SDK_DROME
ID SDK_DROME Reviewed; 2224 AA.
AC O97394; A4V3T7; A9UNG5; Q0KHX5; Q86BQ7; Q9U1M1; Q9UB11; Q9W5D9;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Protein sidekick {ECO:0000303|PubMed:9310325};
DE Flags: Precursor;
GN Name=sdk {ECO:0000312|FlyBase:FBgn0021764}; ORFNames=CG5227;
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), ALTERNATIVE SPLICING (ISOFORM C),
RP AND FUNCTION.
RC TISSUE=Eye imaginal disk;
RX PubMed=9310325; DOI=10.1242/dev.124.17.3303;
RA Nguyen D.N.T., Liu Y., Litsky M.L., Reinke R.;
RT "The sidekick gene, a member of the immunoglobulin superfamily, is required
RT for pattern formation in the Drosophila eye.";
RL Development 124:3303-3312(1997).
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, 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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oregon-R;
RX PubMed=10731137; DOI=10.1126/science.287.5461.2220;
RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G.,
RA Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Borkova D., Minana B., Kafatos F.C.,
RA Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L.,
RA Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P.,
RA Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H.,
RA Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
RA Glover D.M.;
RT "From sequence to chromosome: the tip of the X chromosome of D.
RT melanogaster.";
RL Science 287:2220-2222(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C.,
RA Celniker S.E.;
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-870, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Oregon-R; TISSUE=Head;
RX PubMed=17893096; DOI=10.1093/glycob/cwm097;
RA Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,
RA Panin V.;
RT "Identification of N-glycosylated proteins from the central nervous system
RT of Drosophila melanogaster.";
RL Glycobiology 17:1388-1403(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2071; THR-2074; SER-2113 AND
RP SER-2117, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Participates in homotypic or heterotypic interactions in the
CC eye during pattern formation to prevent extra cells from joining the
CC precluster and differentiating as photoreceptor cells.
CC {ECO:0000269|PubMed:9310325}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A; Synonyms=D;
CC IsoId=O97394-1; Sequence=Displayed;
CC Name=C;
CC IsoId=O97394-2; Sequence=VSP_017529;
CC -!- SIMILARITY: Belongs to the sidekick family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD09632.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U88578; AAD09632.1; ALT_FRAME; mRNA.
DR EMBL; AE014298; AAN09027.4; -; Genomic_DNA.
DR EMBL; AE014298; AAN09028.5; -; Genomic_DNA.
DR EMBL; AE014298; AAN09029.4; -; Genomic_DNA.
DR EMBL; AL132792; CAB65848.1; -; Genomic_DNA.
DR EMBL; BT031329; ABY21742.1; -; mRNA.
DR PIR; T13924; T13924.
DR RefSeq; NP_001162630.1; NM_001169159.2. [O97394-1]
DR RefSeq; NP_001162631.1; NM_001169160.2. [O97394-1]
DR RefSeq; NP_477289.5; NM_057941.5. [O97394-1]
DR RefSeq; NP_477290.6; NM_057942.5. [O97394-2]
DR RefSeq; NP_599141.5; NM_134314.4. [O97394-1]
DR RefSeq; NP_599142.5; NM_134315.4. [O97394-1]
DR AlphaFoldDB; O97394; -.
DR SMR; O97394; -.
DR BioGRID; 57585; 5.
DR DIP; DIP-20914N; -.
DR IntAct; O97394; 46.
DR STRING; 7227.FBpp0291468; -.
DR GlyGen; O97394; 25 sites.
DR iPTMnet; O97394; -.
DR PaxDb; O97394; -.
DR PRIDE; O97394; -.
DR EnsemblMetazoa; FBtr0070130; FBpp0070125; FBgn0021764. [O97394-1]
DR EnsemblMetazoa; FBtr0070131; FBpp0070126; FBgn0021764. [O97394-2]
DR EnsemblMetazoa; FBtr0070132; FBpp0070127; FBgn0021764. [O97394-1]
DR EnsemblMetazoa; FBtr0070133; FBpp0070128; FBgn0021764. [O97394-1]
DR EnsemblMetazoa; FBtr0302259; FBpp0291468; FBgn0021764. [O97394-1]
DR EnsemblMetazoa; FBtr0302260; FBpp0291469; FBgn0021764. [O97394-1]
DR GeneID; 31017; -.
DR KEGG; dme:Dmel_CG5227; -.
DR UCSC; CG5227-RA; d. melanogaster. [O97394-1]
DR CTD; 31017; -.
DR FlyBase; FBgn0021764; sdk.
DR VEuPathDB; VectorBase:FBgn0021764; -.
DR eggNOG; KOG3510; Eukaryota.
DR InParanoid; O97394; -.
DR PhylomeDB; O97394; -.
DR Reactome; R-DME-373752; Netrin-1 signaling.
DR Reactome; R-DME-376176; Signaling by ROBO receptors.
DR Reactome; R-DME-418885; DCC mediated attractive signaling.
DR Reactome; R-DME-418889; Caspase activation via Dependence Receptors in the absence of ligand.
