CELR1_MOUSE
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 03-AUG-2022, entry version 193.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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 receptor
RT 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., 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 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 chromosome
RT 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 SER-2888,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 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 O35161; Q7T0S3: atp6ap2.S; 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 area
CC postrema. Also found in spinal cord and in the eye.
CC {ECO:0000269|PubMed:9339365}.
CC -!- DEVELOPMENTAL STAGE: First detected at 6 dpc. Predominantly expressed
CC in the developing CNS, the emerging dorsal root ganglia and cranial
CC ganglia. In the CNS, expression is uniform along the rostrocaudal axis.
CC During gastrulation, it is expressed in the vicinity of the primitive
CC streak, and becomes predominant in that area at late gastrulation. At
CC 10 dpc, detected in ventricular zones (VZ), but not in marginal zones
CC (MZ), and weakly in other structures. Between 12 dpc and 15 dpc, a high
CC expression is present in the VZ in all brain areas. No expression in
CC differentiated neuronal fields. In the newborn and postnatal stages,
CC expression remains restricted to the VZ. Also found weakly in fetal
CC lungs, kidney and epithelia. {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; 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 SMR; O35161; -.
DR BioGRID; 198673; 1.
DR IntAct; O35161; 1.
DR MINT; O35161; -.
DR STRING; 10090.ENSMUSP00000016172; -.
DR GlyGen; O35161; 23 sites.
DR iPTMnet; O35161; -.
DR PhosphoSitePlus; O35161; -.
DR EPD; O35161; -.
DR MaxQB; O35161; -.
DR PaxDb; O35161; -.
DR PeptideAtlas; O35161; -.
DR PRIDE; O35161; -.
DR ProteomicsDB; 281530; -.
DR Antibodypedia; 13897; 193 antibodies from 30 providers.
DR DNASU; 12614; -.
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 VEuPathDB; HostDB:ENSMUSG00000016028; -.
DR eggNOG; KOG4289; Eukaryota.
DR GeneTree; ENSGT00940000159839; -.
DR HOGENOM; CLU_000158_1_0_1; -.
DR InParanoid; O35161; -.
DR OMA; PPAQDTC; -.
DR OrthoDB; 23882at2759; -.
DR PhylomeDB; O35161; -.
DR TreeFam; TF323983; -.
DR BioGRID-ORCS; 12614; 5 hits in 76 CRISPR screens.
DR ChiTaRS; Celsr1; mouse.
DR PRO; PR:O35161; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; O35161; protein.
DR Bgee; ENSMUSG00000016028; Expressed in ventricular zone and 181 other tissues.
DR ExpressionAtlas; O35161; baseline and differential.
DR Genevisible; O35161; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IEA:UniProtKB-KW.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IMP:MGI.
DR GO; GO:0045176; P:apical protein localization; IMP:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
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: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:0097475; P:motor neuron migration; IMP:MGI.
DR GO; GO:0001843; P:neural tube closure; IMP:UniProtKB.
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:0007266; P:Rho protein signal transduction; IMP:MGI.
DR GO; GO:0042060; P:wound healing; IGI:MGI.
DR CDD; cd00055; EGF_Lam; 1.
DR CDD; cd00110; LamG; 2.
DR Gene3D; 2.60.220.50; -; 1.
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; 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.
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; IPR001791; Laminin_G.
DR InterPro; IPR002049; LE_dom.
