ID   CELR2_MOUSE             Reviewed;        2919 AA.
AC   Q9R0M0; A2AEE7; Q99K26; Q9Z2R4;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   10-APR-2019, sequence version 3.
DT   02-SEP-2026, entry version 201.
DE   RecName: Full=Cadherin EGF LAG seven-pass G-type receptor 2;
DE   AltName: Full=Flamingo homolog;
DE   Flags: Precursor;
GN   Name=Celsr2 {ECO:0000312|MGI:MGI:1858235};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PROTEIN SEQUENCE OF 158-170 AND 205-215, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1912-2795, AND TISSUE SPECIFICITY.
RX   PubMed=10790539; DOI=10.1007/s003350010073;
RA   Formstone C.J., Barclay J., Rees M., Little P.F.R.;
RT   "Chromosomal localization of Celsr2 and Celsr3 in the mouse; Celsr3 is a
RT   candidate for the tippy (tip) lethal mutant on chromosome 9.";
RL   Mamm. Genome 11:392-394(2000).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2013-2919 (ISOFORM 2).
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=11850187; DOI=10.1016/s0925-4773(01)00623-2;
RA   Tissir F., De-Backer O., Goffinet A.M., Lambert de Rouvroit C.A.;
RT   "Developmental expression profiles of Celsr (Flamingo) genes in the
RT   mouse.";
RL   Mech. Dev. 112:157-160(2002).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Kidney;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Receptor that may have an important role in cell/cell
CC       signaling during nervous system formation.
CC   -!- SUBUNIT: Heterodimer of 2 chains generated by proteolytic processing;
CC       the large extracellular N-terminal fragment and the membrane-bound C-
CC       terminal fragment predominantly remain associated and non-covalently
CC       linked. {ECO:0000255|PROSITE-ProRule:PRU00098}.
CC   -!- INTERACTION:
CC       Q9R0M0; Q7T0S3: atp6ap2.S; Xeno; NbExp=2; IntAct=EBI-8294754, EBI-8294706;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9R0M0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9R0M0-2; Sequence=VSP_025765;
CC   -!- TISSUE SPECIFICITY: Expressed in the CNS and in the eye.
CC       {ECO:0000269|PubMed:10790539}.
CC   -!- DEVELOPMENTAL STAGE: Predominantly expressed in the developing CNS, the
CC       emerging dorsal root ganglia and cranial ganglia. In the CNS,
CC       expression is uniform along the rostrocaudal axis. During gastrulation,
CC       it is expressed within the anterior neural ectoderm. At 10 dpc,
CC       expression is strong in the ventricular zones (VZ) in all sectors of
CC       the brain, and lower in the marginal zones (MZ). Between 12 and 15 dpc,
CC       expression is prominent in the brain. It is strong in VZ, lower in MZ,
CC       except in telecephalic MZ where it is predominant. The intensity is
CC       higher in all VZ, and lower in differentiating fields than in VZ,
CC       except in the cerebral hemispheres, and to a lesser extent in the
CC       tectum and cerebellum. A weak expression is also observed in the fetal
CC       lungs, kidney and epithelia. In the newborn and postnatal stages,
CC       expression remains restricted to the VZ as well as in migrating and
CC       postmigratory cells throughout the brain.
CC       {ECO:0000269|PubMed:11850187}.
CC   -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate
CC       and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}.
CC   -!- PTM: Autoproteolytically processed at the GPS region of the GAIN-B
CC       domain; this cleavage modulates receptor activity.
CC       {ECO:0000255|PROSITE-ProRule:PRU00098}.
CC   -!- SIMILARITY: Belongs to the G protein-coupled receptor 2 family. LN-TM7
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AB028499; BAA84070.1; -; mRNA.
DR   EMBL; AF031573; AAC68837.1; -; mRNA.
DR   EMBL; AL671899; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL672200; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466607; EDL01967.1; -; Genomic_DNA.
DR   EMBL; BC005499; AAH05499.1; -; mRNA.
