ID A0A1U8BHE6_MESAU Unreviewed; 3034 AA.
AC A0A1U8BHE6;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Cadherin EGF LAG seven-pass G-type receptor 1 isoform X3 {ECO:0000313|RefSeq:XP_012966657.1};
GN Name=Celsr1 {ECO:0000313|RefSeq:XP_012966657.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_012966657.1};
RN [1] {ECO:0000313|RefSeq:XP_012966657.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Receptor that may have an important role in cell/cell
CC signaling during nervous system formation.
CC {ECO:0000256|ARBA:ARBA00002066}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family. LN-TM7
CC subfamily. {ECO:0000256|ARBA:ARBA00010933}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR RefSeq; XP_012966657.1; XM_013111203.2.
DR STRING; 10036.ENSMAUP00000004099; -.
DR OrthoDB; 4006628at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IEA:Ensembl.
DR GO; GO:0045176; P:apical protein localization; IEA:Ensembl.
DR GO; GO:0048105; P:establishment of body hair planar orientation; IEA:Ensembl.
DR GO; GO:0042249; P:establishment of planar polarity of embryonic epithelium; IEA:Ensembl.
DR GO; GO:0001942; P:hair follicle development; IEA:Ensembl.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0042472; P:inner ear morphogenesis; IEA:Ensembl.
DR GO; GO:0060490; P:lateral sprouting involved in lung morphogenesis; IEA:Ensembl.
DR GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
DR GO; GO:0097475; P:motor neuron migration; IEA:Ensembl.
DR GO; GO:0060488; P:orthogonal dichotomous subdivision of terminal units involved in lung branching morphogenesis; IEA:Ensembl.
DR GO; GO:0090179; P:planar cell polarity pathway involved in neural tube closure; IEA:Ensembl.
DR GO; GO:0060489; P:planar dichotomous subdivision of terminal units involved in lung branching morphogenesis; IEA:Ensembl.
DR GO; GO:0090251; P:protein localization involved in establishment of planar polarity; IEA:Ensembl.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0007266; P:Rho protein signal transduction; IEA:Ensembl.
DR GO; GO:0042060; P:wound healing; IEA:Ensembl.
DR CDD; cd11304; Cadherin_repeat; 9.
DR CDD; cd00054; EGF_CA; 4.
DR CDD; cd00055; EGF_Lam; 1.
DR CDD; cd00110; LamG; 2.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 2.60.220.50; -; 1.
DR Gene3D; 2.60.40.60; Cadherins; 9.
DR Gene3D; 4.10.1240.10; GPCR, family 2, extracellular hormone receptor domain; 1.
DR Gene3D; 2.10.25.10; Laminin; 6.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 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; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR24026:SF126; CADHERIN-89D; 1.
DR PANTHER; PTHR24026; FAT ATYPICAL CADHERIN-RELATED; 1.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF00028; Cadherin; 8.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF16489; GAIN; 1.
DR Pfam; PF01825; GPS; 1.
DR Pfam; PF02793; HRM; 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; 9.
DR SMART; SM00181; EGF; 6.
DR SMART; SM00179; EGF_CA; 5.
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; 9.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS00232; CADHERIN_1; 6.
DR PROSITE; PS50268; CADHERIN_2; 9.
DR PROSITE; PS00022; EGF_1; 5.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 6.
DR PROSITE; PS01248; EGF_LAM_1; 1.
DR PROSITE; PS50027; EGF_LAM_2; 1.
