ID YL_DROME Reviewed; 1984 AA.
AC P98163; Q86P52; Q9VY56;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 27-MAR-2024, entry version 185.
DE RecName: Full=Vitellogenin receptor Yl {ECO:0000303|PubMed:7878005};
DE AltName: Full=Protein yolkless;
DE Short=Yl;
DE Flags: Precursor;
GN Name=yl {ECO:0000312|FlyBase:FBgn0004649};
GN ORFNames=CG1372 {ECO:0000312|FlyBase:FBgn0004649};
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 B), AND FUNCTION.
RC TISSUE=Ovary;
RX PubMed=7878005; DOI=10.1073/pnas.92.5.1485;
RA Schonbaum C.P., Lee S., Mahowald A.P.;
RT "The Drosophila yolkless gene encodes a vitellogenin receptor belonging to
RT the low density lipoprotein receptor superfamily.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:1485-1489(1995).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION.
RX PubMed=2886508; DOI=10.1083/jcb.105.1.199;
RA DiMario P.J., Mahowald A.P.;
RT "Female sterile (1) yolkless: a recessive female sterile mutation in
RT Drosophila melanogaster with depressed numbers of coated pits and coated
RT vesicles within the developing oocytes.";
RL J. Cell Biol. 105:199-206(1987).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=10679010; DOI=10.1091/mbc.11.2.511;
RA Schonbaum C.P., Perrino J.J., Mahowald A.P.;
RT "Regulation of the vitellogenin receptor during Drosophila melanogaster
RT oogenesis.";
RL Mol. Biol. Cell 11:511-521(2000).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1926, AND IDENTIFICATION BY
RP 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 [8]
RP FUNCTION, INTERACTION WITH OSK, AND DISRUPTION PHENOTYPE.
RX PubMed=33891588; DOI=10.1371/journal.pbio.3001183;
RA Tanaka T., Tani N., Nakamura A.;
RT "Receptor-mediated yolk uptake is required for oskar mRNA localization and
RT cortical anchorage of germ plasm components in the Drosophila oocyte.";
RL PLoS Biol. 19:e3001183-e3001183(2021).
CC -!- FUNCTION: Cell surface receptor involved in uptake of vitellogenins
CC (yolk proteins) into developing oocytes by receptor-mediated
CC endocytosis (PubMed:7878005, PubMed:2886508, PubMed:10679010). May also
CC mediate uptake of apolpp/apolipophorins and their incorporation into
CC yolk granules (PubMed:33891588). Along with its ligands, required for
CC maintenance of microtubule plus-end orientation towards the posterior
CC pole of oocytes (PubMed:33891588). Involved in polarized localization
CC of germ plasm components, such as osk mRNA and vas protein, to the
CC oocyte posterior cortex (PubMed:33891588). Receptor-mediated
CC endocytosis of vitellogenin receptor ligands is critical for osk
CC (isoform A) mediated actin reorganization and the anchoring of germ
CC plasm components to the oocyte cortex (PubMed:33891588).
CC {ECO:0000269|PubMed:10679010, ECO:0000269|PubMed:2886508,
CC ECO:0000269|PubMed:33891588, ECO:0000269|PubMed:7878005}.
CC -!- SUBUNIT: Interacts with osk (isoform A). {ECO:0000269|PubMed:33891588}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:10679010}.
CC Cytoplasm, cell cortex {ECO:0000269|PubMed:10679010}. Cytoplasmic
CC vesicle, clathrin-coated vesicle membrane
CC {ECO:0000269|PubMed:10679010}; Single-pass membrane protein
CC {ECO:0000255}. Early endosome membrane {ECO:0000269|PubMed:10679010};
CC Single-pass membrane protein {ECO:0000255}. Endosome, multivesicular
CC body lumen {ECO:0000269|PubMed:10679010}. Note=Distributed throughout
CC the oocyte during oogenesis (PubMed:10679010). At the start of
CC vitellogenesis during stage 8 of oogenesis redistributes to the oocyte
CC cell cortex (PubMed:10679010). Associated with multivesicular
CC structures that mature into yolk granules (PubMed:10679010).
CC {ECO:0000269|PubMed:10679010}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B;
CC IsoId=P98163-1; Sequence=Displayed;
CC Name=A;
CC IsoId=P98163-2; Sequence=VSP_010300;
CC -!- TISSUE SPECIFICITY: Ovary.
CC -!- DEVELOPMENTAL STAGE: Detected in the oocyte from region 3 in the
CC germarium up to stage 10 of oogenesis (at protein level)
CC (PubMed:10679010). During oogenesis expressed in germline-derived nurse
CC cells and oocyte from region 2A in the germarium onwards, and
CC accumulates to high concentration in the oocyte (PubMed:10679010).