DR   CCDS; CCDS17759.1; -. [Q9R0M0-1]
DR   RefSeq; NP_059088.2; NM_017392.4. [Q9R0M0-1]
DR   SMR; Q9R0M0; -.
DR   FunCoup; Q9R0M0; 1159.
DR   IntAct; Q9R0M0; 3.
DR   MINT; Q9R0M0; -.
DR   STRING; 10090.ENSMUSP00000088046; -.
DR   MEROPS; P02.006; -.
DR   MEROPS; P02.953; -.
DR   GlyConnect; Q9R0M0; 4 N-Linked glycans (5 sites).
DR   GlyCosmos; Q9R0M0; 17 sites, 4 glycans.
DR   GlyGen; Q9R0M0; 19 sites, 10 N-linked glycans (11 sites), 1 O-linked glycan (1 site).
DR   iPTMnet; Q9R0M0; -.
DR   PhosphoSitePlus; Q9R0M0; -.
DR   PaxDb; 10090-ENSMUSP00000088046; -.
DR   ProteomicsDB; 281578; -. [Q9R0M0-1]
DR   ProteomicsDB; 281579; -. [Q9R0M0-2]
DR   ProteomicsDB; 336635; -.
DR   Antibodypedia; 2940; 218 antibodies from 31 providers.
DR   DNASU; 53883; -.
DR   Ensembl; ENSMUST00000090558.11; ENSMUSP00000088046.4; ENSMUSG00000068740.15. [Q9R0M0-1]
DR   GeneID; 53883; -.
DR   KEGG; mmu:53883; -.
DR   UCSC; uc008qyx.1; mouse.
DR   AGR; MGI:1858235; -.
DR   CTD; 1952; -.
DR   MGI; MGI:1858235; Celsr2.
DR   VEuPathDB; HostDB:ENSMUSG00000068740; -.
DR   eggNOG; KOG4289; Eukaryota.
DR   GeneTree; ENSGT00940000157493; -.
DR   HOGENOM; CLU_000158_1_0_1; -.
DR   InParanoid; Q9R0M0; -.
DR   OMA; FTLYIVE; -.
DR   OrthoDB; 26203at2759; -.
DR   PhylomeDB; Q9R0M0; -.
DR   BioGRID-ORCS; 53883; 4 hits in 77 CRISPR screens.
DR   PRO; PR:Q9R0M0; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q9R0M0; protein.
DR   Bgee; ENSMUSG00000068740; Expressed in skin of snout and 258 other cell types or tissues.
DR   ExpressionAtlas; Q9R0M0; baseline and differential.
DR   GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR   GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IEA:InterPro.
DR   GO; GO:0007409; P:axonogenesis; IBA:GO_Central.
DR   GO; GO:0044331; P:cell-cell adhesion mediated by cadherin; IBA:GO_Central.
DR   GO; GO:0033326; P:cerebrospinal fluid secretion; IGI:MGI.
DR   GO; GO:0060271; P:cilium assembly; IMP:MGI.
DR   GO; GO:0003341; P:cilium movement; IMP:MGI.
DR   GO; GO:0048813; P:dendrite morphogenesis; ISO:GO_Central.
DR   GO; GO:0007156; P:homophilic cell-cell adhesion; IDA:BHF-UCL.
DR   GO; GO:0021999; P:neural plate anterior/posterior regionalization; IDA:BHF-UCL.
DR   GO; GO:0001764; P:neuron migration; IMP:MGI.
DR   GO; GO:0022407; P:regulation of cell-cell adhesion; ISO:GO_Central.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:BHF-UCL.
DR   GO; GO:0032880; P:regulation of protein localization; IMP:MGI.
DR   GO; GO:0021591; P:ventricular system development; IMP:MGI.
DR   GO; GO:0016055; P:Wnt signaling pathway; IDA:BHF-UCL.
DR   CDD; cd11304; Cadherin_repeat; 9.
DR   CDD; cd00054; EGF_CA; 4.
DR   CDD; cd00055; EGF_Lam; 1.
DR   CDD; cd00110; LamG; 2.