DR Reactome; R-DME-428542; Regulation of commissural axon pathfinding by SLIT and ROBO.
DR BioGRID-ORCS; 31017; 0 hits in 3 CRISPR screens.
DR ChiTaRS; sdk; fly.
DR GenomeRNAi; 31017; -.
DR PRO; PR:O97394; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0021764; Expressed in wing disc and 22 other tissues.
DR ExpressionAtlas; O97394; baseline and differential.
DR Genevisible; O97394; DM.
DR GO; GO:0045177; C:apical part of cell; IDA:FlyBase.
DR GO; GO:0005887; C:integral component of plasma membrane; NAS:FlyBase.
DR GO; GO:0098595; C:perivitelline space; HDA:FlyBase.
DR GO; GO:0004895; F:cell adhesion receptor activity; IMP:FlyBase.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0042675; P:compound eye cone cell differentiation; IMP:FlyBase.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:FlyBase.
DR GO; GO:0046533; P:negative regulation of photoreceptor cell differentiation; IMP:FlyBase.
DR GO; GO:0050931; P:pigment cell differentiation; IMP:FlyBase.
DR CDD; cd00063; FN3; 13.
DR Gene3D; 2.60.40.10; -; 19.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF00041; fn3; 13.
DR Pfam; PF07679; I-set; 4.
DR SMART; SM00060; FN3; 13.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 5.
DR SMART; SM00406; IGv; 3.
DR SUPFAM; SSF48726; SSF48726; 5.
DR SUPFAM; SSF49265; SSF49265; 7.
DR PROSITE; PS50853; FN3; 13.
DR PROSITE; PS50835; IG_LIKE; 5.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Developmental protein; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..47
FT /evidence="ECO:0000255"
FT CHAIN 48..2224
FT /note="Protein sidekick"
FT /id="PRO_0000226983"
FT TOPO_DOM 48..2001
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2002..2022
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2023..2224
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 72..155
FT /note="Ig-like C2-type 1"
FT DOMAIN 261..355
FT /note="Ig-like C2-type 2"
FT DOMAIN 359..445
FT /note="Ig-like C2-type 3"
FT DOMAIN 455..541
FT /note="Ig-like C2-type 4"
FT DOMAIN 546..636
FT /note="Ig-like C2-type 5"
FT DOMAIN 643..753
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 758..855
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 860..967
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 971..1065
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1069..1164
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1169..1270
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1275..1372
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1376..1469
FT /note="Fibronectin type-III 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1474..1570
FT /note="Fibronectin type-III 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1575..1677
FT /note="Fibronectin type-III 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1682..1785
FT /note="Fibronectin type-III 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1789..1883
FT /note="Fibronectin type-III 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1885..1984
FT /note="Fibronectin type-III 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 2068..2157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2171..2195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2068..2086
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2115..2130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2131..2146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2071
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 2074
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 2113
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 2117
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 463
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 485
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 491
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 628
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 661
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 707
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 809
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 870
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17893096"
FT CARBOHYD 942
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1019
