GenomeNet

Database: UniProt
Entry: O35161
LinkDB: O35161
Original site: O35161 
ID   CELR1_MOUSE             Reviewed;        3034 AA.
AC   O35161; E9QK27;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   13-FEB-2019, entry version 175.
DE   RecName: Full=Cadherin EGF LAG seven-pass G-type receptor 1;
DE   Flags: Precursor;
GN   Name=Celsr1;
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].
RX   PubMed=9858697; DOI=10.1016/S0925-4773(98)00153-1;
RA   Hadjantonakis A.-K., Formstone C.J., Little P.F.R.;
RT   "mCelsr1 is an evolutionarily conserved seven-pass transmembrane
RT   receptor and is expressed during mouse embryonic development.";
RL   Mech. Dev. 78:91-95(1998).
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   TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=9339365; DOI=10.1006/geno.1997.4892;
RA   Hadjantonakis A.-K., Sheward W.J., Harmar A.J., de Galan L.,
RA   Hoovers J.M.N., Little P.F.R.;
RT   "Celsr1, a neural-specific gene encoding an unusual seven-pass
RT   transmembrane receptor, maps to mouse chromosome 15 and human
RT   chromosome 22qter.";
RL   Genomics 45:97-104(1997).
RN   [4]
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2776; SER-2886 AND
RP   SER-2888, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=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-8294650, EBI-8294706;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed in the brain, where it is localized
CC       principally in the ependymal cell layer, choroid plexus and the
CC       area postrema. Also found in spinal chord and in the eye.
CC       {ECO:0000269|PubMed:9339365}.
CC   -!- DEVELOPMENTAL STAGE: First detected at 6 dpc. Predominantly
CC       expressed in the developing CNS, the emerging dorsal root ganglia
CC       and cranial ganglia. In the CNS, expression is uniform along the
CC       rostrocaudal axis. During gastrulation, it is expressed in the
CC       vicinity of the primitive streak, and becomes predominant in that
CC       area at late gastrulation. At 10 dpc, detected in ventricular
CC       zones (VZ), but not in marginal zones (MZ), and weakly in other
CC       structures. Between 12 dpc and 15 dpc, a high expression is
CC       present in the VZ in all brain areas. No expression in
CC       differentiated neuronal fields. In the newborn and postnatal
CC       stages, expression remains restricted to the VZ. Also found weakly
CC       in fetal lungs, kidney and epithelia.
CC       {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; AF031572; AAC68836.1; -; mRNA.
DR   EMBL; AC116764; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC139513; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS37172.1; -.
DR   PIR; T14119; T14119.
DR   RefSeq; NP_034016.2; NM_009886.2.
DR   UniGene; Mm.22680; -.
DR   ProteinModelPortal; O35161; -.
DR   SMR; O35161; -.
DR   IntAct; O35161; 1.
DR   MINT; O35161; -.
DR   STRING; 10090.ENSMUSP00000016172; -.
DR   iPTMnet; O35161; -.
DR   PhosphoSitePlus; O35161; -.
DR   MaxQB; O35161; -.
DR   PaxDb; O35161; -.
DR   PeptideAtlas; O35161; -.
DR   PRIDE; O35161; -.
DR   Ensembl; ENSMUST00000016172; ENSMUSP00000016172; ENSMUSG00000016028.
DR   GeneID; 12614; -.
DR   KEGG; mmu:12614; -.
DR   UCSC; uc007xdt.1; mouse.
DR   CTD; 9620; -.
DR   MGI; MGI:1100883; Celsr1.
DR   eggNOG; KOG4289; Eukaryota.
DR   eggNOG; ENOG410XTGH; LUCA.
DR   GeneTree; ENSGT00940000159839; -.
DR   HOGENOM; HOG000231346; -.
DR   HOVERGEN; HBG050887; -.
DR   InParanoid; O35161; -.
DR   KO; K04600; -.
DR   OMA; YVVGWGI; -.
DR   OrthoDB; 23882at2759; -.
DR   TreeFam; TF323983; -.
DR   ChiTaRS; Celsr1; mouse.