CC Expression in nurse cells becomes more pronounced at stage 9 and 10 of
CC oogenesis (PubMed:10679010). {ECO:0000269|PubMed:10679010}.
CC -!- DISRUPTION PHENOTYPE: Disruption of vitellogenesis resulting in failure
CC of oocytes to take up yolk proteins and form yolk granules
CC (PubMed:33891588). Oocytes complete oogenesis without morphological
CC abnormalities but eggs are shrivelled and do not hatch
CC (PubMed:33891588). {ECO:0000269|PubMed:33891588}.
CC -!- SIMILARITY: Belongs to the LDLR family. {ECO:0000305}.
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DR EMBL; U13637; AAB60217.1; -; mRNA.
DR EMBL; AE014298; AAF48349.2; -; Genomic_DNA.
DR EMBL; AE014298; AAS65339.1; -; Genomic_DNA.
DR EMBL; BT003478; AAO39481.1; -; mRNA.
DR PIR; T13171; T13171.
DR RefSeq; NP_511151.2; NM_078596.3. [P98163-2]
DR RefSeq; NP_996433.1; NM_206710.2. [P98163-1]
DR AlphaFoldDB; P98163; -.
DR SMR; P98163; -.
DR BioGRID; 58737; 8.
DR IntAct; P98163; 4.
DR MINT; P98163; -.
DR STRING; 7227.FBpp0073715; -.
DR GlyCosmos; P98163; 13 sites, No reported glycans.
DR GlyGen; P98163; 14 sites, 1 O-linked glycan (1 site).
DR iPTMnet; P98163; -.
DR PaxDb; 7227-FBpp0073715; -.
DR EnsemblMetazoa; FBtr0073897; FBpp0073714; FBgn0004649. [P98163-2]
DR EnsemblMetazoa; FBtr0073898; FBpp0073715; FBgn0004649. [P98163-1]
DR GeneID; 32367; -.
DR KEGG; dme:Dmel_CG1372; -.
DR AGR; FB:FBgn0004649; -.
DR CTD; 32367; -.
DR FlyBase; FBgn0004649; yl.
DR VEuPathDB; VectorBase:FBgn0004649; -.
DR eggNOG; KOG1215; Eukaryota.
DR GeneTree; ENSGT00940000165170; -.
DR InParanoid; P98163; -.
DR OMA; ECLTMAH; -.
DR OrthoDB; 2877710at2759; -.
DR PhylomeDB; P98163; -.
DR Reactome; R-DME-8866427; VLDLR internalisation and degradation.
DR Reactome; R-DME-9758890; Transport of RCbl within the body.
DR BioGRID-ORCS; 32367; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 32367; -.
DR PRO; PR:P98163; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0004649; Expressed in ovary and 7 other cell types or tissues.
DR ExpressionAtlas; P98163; baseline and differential.
DR Genevisible; P98163; DM.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030135; C:coated vesicle; IDA:FlyBase.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:FlyBase.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008196; F:vitellogenin receptor activity; ISS:FlyBase.
DR GO; GO:0048477; P:oogenesis; TAS:FlyBase.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00112; LDLa; 13.
DR Gene3D; 2.10.25.10; Laminin; 4.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 13.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 3.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR026823; cEGF.
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; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR000033; LDLR_classB_rpt.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR PANTHER; PTHR22722; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 2-RELATED; 1.
DR PANTHER; PTHR22722:SF14; MEGALIN, ISOFORM A; 1.
DR Pfam; PF12662; cEGF; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF00057; Ldl_recept_a; 12.
DR Pfam; PF00058; Ldl_recept_b; 3.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 7.
DR SMART; SM00179; EGF_CA; 4.
DR SMART; SM00192; LDLa; 13.
DR SMART; SM00135; LY; 10.
DR SUPFAM; SSF57196; EGF/Laminin; 4.
DR SUPFAM; SSF57424; LDL receptor-like module; 13.
DR SUPFAM; SSF63825; YWTD domain; 3.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS01209; LDLRA_1; 12.
DR PROSITE; PS50068; LDLRA_2; 13.
DR PROSITE; PS51120; LDLRB; 10.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cytoplasm; Cytoplasmic vesicle;
KW Disulfide bond; EGF-like domain; Endocytosis; Endosome; Glycoprotein;
KW Membrane; Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..?
