ID A0A091M118_CARIC Unreviewed; 2691 AA.
AC A0A091M118;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Cadherin EGF LAG seven-pass G-type receptor 1 {ECO:0000313|EMBL:KFP64322.1};
DE Flags: Fragment;
GN ORFNames=N322_01749 {ECO:0000313|EMBL:KFP64322.1};
OS Cariama cristata (Red-legged seriema).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Cariamiformes; Cariamidae; Cariama.
OX NCBI_TaxID=54380 {ECO:0000313|EMBL:KFP64322.1, ECO:0000313|Proteomes:UP000054116};
RN [1] {ECO:0000313|EMBL:KFP64322.1, ECO:0000313|Proteomes:UP000054116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N322 {ECO:0000313|EMBL:KFP64322.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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.
CC Adhesion G-protein coupled receptor (ADGR) subfamily.
CC {ECO:0000256|ARBA:ARBA00007343}.
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 EMBL; KK514580; KFP64322.1; -; Genomic_DNA.
DR Proteomes; UP000054116; Unassembled WGS sequence.
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:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR CDD; cd11304; Cadherin_repeat; 7.
DR CDD; cd00054; EGF_CA; 5.
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; 8.
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; IPR017983; GPCR_2_secretin-like_CS.
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:SF36; CADHERIN EGF LAG SEVEN-PASS G-TYPE RECEPTOR 1; 1.
DR PANTHER; PTHR24026; FAT ATYPICAL CADHERIN-RELATED; 1.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF00028; Cadherin; 7.
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; 8.
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; 8.
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; 4.
DR PROSITE; PS50268; CADHERIN_2; 8.
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; PS00650; G_PROTEIN_RECEP_F2_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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:KFP64322.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054116};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
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 TRANSMEM 2190..2215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2236..2256
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2276..2297
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2318..2339
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2345..2368
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 26..133
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 134..239
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 240..355
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 356..457
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 458..560
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 561..666
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 667..768
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 791..891
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 970..1028
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1030..1066
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1070..1108
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1109..1313
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1316..1352
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1356..1540
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1542..1578
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1579..1616
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1673..1720
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1705..1778
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 2195..2369
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 1962..2003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2430..2691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1967..1985
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1989..2003
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2430..2459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2460..2477
