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Database: UniProt
Entry: Q9R0M0
LinkDB: Q9R0M0
Original site: Q9R0M0 
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   10-APR-2019, entry version 164.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the 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
RT   a 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
RT   project: 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
RT   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       Q7T0S3:atp6ap2 (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         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Expressed in the CNS and in the eye.
CC       {ECO:0000269|PubMed:10790539}.
CC   -!- DEVELOPMENTAL STAGE: Predominantly expressed in the developing
CC       CNS, the emerging dorsal root ganglia and cranial ganglia. In the
CC       CNS, expression is uniform along the rostrocaudal axis. During
CC       gastrulation, it is expressed within the anterior neural ectoderm.
CC       At 10 dpc, expression is strong in the ventricular zones (VZ) in
CC       all sectors of the brain, and lower in the marginal zones (MZ).
CC       Between 12 and 15 dpc, expression is prominent in the brain. It is
CC       strong in VZ, lower in MZ, except in telecephalic MZ where it is
CC       predominant. The intensity is higher in all VZ, and lower in
CC       differentiating fields than in VZ, except in the cerebral
CC       hemispheres, and to a lesser extent in the tectum and cerebellum.
CC       A weak expression is also observed in the fetal lungs, kidney and
CC       epithelia. In the newborn and postnatal stages, expression remains
CC       restricted to the VZ as well as in migrating and postmigratory
CC       cells throughout the brain. {ECO:0000269|PubMed:11850187}.
CC   -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
CC       aspartate and asparagine is (R) stereospecific within EGF domains.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC       LN-TM7 subfamily. {ECO:0000305}.
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   RefSeq; NP_059088.2; NM_017392.3.
DR   UniGene; Mm.39728; -.
DR   ProteinModelPortal; Q9R0M0; -.
DR   SMR; Q9R0M0; -.
DR   IntAct; Q9R0M0; 2.
DR   MINT; Q9R0M0; -.
DR   STRING; 10090.ENSMUSP00000088046; -.
DR   MEROPS; P02.006; -.
DR   iPTMnet; Q9R0M0; -.
DR   PhosphoSitePlus; Q9R0M0; -.
DR   PaxDb; Q9R0M0; -.
DR   PRIDE; Q9R0M0; -.
DR   Ensembl; ENSMUST00000090558; ENSMUSP00000088046; ENSMUSG00000068740.
DR   GeneID; 53883; -.
DR   UCSC; uc008qyx.1; mouse.
DR   CTD; 1952; -.
DR   MGI; MGI:1858235; Celsr2.
DR   eggNOG; KOG4289; Eukaryota.
DR   eggNOG; ENOG410XTGH; LUCA.
DR   GeneTree; ENSGT00940000157493; -.
DR   HOGENOM; HOG000231346; -.
DR   HOVERGEN; HBG050887; -.
DR   InParanoid; Q9R0M0; -.
DR   OMA; AHFPVAN; -.
DR   OrthoDB; 23882at2759; -.
DR   PhylomeDB; Q9R0M0; -.
DR   TreeFam; TF320624; -.
DR   ChiTaRS; Celsr2; mouse.
DR   PRO; PR:Q9R0M0; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   Proteomes; UP000000589; Unplaced.
DR   Bgee; ENSMUSG00000068740; Expressed in 294 organ(s), highest expression level in frontal cortex.
DR   GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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: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: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:MGI.
DR   GO; GO:0032880; P:regulation of protein localization; IMP:MGI.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:BHF-UCL.
DR   GO; GO:0021591; P:ventricular system development; IMP:MGI.
DR   GO; GO:0016055; P:Wnt signaling pathway; IDA:BHF-UCL.
DR   Gene3D; 4.10.1240.10; -; 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; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR032471; GAIN_dom_N.
DR   InterPro; IPR017981; GPCR_2-like.
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; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR002049; Laminin_EGF.
DR   InterPro; IPR001791; Laminin_G.
DR   Pfam; PF00002; 7tm_2; 1.
DR   Pfam; PF00028; Cadherin; 8.
DR   Pfam; PF00008; EGF; 1.
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; SSF49313; 9.
DR   SUPFAM; SSF49899; SSF49899; 2.
DR   SUPFAM; SSF57184; SSF57184; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS00232; CADHERIN_1; 6.
DR   PROSITE; PS50268; CADHERIN_2; 9.
DR   PROSITE; PS00022; EGF_1; 6.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS50026; EGF_3; 5.
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; Complete proteome;
KW   Developmental protein; Direct protein sequencing; Disulfide bond;
KW   EGF-like domain; G-protein coupled receptor; Glycoprotein;
KW   Hydroxylation; Laminin EGF-like domain; Membrane; Receptor;
KW   Reference proteome; Repeat; Signal; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     31       {ECO:0000255}.
