GenomeNet

Database: UniProt
Entry: Q9VW71
LinkDB: Q9VW71
Original site: Q9VW71 
ID   FAT2_DROME              Reviewed;        4699 AA.
AC   Q9VW71; A4V252; Q95S51;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   14-MAY-2014, sequence version 3.
DT   16-JAN-2019, entry version 165.
DE   RecName: Full=Fat-like cadherin-related tumor suppressor homolog;
DE   AltName: Full=Protein kugelei;
DE   Flags: Precursor;
GN   Name=kug; Synonyms=fat2; ORFNames=CG7749;
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 {ECO:0000312|EMBL:AAL28503.1};
RN   [1] {ECO:0000305}
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   [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.,
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3360-4401 (ISOFORMS C/D),
RP   AND NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3821-4699 (ISOFORM C).
RC   STRAIN=Berkeley; TISSUE=Embryo, and Ovary;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
RA   George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
RA   Rubin G.M., Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [4]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=19906848; DOI=10.1242/dev.039099;
RA   Viktorinova I., Konig T., Schlichting K., Dahmann C.;
RT   "The cadherin Fat2 is required for planar cell polarity in the
RT   Drosophila ovary.";
RL   Development 136:4123-4132(2009).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=23369713; DOI=10.1016/j.devcel.2012.12.005;
RA   Lerner D.W., McCoy D., Isabella A.J., Mahowald A.P., Gerlach G.F.,
RA   Chaudhry T.A., Horne-Badovinac S.;
RT   "A Rab10-dependent mechanism for polarized basement membrane secretion
RT   during organ morphogenesis.";
RL   Dev. Cell 24:159-168(2013).
CC   -!- FUNCTION: Required for the planar polarity of actin filament
CC       orientation at the basal side of ovarian follicle cells
CC       (PubMed:19906848, PubMed:23369713). Required for proper egg
CC       chamber shape and elongation of the egg chamber during oogenesis
CC       (PubMed:19906848, PubMed:23369713). Required for the correct
CC       planar polarization of Rab10 within the basal follicle cell
CC       epithelium and is therefore indirectly involved in the Rab10-
CC       dependent remodeling of the basal membrane during egg chamber
CC       elongation (PubMed:23369713). {ECO:0000269|PubMed:19906848,
CC       ECO:0000269|PubMed:23369713}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein. Note=Accumulates on cell membranes where the planar
CC       oriented actin filaments terminate.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=D;
CC         IsoId=Q9VW71-1; Sequence=Displayed;
CC         Note=No experimental confirmation available.;
CC       Name=C;
CC         IsoId=Q9VW71-2; Sequence=VSP_054450;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Localizes where basal actin filaments
CC       terminate. {ECO:0000269|PubMed:19906848}.
CC   -!- DISRUPTION PHENOTYPE: Defects in actin filament orientation
CC       correlate with a failure of egg chambers to elongate during
CC       oogenesis (PubMed:19906848). In follicle cells, Rab10 protein
CC       polarizes normally along the apical-basal axis, but is
CC       mislocalized within the epithelial plane (PubMed:23369713).
CC       Epithelia migration is impaired and the structure of the basal
CC       membrane is disrupted (PubMed:23369713).
CC       {ECO:0000269|PubMed:19906848, ECO:0000269|PubMed:23369713}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL28503.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=AAM50035.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=AAM50035.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
DR   EMBL; AE014296; AAF49078.3; -; Genomic_DNA.
DR   EMBL; AE014296; AAZ66056.2; -; Genomic_DNA.
DR   EMBL; AY060955; AAL28503.1; ALT_INIT; mRNA.
DR   EMBL; AY118666; AAM50035.1; ALT_SEQ; mRNA.
DR   RefSeq; NP_001027138.2; NM_001031967.2. [Q9VW71-1]
DR   RefSeq; NP_001287126.1; NM_001300197.1. [Q9VW71-2]
DR   RefSeq; NP_649171.3; NM_140914.3. [Q9VW71-2]
DR   UniGene; Dm.3778; -.
