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Protein

Cadherin EGF LAG seven-pass G-type receptor 2

Gene

Celsr2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Receptor that may have an important role in cell/cell signaling during nervous system formation.

GO - Molecular functioni

GO - Biological processi

  • cell surface receptor signaling pathway Source: InterPro
  • dendrite morphogenesis Source: BHF-UCL
  • homophilic cell adhesion via plasma membrane adhesion molecules Source: InterPro
  • regulation of cell-cell adhesion Source: BHF-UCL
  • spermatogenesis Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, G-protein coupled receptor, Receptor, Transducer

Keywords - Ligandi

Calcium

Names & Taxonomyi

Protein namesi
Recommended name:
Cadherin EGF LAG seven-pass G-type receptor 2
Alternative name(s):
Multiple epidermal growth factor-like domains protein 3
Short name:
Multiple EGF-like domains protein 3
Gene namesi
Name:Celsr2
Synonyms:Megf3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi69237. Celsr2.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 1605ExtracellularSequence analysisAdd BLAST1605
Transmembranei1606 – 1626Helical; Name=1Sequence analysisAdd BLAST21
Topological domaini1627 – 1641CytoplasmicSequence analysisAdd BLAST15
Transmembranei1642 – 1662Helical; Name=2Sequence analysisAdd BLAST21
Topological domaini1663ExtracellularSequence analysis1
Transmembranei1664 – 1684Helical; Name=3Sequence analysisAdd BLAST21
Topological domaini1685 – 1705CytoplasmicSequence analysisAdd BLAST21
Transmembranei1706 – 1726Helical; Name=4Sequence analysisAdd BLAST21
Topological domaini1727 – 1744ExtracellularSequence analysisAdd BLAST18
Transmembranei1745 – 1765Helical; Name=5Sequence analysisAdd BLAST21
Topological domaini1766 – 1789CytoplasmicSequence analysisAdd BLAST24
Transmembranei1790 – 1810Helical; Name=6Sequence analysisAdd BLAST21
Topological domaini1811 – 1816ExtracellularSequence analysis6
Transmembranei1817 – 1837Helical; Name=7Sequence analysisAdd BLAST21
Topological domaini1838 – 2144CytoplasmicSequence analysisAdd BLAST307

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000070345‹1 – 2144Cadherin EGF LAG seven-pass G-type receptor 2Add BLAST›2144

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi261N-linked (GlcNAc...)Sequence analysis1
Glycosylationi301N-linked (GlcNAc...)Sequence analysis1
Glycosylationi407N-linked (GlcNAc...)Sequence analysis1
Glycosylationi437N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi457 ↔ 468By similarity
Disulfide bondi462 ↔ 499By similarity
Disulfide bondi501 ↔ 510By similarity
Disulfide bondi517 ↔ 528By similarity
Disulfide bondi522 ↔ 537By similarity
Disulfide bondi539 ↔ 548By similarity
Disulfide bondi557 ↔ 568By similarity
Disulfide bondi562 ↔ 578By similarity
Disulfide bondi580 ↔ 590By similarity
Glycosylationi726N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi770 ↔ 796By similarity
Glycosylationi790N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi803 ↔ 814By similarity
Disulfide bondi808 ↔ 823By similarity
Modified residuei816(3R)-3-hydroxyasparagineSequence analysis1
Disulfide bondi825 ↔ 834By similarity
Glycosylationi966N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi986 ↔ 1016By similarity
Disulfide bondi1022 ↔ 1033By similarity
Disulfide bondi1027 ↔ 1042By similarity
Modified residuei1035(3R)-3-hydroxyasparagineSequence analysis1
Disulfide bondi1044 ↔ 1053By similarity
Glycosylationi1052N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1057 ↔ 1068By similarity
Disulfide bondi1062 ↔ 1080By similarity
Disulfide bondi1082 ↔ 1091By similarity
Disulfide bondi1112 ↔ 1124By similarity
Disulfide bondi1114 ↔ 1131By similarity
Glycosylationi1125N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1133 ↔ 1146By similarity
Disulfide bondi1149 ↔ 1161By similarity
Disulfide bondi1151 ↔ 1168By similarity
Disulfide bondi1170 ↔ 1179By similarity
Disulfide bondi1182 ↔ 1194By similarity
Glycosylationi1249N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1268N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1286N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1548N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1570N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

PaxDbiQ9QYP2.
PRIDEiQ9QYP2.

PTM databases

iPTMnetiQ9QYP2.
PhosphoSitePlusiQ9QYP2.
UniCarbKBiQ9QYP2.