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; Developmental protein; Disulfide bond;
KW EGF-like domain; G-protein coupled receptor; Glycoprotein; Hydroxylation;
KW Laminin EGF-like domain; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transducer; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..3034
FT /note="Cadherin EGF LAG seven-pass G-type receptor 1"
FT /id="PRO_0000012915"
FT TOPO_DOM 30..2484
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2485..2505
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2506..2516
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2517..2537
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2538..2542
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2543..2563
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2564..2587
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2588..2608
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2609..2625
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2626..2646
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2647..2670
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2671..2691
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2692..2694
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2695..2715
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2716..3034
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 261..368
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 369..474
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 475..580
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 581..702
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 703..804
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 805..907
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 908..1014
FT /note="Cadherin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1015..1116
FT /note="Cadherin 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1121..1239
FT /note="Cadherin 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1318..1376
FT /note="EGF-like 1; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1378..1414
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1418..1456
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1457..1661
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1664..1700
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1704..1885
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1887..1922
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1923..1961
FT /note="EGF-like 6; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1962..1994
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1996..2031
FT /note="EGF-like 8; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2018..2065
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 2423..2475
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT REGION 222..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2295..2346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2774..3034
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2774..2794
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2814..2828
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2889..2905
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2975..2989
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3018..3034
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1681
FT /note="(3R)-3-hydroxyasparagine"
FT /evidence="ECO:0000255"
FT MOD_RES 1904
FT /note="(3R)-3-hydroxyaspartate"
FT /evidence="ECO:0000255"
FT MOD_RES 2776
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2779
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYQ6"
FT MOD_RES 2886
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2888
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 561
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 649
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 793
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1591
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1638
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1655
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1994
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2452
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2538
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 1322..1333
FT /evidence="ECO:0000250"
FT DISULFID 1327..1364
FT /evidence="ECO:0000250"
FT DISULFID 1366..1375
FT /evidence="ECO:0000250"
FT DISULFID 1382..1393
FT /evidence="ECO:0000250"
FT DISULFID 1387..1402
FT /evidence="ECO:0000250"
FT DISULFID 1404..1413
FT /evidence="ECO:0000250"
FT DISULFID 1422..1433
FT /evidence="ECO:0000250"
FT DISULFID 1427..1443
FT /evidence="ECO:0000250"
FT DISULFID 1445..1455
FT /evidence="ECO:0000250"
FT DISULFID 1635..1661
FT /evidence="ECO:0000250"
FT DISULFID 1668..1679
FT /evidence="ECO:0000250"
FT DISULFID 1673..1688
FT /evidence="ECO:0000250"
FT DISULFID 1690..1699
FT /evidence="ECO:0000250"
FT DISULFID 1855..1885
FT /evidence="ECO:0000250"
FT DISULFID 1891..1902
FT /evidence="ECO:0000250"
FT DISULFID 1896..1911
FT /evidence="ECO:0000250"
FT DISULFID 1913..1922
FT /evidence="ECO:0000250"
FT DISULFID 1926..1937
FT /evidence="ECO:0000250"
FT DISULFID 1931..1949
FT /evidence="ECO:0000250"
FT DISULFID 1951..1960
FT /evidence="ECO:0000250"
FT DISULFID 1968..1981
FT /evidence="ECO:0000250"
FT DISULFID 1983..1993
FT /evidence="ECO:0000250"
FT DISULFID 2000..2015
FT /evidence="ECO:0000250"
FT DISULFID 2002..2018
FT /evidence="ECO:0000250"
FT DISULFID 2020..2030
FT /evidence="ECO:0000250"
FT DISULFID 2039..2048
FT /evidence="ECO:0000250"
FT DISULFID 2051..2063
FT /evidence="ECO:0000250"
FT CONFLICT 218
FT /note="E -> Q (in Ref. 1; AAC68836)"
FT /evidence="ECO:0000305"
FT CONFLICT 1050
FT /note="M -> I (in Ref. 1; AAC68836)"
FT /evidence="ECO:0000305"
FT CONFLICT 1900..1901
FT /note="SH -> RP (in Ref. 1; AAC68836)"
FT /evidence="ECO:0000305"
FT CONFLICT 2524
FT /note="T -> A (in Ref. 1; AAC68836)"
FT /evidence="ECO:0000305"
FT CONFLICT 2805
FT /note="A -> T (in Ref. 1; AAC68836)"
FT /evidence="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