DR   FunFam; 2.10.25.10:FF:000011; Cadherin EGF LAG seven-pass G-type receptor; 1.
DR   FunFam; 2.60.40.60:FF:000013; Cadherin EGF LAG seven-pass G-type receptor; 1.
DR   FunFam; 1.20.1070.10:FF:000112; Cadherin EGF LAG seven-pass G-type receptor 2; 1.
DR   FunFam; 2.60.120.200:FF:000020; Cadherin EGF LAG seven-pass G-type receptor 2; 1.
DR   FunFam; 2.60.120.200:FF:000062; Cadherin EGF LAG seven-pass G-type receptor 2; 1.
DR   FunFam; 2.60.220.50:FF:000005; Cadherin EGF LAG seven-pass G-type receptor 2; 1.
DR   FunFam; 1.25.40.610:FF:000005; cadherin EGF LAG seven-pass G-type receptor 2; 1.
DR   FunFam; 2.10.25.10:FF:000156; cadherin EGF LAG seven-pass G-type receptor 2; 1.
DR   FunFam; 2.10.25.10:FF:000089; Cadherin EGF LAG seven-pass G-type receptor 3; 1.
DR   FunFam; 2.60.40.60:FF:000010; Cadherin EGF LAG seven-pass G-type receptor 3; 2.
DR   FunFam; 2.60.40.60:FF:000023; Cadherin EGF LAG seven-pass G-type receptor 3; 2.
DR   FunFam; 2.60.40.60:FF:000029; Cadherin EGF LAG seven-pass G-type receptor 3; 1.
DR   FunFam; 2.60.40.60:FF:000038; Cadherin EGF LAG seven-pass G-type receptor 3; 1.
DR   FunFam; 2.60.40.60:FF:000040; cadherin EGF LAG seven-pass G-type receptor 3; 1.
DR   FunFam; 2.10.25.10:FF:000113; Cadherin, EGF LAG seven-pass G-type receptor 3; 1.
DR   FunFam; 2.60.40.60:FF:000044; Cadherin, EGF LAG seven-pass G-type receptor 3; 1.
DR   FunFam; 4.10.1240.10:FF:000003; Putative cadherin EGF LAG seven-pass G-type receptor 2; 1.
DR   FunFam; 2.10.25.10:FF:000864; Y-linked cadherin EGF LAG seven-pass G-type receptor 2; 1.
DR   Gene3D; 1.25.40.610; -; 1.
DR   Gene3D; 2.60.120.200; -; 2.
DR   Gene3D; 2.60.220.50; -; 1.
DR   Gene3D; 2.60.40.60; Cadherins; 9.
DR   Gene3D; 4.10.1240.10; GPCR, family 2, extracellular hormone receptor domain; 1.
DR   Gene3D; 2.10.25.10; Laminin; 7.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR032471; AGRL2-4_GAIN_subdom_A.
DR   InterPro; IPR002126; Cadherin-like_dom.
DR   InterPro; IPR015919; Cadherin-like_sf.
DR   InterPro; IPR056286; Cadherin_CELSR1-3_9th.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000742; EGF.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR057244; GAIN_B.
DR   InterPro; IPR046338; GAIN_dom_sf.
DR   InterPro; IPR017981; GPCR_2-like_7TM.
DR   InterPro; IPR036445; GPCR_2_extracell_dom_sf.
DR   InterPro; IPR001879; GPCR_2_extracellular_dom.
DR   InterPro; IPR000832; GPCR_2_secretin-like.
DR   InterPro; IPR000203; GPS.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR002049; LE_dom.
DR   PANTHER; PTHR24026:SF32; CADHERIN EGF LAG SEVEN-PASS G-TYPE RECEPTOR 2; 1.
DR   PANTHER; PTHR24026; FAT ATYPICAL CADHERIN-RELATED; 1.
DR   Pfam; PF00002; 7tm_2; 1.
DR   Pfam; PF00028; Cadherin; 8.
DR   Pfam; PF23592; Cadherin_CELSR2_9th; 1.
