DYIN_DROME
ID DYIN_DROME Reviewed; 663 AA.
AC Q24246; O96508; O96510; O96511; O96512; O96513; O96514; O96515; O96516;
AC Q5U0Z1; Q86BQ5; Q9NG49; Q9TZR7; Q9TZR8; Q9TZR9; Q9TZS0; Q9VR78;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 03-JUL-2003, sequence version 3.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Cytoplasmic dynein 1 intermediate chain;
DE Short=DH IC;
DE AltName: Full=Dynein intermediate chain, cytosolic;
DE AltName: Full=Protein short wing;
GN Name=sw; Synonyms=Cdic, Dic19B; ORFNames=CG18000;
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 [GENOMIC DNA / MRNA] (ISOFORMS 1A; 1B; 1C; 2A; 2B; 2C;
RP 3A; 3B; 4; 5A AND 5B), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Ovary;
RX PubMed=9774695; DOI=10.1128/mcb.18.11.6816;
RA Nurminsky D.I., Nurminskaya M.V., Benevolenskaya E.V., Shevelyov Y.Y.,
RA Hartl D.L., Gvozdev V.A.;
RT "Cytoplasmic dynein intermediate-chain isoforms with different targeting
RT properties created by tissue-specific alternative splicing.";
RL Mol. Cell. Biol. 18:6816-6825(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2B), FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Ovary;
RX PubMed=11071907; DOI=10.1091/mbc.11.11.3791;
RA Boylan K., Serr M., Hays T.S.;
RT "A molecular genetic analysis of the interaction between the cytoplasmic
RT dynein intermediate chain and the glued (Dynactin) complex.";
RL Mol. Biol. Cell 11:3791-3803(2000).
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] (ISOFORM 1B).
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 101-663 (ISOFORM 4).
RC STRAIN=GT WA;
RA Benevolenskaya E.V., Gvozdev V.A.;
RT "Cluster of tandem repeats in Drosophila genome comprising putative genes
RT encoding cytoplasmic dynein intermediate chain and 3'-part of annexin X.";
RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as one of several non-catalytic accessory components of
CC the cytoplasmic dynein 1 complex that are thought to be involved in
CC linking dynein to cargos and to adapter proteins that regulate dynein
CC function. Cytoplasmic dynein 1 acts as a motor for the intracellular
CC retrograde motility of vesicles and organelles along microtubules. The
CC intermediate chains mediate the help dynein bind to dynactin 150 kDa
CC component (By similarity). {ECO:0000250, ECO:0000269|PubMed:11071907}.
CC -!- SUBUNIT: Homodimer. The cytoplasmic dynein 1 complex consists of two
CC catalytic heavy chains (HCs) and a number of non-catalytic subunits
CC presented by intermediate chains (ICs), light intermediate chains
CC (LICs) and light chains (LCs). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:9774695}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2c]: Lysosome membrane; Peripheral
CC membrane protein; Cytoplasmic side. Note=Aggregates in cytoplasm around
CC lysosomes.
CC -!- SUBCELLULAR LOCATION: [Isoform 2a]: Nucleus membrane; Peripheral
CC membrane protein; Cytoplasmic side. Note=Aggregates in cytoplasm around
CC the nucleus.
