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   08-NOV-2023, entry version 162.
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   GlyCosmos; Q9QYP2; 14 sites, 2 glycans.
DR   GlyGen; Q9QYP2; 14 sites, 2 N-linked glycans (1 site).
DR   iPTMnet; Q9QYP2; -.
DR   PhosphoSitePlus; Q9QYP2; -.
DR   PaxDb; 10116-ENSRNOP00000027263; -.
DR   UCSC; RGD:69237; rat.
DR   AGR; RGD:69237; -.
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: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: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:0097475; P:motor neuron migration; ISO:RGD.
DR   GO; GO:0021999; P:neural plate anterior/posterior regionalization; ISO:RGD.
DR   GO; GO:0022407; P:regulation of cell-cell adhesion; IMP:BHF-UCL.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; ISO:RGD.
DR   GO; GO:0032880; P:regulation of protein localization; 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; cd15992; 7tmB2_CELSR2; 1.
DR   CDD; cd11304; Cadherin_repeat; 4.
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; 4.
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; 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; Cadherin-like; 4.
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; 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
//