DR   Pfam; PF00008; EGF; 2.
DR   Pfam; PF00053; EGF_laminin; 1.
DR   Pfam; PF16489; GAIN; 1.
DR   Pfam; PF01825; GPS; 1.
DR   Pfam; PF02210; Laminin_G_2; 2.
DR   PRINTS; PR00205; CADHERIN.
DR   PRINTS; PR00249; GPCRSECRETIN.
DR   SMART; SM00112; CA; 9.
DR   SMART; SM00181; EGF; 6.
DR   SMART; SM00179; EGF_CA; 5.
DR   SMART; SM00180; EGF_Lam; 1.
DR   SMART; SM00303; GPS; 1.
DR   SMART; SM00008; HormR; 1.
DR   SMART; SM00282; LamG; 2.
DR   SUPFAM; SSF49313; Cadherin-like; 9.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR   SUPFAM; SSF57196; EGF/Laminin; 4.
DR   PROSITE; PS00010; ASX_HYDROXYL; 2.
DR   PROSITE; PS00232; CADHERIN_1; 7.
DR   PROSITE; PS50268; CADHERIN_2; 9.
DR   PROSITE; PS00022; EGF_1; 6.
DR   PROSITE; PS01186; EGF_2; 4.
DR   PROSITE; PS50026; EGF_3; 6.
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; GAIN_B; 1.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Cell membrane; Developmental protein;
KW   Direct protein sequencing; Disulfide bond; EGF-like domain;
KW   G protein-coupled receptor; Glycoprotein; Hydroxylation;
KW   Laminin EGF-like domain; Membrane; Receptor; Reference proteome; Repeat;
KW   Signal; Transducer; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..2919
FT                   /note="Cadherin EGF LAG seven-pass G-type receptor 2"
FT                   /id="PRO_0000012917"
FT   TOPO_DOM        32..2380
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2381..2401
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2402..2413
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2414..2433
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2434..2438
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2439..2459
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2460..2480
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2481..2501
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2502..2518
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2519..2539
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2540..2563
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2564..2584
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2585..2591
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2592..2612
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2613..2919
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          182..289
FT                   /note="Cadherin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          290..399
FT                   /note="Cadherin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          400..505
FT                   /note="Cadherin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          506..610
FT                   /note="Cadherin 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          611..712
FT                   /note="Cadherin 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          713..815
FT                   /note="Cadherin 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          816..921
FT                   /note="Cadherin 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          922..1023
FT                   /note="Cadherin 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          1028..1146
FT                   /note="Cadherin 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          1228..1286
FT                   /note="EGF-like 1; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1288..1318
FT                   /note="EGF-like 2; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1328..1366
FT                   /note="EGF-like 3; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1367..1571
FT                   /note="Laminin G-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DOMAIN          1574..1610
FT                   /note="EGF-like 4; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1614..1791
FT                   /note="Laminin G-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DOMAIN          1787..1829
FT                   /note="EGF-like 5; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1830..1867
