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 24-JAN-2024, entry version 191.
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 -!- 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 -!- 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_017392.3. [Q9R0M0-1]
DR SMR; Q9R0M0; -.
DR IntAct; Q9R0M0; 3.
DR MINT; Q9R0M0; -.
DR STRING; 10090.ENSMUSP00000088046; -.
DR MEROPS; P02.006; -.
DR MEROPS; P02.953; -.
DR GlyConnect; 2174; 4 N-Linked glycans (5 sites).
DR GlyCosmos; Q9R0M0; 17 sites, 4 glycans.
DR GlyGen; Q9R0M0; 18 sites, 4 N-linked glycans (5 sites), 1 O-linked glycan (1 site).
DR iPTMnet; Q9R0M0; -.
DR PhosphoSitePlus; Q9R0M0; -.
DR MaxQB; Q9R0M0; -.
DR PaxDb; 10090-ENSMUSP00000088046; -.
DR ProteomicsDB; 281578; -. [Q9R0M0-1]
DR ProteomicsDB; 281579; -. [Q9R0M0-2]
DR ProteomicsDB; 336635; -.
DR Antibodypedia; 2940; 247 antibodies from 30 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; 4006628at2759; -.
DR PhylomeDB; Q9R0M0; -.
DR TreeFam; TF320624; -.
DR BioGRID-ORCS; 53883; 4 hits in 77 CRISPR screens.
DR ChiTaRS; Celsr2; mouse.
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: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:UniProtKB-KW.
DR GO; GO:0098609; P:cell-cell adhesion; 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:MGI.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:BHF-UCL.
DR GO; GO:0097475; P:motor neuron migration; IMP:MGI.
DR GO; GO:0021999; P:neural plate anterior/posterior regionalization; IDA:BHF-UCL.
DR GO; GO:0022407; P:regulation of cell-cell adhesion; ISO:MGI.
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 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; 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; IPR032471; GAIN_dom_N.
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; PF00008; EGF; 2.
DR Pfam; PF16489; GAIN; 1.
DR Pfam; PF01825; GPS; 1.
DR Pfam; PF00053; Laminin_EGF; 1.
DR Pfam; PF02210; Laminin_G_2; 2.
DR PRINTS; PR00205; CADHERIN.
DR PRINTS; PR00249; GPCRSECRETIN.
DR SMART; SM00112; CA; 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; GPS; 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 2316..2368
FT /note="GPS"
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 2690..2884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2226..2240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2849..2868
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 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
//
