STAN_DROME
ID STAN_DROME Reviewed; 3579 AA.
AC Q9V5N8;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 4.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Protocadherin-like wing polarity protein stan;
DE AltName: Full=Protein flamingo;
DE AltName: Full=Protein starry night;
DE Flags: Precursor;
GN Name=stan; Synonyms=fmi; ORFNames=CG11895;
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), FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=10556066; DOI=10.1242/dev.126.23.5421;
RA Chae J.W., Kim M.-J., Goo J.H., Collier S., Gubb D., Charlton J.,
RA Adler P.N., Park W.J.;
RT "The Drosophila tissue polarity gene starry night encodes a member of the
RT protocadherin family.";
RL Development 126:5421-5429(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10490098; DOI=10.1016/s0092-8674(00)80046-x;
RA Usui T., Shima Y., Shimada Y., Hirano S., Burgess R.W., Schwarz T.L.,
RA Takeichi M., Uemura T.;
RT "Flamingo, a seven-pass transmembrane cadherin, regulates planar cell
RT polarity under the control of frizzled.";
RL Cell 98:585-595(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.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3199 AND SER-3200, AND
RP 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).
RN [6]
RP FUNCTION, INTERACTION WITH ATP6AP2, AND SUBCELLULAR LOCATION.
RX PubMed=23292348; DOI=10.1038/emboj.2012.323;
RA Hermle T., Guida M.C., Beck S., Helmstaedter S., Simons M.;
RT "Drosophila ATP6AP2/VhaPRR functions both as a novel planar cell polarity
RT core protein and a regulator of endosomal trafficking.";
RL EMBO J. 32:245-259(2013).
CC -!- FUNCTION: Involved in the fz signaling pathway that controls wing
CC tissue polarity. Also mediates homophilic cell adhesion. May play a
CC role in initiating prehair morphogenesis. May play a critical role in
CC tissue polarity and in formation of normal dendrite fields. During
CC planar cell polarity, stabilizes asymmetric PCP domains together with
CC ATP6AP2 (PubMed:23292348). {ECO:0000269|PubMed:10490098,
CC ECO:0000269|PubMed:10556066, ECO:0000269|PubMed:23292348}.
CC -!- SUBUNIT: Interacts with ATP6AP2 (via N-terminus).
CC {ECO:0000269|PubMed:23292348}.
CC -!- INTERACTION:
CC Q9V5N8; P18537: fz; NbExp=3; IntAct=EBI-119250, EBI-251576;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10490098};
CC Multi-pass membrane protein {ECO:0000269|PubMed:10490098}. Apical cell
CC membrane {ECO:0000269|PubMed:23292348}. Note=Co-localizes at the apical
CC junctions with ATP6AP2. {ECO:0000269|PubMed:23292348}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=Q9V5N8-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q9V5N8-2; Sequence=VSP_036911;
CC -!- TISSUE SPECIFICITY: In the pupal wing, expressed at relatively even
CC levels in all regions. Abundant in 6-9 hours embryos. Expressed at
CC higher levels in pupae than larvae. {ECO:0000269|PubMed:10556066}.
CC -!- DEVELOPMENTAL STAGE: At 12 hours after puparium formation (apf),
CC expressed evenly at cell boundaries. By 30 hours apf, expression is
CC concentrated at proximal and distal cell boundaries with little or no
CC expression at anterior and posterior boundaries. When prehairs emerge
CC at 30-36 hours apf, expression becomes evenly distributed again along
CC the whole cell boundary. {ECO:0000269|PubMed:10556066}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC {ECO:0000305}.
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DR EMBL; AF172329; AAF02618.1; -; mRNA.
DR EMBL; AB028498; BAA84069.1; -; mRNA.
DR EMBL; AE013599; AAF58763.5; -; Genomic_DNA.
DR RefSeq; NP_001188903.1; NM_001201974.2. [Q9V5N8-1]
DR RefSeq; NP_724962.3; NM_165794.4. [Q9V5N8-1]
DR SMR; Q9V5N8; -.
DR BioGRID; 61934; 25.
DR IntAct; Q9V5N8; 3.
DR STRING; 7227.FBpp0292315; -.
DR GlyGen; Q9V5N8; 20 sites.
DR iPTMnet; Q9V5N8; -.
DR PaxDb; Q9V5N8; -.
DR PRIDE; Q9V5N8; -.