FT /evidence="ECO:0000255"
FT CHAIN ?..1984
FT /note="Vitellogenin receptor Yl"
FT /id="PRO_0000007781"
FT TOPO_DOM ?..1799
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1800..1820
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1821..1984
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 89..125
FT /note="LDL-receptor class A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 128..167
FT /note="LDL-receptor class A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 183..221
FT /note="LDL-receptor class A 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 226..263
FT /note="LDL-receptor class A 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 265..305
FT /note="LDL-receptor class A 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 306..343
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 348..388
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 441..485
FT /note="LDL-receptor class B 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 486..528
FT /note="LDL-receptor class B 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 529..572
FT /note="LDL-receptor class B 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 573..615
FT /note="LDL-receptor class B 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 750..792
FT /note="LDL-receptor class B 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 793..836
FT /note="LDL-receptor class B 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 884..925
FT /note="LDL-receptor class B 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 934..940
FT /note="LDL-receptor class B 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT DOMAIN 1024..1063
FT /note="LDL-receptor class A 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1073..1110
FT /note="LDL-receptor class A 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1117..1153
FT /note="LDL-receptor class A 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1157..1194
FT /note="LDL-receptor class A 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1197..1233
FT /note="LDL-receptor class A 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1242..1280
FT /note="LDL-receptor class A 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1282..1319
FT /note="LDL-receptor class A 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1339..1376
FT /note="LDL-receptor class A 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1418..1453
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 1588..1637
FT /note="LDL-receptor class B 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 1638..1687
FT /note="LDL-receptor class B 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1927..1951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1965..1984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 1837
FT /note="Critical for endocytosis"
FT /evidence="ECO:0000255"
FT SITE 1878
FT /note="Critical for endocytosis"
FT /evidence="ECO:0000255"
FT SITE 1892
FT /note="Critical for endocytosis"
FT /evidence="ECO:0000255"
FT MOD_RES 1926
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 384
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 666
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 749
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 782
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1022
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1475
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1490
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 90..102
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 97..115
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 109..124
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 129..144
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 137..157
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 151..166
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 184..197
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 191..210
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 204..220
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 227..239
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 234..253
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 247..262
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 266..281
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 275..294
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 288..304
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 310..321
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 315..331
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 352..363
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 359..372
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 374..387
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1025..1040
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1035..1053
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1047..1062
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1074..1087