DR   SMR; Q9VW71; -.
DR   BioGrid; 65458; 4.
DR   DIP; DIP-24050N; -.
DR   IntAct; Q9VW71; 7.
DR   STRING; 7227.FBpp0304968; -.
DR   PaxDb; Q9VW71; -.
DR   PRIDE; Q9VW71; -.
DR   EnsemblMetazoa; FBtr0332721; FBpp0304967; FBgn0261574. [Q9VW71-2]
DR   EnsemblMetazoa; FBtr0332722; FBpp0304968; FBgn0261574. [Q9VW71-1]
DR   EnsemblMetazoa; FBtr0346077; FBpp0311915; FBgn0261574. [Q9VW71-2]
DR   GeneID; 40191; -.
DR   KEGG; dme:Dmel_CG7749; -.
DR   UCSC; CG7749-RA; d. melanogaster. [Q9VW71-1]
DR   CTD; 40191; -.
DR   FlyBase; FBgn0261574; kug.
DR   eggNOG; KOG1219; Eukaryota.
DR   eggNOG; ENOG410XPEI; LUCA.
DR   GeneTree; ENSGT00940000166124; -.
DR   InParanoid; Q9VW71; -.
DR   KO; K16506; -.
DR   OMA; HVFFGGH; -.
DR   GenomeRNAi; 40191; -.
DR   PRO; PR:Q9VW71; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0261574; Expressed in 30 organ(s), highest expression level in eye disc (Drosophila).
DR   ExpressionAtlas; Q9VW71; baseline and differential.
DR   Genevisible; Q9VW71; DM.
DR   GO; GO:0098858; C:actin-based cell projection; IDA:FlyBase.
DR   GO; GO:0009925; C:basal plasma membrane; IDA:FlyBase.
DR   GO; GO:0031254; C:cell trailing edge; IDA:FlyBase.
DR   GO; GO:0005925; C:focal adhesion; IDA:FlyBase.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISS:FlyBase.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; ISM:FlyBase.
DR   GO; GO:0050839; F:cell adhesion molecule binding; IPI:FlyBase.
DR   GO; GO:0044877; F:protein-containing complex binding; IPI:FlyBase.
DR   GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:FlyBase.
DR   GO; GO:0044331; P:cell-cell adhesion mediated by cadherin; ISM:FlyBase.
DR   GO; GO:0060269; P:centripetally migrating follicle cell migration; IMP:FlyBase.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; HMP:FlyBase.
DR   GO; GO:0042247; P:establishment of planar polarity of follicular epithelium; IMP:UniProtKB.
DR   GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IMP:FlyBase.
DR   GO; GO:0007440; P:foregut morphogenesis; IMP:FlyBase.
DR   GO; GO:0007295; P:growth of a germarium-derived egg chamber; IMP:UniProtKB.
DR   GO; GO:0007442; P:hindgut morphogenesis; IMP:FlyBase.
DR   GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISS:FlyBase.
DR   GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR   GO; GO:0007424; P:open tracheal system development; IMP:FlyBase.
DR   GO; GO:0051491; P:positive regulation of filopodium assembly; IMP:FlyBase.
DR   GO; GO:0045089; P:positive regulation of innate immune response; HMP:FlyBase.
DR   GO; GO:1902463; P:protein localization to cell leading edge; IMP:FlyBase.
DR   GO; GO:0007431; P:salivary gland development; IMP:FlyBase.
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; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR001791; Laminin_G.
DR   Pfam; PF00028; Cadherin; 26.
DR   Pfam; PF02210; Laminin_G_2; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 34.
DR   SMART; SM00181; EGF; 6.
DR   SMART; SM00179; EGF_CA; 4.
DR   SMART; SM00282; LamG; 1.