CC -!- SUBCELLULAR LOCATION: [Isoform 2b]: Nucleus membrane; Peripheral
CC membrane protein; Cytoplasmic side. Note=Aggregates in cytoplasm around
CC the nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=11;
CC Name=5a; Synonyms=J;
CC IsoId=Q24246-11; Sequence=Displayed;
CC Name=1a; Synonyms=A;
CC IsoId=Q24246-2; Sequence=VSP_001345;
CC Name=1b; Synonyms=B;
CC IsoId=Q24246-3; Sequence=VSP_001346;
CC Name=1c; Synonyms=C;
CC IsoId=Q24246-4; Sequence=VSP_001347;
CC Name=2a; Synonyms=D;
CC IsoId=Q24246-5; Sequence=VSP_007686, VSP_001348;
CC Name=2b; Synonyms=E;
CC IsoId=Q24246-6; Sequence=VSP_007686;
CC Name=2c; Synonyms=F;
CC IsoId=Q24246-7; Sequence=VSP_007686, VSP_007687;
CC Name=3a; Synonyms=G;
CC IsoId=Q24246-8; Sequence=VSP_001342, VSP_001348;
CC Name=3b; Synonyms=H;
CC IsoId=Q24246-9; Sequence=VSP_001342;
CC Name=4; Synonyms=I;
CC IsoId=Q24246-10; Sequence=VSP_001343;
CC Name=5b; Synonyms=K;
CC IsoId=Q24246-12; Sequence=VSP_007685;
CC -!- TISSUE SPECIFICITY: High levels of isoform 1b, isoform 1c, isoform 3a
CC and isoform 4 accumulate in early egg chambers and at stage 9 become
CC concentrated at the posterior of the oocyte. Isoform 5a and isoform 5b
CC are highly expressed in adult head and to a lesser extent in adult
CC torso. Isoform 1a, isoform 2a and isoform 2b are found in all tissues
CC examined, including ovaries, midgut, torso and head.
CC {ECO:0000269|PubMed:11071907, ECO:0000269|PubMed:9774695}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Abundant in embryos and adults, low levels in larva and pupae. Isoform
CC 1a, isoform 2a and isoform 2b are constitutively expressed at high
CC levels and isoform 2c at low levels in embryos and adults.
CC {ECO:0000269|PubMed:9774695}.
CC -!- SIMILARITY: Belongs to the dynein intermediate chain family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC70942.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAC78306.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF070687; AAC78306.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF070689; AAC70933.1; -; mRNA.
DR EMBL; AF070690; AAC70934.1; -; mRNA.
DR EMBL; AF070691; AAC70935.1; -; mRNA.
DR EMBL; AF070692; AAC70936.1; -; mRNA.
DR EMBL; AF070693; AAC70937.1; -; mRNA.
DR EMBL; AF070694; AAC70938.1; -; mRNA.
DR EMBL; AF070695; AAC70939.1; -; mRNA.
DR EMBL; AF070696; AAC70940.1; -; mRNA.
DR EMBL; AF070697; AAC70941.1; -; mRNA.
DR EMBL; AF070698; AAC70942.1; ALT_SEQ; mRNA.
DR EMBL; AF070699; AAC70943.1; -; mRNA.
DR EMBL; AF263371; AAF73046.1; -; mRNA.
DR EMBL; AE014298; AAF50928.2; -; Genomic_DNA.
DR EMBL; AE014298; AAN09553.1; -; Genomic_DNA.
DR EMBL; AE014298; AAN09554.1; -; Genomic_DNA.
DR EMBL; AE014298; AAN09555.1; -; Genomic_DNA.
DR EMBL; AE014298; AAN09556.1; -; Genomic_DNA.
DR EMBL; AE014298; AAN09557.1; -; Genomic_DNA.
DR EMBL; AE014298; AAN09558.1; -; Genomic_DNA.
DR EMBL; AE014298; AAN09559.1; -; Genomic_DNA.
DR EMBL; AE014298; AAN09560.1; -; Genomic_DNA.
DR EMBL; AE014298; AAN09561.1; -; Genomic_DNA.
DR EMBL; AE014298; AAN09562.1; -; Genomic_DNA.
DR EMBL; BT016101; AAV36986.1; -; mRNA.
DR EMBL; L41945; AAB51185.1; -; Genomic_DNA.