Expressioni

Tissue specificityi

Expressed in the brain. High expression in cerebellum and olfactory bulb. Weaker expression in cerebral cortex, hippocampus and brain stem.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000027263.

Structurei

3D structure databases

ProteinModelPortaliQ9QYP2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini‹1 – 40Cadherin 1PROSITE-ProRule annotationAdd BLAST›40
Domaini41 – 146Cadherin 2PROSITE-ProRule annotationAdd BLAST106
Domaini147 – 248Cadherin 3PROSITE-ProRule annotationAdd BLAST102
Domaini253 – 371Cadherin 4PROSITE-ProRule annotationAdd BLAST119
Domaini453 – 511EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd BLAST59
Domaini513 – 549EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini553 – 591EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd BLAST39
Domaini592 – 796Laminin G-like 1PROSITE-ProRule annotationAdd BLAST205
Domaini799 – 835EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini839 – 1016Laminin G-like 2PROSITE-ProRule annotationAdd BLAST178
Domaini1018 – 1053EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd BLAST36
Domaini1054 – 1092EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd BLAST39
Domaini1108 – 1147EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd BLAST40
Domaini1149 – 1196Laminin EGF-likePROSITE-ProRule annotationAdd BLAST48
Domaini1541 – 1593GPSPROSITE-ProRule annotationAdd BLAST53

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1968 – 1973Poly-Glu6

Sequence similaritiesi

Contains 4 cadherin domains.PROSITE-ProRule annotation
Contains 7 EGF-like domains.PROSITE-ProRule annotation
Contains 1 GPS domain.PROSITE-ProRule annotation
Contains 1 laminin EGF-like domain.PROSITE-ProRule annotation
Contains 2 laminin G-like domains.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Laminin EGF-like domain, Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4289. Eukaryota.
ENOG410XTGH. LUCA.
HOGENOMiHOG000231346.
HOVERGENiHBG050887.
InParanoidiQ9QYP2.
PhylomeDBiQ9QYP2.

Family and domain databases

Gene3Di2.60.120.200. 2 hits.
2.60.40.60. 4 hits.
InterProiIPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
IPR013320. ConA-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR032471. GAIN_dom_N.
IPR017981. GPCR_2-like.
IPR001879. GPCR_2_extracellular_dom.
IPR000832. GPCR_2_secretin-like.
IPR000203. GPS.
IPR002049. Laminin_EGF.
IPR001791. Laminin_G.
[Graphical view]
PfamiPF00002. 7tm_2. 1 hit.
PF00028. Cadherin. 2 hits.
PF00008. EGF. 2 hits.
PF16489. GAIN. 1 hit.
PF01825. GPS. 1 hit.
PF00053. Laminin_EGF. 1 hit.
PF02210. Laminin_G_2. 2 hits.
[Graphical view]
PRINTSiPR00205. CADHERIN.
PR00249. GPCRSECRETIN.
SMARTiSM00112. CA. 3 hits.
SM00181. EGF. 6 hits.
SM00179. EGF_CA. 4 hits.
SM00180. EGF_Lam. 1 hit.
SM00303. GPS. 1 hit.
SM00008. HormR. 1 hit.
SM00282. LamG. 2 hits.
[Graphical view]
SUPFAMiSSF49313. SSF49313. 4 hits.
SSF49899. SSF49899. 2 hits.
PROSITEiPS00010. ASX_HYDROXYL. 2 hits.
PS00232. CADHERIN_1. 3 hits.
PS50268. CADHERIN_2. 4 hits.
PS00022. EGF_1. 6 hits.
PS01186. EGF_2. 4 hits.
PS50026. EGF_3. 6 hits.
PS01248. EGF_LAM_1. 1 hit.
PS50027. EGF_LAM_2. 2 hits.
PS50227. G_PROTEIN_RECEP_F2_3. 1 hit.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
PS50221. GPS. 1 hit.
PS50025. LAM_G_DOMAIN. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