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 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU00043}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW ECO:0000256|PROSITE-ProRule:PRU00460};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170,
KW ECO:0000313|RefSeq:XP_012966657.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000189706};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transducer {ECO:0000256|ARBA:ARBA00023224};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..3034
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010569180"
FT TRANSMEM 2485..2508
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2520..2538
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2544..2566
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2587..2607
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2627..2647
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2668..2690
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2696..2718
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 261..368
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 369..474
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 475..580
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 581..702
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 703..804
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 805..907
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 908..1014
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1015..1116
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1139..1239
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1318..1376
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1378..1414
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1418..1456
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1457..1661
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1664..1700
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1704..1885
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1887..1923
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1924..1961
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2018..2065
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 2050..2123
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 2483..2720
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 222..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2292..2345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2775..2900
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2908..2927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2936..2991
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2775..2794
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2814..2828
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2975..2989
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1366..1375
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1404..1413
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1690..1699
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1913..1922
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1951..1960
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2018..2030
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2020..2037
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2039..2048
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 3034 AA; 331244 MW; 202FB7E897E1C3C9 CRC64;
MAPSPPRVLP ALVLLAAAAL PALGLGAAAW ELRVPGGGRA FALGPGWIYR LDTTRTSREL
LDVSNEGLVA GRQRRPSAGT RGCARLTGRL LPLQVRLVAR ESPTAPSLVL RARAYGARCG
VRLRRRSVRG GELHSRVVRS VPGLGDALCF PAPGGGAASL SSVLKAITTF PVCSCPPLAG
TRCRRGSICL QPGGSAGLRL VCALGRAAGA VWVELVIEAT SRTPSESPSV SPSSPSLPQP
RTGVVRRSRR GAGSSTSPQF PLPSYQVSVP ENEPAGTAVI ELRAHDPDEG EAGRLSYQME
ALFDERSNGY FLIDAVTGAV TTARALDRET KDTHVLKVSA VDHGSPRRSA ATYLTVTVSD
TNDHSPVFEQ SEYRERIREN LEVGYEVLTI RATDGDAPSN ANMRYRLLEG AGGVFEIDAR
SGVVRTRAVV DREEAAEYQL LVEANDQGRN PGPLSASATV HIVVEDENDN YPQFSEKRYV
VQVPEDVAVN TAVLRVQATD RDQGQNAAIH YSIVSGNLKG QFYLHSLSGS LDVINPLDFE
AIREYTLRIK AQDGGRPPLI NSSGLVSVQV LDVNDNAPIF VSSPFQAAVL ENVPLGHSVL
HIQAVDADAG ENARLQYRLV DTASPILGGS SVDPENPASA PDFPFQIHNS SGWITVCAEL
DREEIEHYSF GVEAVDHGLP PMSASASVSI TVLDVNDNDP VFTQPVYELR LNEDAAVGSS
VLTLRARDRD ANSVITYQLT GGNTRNRFAL SSQSGGGLIT LALPLDYKQE RQYVLAVTAS
DGTRSHTAQV FINVTDANTH RPVFQSSHYT VSVSEDRPVG TSIATISATD EDTGENARIT
YVLEDPVPQF RIDPDTGTIY TMTELDYEDQ AAYTLAITAQ DNGIPQKSDT TSLEILILDA
NDNVPRFLRD FYQGSVFEDA PPSTSVLQVS ATDRDSGPNG RLTYTFQGGD DGDGDFYIEP
TSGVIRTQRR LDRENVAVYN LHALAVDRGT PNPLSASVEI QVTVLDINDN PPVFEKDELE
LFVEENSPVG SVVARIKAND PDEGPNAQIM YQIVEGNVPE VFQLDLLSGD LRALVELDFE
VRRDYMLVVQ ATSAPLVSRA TVHIRLLDQN DNPPELPDFQ ILFNNYVTNK SNSFPSGVIG
RIPAHDPDLS DSLNYTFLQG NELSLLLLDP ATGELQLSRD LDNNRPLEAL MEVSVSDGIH
SVTALCTLRV TIITDDMLTN SITVRLENMS QEKFLSPLLS LFVEGVATVL STTKDDIFVF
NIQNDTDVSS NILNVTFSAL LPGGARGRFF PSEDLQEQIY LNRTLLTTIS AQRVLPFDDN
ICLREPCENY MKCVSVLRFD SSAPFISSTT VLFRPIHPIT GLRCRCPPGF TGDYCETEID
LCYSSPCGAN GRCRSREGGY TCECFEDFTG EHCQVNVRSG RCASGVCKNG GTCVNLLIGG
FHCVCPPGEY EHPYCEVSTR SFPPQSFVTF RGLRQRFHFT VSLSFATQDR NALLLYNGRF
NEKHDFIALE IVDEQLQLTF SAGETTTTVT PQVPGGVSDG RWHSVLVQYY NKPNIGHLGL
PHGPSGEKVA VVTVDDCDAA VAVHFGSYVG NYSCAAQGTQ SGSKKSLDLT GPLLLGGVPN
LPEDFPVHSR QFVGCMRNLS VDGRVVDMAA FIANNGTRAG CASQRNFCGG TSCQNGGTCV
NKWNTYLCEC PLRFGGKNCE QVMPYPQRFS GESIVSWSDL DITISVPWYL GLMFRTRKED
GVLMEATAGT SSRLHLQILN NYIQFEVSHG PSDVASMKLS KSRITDGEWH HVLIELRSAK
EGKDIKYLAV MTLDYGMDQS TVQIGNQLPG LKMRTIVIGG VSEDKLSVRH GFRGCMQGVR
MGETSTNIAT LNMNDALKVR VKDGCDVEDP CASSPCPPHS HCRDTWDSYS CVCDRGYFGR
KCVDACLLNP CKHVAACVRS PNSPRGYSCE CGPGHYGQYC ENKVDLPCPK GWWGNPVCGP
CHCAVSQGFD PDCNKTNGQC QCKENYYKPP AQDACLPCDC FPHGSHSRAC DMDTGQCACK
PGVIGRQCNR CDNPFAEVTS LGCEVIYNGC PRAFEAGIWW PQTKFGQPAA VPCPKGSVGN
AVRHCSGEKG WLPPELFNCT SGYFVDLKAM NEKLSRNETR MDGDRSLRLA KALRNATQHN
GTLFGNDVRT AYQLLARILQ HESHQQGFDL AATREANFHE DVVHTGSALL APATQAAWEQ
IQRSEGGAAQ LLRRFEAYFS NVARNVKRTY LRPFIIITAN MILAVDIFDK FNFTGAQVPR
FEDVQEEFPR ELESSVSFPA DTFKPPEKKE GPMMRLANRR AGPQAPQPES RAERETSFSR
QRRHPDEPGQ FAVALVIIYR TLGQLLPEHY DPDHRSLRLP NRPIINTPVV SAMVYSEGTP
LPSSLQRPVL VEFALLETEE RSKPVCVFWN HSLDIGGTGG WSAKGCELLS RNRTHVTCQC
SHLASCAVLM DISRREHGEV LPLKIITYAA LSLSLVALLV TFILLSLVRT LRSNLHSIHK
NLIVALFFSQ LIFMVGINQT ENPFLCTVVA ILLHYVSMST FAWALVENLH VYRMLTEVRN
IDTGPMRFYH VVGWGIPAIV TGLAVGLDPQ GYGNPDFCWL SLQDSLIWSF AGPVGMVIII
NTVIFVLSAK VACQRKRHYY ERKGVISLLR TAFLLLLLVS ATWLLGLLAV NSDTLSFHYL
FAAFSCLQGI FVLLFHCVTH REVRKHLRAV LAGKKLHLDD SAATRATLLT RSLNCNNTYS
EGPDMLRTAL GESTASLDST TRNEGIQKLS VSSGPARGNH GEPDTSFIPR NSKKPHGPDS
DSDSELSLDE HSSSYASSHS SDSEDDGDDA EDKWNPAGGP VHSTPKADAL ANHVPAGWPD
ESLAGSDSEE LDTETHLKVE TKVSVELHQQ AQGNHCGSRP PDLESGVLGK PVAVLSSQPQ
EQRKGILKNK VTYPPPLPEQ PMKCRLREKL ADCEQSPSSS RTSSLGSGDG VRATDCVITI
KTPRREPGRE HLNGVAMNVC TGSAQTNGSD SEKP
//