FT                   /note="EGF-like 6; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1883..1922
FT                   /note="EGF-like 7; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1924..1971
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          2199..2369
FT                   /note="GAIN-B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT   REGION          156..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2216..2241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2319..2369
FT                   /note="GPS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT   REGION          2690..2884
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        175..194
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2718..2730
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2791..2800
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2803..2815
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2857..2868
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            2356..2357
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT   MOD_RES         1591
FT                   /note="(3R)-3-hydroxyasparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        486
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        557
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        701
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1036
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1076
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1182
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1212
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1501
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1565
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1741
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1827
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1900
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2024
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2043
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2061
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2323
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2345
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        1292..1303
FT                   /evidence="ECO:0000250"
FT   DISULFID        1297..1312
FT                   /evidence="ECO:0000250"
FT   DISULFID        1314..1323
FT                   /evidence="ECO:0000250"
FT   DISULFID        1332..1343
FT                   /evidence="ECO:0000250"
FT   DISULFID        1337..1353
FT                   /evidence="ECO:0000250"
FT   DISULFID        1355..1365
FT                   /evidence="ECO:0000250"
FT   DISULFID        1545..1571
FT                   /evidence="ECO:0000250"
FT   DISULFID        1578..1589
FT                   /evidence="ECO:0000250"
FT   DISULFID        1583..1598
FT                   /evidence="ECO:0000250"
FT   DISULFID        1600..1609
FT                   /evidence="ECO:0000250"
FT   DISULFID        1791..1802
FT                   /evidence="ECO:0000250"
FT   DISULFID        1797..1817
FT                   /evidence="ECO:0000250"
FT   DISULFID        1819..1828
FT                   /evidence="ECO:0000250"
FT   DISULFID        1832..1843
FT                   /evidence="ECO:0000250"
FT   DISULFID        1837..1855
FT                   /evidence="ECO:0000250"
FT   DISULFID        1857..1866
FT                   /evidence="ECO:0000250"
FT   DISULFID        1887..1899
FT                   /evidence="ECO:0000250"
FT   DISULFID        1889..1906
FT                   /evidence="ECO:0000250"
FT   DISULFID        1908..1921
FT                   /evidence="ECO:0000250"
FT   DISULFID        1924..1936
FT                   /evidence="ECO:0000250"
FT   DISULFID        1926..1943
FT                   /evidence="ECO:0000250"
FT   DISULFID        1945..1954
FT                   /evidence="ECO:0000250"
FT   DISULFID        1957..1969
FT                   /evidence="ECO:0000250"
FT   DISULFID        2319..2351
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT   DISULFID        2339..2353