DR   SUPFAM; SSF49313; SSF49313; 34.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS00232; CADHERIN_1; 18.
DR   PROSITE; PS50268; CADHERIN_2; 34.
DR   PROSITE; PS00022; EGF_1; 5.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS50026; EGF_3; 5.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Calcium; Cell adhesion; Cell membrane;
KW   Complete proteome; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     38       {ECO:0000255}.
FT   CHAIN        39   4699       Fat-like cadherin-related tumor
FT                                suppressor homolog.
FT                                /FTId=PRO_0000004016.
FT   TOPO_DOM     39   4285       Extracellular. {ECO:0000255}.
FT   TRANSMEM   4286   4306       Helical. {ECO:0000255}.
FT   TOPO_DOM   4307   4699       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       63    183       Cadherin 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      184    291       Cadherin 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      288    400       Cadherin 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      401    507       Cadherin 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      508    613       Cadherin 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      614    716       Cadherin 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      773    877       Cadherin 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      878    980       Cadherin 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      981   1088       Cadherin 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     1089   1198       Cadherin 10. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     1194   1299       Cadherin 11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     1300   1405       Cadherin 12. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     1408   1506       Cadherin 13. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     1507   1612       Cadherin 14. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     1613   1717       Cadherin 15. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     1718   1815       Cadherin 16. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     1816   1932       Cadherin 17. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     1933   2033       Cadherin 18. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     2034   2140       Cadherin 19. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     2141   2241       Cadherin 20. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     2242   2341       Cadherin 21. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     2342   2449       Cadherin 22. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     2450   2551       Cadherin 23. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     2552   2654       Cadherin 24. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     2655   2763       Cadherin 25. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     2764   2860       Cadherin 26. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     2861   2967       Cadherin 27. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     2968   3072       Cadherin 28. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     3068   3169       Cadherin 29. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     3170   3273       Cadherin 30. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     3274   3378       Cadherin 31. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     3379   3483       Cadherin 32. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     3484   3588       Cadherin 33. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     3589   3696       Cadherin 34. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     3865   3903       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     3921   4105       Laminin G-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN     4113   4150       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     4152   4189       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     4190   4225       EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     4227   4263       EGF-like 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   CARBOHYD     68     68       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    159    159       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    367    367       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    782    782       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    846    846       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    926    926       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1109   1109       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1201   1201       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1315   1315       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1442   1442       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1476   1476       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1514   1514       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID   3807   3819       {ECO:0000255}.
FT   DISULFID   3814   3851       {ECO:0000255}.
FT   DISULFID   3853   3862       {ECO:0000255}.
FT   DISULFID   3869   3880       {ECO:0000255}.
FT   DISULFID   3874   3891       {ECO:0000255}.
FT   DISULFID   3893   3902       {ECO:0000255}.
FT   DISULFID   4071   4105       {ECO:0000250}.
FT   DISULFID   4117   4128       {ECO:0000255}.
FT   DISULFID   4122   4138       {ECO:0000255}.
FT   DISULFID   4140   4149       {ECO:0000255}.
FT   DISULFID   4156   4167       {ECO:0000255}.
FT   DISULFID   4161   4177       {ECO:0000255}.
FT   DISULFID   4179   4188       {ECO:0000255}.
FT   DISULFID   4194   4205       {ECO:0000250}.
FT   DISULFID   4199   4214       {ECO:0000250}.
FT   DISULFID   4216   4224       {ECO:0000250}.
FT   DISULFID   4231   4242       {ECO:0000255}.
FT   DISULFID   4236   4251       {ECO:0000255}.
FT   DISULFID   4253   4262       {ECO:0000255}.
FT   VAR_SEQ    4601   4611       VPLPSKVSHSC -> G (in isoform C).
FT                                {ECO:0000303|PubMed:12537569}.
FT                                /FTId=VSP_054450.
FT   CONFLICT   3946   3946       G -> E (in Ref. 3; AAL28503).
FT                                {ECO:0000305}.