DR EnsemblMetazoa; FBtr0088214; FBpp0087309; FBgn0024836. [Q9V5N8-1]
DR EnsemblMetazoa; FBtr0300578; FBpp0289805; FBgn0024836. [Q9V5N8-2]
DR EnsemblMetazoa; FBtr0303223; FBpp0292315; FBgn0024836. [Q9V5N8-1]
DR EnsemblMetazoa; FBtr0304899; FBpp0293438; FBgn0024836. [Q9V5N8-2]
DR GeneID; 36125; -.
DR KEGG; dme:Dmel_CG11895; -.
DR CTD; 36125; -.
DR FlyBase; FBgn0024836; stan.
DR VEuPathDB; VectorBase:FBgn0024836; -.
DR eggNOG; KOG4289; Eukaryota.
DR GeneTree; ENSGT00940000168029; -.
DR InParanoid; Q9V5N8; -.
DR PhylomeDB; Q9V5N8; -.
DR Reactome; R-DME-350368; Activation of RHO1 by FZ:DSH complex.
DR Reactome; R-DME-350376; Activation of RAC1:GTP by FZ:DSH complex.
DR Reactome; R-DME-350379; Homo-/heterophilic binding of transmembrane components.
DR Reactome; R-DME-350411; Formation and asymmetric localisation of transmembrane complexes.
DR Reactome; R-DME-350480; Activation of non-muscle Myosin II.
DR Reactome; R-DME-450728; Inhibition of actin polymerisation.
DR SignaLink; Q9V5N8; -.
DR BioGRID-ORCS; 36125; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 36125; -.
DR PRO; PR:Q9V5N8; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0024836; Expressed in eye disc (Drosophila) and 24 other tissues.
DR ExpressionAtlas; Q9V5N8; baseline and differential.
DR Genevisible; Q9V5N8; DM.
DR GO; GO:0016324; C:apical plasma membrane; IDA:FlyBase.
DR GO; GO:0005911; C:cell-cell junction; IDA:FlyBase.
DR GO; GO:0016021; C:integral component of membrane; ISM:FlyBase.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISS:FlyBase.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; NAS:UniProtKB.
DR GO; GO:0007411; P:axon guidance; IMP:FlyBase.
DR GO; GO:0007409; P:axonogenesis; IMP:FlyBase.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IMP:UniProtKB.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0016358; P:dendrite development; IEP:UniProtKB.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
DR GO; GO:0070593; P:dendrite self-avoidance; IMP:FlyBase.
DR GO; GO:0001737; P:establishment of imaginal disc-derived wing hair orientation; IGI:FlyBase.
DR GO; GO:0042067; P:establishment of ommatidial planar polarity; IMP:FlyBase.
DR GO; GO:0001736; P:establishment of planar polarity; IMP:FlyBase.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:FlyBase.
DR GO; GO:0001738; P:morphogenesis of a polarized epithelium; IMP:FlyBase.
DR GO; GO:0016319; P:mushroom body development; IMP:FlyBase.
DR GO; GO:0016318; P:ommatidial rotation; IMP:FlyBase.
DR GO; GO:0045773; P:positive regulation of axon extension; IGI:FlyBase.
DR GO; GO:1902669; P:positive regulation of axon guidance; IMP:FlyBase.
DR GO; GO:0048057; P:R3/R4 development; IMP:FlyBase.
DR GO; GO:0050770; P:regulation of axonogenesis; IDA:FlyBase.
DR GO; GO:0051963; P:regulation of synapse assembly; IDA:FlyBase.
DR GO; GO:0035159; P:regulation of tube length, open tracheal system; IMP:FlyBase.
DR GO; GO:0007367; P:segment polarity determination; IMP:UniProtKB.
DR CDD; cd00055; EGF_Lam; 1.
DR CDD; cd00110; LamG; 2.
DR Gene3D; 2.60.220.50; -; 1.
DR Gene3D; 4.10.1240.10; -; 1.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR032471; GAIN_dom_N.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR017981; GPCR_2-like.
DR InterPro; IPR036445; GPCR_2_extracell_dom_sf.
DR InterPro; IPR001879; GPCR_2_extracellular_dom.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR000203; GPS.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR002049; LE_dom.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF00028; Cadherin; 8.
DR Pfam; PF00008; EGF; 2.
DR Pfam; PF16489; GAIN; 1.
DR Pfam; PF00053; Laminin_EGF; 1.
DR Pfam; PF02210; Laminin_G_2; 2.
DR PRINTS; PR00205; CADHERIN.
DR PRINTS; PR00249; GPCRSECRETIN.
DR SMART; SM00112; CA; 8.
DR SMART; SM00181; EGF; 5.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00180; EGF_Lam; 1.