DR   PRO; PR:O35161; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   Bgee; ENSMUSG00000016028; Expressed in 218 organ(s), highest expression level in molar tooth.
DR   ExpressionAtlas; O35161; baseline and differential.
DR   Genevisible; O35161; MM.
DR   GO; GO:0005887; C:integral component of plasma membrane; TAS:UniProtKB.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0005509; F:calcium ion binding; TAS:UniProtKB.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; NAS:UniProtKB.
DR   GO; GO:0046983; F:protein dimerization activity; NAS:UniProtKB.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; NAS:UniProtKB.
DR   GO; GO:0009952; P:anterior/posterior pattern specification; IMP:MGI.
DR   GO; GO:0045176; P:apical protein localization; IMP:MGI.
DR   GO; GO:0007267; P:cell-cell signaling; NAS:UniProtKB.
DR   GO; GO:0007417; P:central nervous system development; NAS:UniProtKB.
DR   GO; GO:0048105; P:establishment of body hair planar orientation; IMP:MGI.
DR   GO; GO:0001736; P:establishment of planar polarity; IMP:UniProtKB.
DR   GO; GO:0042249; P:establishment of planar polarity of embryonic epithelium; IMP:MGI.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; NAS:UniProtKB.
DR   GO; GO:0001702; P:gastrulation with mouth forming second; NAS:UniProtKB.
DR   GO; GO:0001942; P:hair follicle development; IMP:MGI.
DR   GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR   GO; GO:0042472; P:inner ear morphogenesis; IMP:MGI.
DR   GO; GO:0060490; P:lateral sprouting involved in lung morphogenesis; IMP:MGI.
DR   GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR   GO; GO:0001843; P:neural tube closure; IMP:UniProtKB.
DR   GO; GO:0001764; P:neuron migration; IMP:MGI.
DR   GO; GO:0060488; P:orthogonal dichotomous subdivision of terminal units involved in lung branching morphogenesis; IMP:MGI.
DR   GO; GO:0090179; P:planar cell polarity pathway involved in neural tube closure; IGI:MGI.
DR   GO; GO:0060489; P:planar dichotomous subdivision of terminal units involved in lung branching morphogenesis; IMP:MGI.
DR   GO; GO:0090251; P:protein localization involved in establishment of planar polarity; IDA:MGI.
DR   GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:MGI.
DR   GO; GO:0046928; P:regulation of neurotransmitter secretion; NAS:UniProtKB.
DR   GO; GO:0007266; P:Rho protein signal transduction; IMP:MGI.
DR   GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
DR   GO; GO:0042060; P:wound healing; IGI:MGI.
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; 2.
DR   Pfam; PF16489; GAIN; 1.
DR   Pfam; PF01825; GPS; 1.
DR   Pfam; PF02793; HRM; 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; 2.
DR   PROSITE; PS00232; CADHERIN_1; 7.
DR   PROSITE; PS50268; CADHERIN_2; 9.
DR   PROSITE; PS00022; EGF_1; 6.
DR   PROSITE; PS01186; EGF_2; 2.
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   Calcium; Cell membrane; Complete proteome; Developmental protein;
KW   Disulfide bond; EGF-like domain; G-protein coupled receptor;
KW   Glycoprotein; Hydroxylation; Laminin EGF-like domain; Membrane;
KW   Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW   Transducer; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     29       {ECO:0000255}.
FT   CHAIN        30   3034       Cadherin EGF LAG seven-pass G-type
FT                                receptor 1.
FT                                /FTId=PRO_0000012915.
FT   TOPO_DOM     30   2484       Extracellular. {ECO:0000255}.
FT   TRANSMEM   2485   2505       Helical; Name=1. {ECO:0000255}.
FT   TOPO_DOM   2506   2516       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2517   2537       Helical; Name=2. {ECO:0000255}.
FT   TOPO_DOM   2538   2542       Extracellular. {ECO:0000255}.
FT   TRANSMEM   2543   2563       Helical; Name=3. {ECO:0000255}.
FT   TOPO_DOM   2564   2587       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2588   2608       Helical; Name=4. {ECO:0000255}.