DR RefSeq; NP_001285486.1; NM_001298557.1. [Q24246-2]
DR RefSeq; NP_477069.1; NM_057721.4. [Q24246-5]
DR RefSeq; NP_477070.1; NM_057722.4. [Q24246-8]
DR RefSeq; NP_477071.1; NM_057723.4. [Q24246-9]
DR RefSeq; NP_477072.1; NM_057724.4. [Q24246-10]
DR RefSeq; NP_477073.1; NM_057725.4. [Q24246-12]
DR RefSeq; NP_477074.1; NM_057726.4. [Q24246-2]
DR RefSeq; NP_477075.2; NM_057727.5. [Q24246-11]
DR RefSeq; NP_477076.1; NM_057728.4. [Q24246-4]
DR RefSeq; NP_477077.1; NM_057729.4. [Q24246-3]
DR RefSeq; NP_477078.1; NM_057730.5. [Q24246-6]
DR RefSeq; NP_477079.1; NM_057731.4. [Q24246-7]
DR RefSeq; NP_996521.1; NM_206798.2. [Q24246-5]
DR RefSeq; NP_996522.1; NM_206799.2. [Q24246-5]
DR PDB; 2P2T; X-ray; 3.00 A; C=123-138.
DR PDB; 3FM7; X-ray; 3.50 A; C/D=109-135.
DR PDB; 3L9K; X-ray; 3.00 A; W/X/Y/Z=242-279.
DR PDBsum; 2P2T; -.
DR PDBsum; 3FM7; -.
DR PDBsum; 3L9K; -.
DR AlphaFoldDB; Q24246; -.
DR BMRB; Q24246; -.
DR SMR; Q24246; -.
DR BioGRID; 68871; 25.
DR DIP; DIP-19664N; -.
DR ELM; Q24246; -.
DR IntAct; Q24246; 6.
DR STRING; 7227.FBpp0088428; -.
DR PaxDb; Q24246; -.
DR PRIDE; Q24246; -.
DR DNASU; 44160; -.
DR EnsemblMetazoa; FBtr0089397; FBpp0088419; FBgn0003654. [Q24246-2]
DR EnsemblMetazoa; FBtr0089398; FBpp0088420; FBgn0003654. [Q24246-3]
DR EnsemblMetazoa; FBtr0089399; FBpp0088421; FBgn0003654. [Q24246-4]
DR EnsemblMetazoa; FBtr0089400; FBpp0088422; FBgn0003654. [Q24246-5]
DR EnsemblMetazoa; FBtr0089401; FBpp0088423; FBgn0003654. [Q24246-6]
DR EnsemblMetazoa; FBtr0089402; FBpp0088424; FBgn0003654. [Q24246-7]
DR EnsemblMetazoa; FBtr0089403; FBpp0088425; FBgn0003654. [Q24246-8]
DR EnsemblMetazoa; FBtr0089404; FBpp0088426; FBgn0003654. [Q24246-9]
DR EnsemblMetazoa; FBtr0089405; FBpp0088427; FBgn0003654. [Q24246-10]
DR EnsemblMetazoa; FBtr0089406; FBpp0088428; FBgn0003654. [Q24246-11]
DR EnsemblMetazoa; FBtr0089407; FBpp0088429; FBgn0003654. [Q24246-12]
DR EnsemblMetazoa; FBtr0089408; FBpp0089020; FBgn0003654. [Q24246-5]
DR EnsemblMetazoa; FBtr0089409; FBpp0089021; FBgn0003654. [Q24246-5]
DR EnsemblMetazoa; FBtr0340360; FBpp0309318; FBgn0003654. [Q24246-2]
DR GeneID; 44160; -.
DR KEGG; dme:Dmel_CG18000; -.
DR CTD; 44160; -.
DR FlyBase; FBgn0003654; sw.
DR VEuPathDB; VectorBase:FBgn0003654; -.
DR eggNOG; KOG1587; Eukaryota.
DR GeneTree; ENSGT00940000166605; -.
DR InParanoid; Q24246; -.
DR OMA; EEGSIYP; -.
DR PhylomeDB; Q24246; -.
DR Reactome; R-DME-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-DME-6807878; COPI-mediated anterograde transport.
DR Reactome; R-DME-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-DME-9646399; Aggrephagy.
DR SignaLink; Q24246; -.
DR BioGRID-ORCS; 44160; 0 hits in 3 CRISPR screens.
DR EvolutionaryTrace; Q24246; -.
DR GenomeRNAi; 44160; -.
DR PRO; PR:Q24246; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0003654; Expressed in seminal fluid secreting gland and 14 other tissues.
