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Cadherin EGF LAG seven-pass G-type receptor 3 (Multiple epidermal growth factor-like domains protein 2) (Multiple EGF-like domains protein 2)

 CELR3_RAT               Reviewed;        3313 AA.
O88278;
02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
23-MAY-2018, entry version 155.
RecName: Full=Cadherin EGF LAG seven-pass G-type receptor 3;
AltName: Full=Multiple epidermal growth factor-like domains protein 2;
Short=Multiple EGF-like domains protein 2;
Flags: Precursor;
Name=Celsr3; Synonyms=Megf2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Brain;
PubMed=9693030; DOI=10.1006/geno.1998.5341;
Nakayama M., Nakajima D., Nagase T., Nomura N., Seki N., Ohara O.;
"Identification of high-molecular-weight proteins with multiple EGF-
like motifs by motif-trap screening.";
Genomics 51:27-34(1998).
[2]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-2117; TYR-3050 AND
SER-3098, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=16641100; DOI=10.1073/pnas.0600895103;
Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
"Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
regulation of aquaporin-2 phosphorylation at two sites.";
Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
-!- FUNCTION: Receptor that may have an important role in cell/cell
signaling during nervous system formation.
-!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
-!- TISSUE SPECIFICITY: Expressed in the brain. Expressed in
cerebellum, olfactory bulb, cerebral cortex, hippocampus and brain
stem.
-!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
aspartate and asparagine is (R) stereospecific within EGF domains.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
LN-TM7 subfamily. {ECO:0000305}.
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EMBL; AB011528; BAA32459.1; -; mRNA.
RefSeq; NP_112610.1; NM_031320.1.
UniGene; Rn.14558; -.
ProteinModelPortal; O88278; -.
SMR; O88278; -.
STRING; 10116.ENSRNOP00000041011; -.
iPTMnet; O88278; -.
PhosphoSitePlus; O88278; -.
PaxDb; O88278; -.
PRIDE; O88278; -.
Ensembl; ENSRNOT00000084220; ENSRNOP00000068821; ENSRNOG00000053889.
GeneID; 83466; -.
KEGG; rno:83466; -.
UCSC; RGD:621787; rat.
CTD; 1951; -.
RGD; 621787; Celsr3.
eggNOG; KOG4289; Eukaryota.
eggNOG; ENOG410XTGH; LUCA.
GeneTree; ENSGT00760000118805; -.
HOGENOM; HOG000231346; -.
HOVERGEN; HBG050887; -.
InParanoid; O88278; -.
KO; K04602; -.
OMA; ANRHPQF; -.
OrthoDB; EOG091G0039; -.
PhylomeDB; O88278; -.
PRO; PR:O88278; -.
Proteomes; UP000002494; Chromosome 8.
Bgee; ENSRNOG00000053889; -.
Genevisible; O88278; RN.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0004930; F:G-protein coupled receptor activity; IEA:UniProtKB-KW.
GO; GO:0007413; P:axonal fasciculation; IEA:Ensembl.
GO; GO:0060271; P:cilium assembly; IEA:Ensembl.
GO; GO:0036514; P:dopaminergic neuron axon guidance; IEA:Ensembl.
GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
GO; GO:0001764; P:neuron migration; IEA:Ensembl.
GO; GO:1904938; P:planar cell polarity pathway involved in axon guidance; IEA:Ensembl.
GO; GO:0032880; P:regulation of protein localization; IEA:Ensembl.
GO; GO:0001932; P:regulation of protein phosphorylation; IEA:Ensembl.
GO; GO:0036515; P:serotonergic neuron axon guidance; IEA:Ensembl.
Gene3D; 4.10.1240.10; -; 1.
InterPro; IPR002126; Cadherin.
InterPro; IPR015919; Cadherin-like.
InterPro; IPR020894; Cadherin_CS.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR032471; GAIN_dom_N.
InterPro; IPR017981; GPCR_2-like.
InterPro; IPR036445; GPCR_2_extracell_dom_sf.
InterPro; IPR001879; GPCR_2_extracellular_dom.
InterPro; IPR000832; GPCR_2_secretin-like.
InterPro; IPR017983; GPCR_2_secretin-like_CS.
InterPro; IPR000203; GPS.
InterPro; IPR002049; Laminin_EGF.
InterPro; IPR001791; Laminin_G.
Pfam; PF00002; 7tm_2; 1.
Pfam; PF00028; Cadherin; 8.
Pfam; PF00008; EGF; 3.
Pfam; PF16489; GAIN; 1.
Pfam; PF02793; HRM; 1.