FT   TOPO_DOM   2609   2625       Extracellular. {ECO:0000255}.
FT   TRANSMEM   2626   2646       Helical; Name=5. {ECO:0000255}.
FT   TOPO_DOM   2647   2670       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2671   2691       Helical; Name=6. {ECO:0000255}.
FT   TOPO_DOM   2692   2694       Extracellular. {ECO:0000255}.
FT   TRANSMEM   2695   2715       Helical; Name=7. {ECO:0000255}.
FT   TOPO_DOM   2716   3034       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      261    368       Cadherin 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      369    474       Cadherin 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      475    580       Cadherin 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      581    702       Cadherin 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      703    804       Cadherin 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      805    907       Cadherin 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      908   1014       Cadherin 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     1015   1116       Cadherin 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     1121   1239       Cadherin 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     1318   1376       EGF-like 1; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1378   1414       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1418   1456       EGF-like 3; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1457   1661       Laminin G-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN     1664   1700       EGF-like 4; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1704   1885       Laminin G-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN     1887   1922       EGF-like 5; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1923   1961       EGF-like 6; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1962   1994       EGF-like 7; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1996   2031       EGF-like 8; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     2018   2065       Laminin EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN     2423   2475       GPS. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00098}.
FT   COMPBIAS   2674   2678       Poly-Leu.
FT   MOD_RES    1681   1681       (3R)-3-hydroxyasparagine. {ECO:0000255}.
FT   MOD_RES    1904   1904       (3R)-3-hydroxyaspartate. {ECO:0000255}.
FT   MOD_RES    2776   2776       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    2779   2779       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9NYQ6}.
FT   MOD_RES    2886   2886       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    2888   2888       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   CARBOHYD    236    236       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    561    561       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    649    649       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    793    793       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1129   1129       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1154   1154       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1228   1228       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1264   1264       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1274   1274       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1302   1302       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1591   1591       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1638   1638       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1655   1655       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1994   1994       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2118   2118       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2137   2137       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2144   2144       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2155   2155       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2160   2160       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2272   2272       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2430   2430       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2452   2452       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2538   2538       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID   1322   1333       {ECO:0000250}.
FT   DISULFID   1327   1364       {ECO:0000250}.
FT   DISULFID   1366   1375       {ECO:0000250}.
FT   DISULFID   1382   1393       {ECO:0000250}.
FT   DISULFID   1387   1402       {ECO:0000250}.
FT   DISULFID   1404   1413       {ECO:0000250}.
FT   DISULFID   1422   1433       {ECO:0000250}.
FT   DISULFID   1427   1443       {ECO:0000250}.
FT   DISULFID   1445   1455       {ECO:0000250}.
FT   DISULFID   1635   1661       {ECO:0000250}.
FT   DISULFID   1668   1679       {ECO:0000250}.
FT   DISULFID   1673   1688       {ECO:0000250}.
FT   DISULFID   1690   1699       {ECO:0000250}.
FT   DISULFID   1855   1885       {ECO:0000250}.
FT   DISULFID   1891   1902       {ECO:0000250}.
FT   DISULFID   1896   1911       {ECO:0000250}.
FT   DISULFID   1913   1922       {ECO:0000250}.
FT   DISULFID   1926   1937       {ECO:0000250}.
FT   DISULFID   1931   1949       {ECO:0000250}.
FT   DISULFID   1951   1960       {ECO:0000250}.
FT   DISULFID   1968   1981       {ECO:0000250}.
FT   DISULFID   1983   1993       {ECO:0000250}.
FT   DISULFID   2000   2015       {ECO:0000250}.
FT   DISULFID   2002   2018       {ECO:0000250}.
FT   DISULFID   2020   2030       {ECO:0000250}.
FT   DISULFID   2039   2048       {ECO:0000250}.
FT   DISULFID   2051   2063       {ECO:0000250}.
FT   CONFLICT    218    218       E -> Q (in Ref. 1; AAC68836).
FT                                {ECO:0000305}.
FT   CONFLICT   1050   1050       M -> I (in Ref. 1; AAC68836).