FT   CHAIN        32   2919       Cadherin EGF LAG seven-pass G-type
FT                                receptor 2.
FT                                /FTId=PRO_0000012917.
FT   TOPO_DOM     32   2380       Extracellular. {ECO:0000255}.
FT   TRANSMEM   2381   2401       Helical; Name=1. {ECO:0000255}.
FT   TOPO_DOM   2402   2413       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2414   2433       Helical; Name=2. {ECO:0000255}.
FT   TOPO_DOM   2434   2438       Extracellular. {ECO:0000255}.
FT   TRANSMEM   2439   2459       Helical; Name=3. {ECO:0000255}.
FT   TOPO_DOM   2460   2480       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2481   2501       Helical; Name=4. {ECO:0000255}.
FT   TOPO_DOM   2502   2518       Extracellular. {ECO:0000255}.
FT   TRANSMEM   2519   2539       Helical; Name=5. {ECO:0000255}.
FT   TOPO_DOM   2540   2563       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2564   2584       Helical; Name=6. {ECO:0000255}.
FT   TOPO_DOM   2585   2591       Extracellular. {ECO:0000255}.
FT   TRANSMEM   2592   2612       Helical; Name=7. {ECO:0000255}.
FT   TOPO_DOM   2613   2919       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      182    289       Cadherin 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      290    399       Cadherin 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      400    505       Cadherin 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      506    610       Cadherin 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      611    712       Cadherin 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      713    815       Cadherin 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      816    921       Cadherin 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      922   1023       Cadherin 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     1028   1146       Cadherin 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     1228   1286       EGF-like 1; atypical.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1288   1318       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1328   1366       EGF-like 3; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1367   1571       Laminin G-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN     1574   1610       EGF-like 4; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1614   1791       Laminin G-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN     1787   1829       EGF-like 5; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1830   1867       EGF-like 6; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1883   1922       EGF-like 7; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1924   1971       Laminin EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN     2316   2368       GPS. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00098}.
FT   COMPBIAS   2743   2748       Poly-Glu.
FT   MOD_RES    1591   1591       (3R)-3-hydroxyasparagine. {ECO:0000255}.
FT   CARBOHYD    486    486       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    557    557       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    701    701       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1036   1036       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1076   1076       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1182   1182       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1212   1212       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1501   1501       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1565   1565       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1741   1741       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1827   1827       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1900   1900       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2024   2024       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2043   2043       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2061   2061       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2323   2323       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2345   2345       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID   1292   1303       {ECO:0000250}.
FT   DISULFID   1297   1312       {ECO:0000250}.
FT   DISULFID   1314   1323       {ECO:0000250}.
FT   DISULFID   1332   1343       {ECO:0000250}.
FT   DISULFID   1337   1353       {ECO:0000250}.
FT   DISULFID   1355   1365       {ECO:0000250}.
FT   DISULFID   1545   1571       {ECO:0000250}.
FT   DISULFID   1578   1589       {ECO:0000250}.
FT   DISULFID   1583   1598       {ECO:0000250}.
FT   DISULFID   1600   1609       {ECO:0000250}.
FT   DISULFID   1791   1802       {ECO:0000250}.
FT   DISULFID   1797   1817       {ECO:0000250}.
FT   DISULFID   1819   1828       {ECO:0000250}.
FT   DISULFID   1832   1843       {ECO:0000250}.
FT   DISULFID   1837   1855       {ECO:0000250}.
FT   DISULFID   1857   1866       {ECO:0000250}.
FT   DISULFID   1887   1899       {ECO:0000250}.
FT   DISULFID   1889   1906       {ECO:0000250}.
FT   DISULFID   1908   1921       {ECO:0000250}.
FT   DISULFID   1924   1936       {ECO:0000250}.
FT   DISULFID   1926   1943       {ECO:0000250}.
FT   DISULFID   1945   1954       {ECO:0000250}.
FT   DISULFID   1957   1969       {ECO:0000250}.
FT   VAR_SEQ    2912   2919       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_025765.
FT   CONFLICT      3      3       S -> T (in Ref. 1; BAA84070).
FT                                {ECO:0000305}.
FT   CONFLICT    334    334       G -> D (in Ref. 1; BAA84070).
FT                                {ECO:0000305}.
FT   CONFLICT    638    638       D -> H (in Ref. 1; BAA84070).
FT                                {ECO:0000305}.
FT   CONFLICT    721    721       V -> G (in Ref. 1; BAA84070).