DR SMART; SM00303; GPS; 1.
DR SMART; SM00008; HormR; 1.
DR SMART; SM00282; LamG; 2.
DR SUPFAM; SSF49313; SSF49313; 9.
DR SUPFAM; SSF49899; SSF49899; 2.
DR PROSITE; PS00232; CADHERIN_1; 6.
DR PROSITE; PS50268; CADHERIN_2; 8.
DR PROSITE; PS00022; EGF_1; 4.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS01248; EGF_LAM_1; 1.
DR PROSITE; PS50027; EGF_LAM_2; 1.
DR PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR PROSITE; PS50221; GPS; 1.
DR PROSITE; PS50025; LAM_G_DOMAIN; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell adhesion; Cell membrane;
KW Developmental protein; Disulfide bond; EGF-like domain;
KW G-protein coupled receptor; Glycoprotein; Laminin EGF-like domain;
KW Membrane; Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..3579
FT /note="Protocadherin-like wing polarity protein stan"
FT /id="PRO_0000012921"
FT TOPO_DOM 30..2816
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2817..2837
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2838..2845
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2846..2866
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2867..2883
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2884..2904
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2905..2919
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2920..2940
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2941..2959
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2960..2980
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2981..3000
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 3001..3021
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3022..3031
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 3032..3052
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3053..3579
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 360..464
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 465..581
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 582..689
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 690..794
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 795..897
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 898..1007
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1008..1113
FT /note="Cadherin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1114..1220
FT /note="Cadherin 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1482..1518
FT /note="EGF-like 1; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1556..1753
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1756..1792
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1796..1963
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1965..2000
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2095..2142
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 2744..2802
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT REGION 2553..2582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2610..2635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2654..2684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3111..3225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3343..3377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3458..3486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3499..3579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2560..2582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2665..2679