SQ   SEQUENCE   4699 AA;  523781 MW;  1798A54345758C36 CRC64;
     MFTMKIKKYV TPVKRKAFTI LQWISLLCSL WLIPTVQSKA DEKHTATLEY RLENQLQDLY
     RFSHSVYNVT IPENSLGKTY AKGVLHERLA GLRVGLNAEV KYRIISGDKE KLFKAEEKLV
     GDFAFLAIRT RTNNVVLNRE KTEEYVIRVK AHVHLHDRNV SSYETEANIH IKVLDRNDLS
     PLFYPTQYTV VIPEDTPKYQ SILKVTADDA DLGINGEIYY SLLMDSEYFA IHPTTGEITL
     LQQLQYAENS HFELTVVAYD RGSWVNHQNH QASKTKVSIS VKQVNFYAPE IFTKTFSSVT
     PTSNPLIYGI VRVNDKDTGI NGNIGRLEIV DGNPDGTFLL KAAETKDEYY IELNQFAHLN
     QQHFIYNLTL LAEDLGTPRR FAYKSVPIQI KPESKNIPIF TQEIYEVSIP ETAPINMPVI
     RLKVSDPDLG KNALVYLEIV GGNEGDEFRI NPDSGMLYTA KQLDAEKKSS YTLTVSAIDQ
     ANVGSRKQSS AKVKISVQDM NDNDPIFENV NKVISINENN LAGSFVVKLT AKDRDSGENS
     YISYSIANLN AVPFEIDHFS GIVKTTSLLD FETMKRNYEL IIRASDWGLP YRRQTEIKLS
     IVVKDINDNR PQFERVNCYG KVTKSAPMGT EVFVTSAIDF DAGDIISYRL SDGNEDGCFN
     LDPTSGSLSI SCDLKKTTLT NRILKVSATD GTHFSDDLII NVHLMPEDLG GDSSILHGFG
     SFECRETGVA RRLAETLSLA EKNNVKSASP SVFSDLSLTP SRYGQNVHRP EFVNFPQELS
     INESVQLGET VAWIEAKDRD LGYNGKLVFA ISDGDYDSVF RIDPDRGELQ IIGYLDRERQ
     NEYVLNITVY DLGNPTKSTS KMLPITILDV NDNRPVIQKT LATFRLTESA RIGTVVHCLH
     ATDADSGINA QVTYALSVEC SDFTVNATTG CLRLNKPLDR EKQDNYALHI TAKDGGSPVL
     SSEALVYVLV DDVNDNAPVF GVQEYIFKVR EDLPRGTVLA VIEAVDEDIG PNAEIQFSLK
     EETQDEELFR IDKHTGAIRT QGYLDYENKQ VHNLIVSAID GGDPSLTSDM SIVIMIIDVN
     ENRFAPEFDD FVYEGKVKEN KPKGTFVMNV TARDMDTVDL NSKITYSITG GDGLGIFAVN
     DQGSITSLSQ LDAETKNFYW LTLCAQDCAI VPLSNCVEVY IQVENENDNI PLTDKPVYYV
     NVTEASVENV EIITLKAFDP DIDPTQTITY NIVSGNLVGY FEIDSKTGVI KTTERKLDRE
     NQAEHILEVA ISDNGSPVLS STSRIVVSVL DINDNSPEFD QRVYKVQVPS SATVNQSIFQ
     VHAIDSDSGE NGRITYSIKS GKGKNKFRID SQRGHIHIAK PLDSDNEFEI HIKAEDNGIP
     KKSQTARVNI VVVPVNPNSQ NAPLIVRKTS ENVVDLTEND KPGFLVTQIL AVDDDNDQLW
     YNISNGNDDN TFYIGQDNGN ILLSKYLDYE TQQSYNLTIS VTDGTFTAFT NLLVQVIDIN
     DNPPQFAKDV YHVNISENIE EESVIMQLHA TDRDEDKKLF YHLHATQDPS SLALFRIDSI