DR ExpressionAtlas; Q24246; baseline and differential.
DR Genevisible; Q24246; DM.
DR GO; GO:0005868; C:cytoplasmic dynein complex; IDA:FlyBase.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IEA:GOC.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IMP:CAFA.
DR GO; GO:0034452; F:dynactin binding; IPI:FlyBase.
DR GO; GO:0045504; F:dynein heavy chain binding; ISS:FlyBase.
DR GO; GO:0045503; F:dynein light chain binding; IPI:CAFA.
DR GO; GO:0008088; P:axo-dendritic transport; IMP:FlyBase.
DR GO; GO:0007349; P:cellularization; IGI:FlyBase.
DR GO; GO:0051642; P:centrosome localization; IMP:FlyBase.
DR GO; GO:0001754; P:eye photoreceptor cell differentiation; IGI:FlyBase.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:FlyBase.
DR GO; GO:0007018; P:microtubule-based movement; IDA:FlyBase.
DR GO; GO:0034501; P:protein localization to kinetochore; IMP:FlyBase.
DR GO; GO:0007291; P:sperm individualization; IMP:FlyBase.
DR GO; GO:0007051; P:spindle organization; IMP:FlyBase.
DR GO; GO:0010970; P:transport along microtubule; IBA:GO_Central.
DR DisProt; DP00605; -.
DR Gene3D; 2.130.10.10; -; 2.
DR IDEAL; IID50052; -.
DR InterPro; IPR025956; DYNC1I1/DYNC1I2.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF11540; Dynein_IC2; 1.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Cytoskeleton; Dynein;
KW Lysosome; Membrane; Microtubule; Motor protein; Nucleus;
KW Reference proteome; Repeat; Transport; WD repeat.
FT CHAIN 1..663
FT /note="Cytoplasmic dynein 1 intermediate chain"
FT /id="PRO_0000114661"
FT REPEAT 311..360
FT /note="WD 1"
FT REPEAT 364..404
FT /note="WD 2"
FT REPEAT 413..454
FT /note="WD 3"
FT REPEAT 463..503
FT /note="WD 4"
FT REPEAT 508..553
FT /note="WD 5"
FT REPEAT 556..596
FT /note="WD 6"
FT REPEAT 602..641
FT /note="WD 7"
FT REGION 17..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 75..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 144..187
FT /note="VLSCHSSPLSGYMEDWWRPRKAHATDYYDEYNLNPGLEWEDEFT -> AHAT
FT DYYVLAFDAQG (in isoform 1a)"
FT /evidence="ECO:0000303|PubMed:9774695"
FT /id="VSP_001345"
FT VAR_SEQ 144..187
FT /note="VLSCHSSPLSGYMEDWWRPRKAHATDYYDEYNLNPGLEWEDEFT -> AHAT
FT DYYG (in isoform 1b)"
FT /evidence="ECO:0000303|PubMed:9774695, ECO:0000303|Ref.5"
FT /id="VSP_001346"
FT VAR_SEQ 144..187
FT /note="VLSCHSSPLSGYMEDWWRPRKAHATDYYDEYNLNPGLEWEDEFT -> AHAT
FT DYY (in isoform 1c)"
FT /evidence="ECO:0000303|PubMed:9774695"
FT /id="VSP_001347"
FT VAR_SEQ 144..171
FT /note="Missing (in isoform 3a and isoform 3b)"
FT /evidence="ECO:0000303|PubMed:9774695"
FT /id="VSP_001342"
FT VAR_SEQ 144..164
FT /note="Missing (in isoform 2a, isoform 2b and isoform 2c)"