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3111..3164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3165..3187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3195..3210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3211..3225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3472..3486
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3536..3553
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 3199
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 3200
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 671
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 886
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1374
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1650
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1678
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1747
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 1975
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2016
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2028
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2071
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2088
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2784
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 1486..1497
FT /evidence="ECO:0000255"
FT DISULFID 1491..1506
FT /evidence="ECO:0000255"
FT DISULFID 1508..1517
FT /evidence="ECO:0000255"
FT DISULFID 1727..1753
FT /evidence="ECO:0000250"
FT DISULFID 1760..1771
FT /evidence="ECO:0000255"
FT DISULFID 1765..1780
FT /evidence="ECO:0000255"
FT DISULFID 1782..1791
FT /evidence="ECO:0000255"
FT DISULFID 1937..1963
FT /evidence="ECO:0000250"
FT DISULFID 1969..1979
FT /evidence="ECO:0000255"
FT DISULFID 1973..1988
FT /evidence="ECO:0000255"
FT DISULFID 1990..1999
FT /evidence="ECO:0000255"
FT DISULFID 2092..2095
FT /evidence="ECO:0000255"
FT DISULFID 2097..2114
FT /evidence="ECO:0000255"
FT DISULFID 2116..2125
FT /evidence="ECO:0000255"
FT DISULFID 2128..2140
FT /evidence="ECO:0000250"
FT VAR_SEQ 3569..3579
FT /note="ERNIDDDETTV -> DSEAEY (in isoform B)"
FT /evidence="ECO:0000303|PubMed:10490098"
FT /id="VSP_036911"
FT CONFLICT 181
FT /note="T -> S (in Ref. 1; AAF02618)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="Q -> L (in Ref. 1; AAF02618)"
FT /evidence="ECO:0000305"
FT CONFLICT 395..401
FT /note="MVSLLDS -> NGLTVGLP (in Ref. 2; BAA84069)"
FT /evidence="ECO:0000305"
FT CONFLICT 1968
FT /note="Q -> H (in Ref. 1; AAF02618)"
FT /evidence="ECO:0000305"
FT CONFLICT 2271
FT /note="G -> E (in Ref. 1; AAF02618)"
FT /evidence="ECO:0000305"
FT CONFLICT 2502
FT /note="R -> C (in Ref. 2; BAA84069)"
FT /evidence="ECO:0000305"
FT CONFLICT 2627
FT /note="D -> G (in Ref. 2; BAA84069)"
FT /evidence="ECO:0000305"
FT CONFLICT 2709
FT /note="T -> S (in Ref. 2; BAA84069)"
FT /evidence="ECO:0000305"
FT CONFLICT 2756
FT /note="Q -> R (in Ref. 2; BAA84069)"
FT /evidence="ECO:0000305"
FT CONFLICT 2901
FT /note="C -> Y (in Ref. 1; AAF02618)"
FT /evidence="ECO:0000305"
FT CONFLICT 3098
FT /note="L -> P (in Ref. 1; AAF02618)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3579 AA; 397143 MW; 4E801C493031FB19 CRC64;
MQTREFPQRP LGLLLVLLVV LLQSSLIKSY LIIVHEDTPP GTVIFNASVY KLGSERHYKI
NAHKSANFVH HLVSVNHKDG QIQLRKALKC DGIYYPNLFT FYVDSTSNRL RSIDYYSLPV
RIFVSGHSCN EDRRIEQELH HHHYEEEDNT GYSKRRRRRS TQEMIQLNGN QLEEVFRQNS
TEFRAGDLIF GDSFDNEMRH RILSRKRRAV GSPDPLHLQP ALHRRISDAK QWISETYASY
AIHTTDKWNQ ICLRRSQFIN SLNAFLPRSV CQHCKVSFLD VNDERFAIEH QSRDLVASRD
VCIAESMWKV SITFNIRCDR RDIVDSDHRL KIVYHHQEFN DTDIARRVRR ELRNQSPYFE
QALYVASVLE EQPAGAAVTT VRARDPEDSP VVYSMVSLLD SRSQSLFKVD SRTGVVTTSA