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2491..2507
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2548..2586
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2587..2603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2629..2660
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1018..1027
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1056..1065
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1342..1351
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1568..1577
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1606..1615
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1673..1685
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1675..1692
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1694..1703
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP64322.1"
FT NON_TER 2691
FT /evidence="ECO:0000313|EMBL:KFP64322.1"
SQ SEQUENCE 2691 AA; 299527 MW; E9B33FC2FB5A8C8C CRC64;
SPRRRSATTY LTVTVSDTND HEPVFEQPEY RESIRENLEV GYEVLTIRAT DGDAPANANM
LYRLLEPGAG DGVFEIDPRS GVVRTRALVD REEVSEYHLV VEANDQGKDP GPRSATAMVH
ITVEDENDNY PQFSEKRYLV QVPEDAPVNS QILQVQATDR DRGSNAQVHY SIVSGNLKGQ
FYIHSFSGAI DLINPLDYET IREYTLRIKA QDGGRPPLIN SSGMVSVQVV DVNDNAPIFV
STPFQATVLE NVPLGYSVLH IQAVDADSGE NARLEYKLIE MAPSTGGASV AGDSTFPFQI
NNSTGWITVS AELDRETVEN YHFGVEARDH GVPVMTSSAS VSITVLDVND NNPTFTEKVY
HLRLNEDAAV GSSVLTLTAV DRDVNSVVTY QITSGNTRNR FAITSQSGGG LITLALPLDY
KQERQYVLTV TASDGTRFDT VQVFINVTDA NTHRPVFQSS HYTVSVSEDK PIGTSIVTIS
ATDEDTGENA RITYILDDNI PQFRIDPDTG TITTLMELDY EDQASYTLAI TAHDNGIPQK
SDTTYVEILI LDANDNAPRF LRDRYQGSVF EDVPLSTSVL QLSATDRDSG LNGRLLYTFQ
GGDDGDGDFY IEPTSGVIRT LRKLDRENVA VYSLRAFAVD RGSPPLKASV DIQVTVLDIN
DNPPVFEKDE FDIFVEENSP VGSIVARISA ADPDEGTNAQ IMYQIIEGNI PEVFQLDLLN
GDLTALMDLD YESRTEYVIV VQATSAPLVS RATVHIRLLD QNDNPPVLQD FQILFNNYVT
NKSNSFPSGV IGKIPAHDPD VSDSLAYTFV QGNELNLLLL DSATGELKLS RDLDNNRPLE
ALMKVSVSDG VHSVTAVCTL RVTIITDDML TNSITVRLEN MSQERFLSPL LSLFVEGVAT
VLSTAKDGIF VFNIQNDTDV SSNILNVTFS ALLPGGIRNK FFPSEDLQEQ IYLNRTLLTM
ISTQRVLPFD DNICLREPCE NYMKCVSVLK FDSSAPFISS NTVLFRPIHP INGLRCRCPP
GFTGDYCETE IDLCYSNPCG SNGLCRSREG GYTCECYEDY TGEYCEVNAR SGRCAPGVCK
NGGTCVNLLI GGFKCECPPG EYERPYCEMT TRSFPPQSFI TFKGLRQRFH FTVSLMFATR
ERNALLLYNG RFNEKHDFIA LEIIEEQIQL TFSAGETTTM VAPFVPGGVS DGQWHSVQVQ
YYNKPNIGRL GIPHGPSGEK VAVVTVDDCD TAVAVRFGSL IGNYTCAAQG TQTGSKKSLD
LTGPLLLGGV PNLPEDFPVQ NRQFVGCMRN LSIDSKPIDM ASFIANNGTL PGCAAQRNYC
ETNWCQNGGT CINKWNTYIC ECPVRYGGKN CEQAMPSPQR FSGESIIIWS DLDITISVPW
YIGLMFRTRK VNGMLMQANA GTASKINIQI LNNYVQFEVY SGLSQVASLK MSQSRVSDGE
WHHLLIELKS AKDGKDIKYL AVMSLDYGMY QSTVQIGNQL PGLKMKSIIV GGVSGDQVSV
HSNLKIIVFC HQGVRMGETS TNIATLNMKQ AIKINVKEGC EVDNPCDSNP CPQHSYCSDD
WDSYSCVCDP GYFGRDCVDV CNLNPCEHVS TCVHKPSSSH GYTCECGQSY YGQYCESKID
LPCPRGWWGN PICGPCNCET SKGFDSDCNK TNGECHCKAN YYRPQSSDTC YPCDCFPSGS
HTRACDMETG QCPCKPGVIG RQCNRCDNPF AEVTMKGCEV IYNGCPKAFE AGIWWPQTKF
GQPAAVPCPK GSVGNAVRHC NIEKGWLPPE LFNCTTSTFV DLKIMNEKLH HNETKLDGGK
TIRIVRVLQN ATKYTHSLYG NDVRTAYQMM IRVLQYESQQ QGFDLAATRD VEFNENIIKV
GSALLDPSNK EHWEQIQRTE GGTAHLLRHY EEYFNNVAQN MKKTYMRPFV IVATNMIIAV
DIFDKSNFTG ARIPRFHEIK EDYPKDLESS VVFPDTLFRP SDRKAVPTMK PSNQKLSSKV
NSDALSPDSA FAKRKKRHPD DSTHHTVAMV TIYRSLGHLL PENYDPDRRS LRLPNRPIIN
TPVVSTAIHS DGELPPNLME KPIIVEYAML ETEERTKPVC VFWNHSITIG GTGAWSSRGC
ELFSRNQSHI ACQCNHITSF AVLMDISKRE VGDIRLMIFE SFWFSRALIQ SLSLSFEHDS
EHRQRIDPML QLTHQIVIQK SNFNFPALSL LQFVCTVIAI LLHYFYMSTF AWMFVEQLHI
YRMLTEVRNI NFGHMRFYYV VGWGITAIIT GLAVGLDPQG YGNPDFCWLS VHDTLIWSFA
GPIVIVVLIN TVIFILAMKA SCRRRQRSFE KTGVVSGLRT AFLLLLLISA TWLLGLMAVN
SDVMMFHYLF AIFSCLQGLF IFFFHCVFNK EVRKHLKNTL TGKKPLPDDS TATRATLLTR
SLNCNNTYIE EPNMYRTTIG ESTVSLESTV RDEAAHKLSG SSSQARAGQT EADSSIFHRN
PSKSNEHDSD SDSELSLDEH SSSYASSHSS DSEEDGLETE KKWNTSTSKN NEHGPLHSTP
KVDTLPNHVK PYWPTECITA SDGEDPSGIQ KLKVETKVNV ELHRENQVNH SNEAPQDKEN
EGQQKENRPL SHQNNQQPEQ RKGILKNKVT YPPPLMDKNM KNRLREKLSD YNQTTISSRT
TSLGTNDGVR SPSDSGVTVK NARREQSRDQ LNGMAMNIHV GTGHADTSDS E
//