FT /evidence="ECO:0000303|PubMed:11071907,
FT ECO:0000303|PubMed:9774695"
FT /id="VSP_007686"
FT VAR_SEQ 144..153
FT /note="Missing (in isoform 5b)"
FT /evidence="ECO:0000303|PubMed:9774695"
FT /id="VSP_007685"
FT VAR_SEQ 146..187
FT /note="SCHSSPLSGYMEDWWRPRKAHATDYYDEYNLNPGLEWEDEFT -> AFDAQG
FT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:9774695"
FT /id="VSP_001343"
FT VAR_SEQ 187
FT /note="T -> TG (in isoform 2a and isoform 3a)"
FT /evidence="ECO:0000303|PubMed:9774695"
FT /id="VSP_001348"
FT VAR_SEQ 187
FT /note="T -> TVLAFDAQG (in isoform 2c)"
FT /evidence="ECO:0000303|PubMed:9774695"
FT /id="VSP_007687"
FT CONFLICT 47
FT /note="D -> G (in Ref. 1; AAC78306/AAC70933/AAC70934/
FT AAC70935/AAC70936/AAC70937/AAC70938/AAC70939/AAC70940/
FT AAC70941/AAC70942/AAC70943)"
FT /evidence="ECO:0000305"
FT CONFLICT 139..145
FT /note="GGNGDVL -> AETAMV (in Ref. 6; AAB51185)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="V -> L (in Ref. 6; AAB51185)"
FT /evidence="ECO:0000305"
FT CONFLICT 296..297
FT /note="HA -> SM (in Ref. 6; AAB51185)"
FT /evidence="ECO:0000305"
FT CONFLICT 521..522
FT /note="NQ -> KP (in Ref. 6; AAB51185)"
FT /evidence="ECO:0000305"
FT CONFLICT 537..548
FT /note="DWTIKLWSLKDT -> KIWSLKLPISSCQFSVVSGINSN (in Ref. 6;
FT AAB51185)"
FT /evidence="ECO:0000305"
FT CONFLICT 579
FT /note="G -> A (in Ref. 6; AAB51185)"
FT /evidence="ECO:0000305"
FT CONFLICT 593
FT /note="E -> K (in Ref. 6; AAB51185)"
FT /evidence="ECO:0000305"
FT CONFLICT 628
FT /note="L -> Q (in Ref. 6; AAB51185)"
FT /evidence="ECO:0000305"
FT CONFLICT 645..663
FT /note="WSRFNTHLSEIKMNQSDEV -> IKMNQSVRSRTI (in Ref. 6;
FT AAB51185)"
FT /evidence="ECO:0000305"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:3FM7"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:2P2T"
FT HELIX 244..251
FT /evidence="ECO:0007829|PDB:3L9K"
FT HELIX 254..273
FT /evidence="ECO:0007829|PDB:3L9K"
SQ SEQUENCE 663 AA; 73917 MW; 4C726D4C5F47FAF7 CRC64;
MDRKAELERK KAKLAALREE KDRRRREKEI KDMEEAAGRI GGGAGIDKDQ RKDLDEMLSS
LGVAPVSEVL SSLSSVNSMT SDNSNTQTPD ASLQATVNGQ SGGKKQPLNL SVYNVQATNI
PPKETLVYTK QTQTTSTGGG NGDVLSCHSS PLSGYMEDWW RPRKAHATDY YDEYNLNPGL
EWEDEFTDDE ESSLQNLGNG FTSKLPPGYL THGLPTVKDV APAITPLEIK KETEVKKEVN
ELSEEQKQMI ILSENFQRFV VRAGRVIERA LSENVDIYTD YIGGGDSEEA NDERSHARLS
LNRVFYDERW SKNRCITSMD WSTHFPELVV GSYHNNEESP NEPDGVVMVW NTKFKKSTPE
DVFHCQSAVM STCFAKFNPN LILGGTYSGQ IVLWDNRVQK RTPIQRTPLS AAAHTHPVYC
LQMVGTQNAH NVISISSDGK LCSWSLDMLS QPQDTLELQQ RQSKAIAITS MAFPANEINS
LVMGSEDGYV YSASRHGLRS GVNEVYERHL GPITGISTHY NQLSPDFGHL FLTSSIDWTI
KLWSLKDTKP LYSFEDNSDY VMDVAWSPVH PALFAAVDGS GRLDLWNLNQ DTEVPTASIV
VAGAPALNRV SWTPSGLHVC IGDEAGKLYV YDVAENLAQP SRDEWSRFNT HLSEIKMNQS
DEV