     SGNVIVTQRL DFEKTAQHIL IVFVKDQGAP GKRNYAKIIV NVHDHNDHHP EFTAKIIQSK
     VPESAAIGSK LAEVRAIDRD SGHNAEIQYS IITGNVGSVF EIDPTFGIIT LAGNLNINKI
     QEYMLQVKAV DLGNPPLSSQ IPVHIIVTMS ENDPPKFPTN NIAIEIFENL PIGTFVTQVT
     ARSSSSIFFN IISGNINESF RINPSTGVIV INGNIDYESI KVFNLTVKGT NMAAESSCQN
     IIIHILDAND NIPYFVQNEY VGALPESAAI GSYVLKVHDS SKDHLTLQVK DADVGVNGMV
     EYHIVDDLAK NFFKIDSTTG AIELLRQLDY ETNAGYTFDV TVSDMGKPKL HSTTTAHVTI
     RVINVNDCPP VFNERELNVT LFLPTFENVF VRQVSAKDAD NDTLRFDIVD GNTNECFQIE
     KYTGIITTRN FEILNNENDR DYALHVRASD GIFSAILIVK IKVLSAIDSN FAFQRESYRF
     SAFENNTKVA TIGLVNVIGN TLDENVEYRI LNPTQLFDIG ISSGALKTTG VIFDREVKDL
     YRLFVEAKSM LYDGMNSNVR RAVTSIDISV LDVNDNCPLF VNMPYYATVS IDDPKGTIIM
     QVKAIDLDSA ENGEVRYELK KGNGELFKLD RKSGELSIKQ HVEGHNRNYE LTVAAYDGAI
     TPCSSEAPLQ VKVIDRSMPV FEKQFYTVSV KEDVEMYSAL SVSIEAESPL GRSLIYTISS
     ESQSFEIDYN TGSIFVVNEL DYEKISSHDV SIRATDSLSG VYAEVVLSVS IMDVNDCYPE
     IESDIYNLTI PENASFGTQI LKINATDNDS GANAKLSYYI ESINGQNNSE LFYIDVTDGN
     LYLKTPLDYE QIKYHHIVVN VKDHGSPSLS SRSNVFITVK DLNDNAPCFV EPSYFTKVSV
     AAVRGQFVAL PKAYDKDISD TDSLEYKIVY GNELQTYSID KLTGVISLQN MLNFTDKSST
     VLNISVSDGV HTAYARLKIS LLPENVYSPL FDQSTYEAQV PENLLHGHNI ITVKASDGDF
     GTYANLYYEI VSEEMKKIFL IDQTTGVITS KVTFDREKKD EYVVLLKVSD GGGKFGFASL
     KVIVVDVNDN VPYFLLKEYK MVVSTTVEAN QTILTVKAKD DDIVDNGSVH FQIVQKSNDK
     AVKDVIEINE KTGDIVFKSK AESYGVNSYQ FFVRASDRGE PQFHSEVPVS IEIIETDANI
     PTFEKSSVLL KIIESTPPGT VLTKLHMIGN YTFKFSIAAD QDHFMISDSG ELILQQTLDR
     EQQESHNLIV VAETSTVPVF FAYADVLIDV RDENDNYPKF DNTFYSASVA ENSEKVISLV
     KVSATDADTG PNGDIRYYLE SDTENIQNIF DIDIYSGWIT LLTSLDREVQ SEYNFKVIAA
     DNGHPKHDAK VPVTIKIVDY NDNAPVFKLP IEGLSVFENA LPGTVLINLL LIDPDIEKQE
     MDFFIVSGDK QAQFQIGKSG ELFIAKPLDR EQLMFYNLSI IATDGKFTAK ANVEIDVKDI
     NDNTPYCLKP RYHISTNESI SIGTTLVEVK AIDFDFQSKL RFYLSGKGAD DFSIGKESGI