Q9QYP2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
EDQVSYTLAI TARDNGIPQK SDTTYLEILV NDVNDNAPQF LRDSYQGSVY
60 70 80 90 100
EDVPPFTSVL QISATDRDSG LNGRVFYTFQ GGDDGDGDFI VESTSGIVRT
110 120 130 140 150
LRRLDRENVA QYILRAYAVD KGMPPARTPM EVTVTVLDVN DNPPVFEQDE
160 170 180 190 200
FDVFVEENSP IGLAVARVTA TDPDEGTNAQ IMYQIVEGNI PEVFQLDIFS
210 220 230 240 250
GELTALVDLD YEDRPEYILV IQATSAPLVS RATVHVRLLD RNDNPPVLGN
260 270 280 290 300
FEILFNNYVT NRSSSFPGGA IGRVPAHDPD ISDSLTYSFE RGNELSLVLL
310 320 330 340 350
NASTGELRLS RALDNNRPLE AIMSVLVSDG VHSVTAQCSL RVTIITDEML
360 370 380 390 400
THSITLRLED MSPERFLSPL LGLFIQAVAA TLATPPDHVV VFNVQRDTDA
410 420 430 440 450
PGGHILNVSL SVGQPPGPGG GPPFLPSEDL QERLYLNRSL LTAISAQRVL
460 470 480 490 500
PFDDNICLRE PCENYMRCVS VLRFDSSAPF IASSSVLFRP IHPVGGLRCR
510 520 530 540 550
CPPGFTGDYC ETEVDLCYSR PCGPHGHCRS REGGYTCLCR DGYTGEHCEV
560 570 580 590 600
SARSGRCTPG VCKNGGTCVN LLVGGFKCDC PSGDFEKPFC QVTTRSFPAR
610 620 630 640 650
SFITFRGLRQ RFHFTLALSF ATKERDGLLL YNGRFNEKHD FVALEVIQEQ
660 670 680 690 700
VQLTFSAGES TTTVSPFVPG GVSDGQWHTV QLKYYNKPLL GQTGLPQGPS
710 720 730 740 750
EQKVAVVSVD GCDTGVALRF GAMLGNYSCA AQGTQGGSKK SLDLTGPLLL
760 770 780 790 800
GGVPDLPESF PVRMRHFVGC MKNLQVDSRH VDMADFIANN GTVPGCPTKK
810 820 830 840 850
NVCDSNTCHN GGTCVNQWDA FSCECPLGFG GKSCAQEMAN PQRFLGSSLV
860 870 880 890 900
AWHGLSLPIS QPWHLSLMFR TRQADGVLLQ AVTRGRSTIT LQLRAGHVVL
910 920 930 940 950
SVEGTGLQAS SLRLEPGRAN DGDWHHAQLS LGASGGPGHA ILSFDYGQQK
960 970 980 990 1000
AEGNLGPRLH GLHLSNMTVG GVPGPASSVA RGFRGCLQGV RVSETPEGVS
1010 1020 1030 1040 1050
SLDPSRGESI NVEPGCSWPD PCDSNPCPTN SYCSNDWDSY SCSCDPGYYG
1060 1070 1080 1090 1100
DNCTNVCDLN PCEHQSACTR KPSAPHGYIC ECLPNYLGPY CETRIDQPCP
1110 1120 1130 1140 1150
RGWWGHPTCG PCNCDVSKGF DPDCNKTSGE CHCKENHYRP PSSPTCLLCD
1160 1170 1180 1190 1200
CYPTGSLSRV CDPEDGQCPC KPGVIGRQCD RCDNPFAEVT TNGCEVNYDS
1210 1220 1230 1240 1250
CPRAIEAGIW WPRTRFGLPA AAPCPKGSFG TAVRHCDEHR GWLPPNLFNC
1260 1270 1280 1290 1300
TSVTFSELKG FAERLQRNES GLDSGRSQRL ALLLRNATQH TSGYFGSDVK
1310 1320 1330 1340 1350
VAYQLATRLL AHESAQRGFG LSATQDVHFT ENLLRVGSAL LDAANKRHWE
1360 1370 1380 1390 1400
LIQQTEGGTA WLLQHYEAYA SALAQNMRHT YLSPFTIVTP NIVISVVRLD
1410 1420 1430 1440 1450
KGNFAGTKLP RYEALRGERP PDLETTVILP ESVFREMPPM VRSAGPGEAQ
1460 1470 1480 1490 1500
ETEELARRQR RHPELSQGEA VASVIIYHTL AGLLPHNYDP DKRSLRVPKR
1510 1520 1530 1540 1550
PVINTPVVSI SVHDDEELLP RALDKPVTVQ FRLLETEERT KPICVFWNHS
1560 1570 1580 1590 1600
ILVSGTGGWS ARGCEVVFRN ESHVSCQCNH MTSFAVLMDV SRRENGEILP
1610 1620 1630 1640 1650
LKTLTYVALG VTLAALMITF LFLTLLRALR SNQHGIRRNL TAALGLAQLV
1660 1670 1680 1690 1700
FLLGINQADL PFACTVIAIL LHFLYLCTFS WALLEALHLY RALTEVRDVN
1710 1720 1730 1740 1750
ASPMRFYYML GWGVPAFITG LAVGLDPEGY GNPDFCWLSI YDTLIWSFAG
1760 1770 1780 1790 1800
PVAFAVSMSV FLYILSARAS CAAQRQGFEK KGPVSGLRSS FTVLLLLSAT
1810 1820 1830 1840 1850
WLLALLSVNS DTLLFHYLFA ACNCVQGPFI FLSYVVLSKE VRKALKFACS
1860 1870 1880 1890 1900
RKPSPDPALT TKSTLTSSYN CPSPYADGRL YQPYGDSAGS LHSASRSGKS
1910 1920 1930 1940 1950
QPSYIPFLLR EESTLNPGQV PPGLGDPSGL FMEGQAQQHD PDTDSDSDLS
1960 1970 1980 1990 2000
LEDDQSGSYA STHSSDSEEE EEEAAFPGEQ GWDSLLGPGA ERLPLHSTPK
2010 2020 2030 2040 2050
DGGPGSGKVP WPGDFGTTTK ENSGSGPLEE RPRENGDALT REGSLGPLPG
2060 2070 2080 2090 2100
PSTQPHKGIL KKKCLPTISE KSSLLRLPLE QGTGSSRGST ASEGSRNGPP
2110 2120 2130 2140
PRPPPRQSLQ EQLNGVMPIA MSIKAGTVDE DSSGSEFLFF NFLH
Length:2,144
Mass (Da):233,481
Last modified:May 1, 2000 - v1
Checksum:i6EA898C1BA655ECA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB011529 mRNA. Translation: BAA88687.1.
UniGeneiRn.222746.