Pfam; PF00053; Laminin_EGF; 1.
Pfam; PF02210; Laminin_G_2; 2.
PRINTS; PR00205; CADHERIN.
PRINTS; PR00249; GPCRSECRETIN.
SMART; SM00112; CA; 9.
SMART; SM00181; EGF; 6.
SMART; SM00179; EGF_CA; 5.
SMART; SM00180; EGF_Lam; 1.
SMART; SM00303; GPS; 1.
SMART; SM00008; HormR; 1.
SMART; SM00282; LamG; 2.
SUPFAM; SSF111418; SSF111418; 1.
SUPFAM; SSF49313; SSF49313; 9.
SUPFAM; SSF49899; SSF49899; 2.
PROSITE; PS00010; ASX_HYDROXYL; 1.
PROSITE; PS00232; CADHERIN_1; 7.
PROSITE; PS50268; CADHERIN_2; 8.
PROSITE; PS00022; EGF_1; 6.
PROSITE; PS01186; EGF_2; 4.
PROSITE; PS50026; EGF_3; 6.
PROSITE; PS01248; EGF_LAM_1; 1.
PROSITE; PS50027; EGF_LAM_2; 1.
PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PROSITE; PS50221; GPS; 1.
PROSITE; PS50025; LAM_G_DOMAIN; 2.
1: Evidence at protein level;
Calcium; Cell membrane; Complete proteome; Developmental protein;
Disulfide bond; EGF-like domain; G-protein coupled receptor;
Glycoprotein; Hydroxylation; Laminin EGF-like domain; Membrane;
Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
Transducer; Transmembrane; Transmembrane helix.
SIGNAL 1 31 {ECO:0000255}.
CHAIN 32 3313 Cadherin EGF LAG seven-pass G-type
receptor 3.
/FTId=PRO_0000012920.
TOPO_DOM 32 2538 Extracellular. {ECO:0000255}.
TRANSMEM 2539 2559 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 2560 2570 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2571 2591 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 2592 2599 Extracellular. {ECO:0000255}.
TRANSMEM 2600 2620 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 2621 2641 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2642 2662 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 2663 2679 Extracellular. {ECO:0000255}.
TRANSMEM 2680 2700 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 2701 2724 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2725 2745 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 2746 2752 Extracellular. {ECO:0000255}.
TRANSMEM 2753 2773 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 2774 3313 Cytoplasmic. {ECO:0000255}.
DOMAIN 317 424 Cadherin 1. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 425 536 Cadherin 2. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 537 642 Cadherin 3. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 643 747 Cadherin 4. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 748 849 Cadherin 5. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 850 952 Cadherin 6. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 953 1058 Cadherin 7. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1059 1160 Cadherin 8. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1161 1257 Cadherin 9. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1366 1424 EGF-like 1; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 1426 1462 EGF-like 2; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 1466 1505 EGF-like 3; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 1506 1710 Laminin G-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
DOMAIN 1713 1749 EGF-like 4; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 1753 1935 Laminin G-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
DOMAIN 1937 1972 EGF-like 5; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 1973 2011 EGF-like 6; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 2012 2044 EGF-like 7; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 2046 2081 EGF-like 8; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 2068 2115 Laminin EGF-like. {ECO:0000255|PROSITE-
ProRule:PRU00460}.
DOMAIN 2475 2527 GPS. {ECO:0000255|PROSITE-
ProRule:PRU00098}.
MOD_RES 1954 1954 (3R)-3-hydroxyaspartate. {ECO:0000255}.
MOD_RES 2117 2117 Phosphotyrosine.
{ECO:0000244|PubMed:16641100}.
MOD_RES 3050 3050 Phosphotyrosine.
{ECO:0000244|PubMed:16641100}.
MOD_RES 3098 3098 Phosphoserine.
{ECO:0000244|PubMed:16641100}.
CARBOHYD 623 623 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 838 838 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1173 1173 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1213 1213 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1308 1308 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1318 1318 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1640 1640 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1704 1704 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1761 1761 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2044 2044 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2173 2173 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2192 2192 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2382 2382 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2472 2472 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2504 2504 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 1370 1381 {ECO:0000250}.
DISULFID 1375 1412 {ECO:0000250}.
DISULFID 1414 1423 {ECO:0000250}.
DISULFID 1430 1441 {ECO:0000250}.
DISULFID 1435 1450 {ECO:0000250}.
DISULFID 1452 1461 {ECO:0000250}.
DISULFID 1470 1481 {ECO:0000250}.
DISULFID 1475 1491 {ECO:0000250}.
DISULFID 1493 1504 {ECO:0000250}.