     LKVASALDRE TTPKYKLVAH VQDGKDFTQE CFSEIIITVN DINDNMPIFS MAQYRVSVPE
     DAQLNTLITK VHAMDKDFGV NRQIKYSLMG ENHDYFKISK STGIIRLHKS LDRETISLFN
     LTVKAEDCGV PKLHSIATVA VNILDINDNP PEFSMRQYSC KILENATHGT EVCKVYATSI
     DIGVNADIHY FIMSGNEQGK FKMDSTTGDL VLNATLDYEM SKFYFLTIQA IDGGTPPLSN
     NAYVNISILD INDNSPTFLQ NLYRINVNED IFVGSKILDV KATDEDSDVN GLVTYNIERG
     DNIGQFSIDP KNGTISVSRP LDRETISHYT LEIQACDQGD PQRCNSVPIN INILDTNDNA
     PIFSSSNYSV VLQENRLLGY VFLTFKISDA DETPNTTPYT FDIRSGNEGG LFRLEQDGSL
     RTASRFNHNL QDEFVIQVRV FDNGTPPLYS DAWVVVKIIE ESQYPPIVTP LEVTINSFED
     DFSGAFIGKV HASDQDKYDE LNFSLVSGPD DMYQSSKLFN ISNNTGKIYA ISNLDIGLYK
     LNVSVSDGKF HVFSIVKINV ELVTNDMLKE SVVIRFRRIS ASEFLLSHRK TFMRSIRNIM
     RCRQKDVILI TLQSDYQKAS QHAVGNRRAR SIDSDLNVVF AVRKQQIIPD SDEFFTSDEI
     RQTLIDKKNE IENETNLVVE DVLPSTCQSN KNDCVHGECK QILQILKNNV TTTFTDVISF
     AAPSYIPVNT CVCRPGFDGK HCKETVNACS TDPCSPQRIC MPSGSALGYQ CVCPKGFSGT
     YCERKSSKCS NESCDMGLFT AVSFGGKSYA HYKINKVKAK FTLENGFSYS LQIRTVQQTG
     TLLYASGKVD YNILEIINGA VQYRFDLGSG EGVISVSSIN ISDGEWHQIS LERSLNSAKV
     MVDNKHVSHG SAPGVNGILN IQSNDIFVGA EVRPHPSIIG YEDIQRGFIG CMANIKIAKE
     SLPLYISGGS TIAALKRFTN VEFKCDPSNV LVRLGICGSQ PCANSGICKE LDTDVFECAC
     QPRYSGKHCE IDLDPCSSGP CLFGGRCDYH GPNNYSCTCP IHLSGKRCEY GKFCTPNPCK
     NGGICEEGDG ISHCMCRGYT GPTCEIDVDE CENQPCGNGA TCINEPGSFR CICPSYLTGA
     SCGDPLYSNS ISTKLKNFSI EHISGIISGV AVVLVIISCV LCCVVLKRSS SSKRRNRLEK
     DKNKSSYKEA NLNSLVDKDN YCKPNVKLSN LEVNQRPISY TAVPNDNLVL SNRNFVNNLD
     ILRSYGSAGD ELENVPFEYQ KVNRNKQHVN INSCHSTDAD NAYKQEWCEQ MHLRTFSENK
     LNNELKRDFG PSVSRFSTGK LIQVEMPNVC HSSSANFVDY SALANGQYHW DCSDWVRKSH
     NPLPDITEVP GAEIADSSSL HSNDSNESKS KKAFFVHRED GDVDPTRDIA ALNEDIGSEY
     LDSEAESCLE PFMLPRSSNQ PLSRLSSFNN IENEDYKSNT VPLPSKVSHS CKVYLRHPDS
     YLPTMHFPSE TDGESSMTEG PISRMEIKTR RTISENSEEA YLFPCTVGEI GSNSNISVRL
     CEIEDSELEE FLPQQQTNN
//
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