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1094
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1414
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1420
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1843
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1876
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 95..138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 283..336
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 382..433
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 476..525
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 567..620
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1926
FT /note="D -> EKGEPSFVY (in isoform C)"
FT /evidence="ECO:0000305"
FT /id="VSP_017529"
FT CONFLICT 207
FT /note="K -> Q (in Ref. 5; ABY21742)"
FT /evidence="ECO:0000305"
FT CONFLICT 521
FT /note="G -> P (in Ref. 1; AAD09632)"
FT /evidence="ECO:0000305"
FT CONFLICT 536
FT /note="G -> A (in Ref. 1; AAD09632)"
FT /evidence="ECO:0000305"
FT CONFLICT 658
FT /note="R -> A (in Ref. 1; AAD09632)"
FT /evidence="ECO:0000305"
FT CONFLICT 755
FT /note="P -> H (in Ref. 1; AAD09632)"
FT /evidence="ECO:0000305"
FT CONFLICT 1047
FT /note="R -> A (in Ref. 1; AAD09632)"
FT /evidence="ECO:0000305"
FT CONFLICT 1175
FT /note="V -> E (in Ref. 1; AAD09632)"
FT /evidence="ECO:0000305"
FT CONFLICT 1270
FT /note="A -> R (in Ref. 1; AAD09632)"
FT /evidence="ECO:0000305"
FT CONFLICT 1697
FT /note="R -> D (in Ref. 1; AAD09632)"
FT /evidence="ECO:0000305"
FT CONFLICT 1818
FT /note="L -> K (in Ref. 1; AAD09632)"
FT /evidence="ECO:0000305"
FT CONFLICT 1897
FT /note="T -> S (in Ref. 1; AAD09632)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2224 AA; 246254 MW; AC41929E879455C5 CRC64;
MLKSAASSLR RRRPKTTITA TLAIEMPSQP KLASLLAVLV LLCYCDSCFF CYADANLQQQ
NSIVQQQQLQ APRFTTHPSS SGSIVSEGST KILQCHALGY PQPTYRWLKD GVPVGDFSSS
QFYRFHSTRR EDAGSYQCIA RNDAGSIFSE KSDVVVAYMG IFENTTEGRL TVISGHPAIF
DMPPIESIPV PSVMWQSEDG PLNYDIKYAF THANQLIILS ADENDRKGYR AKAINTQLGK
EESSAFVHLN VSGDPYIEVA PEIIVRPQDV KVKVGTGVVE LQCIANARPL HELETLWLKD
GLAVETAGVR HTLNDPWNRT LALLQANSSH SGEYTCQVRL RSGGYPAVSA SARLQILEPP
LFFTPMRAET FGEFGGQVQL TCDVVGEPTP QVKWFRNAES VDAHIESGRY TLNTDNTLVI
KKLILDDAAM FQCLAINEAG ENSASTWLRV KTSAPIMELP PQNVTALDGK DATISCRAVG
SPNPNITWIY NETQLVDISS RVQILESGDL LISNIRSVDA GLYICVRANE AGSVKGEAYL
SVLVRTQIIQ PPVDTTVLLG LTATLQCKVS SDPSVPYNID WYREGQSSTP ISNSQRIGVQ
ADGQLEIQAV RASDVGSYAC VVTSPGGNET RAARLSVIEL PFPPSNVKVE RLPEPQQRSI
NVSWTPGFDG NSPISKFIIQ RREVSELEKF VGPVPDPLLN WITELSNVSA DQRWILLENL
KAATVYQFRV SAVNRVGEGS PSEPSNVVEL PQEAPSGPPV GFVGSARSMS EIITQWQPPL
EEHRNGQILG YILRYRLFGY NNVPWSYQNI TNEAQRNFLI QELITWKDYI VQIAAYNNMG
VGVYTEGSKI KTKEGVPEAP PTNVKVEAIN STAARCRWTP PNPQQINGIN QGYKIQAWQR
RLIDGEWRDI ERRMKTVPPS LIDPLAEQTA ILGGLEKFTE YNISVLCFTD PGDGVASSQV
AVMTMDDVPD EVTGLHFDDV SDRSVKVLWA PPRASNGILT GYTVRYQVKD RPDTLKSFNL
TADDTELTVN QLQATTHYWF EIVAWTRVGS GIPKTATIQS GVEPVLPHAP TALALSNIEA
FSVVLQFTPG FDGNSSITKW KVEGQTARNM TWFTICEIND PDAETLTVTG LVPFTQYRLR
LSASNVVGSS KPSEATKDFQ TIQARPKHPP FNVTVRAMSA QQLRVRWIPL QQTEWYGNPR
GYNISYKQLV KTPGTIKYVP RSVVIEDHTA NSHVLDSLEE WTLYEVKMNA CNDVGCSKES
DTAVERTREA VPSYGPLDVQ ANATSSTTVV VQWGEVPRQH RNGQIDGYKV FYAAADRGQQ
VLHKTIPNNA TFTTTLTELK KYVVYHVQVL AYTRLGNGAL STPPIRVQTF EDTPGVPSNV
SFPDVSLTMA RIIWDVPVDP NGKILAYQVT YTLNGSAMLN YSREFPPSDR TFRATELLPG
KYYSFSCTAQ TRLGWGKIAT ALVYTTNNRE RPQAPSVPQI SRSQIQAHQI TFSWTPGRDG
FAPLRYYTVE MRENEGRWQP LPERVDPSLS SFTAVGLRPY MTYQFRIQAT NDLGPSAFSR
ESVIVRTLPA APAVGVGGLK VVPITTTSVR VQWSALETAL WNGDASTGGY RILYQQLSDF
PTALQSTPKT DVHGINENSV VLSDLQQDRN YEIVVLPFNS QGPGPATPPA AVYVGEAVPT
GEPRAVDAAP ISSTEVRLLW KPPKQSMQNG DILGYKIYYL VTYSPQALEP GRKWEEEIEV
VSATATSHSL VFLDKFTEYR IQLLAFNPAG DGPRSAPITV KTLPGVPSAP LHLRFSDITM
QSLEVTWDPP KFLNGEILGY LVTYETTEEN EKFSKQVKQK VSNTTLRVQN LEEEVTYTFT
VRAQTSVDYG PGISENVTTG PQDGSPVAPR DLILTKTLSS VEMHWINGPS GRGPILGYLI
EAKKRDDSRW TKIEQTRKGM MQDFTVSYHI LMPSTAYTFR VIAYNRYGIS FPVYSKDSIL
TPSKLHLEYG YLQHKPFYRQ TWFMVSLAAT SIVIIVMVIA VLCVKSKSYK YKQEAQKTLE
ESMAMSIDER QELALELYRS RHGVGTGTLN SVGTLRSGTL GTLGRKSTSR PPPGVHLGKS
PPRPSPASVA YHSDEESLKC YDENPDDSSV TEKPSEVSSS EASQHSESEN ESVRSDPHSF
VNHYANVNDS LRQSWKKTKP VRNYSSYTDS EPEGSAVMSL NGGQIIVNNM ARSRAPLPGF
SSFV