DISULFID 1684 1710 {ECO:0000250}.
DISULFID 1717 1728 {ECO:0000250}.
DISULFID 1722 1737 {ECO:0000250}.
DISULFID 1739 1748 {ECO:0000250}.
DISULFID 1906 1935 {ECO:0000250}.
DISULFID 1941 1952 {ECO:0000250}.
DISULFID 1946 1961 {ECO:0000250}.
DISULFID 1963 1972 {ECO:0000250}.
DISULFID 1976 1987 {ECO:0000250}.
DISULFID 1981 1999 {ECO:0000250}.
DISULFID 2001 2010 {ECO:0000250}.
DISULFID 2018 2031 {ECO:0000250}.
DISULFID 2033 2043 {ECO:0000250}.
DISULFID 2050 2065 {ECO:0000250}.
DISULFID 2052 2068 {ECO:0000250}.
DISULFID 2070 2080 {ECO:0000250}.
DISULFID 2089 2098 {ECO:0000250}.
DISULFID 2101 2113 {ECO:0000250}.
SEQUENCE 3313 AA; 359355 MW; B11DA09517288764 CRC64;
MARRPLWWGL PGPSTPLLLL LLFSLFPSSR EEMGGGGDQG WDPGVATATG PRAQIGSGAV
ALCPESPGVW EDGDPGLGVR EPVFMKLRVG RQNARNGRGA PEQPNREPVV QALGSREQEA
GQGSGYLLCW HPEISSCGRT GHLRRGSLPL DALSPGDSDL RNSSPHPSEL LAQPDSPRPV
AFQRNGRRSI RKRVETFRCC GKLWEPGHKG QGERSATSTV DRGPLRRDCL PGSLGSGLGE
DSAPRAVRTA PAPGSAPHES RTAPERMRSR GLFRRGFLFE RPGPRPPGFP TGAEAKRILS
TNQARSRRAA NRHPQFPQYN YQTLVPENEA AGTAVLRVVA QDPDPGEAGR LVYSLAALMN
SRSLELFSID PQSGLIRTAA ALDRESMERH YLRVTAQDHG SPRLSATTMV AVTVADRNDH
APVFEQAQYR ETLRENVEEG YPILQLRATD GDAPPNANLR YRFVGSPAAR TAAAAAFEID
PRSGLISTSG RVDREHMESY ELVVEASDQG QEPGPRSATV RVHITVLDEN DNAPQFSEKR
YVAQVREDVR PHTVVLRVTA TDKDKDANGL VHYNIISGNS RGHFAIDSLT GEIQVMAPLD
FEAEREYALR IRAQDAGRPP LSNNTGLASI QVVDINDHSP IFVSTPFQVS VLENAPLGHS
VIHIQAVDAD HGENSRLEYS LTGVASDTPF VINSATGWVS VSGPLDRESV EHYFFGVEAR
DHGSPPLSAS ASVTVTVLDV NDNRPEFTMK EYHLRLNEDA AVGTSVVSVT AVDRDANSAI
SYQITGGNTR NRFAISTQGG MGLVTLALPL DYKQERYFKL VLTASDRALH DHCYVHINIT
DANTHRPVFQ SAHYSVSMNE DRPVGSTVVV ISASDDDVGE NARITYLLED NLPQFRIDAD
SGAITLQAPL DYEDQVTYTL AITARDNGIP QKADTTYVEV MVNDVNDNAP QFVASHYTGL
VSEDAPPFTS VLQISATDRD AHANGRVQYT FQNGEDGDGD FTIEPTSGIV RTVRRLDREA
VPVYELTAYA VDRGVPPLRT PVSIQVTVQD VNDNAPVFPA EEFEVRVKEN SIVGSVVAQI
TAVDPDDGPN AHIMYQIVEG NIPELFQMDI FSGELTALID LDYEARQEYV IVVQATSAPL
VSRATVHVRL VDQNDNSPVL NNFQILFNNY VSNRSDTFPS GIIGRIPAYD PDVSDHLFYS
FERGNELQLL VVNQTSGELR LSRKLDNNRP LVASMLVTVT DGLHSVTAQC VLRVVIITEE
LLANSLTVRL ENMWQERFLS PLLGHFLEGV AAVLATPTED VFIFNIQNDT DVGGTVLNVS
FSALAPRGAG AGAAGPWFSS EELQEQLYVR RAALAARSLL DVLPFDDNVC LREPCENYMK