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1081..1100
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1094..1109
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1118..1130
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1125..1143
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1137..1152
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1158..1170
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1165..1183
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1177..1193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1198..1210
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1205..1223
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1217..1232
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1243..1257
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1250..1270
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1264..1279
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1283..1296
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1290..1309
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1303..1318
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1340..1352
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1347..1365
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1359..1375
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1422..1432
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1428..1441
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VAR_SEQ 1925..1984
FT /note="ESKLHALDGGGAGGDGDGGRGVGRQVPDILVADMDDDAAKSAGQFGGNYAGN
FT DANARFVS -> VSSDGGQMAVEDM (in isoform A)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_010300"
FT CONFLICT 457
FT /note="K -> E (in Ref. 4; AAO39481)"
FT /evidence="ECO:0000305"
FT CONFLICT 470
FT /note="T -> S (in Ref. 4; AAO39481)"
FT /evidence="ECO:0000305"
FT CONFLICT 727
FT /note="R -> A (in Ref. 1; AAB60217)"
FT /evidence="ECO:0000305"
FT CONFLICT 1068
FT /note="R -> H (in Ref. 1; AAB60217)"
FT /evidence="ECO:0000305"
FT CONFLICT 1077
FT /note="N -> S (in Ref. 1; AAB60217)"
FT /evidence="ECO:0000305"
FT CONFLICT 1156
FT /note="S -> L (in Ref. 1; AAB60217)"
FT /evidence="ECO:0000305"
FT CONFLICT 1203
FT /note="Q -> H (in Ref. 1; AAB60217)"
FT /evidence="ECO:0000305"
FT CONFLICT 1207
FT /note="L -> S (in Ref. 1; AAB60217)"
FT /evidence="ECO:0000305"
FT CONFLICT 1261
FT /note="T -> A (in Ref. 1; AAB60217)"
FT /evidence="ECO:0000305"
FT CONFLICT 1519
FT /note="I -> V (in Ref. 1; AAB60217)"
FT /evidence="ECO:0000305"
FT CONFLICT 1696
FT /note="V -> M (in Ref. 1; AAB60217)"
FT /evidence="ECO:0000305"
FT CONFLICT 1884
FT /note="T -> S (in Ref. 1; AAB60217)"
FT /evidence="ECO:0000305"
FT CONFLICT 1944
FT /note="R -> C (in Ref. 1; AAB60217)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1984 AA; 219521 MW; 0B6F9CF4EFC4914C CRC64;
MCQAEHQVHP SEQRIRVESP KMTASRRGFN LTSQTRAHPS SGGSTSSRYG NCQRTHLIIN
GRHVAISLLL LVGLCGGTAA GTPGSADTRC DAGQFQCRDG GCILQAKMCD GRGDCKDSSD
ELDCDYRLCR PPHWFPCAQP HGACLAAELM CNGIDNCPGG EDELNCPVRP GFRFGDTAHR
MRSCSKYEFM CQQDRTCIPI DFMCDGRPDC TDKSDEVAGC KQAEITCPGE GHLCANGRCL
RRKQWVCDGV DDCGDGSDER GCLNLCEPQK GKFLCRNRET CLTLSEVCDG HSDCSDGSDE
TDLCHSKPDC DAKKCALGAK CHMMPASGAE CFCPKGFRLA KFEDKCEDVD ECKEQDDLCS
QGCENTSGGY RCVCDAGYLL DKDNRTCRAV VYGSKEQQPL LLYTTQMTIM GMHLREDNVR
NHVYQVAGNL SKVIGVAYDG SHIYWTNIQN EAESIVKANG DGSNAEILLT SGLDAPEDLA
VDWLTQNIYF SDNIMRHIAV CSNDGLNCAV LVTQDVHQPR SLAVWPQKGL MFWTDWGEKP
MIGRASMDGS RSRPIVSDNI EWPNGIALDM HQQRIYWVDA KLGSVQTVRP DGTGRRTVLD
GMLKHPYGLA IFEDQLYWSD WATKSVHACH KFSGKDHRIL AKDRTIYAVH IYHPAKQPNS
PHGCENATCS HLCLLAEPEI GGHSCACPDG MRLAPDHRRC MLMEKRQRLF IGLGQVLLEI
EHTAFGRHQV SKSYTLPCLI NEMVYNRING SLIIADNDQR LILEFQPESH ESNVLVRSNL
GNVSALAFDH LSRNLYWADT ERAVIEVLSL QTRHRALIRF FPGQEVPIGL TVMPAEGYLY
VVLKAKRHSH IDKIPLSGKG EQVHVFEDDL GDDDIKLVTD YETQTIFWSD SDLGRISYSN
YRVPHSQIFR GKLRRPYSLA MVHHDLFWNE LGTPRIYWTH KSNMGPRKVI DIMEKDDPAA
IMPYVPVATP NGIPLAASSP VGQESHPCQQ QNGGCSHICV GEGPYHSICL CPAGFVYRDA
GNRTCVEALD CEFRCHSGEC LTMNHRCNGR RDCVDNSDEM NCDEEHRRKP KVLCSPNQFA
CHSGEQCVDK ERRCDNRKDC HDHSDEQHCE KFDKSKKCHV HQHGCDNGKC VDSSLVCDGT
NDCGDNSDEL LCEATSRCEP GMFQCGSGSC IAGSWECDGR IDCSDGSDEH DKCVHRSCPP
DMQRCLLGQC LDRSLVCDGH NDCGDKSDEL NCGTDSSTMN ISCAEDQYQC TSNLKICLPS
TVRCNGTTEC PRGEDEADCG DVCSIYEFKC RSGRECIRRE FRCDGQKDCG DGSDELSCEL
EKGHHNQSQI QPWSTSSRSC RPHLFDCQDG ECVDLSRVCN NFPDCTNGHD EGPKCATACR
SASGRQVCQH KCRATPAGAV CSCFDGYRLD ADQKSCLDID ECQEQQPCAQ LCENTLGGYQ
CQCHADFMLR QDRVSCKSLQ SGATLLFSSF NEVRNLSEQP VMLNVAWSAN DSRITGFDLA
MHRQMGYFSA EDEGIVYQID LQTKVIVRAL GLPAPTKLSV DWVTGNVYVL SGAQEIQACS
FVGRMCGRIV HVKSPRHVKH LAVDGYHARI FYIVIRTEGY GQTSSEIHMA RLDGSRRDML
LQRSESFMTA LTTDPHQQLL YFVDQHMRTL ERISYRLKTG PMRRPEIMLQ KSNALMHPSG
LSVYENNAFI VNLGSVEAVQ CALYGSRICH KISINVLNAQ DIVVAGRSRQ PQKASHPCAH
AHCHGLCLQA DYGYECMCGN RLVAEGERCP HGSGNEVAVL GAVNSLELEH EHEQNGHFHW
LMALFVLAAG SLIAGLGYMY YQYRQRGHTD LNINMHFQNP LATLGGTKAF LEHERAEAGV
GFTTETGTVS SRGSNDTFTT TSATSSFAAQ QFSVPNALQR LLRPRQSASG DPMAQELLLE
SPSRESKLHA LDGGGAGGDG DGGRGVGRQV PDILVADMDD DAAKSAGQFG GNYAGNDANA
RFVS
//
