CELR2_RAT
ID CELR2_RAT Reviewed; 2144 AA.
AC Q9QYP2;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Cadherin EGF LAG seven-pass G-type receptor 2 {ECO:0000305};
DE AltName: Full=Multiple epidermal growth factor-like domains protein 3;
DE Short=Multiple EGF-like domains protein 3;
DE Flags: Fragment;
GN Name=Celsr2 {ECO:0000312|RGD:69237}; Synonyms=Megf3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=9693030; DOI=10.1006/geno.1998.5341;
RA Nakayama M., Nakajima D., Nagase T., Nomura N., Seki N., Ohara O.;
RT "Identification of high-molecular-weight proteins with multiple EGF-like
RT motifs by motif-trap screening.";
RL Genomics 51:27-34(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Receptor that may have an important role in cell/cell
CC signaling during nervous system formation.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in the brain. High expression in
CC cerebellum and olfactory bulb. Weaker expression in cerebral cortex,
CC hippocampus and brain stem.
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; AB011529; BAA88687.1; -; mRNA.
DR AlphaFoldDB; Q9QYP2; -.
DR SMR; Q9QYP2; -.
DR STRING; 10116.ENSRNOP00000027263; -.
DR GlyGen; Q9QYP2; 14 sites, 2 N-linked glycans (1 site).
DR iPTMnet; Q9QYP2; -.
DR PhosphoSitePlus; Q9QYP2; -.
DR PaxDb; Q9QYP2; -.
DR PRIDE; Q9QYP2; -.
DR UCSC; RGD:69237; rat.
DR RGD; 69237; Celsr2.
DR eggNOG; KOG4289; Eukaryota.
DR InParanoid; Q9QYP2; -.
DR PhylomeDB; Q9QYP2; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0060271; P:cilium assembly; ISO:RGD.
DR GO; GO:0003341; P:cilium movement; ISO:RGD.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:BHF-UCL.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISO:RGD.
DR GO; GO:0021999; P:neural plate anterior/posterior regionalization; ISO:RGD.
DR GO; GO:0001764; P:neuron migration; ISO:RGD.
DR GO; GO:0022407; P:regulation of cell-cell adhesion; IMP:BHF-UCL.
DR GO; GO:0032880; P:regulation of protein localization; ISO:RGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0007283; P:spermatogenesis; IEP:RGD.
DR GO; GO:0021591; P:ventricular system development; ISO:RGD.
DR GO; GO:0016055; P:Wnt signaling pathway; ISO:RGD.
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; IPR001791; Laminin_G.
DR InterPro; IPR002049; LE_dom.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF00028; Cadherin; 2.
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; 3.
DR SMART; SM00181; EGF; 6.
DR SMART; SM00179; EGF_CA; 4.
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; 4.
DR SUPFAM; SSF49899; SSF49899; 2.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS00232; CADHERIN_1; 3.
DR PROSITE; PS50268; CADHERIN_2; 4.
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; 2.
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; Receptor; Reference proteome; Repeat;
KW Transducer; Transmembrane; Transmembrane helix.
FT CHAIN <1..2144
FT /note="Cadherin EGF LAG seven-pass G-type receptor 2"
FT /id="PRO_0000070345"
FT TOPO_DOM 1..1605
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1606..1626
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1627..1641
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1642..1662
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1663
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1664..1684
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1685..1705
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1706..1726
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1727..1744
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1745..1765
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1766..1789
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1790..1810
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1811..1816
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1817..1837
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1838..2144
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN <1..40
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 41..146
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 147..248
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 253..371
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 453..511
FT /note="EGF-like 1; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 513..549
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 553..591
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 592..796
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 799..835
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 839..1016
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1018..1053
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1054..1092
FT /note="EGF-like 6; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1108..1147