Genome annotation databases

UCSCiRGD:69237. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB011529 mRNA. Translation: BAA88687.1.
UniGeneiRn.222746.

3D structure databases

ProteinModelPortaliQ9QYP2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000027263.

Protein family/group databases

GPCRDBiSearch...

PTM databases

iPTMnetiQ9QYP2.
PhosphoSitePlusiQ9QYP2.
UniCarbKBiQ9QYP2.

Proteomic databases

PaxDbiQ9QYP2.
PRIDEiQ9QYP2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:69237. rat.

Organism-specific databases

RGDi69237. Celsr2.

Phylogenomic databases

eggNOGiKOG4289. Eukaryota.
ENOG410XTGH. LUCA.
HOGENOMiHOG000231346.
HOVERGENiHBG050887.
InParanoidiQ9QYP2.
PhylomeDBiQ9QYP2.

Family and domain databases

Gene3Di2.60.120.200. 2 hits.
2.60.40.60. 4 hits.
InterProiIPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
IPR013320. ConA-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR032471. GAIN_dom_N.
IPR017981. GPCR_2-like.
IPR001879. GPCR_2_extracellular_dom.
IPR000832. GPCR_2_secretin-like.
IPR000203. GPS.
IPR002049. Laminin_EGF.
IPR001791. Laminin_G.
[Graphical view]
PfamiPF00002. 7tm_2. 1 hit.
PF00028. Cadherin. 2 hits.
PF00008. EGF. 2 hits.
PF16489. GAIN. 1 hit.
PF01825. GPS. 1 hit.
PF00053. Laminin_EGF. 1 hit.
PF02210. Laminin_G_2. 2 hits.
[Graphical view]
PRINTSiPR00205. CADHERIN.
PR00249. GPCRSECRETIN.
SMARTiSM00112. CA. 3 hits.
SM00181. EGF. 6 hits.
SM00179. EGF_CA. 4 hits.
SM00180. EGF_Lam. 1 hit.
SM00303. GPS. 1 hit.
SM00008. HormR. 1 hit.
SM00282. LamG. 2 hits.
[Graphical view]
SUPFAMiSSF49313. SSF49313. 4 hits.
SSF49899. SSF49899. 2 hits.
PROSITEiPS00010. ASX_HYDROXYL. 2 hits.
PS00232. CADHERIN_1. 3 hits.
PS50268. CADHERIN_2. 4 hits.
PS00022. EGF_1. 6 hits.
PS01186. EGF_2. 4 hits.
PS50026. EGF_3. 6 hits.
PS01248. EGF_LAM_1. 1 hit.
PS50027. EGF_LAM_2. 2 hits.
PS50227. G_PROTEIN_RECEP_F2_3. 1 hit.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
PS50221. GPS. 1 hit.
PS50025. LAM_G_DOMAIN. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCELR2_RAT
AccessioniPrimary (citable) accession number: Q9QYP2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: May 1, 2000
Last modified: November 2, 2016
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.