GenomeNet

Database: UniProt
Entry: Q9V5N8
LinkDB: Q9V5N8
Original site: Q9V5N8 
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   10-APR-2019, entry version 181.
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;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, TISSUE SPECIFICITY,
RP   AND DEVELOPMENTAL STAGE.
RC   TISSUE=Embryo;
RX   PubMed=10556066;
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
RT   the protocadherin family.";
RL   Development 126:5421-5429(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), FUNCTION, AND SUBCELLULAR
RP   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.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   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.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   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.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., 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.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic 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).
CC   -!- FUNCTION: Involved in the fz signaling pathway that controls wing
CC       tissue polarity. Also mediates homophilic cell adhesion. May play
CC       a role in initiating prehair morphogenesis. May play a critical
CC       role in tissue polarity and in formation of normal dendrite
CC       fields. {ECO:0000269|PubMed:10490098,
CC       ECO:0000269|PubMed:10556066}.
CC   -!- INTERACTION:
CC       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}.
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
CC       even levels in all regions. Abundant in 6-9 hours embryos.
CC       Expressed at higher levels in pupae than larvae.
CC       {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
CC       is concentrated at proximal and distal cell boundaries with little
CC       or no expression at anterior and posterior boundaries. When
CC       prehairs emerge at 30-36 hours apf, expression becomes evenly
CC       distributed again along the whole cell boundary.
CC       {ECO:0000269|PubMed:10556066}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC       {ECO:0000305}.
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   UniGene; Dm.4360; -.
DR   ProteinModelPortal; Q9V5N8; -.
DR   SMR; Q9V5N8; -.
DR   BioGrid; 61934; 24.
DR   IntAct; Q9V5N8; 3.
DR   STRING; 7227.FBpp0292315; -.
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   eggNOG; KOG4289; Eukaryota.
DR   eggNOG; ENOG410XTGH; LUCA.
DR   GeneTree; ENSGT00940000168029; -.
DR   InParanoid; Q9V5N8; -.
DR   KO; K04600; -.
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   GenomeRNAi; 36125; -.
DR   PRO; PR:Q9V5N8; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0024836; Expressed in 26 organ(s), highest expression level in eye disc (Drosophila).
DR   ExpressionAtlas; Q9V5N8; baseline and differential.
DR   Genevisible; Q9V5N8; DM.
DR   GO; GO:0005911; C:cell-cell junction; IDA:FlyBase.
DR   GO; GO:0016021; C:integral component of membrane; ISS:FlyBase.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISS: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: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: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:0045746; P:negative regulation of Notch signaling pathway; 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:0007464; P:R3/R4 cell fate commitment; NAS:FlyBase.
DR   GO; GO:0048057; P:R3/R4 development; IMP:FlyBase.
DR   GO; GO:0050770; P:regulation of axonogenesis; IDA:FlyBase.
DR   GO; GO:0090175; P:regulation of establishment of planar polarity; IGI: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   GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; TAS:Reactome.
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; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR032471; GAIN_dom_N.
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; IPR002049; Laminin_EGF.
DR   InterPro; IPR001791; Laminin_G.
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   Complete proteome; Developmental protein; Disulfide bond;
KW   EGF-like domain; G-protein coupled receptor; Glycoprotein;
KW   Laminin EGF-like domain; Membrane; Phosphoprotein; Receptor;
KW   Reference proteome; Repeat; Signal; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     29       {ECO:0000255}.
FT   CHAIN        30   3579       Protocadherin-like wing polarity protein
FT                                stan.
FT                                /FTId=PRO_0000012921.
FT   TOPO_DOM     30   2816       Extracellular. {ECO:0000255}.
FT   TRANSMEM   2817   2837       Helical; Name=1. {ECO:0000255}.
FT   TOPO_DOM   2838   2845       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2846   2866       Helical; Name=2. {ECO:0000255}.
FT   TOPO_DOM   2867   2883       Extracellular. {ECO:0000255}.
FT   TRANSMEM   2884   2904       Helical; Name=3. {ECO:0000255}.
FT   TOPO_DOM   2905   2919       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2920   2940       Helical; Name=4. {ECO:0000255}.
FT   TOPO_DOM   2941   2959       Extracellular. {ECO:0000255}.