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT   VAR_SEQ         2912..2919
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_025765"
FT   CONFLICT        3
FT                   /note="S -> T (in Ref. 1; BAA84070)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        334
FT                   /note="G -> D (in Ref. 1; BAA84070)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        638
FT                   /note="D -> H (in Ref. 1; BAA84070)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        721
FT                   /note="V -> G (in Ref. 1; BAA84070)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        762
FT                   /note="A -> G (in Ref. 1; BAA84070)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        823
FT                   /note="S -> T (in Ref. 1; BAA84070)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        838
FT                   /note="S -> L (in Ref. 1; BAA84070)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        914
FT                   /note="V -> G (in Ref. 1; BAA84070)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1222
FT                   /note="Q -> K (in Ref. 1; BAA84070)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1268
FT                   /note="P -> L (in Ref. 1; BAA84070)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1280
FT                   /note="F -> L (in Ref. 1; BAA84070)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1296
FT                   /note="P -> T (in Ref. 1; BAA84070)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1315..1317
FT                   /note="LDG -> RGC (in Ref. 1; BAA84070)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1351
FT                   /note="F -> I (in Ref. 1; BAA84070)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1359
FT                   /note="D -> H (in Ref. 1; BAA84070)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1376
FT                   /note="S -> P (in Ref. 1; BAA84070)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1384
FT                   /note="R -> H (in Ref. 1; BAA84070)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1595
FT                   /note="A -> T (in Ref. 1; BAA84070)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1631
FT                   /note="S -> Y (in Ref. 1; BAA84070)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1641
FT                   /note="S -> N (in Ref. 1; BAA84070)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1674..1677
FT                   /note="VLSV -> RLSM (in Ref. 1; BAA84070)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1688
FT                   /note="R -> H (in Ref. 1; BAA84070)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1710
FT                   /note="G -> R (in Ref. 1; BAA84070)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1720
FT                   /note="D -> N (in Ref. 1; BAA84070)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1725
FT                   /note="K -> T (in Ref. 1; BAA84070)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1774..1775
FT                   /note="IS -> VH (in Ref. 1; BAA84070)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1793
FT                   /note="W -> L (in Ref. 1; BAA84070)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1808
FT                   /note="C -> Y (in Ref. 1; BAA84070)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1813
FT                   /note="D -> N (in Ref. 1; BAA84070)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1911
FT                   /note="N -> K (in Ref. 1; BAA84070)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2198
FT                   /note="L -> V (in Ref. 5; AAC68837 and 1; BAA84070)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2282
FT                   /note="V -> A (in Ref. 5; AAC68837 and 1; BAA84070)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2534
FT                   /note="S -> R (in Ref. 1; BAA84070)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2570
FT                   /note="L -> R (in Ref. 5; AAC68837)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2638