CVSVLRFDSS APFLASASTL FRPIQPIAGL RCRCPPGFTG DFCETELDLC YSNPCRNGGA
CARREGGYTC VCRPRFTGED CELDTEAGRC VPGVCRNGGT CTNAPNGGFR CQCPAGGAFE
GPRCEVAARS FPPSSFVMFR GLRQRFHLTL SLSFATVQPS GLLFYNGRLN EKHDFLALEL
VAGQVRLTYS TGESSTVVSP TVPGGLSDGQ WHTVHLRYYN KPRTDALGGA QGPSKDKVAV
LSVDDCNVAV ALRFGAEIGN YSCAAAGVQT SSKKSLDLTG PLLLGGVPNL PENFPVSRKD
FIGCMRDLHI DGRRVDMAAF VANNGTTAGC QAKSHFCASG PCKNGGLCSE RWGGFSCDCP
VGFGGKDCRL TMAHPYHFQG NGTLSWDFGN DMPVSVPWYL GLSFRTRATK GVLMQVQLGP
HSVLLCKLDQ GLLSVTLSRA SGHAVHLLLD QMTVSDGRWH DLRLELQEEP GGRRGHHIFM
VSLDFTLFQD TMAMGSELEG LKVKHLHVGG PPPSSKEEGP QGLVGCIQGV WTGFTPFGSS
ALPPPSHRIN VEPGCTVTNP CASGPCPPHA NCKDLWQTFS CTCWPGYYGP GCVDACLLNP
CQNQGSCRHL QGGPHGYTCD CASGYFGQHC EHRMDQQCPR GWWGSPTCGP CNCDVHKGFD
PNCNKTSGQC HCKEFHYRPR GSDSCLPCDC YPVGSTSRSC APHSGQCPCR PGALGRQCNS
CDSPFAEVTA SGCRVLYDAC PKSLRSGVWW PQTKFGVLAT VPCPRGALGL RGTGAAVRLC
DEDHGWLEPD FFNCTSPAFR ELSLLLDGLE LNKTALDTVE AKKLAQRLRE VTGQTDHYFS
QDVRVTARLL AYLLAFESHQ QGFGLTATQD AHFNENLLWA GSALLAPETG DLWAALGQRA
PGGSPGSAGL VRHLEEYAAT LARNMDLTYL NPVGLVTPNI MLSIDRMEQP SSSQGAHRYP
RYHSNLFRGQ DAWDPHTHVL LPSQSPQPSP SEVLPTSSNA ENATASGVVS PPAPLEPESE
PGISIVILLV YRALGGLLPA QFQAERRGAR LPQNPVMNSP VVSVAVFRGR NFLRGALVSP
INLEFRLLQT ANRSKAICVQ WDPPGPADQH GMWTARDCEL VHRNGSHARC RCSRTGTFGV
LMDASPRERL EGDLELLAVF THVVVAASVT ALVLTAAVLL SLRSLKSNVR GIHANVAAAL
GVAELLFLLG IHRTHNQLLC TVVAILLHYF FLSTFAWLLV QGLHLYRMQV EPRNVDRGAM
RFYHALGWGV PAVLLGLAVG LDPEGYGNPD FCWISIHEPL IWSFAGPIVL VIVMNGIMFL
LAARTSCSTG QREAKKTSVL RTLRSSFLLL LLVSASWLFG LLAVNHSVLA FHYLHAGLCG
LQGLAVLLLF CVLNADARAA WTPACLGKKA APEETRPAPG PGSGAYNNTA LFEESGLIRI
TLGASTVSSV SSARSGRAQD QDSQRGRSYL RDNVLVRHGS TAEHAEHSLQ AHAGPTDLDV
AMFHRDAGAD SDSDSDLSLE EERSLSIPSS ESEDNGRTRG RFQRPLRRAA QSERLLAHPK
DVDGNDLLSY WPALGECEAA PCALQAWGSE RRLGLDSNKD AANNNQPELA LTSGDETSLG
RAQRQRKGIL KNRLQYPLVP QTRGTPELSW CRAATLGHRA VPAASYGRIY AGGGTGSLSQ
PASRYSSREQ LDLLLRRQLS RERLEEVPVP APVLHPLSRP GSQERLDTAP ARLEPRDRGS
TLPRRQPPRD YPGTMAGRFG SRDALDLGAP REWLSTLPPP RRNRDLDPQH PPLPLSPQRP
LSRDPLLPSR PLDSLSRISN SRERLDQVPS RHPSREALGP APQLLRARED PASGPSHGPS
TEQLDILSSI LASFNSSALS SVQSSSTPSG PHTTATPSAT ASALGPSTPR SATSHSISEL
SPDSEVPRSE GHS


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