FT   TRANSMEM   2960   2980       Helical; Name=5. {ECO:0000255}.
FT   TOPO_DOM   2981   3000       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   3001   3021       Helical; Name=6. {ECO:0000255}.
FT   TOPO_DOM   3022   3031       Extracellular. {ECO:0000255}.
FT   TRANSMEM   3032   3052       Helical; Name=7. {ECO:0000255}.
FT   TOPO_DOM   3053   3579       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      360    464       Cadherin 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      465    581       Cadherin 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      582    689       Cadherin 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      690    794       Cadherin 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      795    897       Cadherin 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      898   1007       Cadherin 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     1008   1113       Cadherin 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     1114   1220       Cadherin 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     1482   1518       EGF-like 1; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1556   1753       Laminin G-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN     1756   1792       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1796   1963       Laminin G-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN     1965   2000       EGF-like 3; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     2095   2142       Laminin EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN     2744   2802       GPS. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00098}.
FT   COMPBIAS    140    143       Poly-His.
FT   COMPBIAS    155    159       Poly-Arg.
FT   COMPBIAS   2567   2579       Poly-Ser.
FT   COMPBIAS   3460   3467       Poly-Gln.
FT   MOD_RES    3199   3199       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES    3200   3200       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   CARBOHYD     46     46       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    179    179       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    340    340       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    671    671       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    886    886       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1269   1269       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1374   1374       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1441   1441       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1650   1650       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1678   1678       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1747   1747       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1843   1843       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1975   1975       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2016   2016       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2028   2028       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2071   2071       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2088   2088       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2196   2196       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2320   2320       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2784   2784       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID   1486   1497       {ECO:0000255}.
FT   DISULFID   1491   1506       {ECO:0000255}.
FT   DISULFID   1508   1517       {ECO:0000255}.
FT   DISULFID   1727   1753       {ECO:0000250}.
FT   DISULFID   1760   1771       {ECO:0000255}.
FT   DISULFID   1765   1780       {ECO:0000255}.
FT   DISULFID   1782   1791       {ECO:0000255}.
FT   DISULFID   1937   1963       {ECO:0000250}.
FT   DISULFID   1969   1979       {ECO:0000255}.
FT   DISULFID   1973   1988       {ECO:0000255}.
FT   DISULFID   1990   1999       {ECO:0000255}.
FT   DISULFID   2092   2095       {ECO:0000255}.
FT   DISULFID   2097   2114       {ECO:0000255}.
FT   DISULFID   2116   2125       {ECO:0000255}.
FT   DISULFID   2128   2140       {ECO:0000250}.
FT   VAR_SEQ    3569   3579       ERNIDDDETTV -> DSEAEY (in isoform B).
FT                                {ECO:0000303|PubMed:10490098}.
FT                                /FTId=VSP_036911.
FT   CONFLICT    181    181       T -> S (in Ref. 1; AAF02618).
FT                                {ECO:0000305}.
FT   CONFLICT    361    361       Q -> L (in Ref. 1; AAF02618).
FT                                {ECO:0000305}.
FT   CONFLICT    395    401       MVSLLDS -> NGLTVGLP (in Ref. 2;
FT                                BAA84069). {ECO:0000305}.
FT   CONFLICT   1968   1968       Q -> H (in Ref. 1; AAF02618).
FT                                {ECO:0000305}.
FT   CONFLICT   2271   2271       G -> E (in Ref. 1; AAF02618).
FT                                {ECO:0000305}.
FT   CONFLICT   2502   2502       R -> C (in Ref. 2; BAA84069).
FT                                {ECO:0000305}.
FT   CONFLICT   2627   2627       D -> G (in Ref. 2; BAA84069).
FT                                {ECO:0000305}.
FT   CONFLICT   2709   2709       T -> S (in Ref. 2; BAA84069).
FT                                {ECO:0000305}.
FT   CONFLICT   2756   2756       Q -> R (in Ref. 2; BAA84069).
FT                                {ECO:0000305}.
FT   CONFLICT   2901   2901       C -> Y (in Ref. 1; AAF02618).
FT                                {ECO:0000305}.
FT   CONFLICT   3098   3098       L -> P (in Ref. 1; AAF02618).
FT                                {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
//
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