FT                   /note="S -> Y (in Ref. 5; AAC68837 and 1; BAA84070)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2760
FT                   /note="L -> C (in Ref. 1; BAA84070)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2795
FT                   /note="K -> R (in Ref. 5; AAC68837)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2802
FT                   /note="P -> A (in Ref. 1; BAA84070)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2899
FT                   /note="K -> N (in Ref. 1; BAA84070)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   2919 AA;  316986 MW;  A8F35C88C5808300 CRC64;
     MRSRAASAPL PTPLLPLLLL LLLLPPSPLL GDQVGPCRSL GSGGRSSSGA CAPVGWLCPA
     SASNLWLYTS RCRESGIELT GHLVPHHDGL RVWCPESGAH IPLPPSSEGC PWSCRLLGIG
     GHLSPQGTLT LPEEHPCLKA PRLRCQSCKL AQAPGLRAGE GSPEESLGGR RKRNVNTAPQ
     FQPPSYQATV PENQPAGTSV ASLRAIDPDE GEAGRLEYTM DALFDSRSNH FFSLDPITGV
     VTTAEELDRE TKSTHVFRVT AQDHGMPRRS ALATLTILVT DTNDHDPVFE QQEYKESLRE
     NLEVGYEVLT VRATDGDAPP NANILYRLLE GAGGSPSDAF EIDPRSGVIR TRGPVDREEV
     ESYKLTVEAS DQGRDPGPRS STAIVFLSVE DDNDNAPQFS EKRYVVQVRE DVTPGAPVLR
     VTASDRDKGS NALVHYSIMS GNARGQFYLD AQTGALDVVS PLDYETTKEY TLRIRAQDGG
     RPPLSNVSGL VTVQVLDIND NAPIFVSTPF QATVLESVPL GYLVLHVQAI DADAGDNARL
     EYSLAGVGHD FPFTINNGTG WISVAAELDR EEVDFYSFGV EARDHGTPAL TASASVSVTI
     LDVNDNNPTF TQPEYTVRLN EDAAVGTSVV TVSAVDRDAH SVITYQITSG NTRNRFSITS
     QSGGGLVSLA LPLDYKLERQ YVLAVTASDG TRQDTAQIVV NVTDANTHRP VFQSSHYTVN
     VNEDRPAGTT VVLISATDED TGENARITYF MEDSIPQFRI DADTGAVTTQ AELDYEDQVS
     YTLAITARDN GIPQKSDTTY LEILVNDVND NAPQFLRDSY QGSVYEDVPP FTSVLQISAT
     DRDSGLNGRV FYTFQGGDDG DGDFIVESTS GIVRTLRRLD RENVAQYVLR AYAVDKGMPP
     ARTPMEVTVT VLDVNDNPPV FEQDEFDVFV EENSPIGLAV ARVTATDPDE GTNAQIMYQI
     VEGNIPEVFQ LDIFSGELTA LVDLDYEDRP EYVLVIQATS APLVSRATVH VRLLDRNDNP
     PVLGNFEILF NNYVTNRSSS FPGGAIGRVP AHDPDISDSL TYSFERGNEL SLVLLNASTG
     ELRLSRALDN NRPLEAIMSV LVSDGVHSVT AQCSLRVTII TDEMLTHSIT LRLEDMSPER
     FLSPLLGLFI QAVAATLATP PDHVVVFNVQ RDTDAPGGHI LNVSLSVGQP PGPGGGPPFL
     PSEDLQERLY LNRSLLTAIS AQRVLPFDDN ICLREPCENY MRCVSVLRFD SSAPFIASSS
     VLFRPIHPVG GLRCRCPPGF TGDYCETEVD LCYSRPCGPH GRCRSREGGY TCLCLDGYTG
     EHCEASTHSG RCTPGVCKNG GTCVNLLVGG FKCDCPSGDF EKPFCQVTTR SFPARSFITF
     RGLRQRFHFT LALSFATKER NGLLLYNGRF NEKHDFVALE VIQEQVQLTF SAGESTTTVS
     PFVPGGVSDG QWHTVQLKYY NKPLLGQTGL PQGPSEQKVA VVSVDGCDTG VALRFGAMLG
     NYSCAAQGTQ GGSKKSLDLT GPLLLGGVPD LPESFPVRMR HFVGCMKDLQ VDSRHIDMAD
     FIANNGTVPG CPTKKIVCDS SICHNGGTCV NQWNAFSCEC PLGFGGKSCA QEMANPQRFL
     GSSLVAWHGL SLPISQPWHL SLMFRTRQAD GVLLQAVTRG RSTITLQLRA GHVVLSVEGT
     GLQASSLRLE PGRANDGDWH HAQLALGASG GPGHAILSFD YGQQKAEGNL GPRLHGLHLS
     NITVGGVPGP ASGVARGFRG CLQGVRVSET PEGISSLDPS RGESINVEPG CSWPDPCDSN
     PCPTNSYCSN DWDSYSCSCV LGYYGDNCTN VCDLNPCEHQ SVCTRKPNTP HGYICECLPN
     YLGPYCETRI DQPCPRGWWG HPTCGPCNCD VSKGFDPDCN KTSGECHCKE NHYRPPGSPT
     CLLCDCYPTG SLSRVCDPED GQCPCKPGVI GRQCDRCDNP FAEVTTNGCE VNYDSCPRAI
     EAGIWWPRTR FGLPAAAPCP KGSFGTAVRH CDEHRGWLPP NLFNCTSVTF SELKGFAERL
     QRNESGLDSG RSQRLALLLR NATQHTSGYF GSDVKVAYQL ATRLLAHESA QRGFGLSATQ
     DVHFTENLLR VGSALLDAAN KRHWELIQQT EGGTAWLLQH YEAYASALAQ NMRHTYLSPF
     TIVTPNIVIS VVRLDKGNFA GTKLPRYEAL RGERPPDLET TVILPESVFR EMPSMVRSAG
     PGEAQETEEL ARRQRRHPEL SQGEAVASVI IYHTLAGLLP HNYDPDKRSL RVPKRPVINT
     PVVSISVHDD EELLPRALDK PVTVQFRLLE TEERTKPICV FWNHSILVSG TGGWSARGCE
     VVFRNESHVS CQCNHMTSFA VLMDMSRREN GEILPLKTLT YVALGVTLAA LMLTFLFLTL
     LRALRSNQHG IRRNLTAALG LAQLVFLLGI NQADLPFACT VIAILLHFLY LCTFSWALLE
     ALHLYRALTE VRDVNASPMR FYYMLGWGVP AFITGLAVGL DPEGYGNPDF CWLSVYDTLI
     WSFAGPVAFA VSMSVFLYIL SARASCAAQR QGFEKKGPVS GLRSSFTVLL LLSATWLLAL
     LSVNSDTLLF HYLFAACNCV QGPFIFLSYV VLSKEVRKAL KFACSRKPSP DPALTTKSTL
     TSSYNCPSPY ADGRLYQPYG DSAGSLHSAS RSGKSQPSYI PFLLREESTL NPGQVPPGLG
     DPSGLFLEGQ AQQHDPDTDS DSDLSLEDDQ SGSYASTHSS DSEEEEEEAA FPGEQGWDSL
     LGPGAERLPL HSTPKDGGPG SGKVPWLGDF GTTTKENSGS GPLEERPREN GDALTREGSL
     GPLPGPSTQP HKGILKKKCL PTISEKSSLL RLPLEQGTGS SRGSSISEGS RHGPPPRPPP
     RQSLQEQLNG VMPVAMSIKA GTVDEDSSGS EFLFFNFLH
//