SLDRELMDVH YFRVVATDDS FPPRSGTTTL QVNVLDCNDH SPTFEAEQFE ASIREGATVG
STVITLRATD QDIGKNAEIE YGIEAVTDGA GLAQDQEMPI FRIDSRSGVI STRSSLDRET
SDSYHLLVTA ADLASAQSER RTATASVQVK VLDDNDNYPQ FSERTYTVQV PEDQWGGTED
NTVAHIRATD ADQGNNAAIR YAIIGGNTQS QFSIDSMSGD VSLVKPLDYE SVRSYRLVIR
AQDGGSPSRS NTTQLLVNVI DANDNAPRFY TSQFQESVLE NVPVGYNIIR VQAYDSDEGA
NAEITYSISE RDDNFPLAVD PRTGWVQTIK PLDREEQGRF AFQVVAKDGG VPPKSASSSV
VITVQDVNDN DPAFNPKYYE ANVGEDQPPG TPVTTVTATD PDEDSRLHYE ITTGNTRGRF
AITSQNGRGL ITIAQSLDYK QEKRFLLTVA ATDSGGRSDT ATVHINITDA NNFAPIFENA
PYSASVFEDA PVGTTVLVVS ATDSDVGVNA QITYSLNEES INGLGSPDPF SINPQTGAIV
TNAPLDRETT SGYLLTVTAK DGGNPSLSDT TDVEIGVTDV NDNAPAFKSP LYQASILEDA
LVGTSVIQVA ASDPDVGLNG RIKYLLSDRD IEDGSFVIDP TSGTIRTNKG LDRESVAVFH
LTAIAVDKGS PPLSSTVEVQ IRLEDVNDSP PTFASDKITL YVPENSPVGS VVGEIHAHDP
DEGVNAVVHY SIIGGDDSNA FSLVTRPGSE RAQLLTMTEL DYESTRKRFE LVVRAASPPL
RNDAHIEILV TDVNDNAPVL RDFQVIFNNF RDHFPSGEIG RIPAFDADVS DKLHYRILSG
NNANLLRLNS SSGGLVLSPQ LNTNVPKFAT MEVSVSDGIN EAKAIMQLSV RLITEDMLFN
SVTVRLNEMT EEAFLSPLLN FFLDGLAAII PCPKEHIFVF SIQDDTDVSS RILNVSFSAR
RPDVSHEEFY TPQYLQERVY LNRAILARLA TVEVLPFDDN LCVREPCLNF EECLTVLKFG
NASEFIHSDT VLFRPIYPVN TFACSCPEGF TGSKEHYLCD TEVDLCYSDP CQNGGTCVRR
EGGYTCVCPS THTGQNCETG VGHLRPCPSE TCEGGLSCLS NYPSSQPPPY TATCELRARA
FGRNSFLTFE SLKQRHRFNL KLRFATVQEN GLLLYNGRYN ELHDFIALEI HEGHVSFSFS
LGDHSERISV IQEAKVSDGK WHQVEVVYLN RSVTLVLDNC DTAIALSGQL GDRWSCANRT
TLKLDKRCSL LTETCHRFLD LTGPLQVGGL PRIPAHFPVT NRDFVGCISD LRIDDRFVDL
NSYVADNGTL AGCPQKAPLC QSEPCFNGGT CREGWGTYSC ECPEGYAGNS CQDNIPAPWR
FSGDGSLSFN PLLRPIQLPW TTSFSLRTRQ KEAFLLQIQI GQNSSAAVCL RQGVLYYIFD
GEPMYLAGAF LSDGEWHRVE IRWQQGSEIH FSVDYGQRSG SVPMSQKVQG LYVGKIVMGS
PDGSIGAVPE ASPFEGCIQD VRIGAGQSVL SRPTIRENVE DGCESRAQCP DHCPNHSSCQ
SSWDLSTCEC DSGYVGTDCA PICTVRPCAS GVCRANTSLP RGYDCECNSS SRHGDYCEKE
LQQPCPGGWW GERVCGPCRC DLAQGYHPDC NKTTGQCYCK TNHYQPPNET ACLSCDCYSI
GSFSGACNPL TGQCECREGV IGRRCDSCSN PYAEVTLSGC EVVYDACPRS FAGGVWWPRT
PLGGVAIEGC PPPARGKGQR SCDVQSGSWN TPDMYNCTSE PFVELRRQLS QLEKLELELN
SFVAIKMAEQ LRKACEAVDR RGASKDQKIS GNGRPNRRYK MESSFLLSNG GNVWSHELEM
DYLSDELKFT HDRLYGADLL VTEGLLQELI NYELMQSGLN LSHSQDKYFI KNLVDAASVI
LDRKYEAEWR RATELIQRGP DDLVDAFNKY LVVLARSQHD TYTSPFEIVQ PNMALGLDIV
TTESLFGYEP EQLSEYHRSK YLKPNAFTTE SVVLPDTSGF LQHSARQRPV ISFPKYNNYI
LDRRKFDQHT KVLVPLEMLG ITPPESDEIS QSGRRGSSHD HRAIVAYAQY KDVGQLLPDL
YDETITRRWG VDVELATPIL SLQILVPSME REQETQRLEI PSRKIFSSSS PSSSSSSGST
EQQFVEVFDV PKAPTSSSEQ QIEDIRITAH EIPPPVSSVE QQEASSDEDG EEREPHIRLN
LDDIEFHGNS GEEVISPDSP EMLNPNYEGV SSTGSDEQPK GENEAVYRDR RLVKRQVEIT
YPSEQMQQTE QVVYRSLGSP HLAQPIKLQM WLDVDSARFG PRSNPQCVRW NSFTNQWTRL
GCQTEIPDFD GDFNPAAQQA ILVNCSCTHI SSYAVIVDVI DPEDIPEPSL LVQITSYSAF
LVSLPLLLGV LLALALLRGQ QTNSNTIHQN IVLCVFCAEL LFFVGMQSRR QLLESEFPCK
LTAICLHYFW LAAFAWTTVD CVHLYRMLTE MRDINHGPMG FYFAMGYGAP AIVVGLSVGV
RAHEYGNSLF CWLSVYEPVV WWLVGPIAGM SVVNLLILFV SVKAAFTLKD HVLGFGNLRT
LLWLSVVSLP LMGVMWVLAV LAASEHSQLL SLLLSGVVLL HALFCLIGYC IINKRVRENL
QRTCLRCMGR KVPLLDSSMV VSNSSHNVNA AARPSNFLAS GYDTTTRRNI GISASSTTSR
STAKTSSSPY SDGQLRQTST STSNYNSASD APSFLRGFES STTGRSRGGE EKPSRRQRKD
SDSGSETDGR SLELASSHSS DDDESRTARS SGTHRSTAVS STPAYLPNIT EHVQATTPPE
LNVVQSPQLF PSVNKPVYAP RWSSQLPDAY LQSPPNIGRW SQDTGSDNEH VHGQAKMTIS
PNPLPNPDLT DTSYLQQHHN KINMPPSILE NIRDAREGYE DSLYGRRGEY PDKYGSYKPP
SHYGSEKDYP GGGSGSQTIG HMRSFHPDAA YLSDNIYDKQ RTLGSGYLGA KSESPYLSKD
RITPDIYGSR DGHYSLKRQP AYATDSLHSV HSLLKNDYHQ QQQQQQQHHL QDRLSEGSDK
NGYHFPYTAE EDHLPARKLS HTQPPSLHGS QLMQPPGVGL VNDVNNPGLM GRHTLNGGSR
HSSRASSPPS TMVAPMQPLG PLTSITDTER NIDDDETTV