FT                                {ECO:0000305}.
FT   CONFLICT    762    762       A -> G (in Ref. 1; BAA84070).
FT                                {ECO:0000305}.
FT   CONFLICT    823    823       S -> T (in Ref. 1; BAA84070).
FT                                {ECO:0000305}.
FT   CONFLICT    838    838       S -> L (in Ref. 1; BAA84070).
FT                                {ECO:0000305}.
FT   CONFLICT    914    914       V -> G (in Ref. 1; BAA84070).
FT                                {ECO:0000305}.
FT   CONFLICT   1222   1222       Q -> K (in Ref. 1; BAA84070).
FT                                {ECO:0000305}.
FT   CONFLICT   1268   1268       P -> L (in Ref. 1; BAA84070).
FT                                {ECO:0000305}.
FT   CONFLICT   1280   1280       F -> L (in Ref. 1; BAA84070).
FT                                {ECO:0000305}.
FT   CONFLICT   1296   1296       P -> T (in Ref. 1; BAA84070).
FT                                {ECO:0000305}.
FT   CONFLICT   1315   1317       LDG -> RGC (in Ref. 1; BAA84070).
FT                                {ECO:0000305}.
FT   CONFLICT   1351   1351       F -> I (in Ref. 1; BAA84070).
FT                                {ECO:0000305}.
FT   CONFLICT   1359   1359       D -> H (in Ref. 1; BAA84070).
FT                                {ECO:0000305}.
FT   CONFLICT   1376   1376       S -> P (in Ref. 1; BAA84070).
FT                                {ECO:0000305}.
FT   CONFLICT   1384   1384       R -> H (in Ref. 1; BAA84070).
FT                                {ECO:0000305}.
FT   CONFLICT   1595   1595       A -> T (in Ref. 1; BAA84070).
FT                                {ECO:0000305}.
FT   CONFLICT   1631   1631       S -> Y (in Ref. 1; BAA84070).
FT                                {ECO:0000305}.
FT   CONFLICT   1641   1641       S -> N (in Ref. 1; BAA84070).
FT                                {ECO:0000305}.
FT   CONFLICT   1674   1677       VLSV -> RLSM (in Ref. 1; BAA84070).
FT                                {ECO:0000305}.
FT   CONFLICT   1688   1688       R -> H (in Ref. 1; BAA84070).
FT                                {ECO:0000305}.
FT   CONFLICT   1710   1710       G -> R (in Ref. 1; BAA84070).
FT                                {ECO:0000305}.
FT   CONFLICT   1720   1720       D -> N (in Ref. 1; BAA84070).
FT                                {ECO:0000305}.
FT   CONFLICT   1725   1725       K -> T (in Ref. 1; BAA84070).
FT                                {ECO:0000305}.
FT   CONFLICT   1774   1775       IS -> VH (in Ref. 1; BAA84070).
FT                                {ECO:0000305}.
FT   CONFLICT   1793   1793       W -> L (in Ref. 1; BAA84070).
FT                                {ECO:0000305}.
FT   CONFLICT   1808   1808       C -> Y (in Ref. 1; BAA84070).
FT                                {ECO:0000305}.
FT   CONFLICT   1813   1813       D -> N (in Ref. 1; BAA84070).
FT                                {ECO:0000305}.
FT   CONFLICT   1911   1911       N -> K (in Ref. 1; BAA84070).
FT                                {ECO:0000305}.
FT   CONFLICT   2198   2198       L -> V (in Ref. 5; AAC68837 and 1;
FT                                BAA84070). {ECO:0000305}.
FT   CONFLICT   2282   2282       V -> A (in Ref. 5; AAC68837 and 1;
FT                                BAA84070). {ECO:0000305}.
FT   CONFLICT   2534   2534       S -> R (in Ref. 1; BAA84070).
FT                                {ECO:0000305}.
FT   CONFLICT   2570   2570       L -> R (in Ref. 5; AAC68837).
FT                                {ECO:0000305}.
FT   CONFLICT   2638   2638       S -> Y (in Ref. 5; AAC68837 and 1;
FT                                BAA84070). {ECO:0000305}.
FT   CONFLICT   2760   2760       L -> C (in Ref. 1; BAA84070).
FT                                {ECO:0000305}.
FT   CONFLICT   2795   2795       K -> R (in Ref. 5; AAC68837).
FT                                {ECO:0000305}.
FT   CONFLICT   2802   2802       P -> A (in Ref. 1; BAA84070).
FT                                {ECO:0000305}.
FT   CONFLICT   2899   2899       K -> N (in Ref. 1; BAA84070).
FT                                {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
//
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