FT                                {ECO:0000305}.
FT   CONFLICT   1900   1901       SH -> RP (in Ref. 1; AAC68836).
FT                                {ECO:0000305}.
FT   CONFLICT   2524   2524       T -> A (in Ref. 1; AAC68836).
FT                                {ECO:0000305}.
FT   CONFLICT   2805   2805       A -> T (in Ref. 1; AAC68836).
FT                                {ECO:0000305}.
SQ   SEQUENCE   3034 AA;  330471 MW;  FD9C4812AA1F0BCD CRC64;
     MAPSSPRVLP ALVLLAAAAL PALELGAAAW ELRVPGGARA FALGPGWSYR LDTTRTPREL
     LDVSREGPAA GRRLGLGAGT LGCARLAGRL LPLQVRLVAR GAPTAPSLVL RARAYGARCG
     VRLLRRSARG AELRSPAVRS VPGLGDALCF PAAGGGAASL TSVLEAITNF PACSCPPVAG
     TGCRRGPICL RPGGSAELRL VCALGRAAGA VWVELVIEAT SGTPSESPSV SPSLLNLSQP
     RAGVVRRSRR GTGSSTSPQF PLPSYQVSVP ENEPAGTAVI ELRAHDPDEG DAGRLSYQME
     ALFDERSNGY FLIDAATGAV TTARSLDRET KDTHVLKVSA VDHGSPRRSA ATYLTVTVSD
     TNDHSPVFEQ SEYRERIREN LEVGYEVLTI RATDGDAPSN ANMRYRLLEG AGGVFEIDAR
     SGVVRTRAVV DREEAAEYQL LVEANDQGRN PGPLSASATV HIVVEDENDN YPQFSEKRYV
     VQVPEDVAVN TAVLRVQATD RDQGQNAAIH YSIVSGNLKG QFYLHSLSGS LDVINPLDFE
     AIREYTLRIK AQDGGRPPLI NSSGLVSVQV LDVNDNAPIF VSSPFQAAVL ENVPLGHSVL
     HIQAVDADAG ENARLQYRLV DTASTIVGGS SVDSENPASA PDFPFQIHNS SGWITVCAEL
     DREEVEHYSF GVEAVDHGSP AMSSSASVSI TVLDVNDNDP MFTQPVYELR LNEDAAVGSS
     VLTLRARDRD ANSVITYQLT GGNTRNRFAL SSQSGGGLIT LALPLDYKQE RQYVLAVTAS
     DGTRSHTAQV FINVTDANTH RPVFQSSHYT VSVSEDRPVG TSIATISATD EDTGENARIT
     YVLEDPVPQF RIDPDTGTIY TMTELDYEDQ AAYTLAITAQ DNGIPQKSDT TSLEILILDA
     NDNAPRFLRD FYQGSVFEDA PPSTSVLQVS ATDRDSGPNG RLLYTFQGGD DGDGDFYIEP
     TSGVIRTQRR LDRENVAVYN LWALAVDRGS PNPLSASVGI QVSVLDINDN PPVFEKDELE
     LFVEENSPVG SVVARIRAND PDEGPNAQIM YQIVEGNVPE VFQLDLLSGD LRALVELDFE
     VRRDYMLVVQ ATSAPLVSRA TVHIRLLDQN DNPPELPDFQ ILFNNYVTNK SNSFPSGVIG
     RIPAHDPDLS DSLNYTFLQG NELSLLLLDP ATGELQLSRD LDNNRPLEAL MEVSVSDGIH
     SVTALCTLRV TIITDDMLTN SITVRLENMS QEKFLSPLLS LFVEGVATVL STTKDDIFVF
     NIQNDTDVSS NILNVTFSAL LPGGTRGRFF PSEDLQEQIY LNRTLLTTIS AQRVLPFDDN
