFP LKPAPAESIV
PGYATVPAAT KMLTAPPPGF LQQQQQQQQR SAFSGYQATT SSVQQSSFAS SSKATTSSLS
SSSASASASA SVARSSQSLT QASAITTTTN NQATTAYRSS NGSITKPNLA SRPSIASITA
PGSASAPAPV PSAAPTKATA PFKAPIVPKS VIANAVNAAA PPAPAVFPPD LSDLNLNSNV
DNSPGAGGKS AGAFGATSAP KRGRGILNKA AGPGVRIPLC NSCNVQIRGP FITALGRIWC
PDHFICVNGN CRRPLQDIGF VEEKGDLYCE YCFEKYLAPT CSKCAGKIKG DCLNAIGKHF
HPECFTCGQC GKIFGNRPFF LEDGNAYCEA DWNELFTTKC FACGFPVEAG DRWVEALNHN
YHSQCFNCTF CKQNLEGQSF YNKGGRPFCK NHAR