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1149..1196
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1541..1593
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT REGION 1439..1466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1914..2109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1451..1465
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2074..2096
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 816
FT /note="(3R)-3-hydroxyasparagine"
FT /evidence="ECO:0000255"
FT MOD_RES 1035
FT /note="(3R)-3-hydroxyasparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 437
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 726
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 790
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 966
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1052
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1548
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1570
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 457..468
FT /evidence="ECO:0000250"
FT DISULFID 462..499
FT /evidence="ECO:0000250"
FT DISULFID 501..510
FT /evidence="ECO:0000250"
FT DISULFID 517..528
FT /evidence="ECO:0000250"
FT DISULFID 522..537
FT /evidence="ECO:0000250"
FT DISULFID 539..548
FT /evidence="ECO:0000250"
FT DISULFID 557..568
FT /evidence="ECO:0000250"
FT DISULFID 562..578
FT /evidence="ECO:0000250"
FT DISULFID 580..590
FT /evidence="ECO:0000250"
FT DISULFID 770..796
FT /evidence="ECO:0000250"
FT DISULFID 803..814
FT /evidence="ECO:0000250"
FT DISULFID 808..823
FT /evidence="ECO:0000250"
FT DISULFID 825..834
FT /evidence="ECO:0000250"
FT DISULFID 986..1016
FT /evidence="ECO:0000250"
FT DISULFID 1022..1033
FT /evidence="ECO:0000250"
FT DISULFID 1027..1042
FT /evidence="ECO:0000250"
FT DISULFID 1044..1053
FT /evidence="ECO:0000250"
FT DISULFID 1057..1068
FT /evidence="ECO:0000250"
FT DISULFID 1062..1080
FT /evidence="ECO:0000250"
FT DISULFID 1082..1091
FT /evidence="ECO:0000250"
FT DISULFID 1112..1124
FT /evidence="ECO:0000250"
FT DISULFID 1114..1131
FT /evidence="ECO:0000250"
FT DISULFID 1133..1146
FT /evidence="ECO:0000250"
FT DISULFID 1149..1161
FT /evidence="ECO:0000250"
FT DISULFID 1151..1168
FT /evidence="ECO:0000250"
FT DISULFID 1170..1179
FT /evidence="ECO:0000250"
FT DISULFID 1182..1194
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 2144 AA; 233481 MW; 6EA898C1BA655ECA CRC64;
EDQVSYTLAI TARDNGIPQK SDTTYLEILV NDVNDNAPQF LRDSYQGSVY EDVPPFTSVL
QISATDRDSG LNGRVFYTFQ GGDDGDGDFI VESTSGIVRT LRRLDRENVA QYILRAYAVD
KGMPPARTPM EVTVTVLDVN DNPPVFEQDE FDVFVEENSP IGLAVARVTA TDPDEGTNAQ
IMYQIVEGNI PEVFQLDIFS GELTALVDLD YEDRPEYILV IQATSAPLVS RATVHVRLLD
RNDNPPVLGN FEILFNNYVT NRSSSFPGGA IGRVPAHDPD ISDSLTYSFE RGNELSLVLL
NASTGELRLS RALDNNRPLE AIMSVLVSDG VHSVTAQCSL RVTIITDEML THSITLRLED
MSPERFLSPL LGLFIQAVAA TLATPPDHVV VFNVQRDTDA PGGHILNVSL SVGQPPGPGG
GPPFLPSEDL QERLYLNRSL LTAISAQRVL PFDDNICLRE PCENYMRCVS VLRFDSSAPF
IASSSVLFRP IHPVGGLRCR CPPGFTGDYC ETEVDLCYSR PCGPHGHCRS REGGYTCLCR
DGYTGEHCEV SARSGRCTPG VCKNGGTCVN LLVGGFKCDC PSGDFEKPFC QVTTRSFPAR
SFITFRGLRQ RFHFTLALSF ATKERDGLLL YNGRFNEKHD FVALEVIQEQ VQLTFSAGES
TTTVSPFVPG GVSDGQWHTV QLKYYNKPLL GQTGLPQGPS EQKVAVVSVD GCDTGVALRF
GAMLGNYSCA AQGTQGGSKK SLDLTGPLLL GGVPDLPESF PVRMRHFVGC MKNLQVDSRH
VDMADFIANN GTVPGCPTKK NVCDSNTCHN GGTCVNQWDA FSCECPLGFG GKSCAQEMAN
PQRFLGSSLV AWHGLSLPIS QPWHLSLMFR TRQADGVLLQ AVTRGRSTIT LQLRAGHVVL
SVEGTGLQAS SLRLEPGRAN DGDWHHAQLS LGASGGPGHA ILSFDYGQQK AEGNLGPRLH
GLHLSNMTVG GVPGPASSVA RGFRGCLQGV RVSETPEGVS SLDPSRGESI NVEPGCSWPD
PCDSNPCPTN SYCSNDWDSY SCSCDPGYYG DNCTNVCDLN PCEHQSACTR KPSAPHGYIC
ECLPNYLGPY CETRIDQPCP RGWWGHPTCG PCNCDVSKGF DPDCNKTSGE CHCKENHYRP
PSSPTCLLCD CYPTGSLSRV CDPEDGQCPC KPGVIGRQCD RCDNPFAEVT TNGCEVNYDS
CPRAIEAGIW WPRTRFGLPA AAPCPKGSFG TAVRHCDEHR GWLPPNLFNC TSVTFSELKG
FAERLQRNES GLDSGRSQRL ALLLRNATQH TSGYFGSDVK VAYQLATRLL AHESAQRGFG
LSATQDVHFT ENLLRVGSAL LDAANKRHWE LIQQTEGGTA WLLQHYEAYA SALAQNMRHT
YLSPFTIVTP NIVISVVRLD KGNFAGTKLP RYEALRGERP PDLETTVILP ESVFREMPPM
VRSAGPGEAQ ETEELARRQR RHPELSQGEA VASVIIYHTL AGLLPHNYDP DKRSLRVPKR
PVINTPVVSI SVHDDEELLP RALDKPVTVQ FRLLETEERT KPICVFWNHS ILVSGTGGWS
ARGCEVVFRN ESHVSCQCNH MTSFAVLMDV SRRENGEILP LKTLTYVALG VTLAALMITF
LFLTLLRALR SNQHGIRRNL TAALGLAQLV FLLGINQADL PFACTVIAIL LHFLYLCTFS
WALLEALHLY RALTEVRDVN ASPMRFYYML GWGVPAFITG LAVGLDPEGY GNPDFCWLSI
YDTLIWSFAG PVAFAVSMSV FLYILSARAS CAAQRQGFEK KGPVSGLRSS FTVLLLLSAT
WLLALLSVNS DTLLFHYLFA ACNCVQGPFI FLSYVVLSKE VRKALKFACS RKPSPDPALT
TKSTLTSSYN CPSPYADGRL YQPYGDSAGS LHSASRSGKS QPSYIPFLLR EESTLNPGQV
PPGLGDPSGL FMEGQAQQHD PDTDSDSDLS LEDDQSGSYA STHSSDSEEE EEEAAFPGEQ
GWDSLLGPGA ERLPLHSTPK DGGPGSGKVP WPGDFGTTTK ENSGSGPLEE RPRENGDALT
REGSLGPLPG PSTQPHKGIL KKKCLPTISE KSSLLRLPLE QGTGSSRGST ASEGSRNGPP
PRPPPRQSLQ EQLNGVMPIA MSIKAGTVDE DSSGSEFLFF NFLH