     ICLREPCENY MKCVSVLRFD SSAPFISSTT VLFRPIHPIT GLRCRCPPGF TGDYCETEID
     LCYSNPCGAN GRCRSREGGY TCECFEDFTG EHCQVNVRSG RCASGVCKNG GTCVNLLIGG
     FHCVCPPGEY EHPYCEVSTR SFPPQSFVTF RGLRQRFHFT VSLAFATQDR NALLLYNGRF
     NEKHDFIALE IVEEQLQLTF SAGETTTTVT PQVPGGVSDG RWHSVLVQYY NKPNIGHLGL
     PHGPSGEKVA VVTVDDCDAA VAVHFGSYVG NYSCAAQGTQ SGSKKSLDLT GPLLLGGVPN
     LPEDFPVHSR QFVGCMRNLS IDGRIVDMAA FIANNGTRAG CASQRNFCDG TSCQNGGTCV
     NRWNTYLCEC PLRFGGKNCE QAMPHPQRFT GESVVLWSDL DITISVPWYL GLMFRTRKED
     GVLMEATAGT SSRLHLQILN SYIRFEVSYG PSDVASMQLS KSRITDGGWH HLLIELRSAK
     EGKDIKYLAV MTLDYGMDQS TVQIGNQLPG LKMRTIVIGG VTEDKVSVRH GFRGCMQGVR
     MGETSTNIAT LNMNDALKVR VKDGCDVEDP CASSPCPPHS HCRDTWDSYS CICDRGYFGK
     KCVDACLLNP CKHVAACVRS PNTPRGYSCE CGPGHYGQYC ENKVDLPCPK GWWGNPVCGP
     CHCAVSQGFD PDCNKTNGQC QCKENYYKPP AQDACLPCDC FPHGSHSRAC DMDTGQCACK
     PGVIGRQCNR CDNPFAEVTS LGCEVIYNGC PRAFEAGIWW PQTKFGQPAA VPCPKGSVGN
     AVRHCSGEKG WLPPELFNCT SGSFVDLKAL NEKLNRNETR MDGNRSLRLA KALRNATQGN
     STLFGNDVRT AYQLLARILQ HESRQQGFDL AATREANFHE DVVHTGSALL APATEASWEQ
     IQRSEAGAAQ LLRHFEAYFS NVARNVKRTY LRPFVIVTAN MILAVDIFDK LNFTGAQVPR
     FEDIQEELPR ELESSVSFPA DTFKPPEKKE GPVVRLTNRR TTPLTAQPEP RAERETSSSR
     RRRHPDEPGQ FAVALVVIYR TLGQLLPEHY DPDHRSLRLP NRPVINTPVV SAMVYSEGTP
     LPSSLQRPIL VEFSLLETEE RSKPVCVFWN HSLDTGGTGG WSAKGCELLS RNRTHVTCQC
     SHSASCAVLM DISRREHGEV LPLKIITYAA LSLSLVALLV AFVLLSLVRT LRSNLHSIHK
     NLITALFFSQ LIFMVGINQT ENPFLCTVVA ILLHYVSMGT FAWTLVENLH VYRMLTEVRN
     IDTGPMRFYH VVGWGIPAIV TGLAVGLDPQ GYGNPDFCWL SLQDTLIWSF AGPVGTVIII
     NTVIFVLSAK VSCQRKHHYY ERKGVVSMLR TAFLLLLLVT ATWLLGLLAV NSDTLSFHYL
     FAAFSCLQGI FVLLFHCVAH REVRKHLRAV LAGKKLQLDD SATTRATLLT RSLNCNNTYS
     EGPDMLRTAL GESTASLDST TRDEGVQKLS VSSGPARGNH GEPDASFIPR NSKKAHGPDS
     DSDSELSLDE HSSSYASSHT SDSEDDGGEA EDKWNPAGGP AHSTPKADAL ANHVPAGWPD
     ESLAGSDSEE LDTEPHLKVE TKVSVELHRQ AQGNHCGDRP SDPESGVLAK PVAVLSSQPQ
     EQRKGILKNK VTYPPPLPEQ PLKSRLREKL ADCEQSPTSS RTSSLGSGDG VHATDCVITI
     KTPRREPGRE HLNGVAMNVR TGSAQANGSD SEKP
//
DBGET integrated database retrieval system