GenomeNet

Database: UniProt
Entry: Q9QYP2
LinkDB: Q9QYP2
Original site: Q9QYP2 
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   10-APR-2019, entry version 144.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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-
RT   like 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.,
RA   Lundby C., Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14
RT   different rat 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
CC       cortex, hippocampus and brain stem.
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; AB011529; BAA88687.1; -; mRNA.
DR   UniGene; Rn.222746; -.
DR   ProteinModelPortal; Q9QYP2; -.
DR   SMR; Q9QYP2; -.
DR   STRING; 10116.ENSRNOP00000027263; -.
DR   iPTMnet; Q9QYP2; -.
DR   PhosphoSitePlus; Q9QYP2; -.
DR   UniCarbKB; Q9QYP2; -.
DR   jPOST; Q9QYP2; -.
DR   PaxDb; Q9QYP2; -.
DR   PRIDE; Q9QYP2; -.
DR   UCSC; RGD:69237; rat.
DR   RGD; 69237; Celsr2.
DR   eggNOG; KOG4289; Eukaryota.
DR   eggNOG; ENOG410XTGH; LUCA.
DR   HOGENOM; HOG000231346; -.
DR   HOVERGEN; HBG050887; -.
DR   InParanoid; Q9QYP2; -.
DR   PhylomeDB; Q9QYP2; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0048813; P:dendrite morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR   GO; GO:0022407; P:regulation of cell-cell adhesion; IMP:BHF-UCL.
DR   GO; GO:0007283; P:spermatogenesis; IEP:RGD.
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; IPR002049; Laminin_EGF.
DR   InterPro; IPR001791; Laminin_G.
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; Complete proteome; Developmental protein;
KW   Disulfide bond; EGF-like domain; G-protein coupled receptor;
KW   Glycoprotein; Hydroxylation; Laminin EGF-like domain; Membrane;
KW   Receptor; Reference proteome; Repeat; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN        <1   2144       Cadherin EGF LAG seven-pass G-type
FT                                receptor 2.
FT                                /FTId=PRO_0000070345.
FT   TOPO_DOM      1   1605       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1606   1626       Helical; Name=1. {ECO:0000255}.
FT   TOPO_DOM   1627   1641       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1642   1662       Helical; Name=2. {ECO:0000255}.
FT   TOPO_DOM   1663   1663       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1664   1684       Helical; Name=3. {ECO:0000255}.
FT   TOPO_DOM   1685   1705       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1706   1726       Helical; Name=4. {ECO:0000255}.
FT   TOPO_DOM   1727   1744       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1745   1765       Helical; Name=5. {ECO:0000255}.
FT   TOPO_DOM   1766   1789       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1790   1810       Helical; Name=6. {ECO:0000255}.
FT   TOPO_DOM   1811   1816       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1817   1837       Helical; Name=7. {ECO:0000255}.
FT   TOPO_DOM   1838   2144       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       <1     40       Cadherin 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN       41    146       Cadherin 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      147    248       Cadherin 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      253    371       Cadherin 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      453    511       EGF-like 1; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      513    549       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      553    591       EGF-like 3; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      592    796       Laminin G-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN      799    835       EGF-like 4; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      839   1016       Laminin G-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN     1018   1053       EGF-like 5; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1054   1092       EGF-like 6; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1108   1147       EGF-like 7; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1149   1196       Laminin EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN     1541   1593       GPS. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00098}.
FT   COMPBIAS   1968   1973       Poly-Glu.
FT   MOD_RES     816    816       (3R)-3-hydroxyasparagine. {ECO:0000255}.
FT   MOD_RES    1035   1035       (3R)-3-hydroxyasparagine. {ECO:0000255}.
FT   CARBOHYD    261    261       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    301    301       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    407    407       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    437    437       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    726    726       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    790    790       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    966    966       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1052   1052       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1125   1125       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1249   1249       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1268   1268       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1286   1286       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1548   1548       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1570   1570       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    457    468       {ECO:0000250}.
FT   DISULFID    462    499       {ECO:0000250}.
FT   DISULFID    501    510       {ECO:0000250}.
FT   DISULFID    517    528       {ECO:0000250}.
FT   DISULFID    522    537       {ECO:0000250}.
FT   DISULFID    539    548       {ECO:0000250}.
FT   DISULFID    557    568       {ECO:0000250}.
FT   DISULFID    562    578       {ECO:0000250}.
FT   DISULFID    580    590       {ECO:0000250}.
FT   DISULFID    770    796       {ECO:0000250}.
FT   DISULFID    803    814       {ECO:0000250}.
FT   DISULFID    808    823       {ECO:0000250}.
FT   DISULFID    825    834       {ECO:0000250}.
FT   DISULFID    986   1016       {ECO:0000250}.
FT   DISULFID   1022   1033       {ECO:0000250}.
FT   DISULFID   1027   1042       {ECO:0000250}.
FT   DISULFID   1044   1053       {ECO:0000250}.
FT   DISULFID   1057   1068       {ECO:0000250}.
FT   DISULFID   1062   1080       {ECO:0000250}.
FT   DISULFID   1082   1091       {ECO:0000250}.
FT   DISULFID   1112   1124       {ECO:0000250}.
FT   DISULFID   1114   1131       {ECO:0000250}.
FT   DISULFID   1133   1146       {ECO:0000250}.
FT   DISULFID   1149   1161       {ECO:0000250}.
FT   DISULFID   1151   1168       {ECO:0000250}.
FT   DISULFID   1170   1179       {ECO:0000250}.
FT   DISULFID   1182   1194       {ECO:0000250}.
FT   NON_TER       1      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
//
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