FAT2_DROME
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 03-AUG-2022, entry version 180.
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; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC 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., 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 [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., 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3360-4401 (ISOFORMS C/D), AND
RP 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., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA 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 Drosophila
RT 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 chamber
CC shape and elongation of the egg chamber during oogenesis
CC (PubMed:19906848, PubMed:23369713). Required for the correct planar
CC polarization of Rab10 within the basal follicle cell epithelium and is
CC therefore indirectly involved in the Rab10-dependent remodeling of the
CC basal membrane during egg chamber elongation (PubMed:23369713).
CC {ECO:0000269|PubMed:19906848, ECO:0000269|PubMed:23369713}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein. Note=Accumulates on cell membranes where the planar oriented
CC actin filaments terminate.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=D;
CC IsoId=Q9VW71-1; Sequence=Displayed;
CC Name=C;
CC IsoId=Q9VW71-2; Sequence=VSP_054450;
CC -!- TISSUE SPECIFICITY: Localizes where basal actin filaments terminate.
CC {ECO:0000269|PubMed:19906848}.
CC -!- DISRUPTION PHENOTYPE: Defects in actin filament orientation correlate
CC with a failure of egg chambers to elongate during oogenesis
CC (PubMed:19906848). In follicle cells, Rab10 protein polarizes normally
CC along the apical-basal axis, but is mislocalized within the epithelial
CC plane (PubMed:23369713). Epithelia migration is impaired and the
CC structure of the basal 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=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAM50035.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAM50035.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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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 SMR; Q9VW71; -.
DR BioGRID; 65458; 5.
DR DIP; DIP-24050N; -.
DR IntAct; Q9VW71; 7.
DR STRING; 7227.FBpp0304968; -.
DR GlyGen; Q9VW71; 12 sites.
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 VEuPathDB; VectorBase:FBgn0261574; -.
DR eggNOG; KOG1219; Eukaryota.
DR GeneTree; ENSGT00940000166124; -.
DR InParanoid; Q9VW71; -.
DR OMA; NPPCFVE; -.
DR BioGRID-ORCS; 40191; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 40191; -.
DR PRO; PR:Q9VW71; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0261574; Expressed in eye disc (Drosophila) and 26 other tissues.
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:0098609; P:cell-cell adhesion; IBA:GO_Central.
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 CDD; cd00110; LamG; 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; 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 Disulfide bond; EGF-like domain; Glycoprotein; Membrane;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..38
FT /evidence="ECO:0000255"
FT CHAIN 39..4699
FT /note="Fat-like cadherin-related tumor suppressor homolog"
FT /id="PRO_0000004016"
FT TOPO_DOM 39..4285
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 4286..4306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 4307..4699
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 63..183
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 184..291
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 288..400
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 401..507
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 508..613
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 614..716
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 773..877
FT /note="Cadherin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 878..980
FT /note="Cadherin 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 981..1088
FT /note="Cadherin 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1089..1198
FT /note="Cadherin 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1194..1299
FT /note="Cadherin 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1300..1405
FT /note="Cadherin 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1408..1506
FT /note="Cadherin 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1507..1612
FT /note="Cadherin 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1613..1717
FT /note="Cadherin 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1718..1815
FT /note="Cadherin 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1816..1932
FT /note="Cadherin 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1933..2033
FT /note="Cadherin 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2034..2140
FT /note="Cadherin 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2141..2241
FT /note="Cadherin 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2242..2341
FT /note="Cadherin 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2342..2449
FT /note="Cadherin 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2450..2551
FT /note="Cadherin 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2552..2654
FT /note="Cadherin 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2655..2763
FT /note="Cadherin 25"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2764..2860
FT /note="Cadherin 26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2861..2967
FT /note="Cadherin 27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2968..3072
FT /note="Cadherin 28"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3068..3169
FT /note="Cadherin 29"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3170..3273
FT /note="Cadherin 30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3274..3378
FT /note="Cadherin 31"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3379..3483
FT /note="Cadherin 32"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3484..3588
FT /note="Cadherin 33"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3589..3696
FT /note="Cadherin 34"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3865..3903
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 3921..4105
FT /note="Laminin G-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 4113..4150
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 4152..4189
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 4190..4225
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 4227..4263
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 782
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 846
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 926
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 1201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1442
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1476
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1514
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 3807..3819
FT /evidence="ECO:0000255"
FT DISULFID 3814..3851
FT /evidence="ECO:0000255"
FT DISULFID 3853..3862
FT /evidence="ECO:0000255"
FT DISULFID 3869..3880
FT /evidence="ECO:0000255"
FT DISULFID 3874..3891
FT /evidence="ECO:0000255"
FT DISULFID 3893..3902
FT /evidence="ECO:0000255"
FT DISULFID 4071..4105
FT /evidence="ECO:0000250"
FT DISULFID 4117..4128
FT /evidence="ECO:0000255"
FT DISULFID 4122..4138
FT /evidence="ECO:0000255"
FT DISULFID 4140..4149
FT /evidence="ECO:0000255"
FT DISULFID 4156..4167
FT /evidence="ECO:0000255"
FT DISULFID 4161..4177
FT /evidence="ECO:0000255"
FT DISULFID 4179..4188
FT /evidence="ECO:0000255"
FT DISULFID 4194..4205
FT /evidence="ECO:0000250"
FT DISULFID 4199..4214
FT /evidence="ECO:0000250"
FT DISULFID 4216..4224
FT /evidence="ECO:0000250"
FT DISULFID 4231..4242
FT /evidence="ECO:0000255"
FT DISULFID 4236..4251
FT /evidence="ECO:0000255"
FT DISULFID 4253..4262
FT /evidence="ECO:0000255"
FT VAR_SEQ 4601..4611
FT /note="VPLPSKVSHSC -> G (in isoform C)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_054450"
FT CONFLICT 3946
FT /note="G -> E (in Ref. 3; AAL28503)"
FT /evidence="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
