ID A0A0P7TYR1_SCLFO Unreviewed; 1451 AA.
AC A0A0P7TYR1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Cadherin EGF LAG seven-pass G-type receptor 1-like {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=Z043_118945 {ECO:0000313|EMBL:KPP62847.1};
OS Scleropages formosus (Asian bonytongue) (Osteoglossum formosum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Osteoglossidae; Scleropages.
OX NCBI_TaxID=113540 {ECO:0000313|EMBL:KPP62847.1, ECO:0000313|Proteomes:UP000034805};
RN [1] {ECO:0000313|EMBL:KPP62847.1, ECO:0000313|Proteomes:UP000034805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Aro1 {ECO:0000313|EMBL:KPP62847.1};
RA Tan M.H., Gan H.M., Croft L.J., Austin C.M.;
RT "The genome of the Asian arowana (Scleropages formosus).";
RL Submitted (AUG-2015) 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. 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPP62847.1}.
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DR EMBL; JARO02008341; KPP62847.1; -; Genomic_DNA.
DR STRING; 113540.ENSSFOP00015062679; -.
DR Proteomes; UP000034805; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0048731; P:system development; IEA:UniProt.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00055; EGF_Lam; 2.
DR CDD; cd00110; LamG; 1.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 2.60.220.50; -; 1.
DR Gene3D; 4.10.1240.10; GPCR, family 2, extracellular hormone receptor domain; 1.
DR Gene3D; 2.10.25.10; Laminin; 3.
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; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
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; IPR001791; Laminin_G.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR12011; ADHESION G-PROTEIN COUPLED RECEPTOR; 1.
DR PANTHER; PTHR12011:SF470; LATROPHILIN-LIKE PROTEIN LAT-2; 1.
DR Pfam; PF00002; 7tm_2; 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; 1.
DR PRINTS; PR00249; GPCRSECRETIN.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00180; EGF_Lam; 1.
DR SMART; SM00303; GPS; 1.
DR SMART; SM00008; HormR; 1.
DR SMART; SM00282; LamG; 1.
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 PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS50026; EGF_3; 2.
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 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}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040};
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 Reference proteome {ECO:0000313|Proteomes:UP000034805};
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 898..921
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 933..951
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 957..979
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1000..1018
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1030..1048
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1060..1080
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1092..1114
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..109
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 125..306
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 308..344
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 345..382
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 439..486
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 471..544
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 896..1115
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 726..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1191..1305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1322..1362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1387..1451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..748
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1262..1283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1322..1341
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1390..1405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 334..343
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 372..381
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 439..451
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 441..458
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 460..469
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KPP62847.1"
SQ SEQUENCE 1451 AA; 160863 MW; 979EBCD15C364705 CRC64;
PNIGRLGVPH GPSGEKVAVV AVDDCDIAMA VHFGNHIGNY SCAAQGTQTG QKKSLDLTGP
LLLGGVPNLP EDFPVHNLDF VGCMRNLTID SQPIDMASFI ANNGTTAGCT AKRDFCTKNV
CQNGGTCINK WNTYSLSWSE PDITVAIPWY LGLMFRTRRS SGTLLHTSIG MSSRINLEIS
NKHLSFKVFL GEQRVASLEF AQVRVNDGDW HHVLVELKSI KDGKDIQYMA TVSLDYGMFQ
STVEIGNELP GQRLKSLFVG GVLGPDGLVK HGFQGCMQGV RMGETATNTG NINMLQGLKI
RVEEGCDLAD PCDANLCPEH SHCSDDWSAH TCVCDPGYFG KDCVDACQLN PCEHTSSCIH
KPSSSHGYTC ECGQNYYGQY CEKKVDQPCP RGWWGNPVCG PCSCDVIKGF NPDCNKTTGE
CYCKDNYYRP KGEDTCYPCD CYPLGAHTRT CDPHTGQCSC KAGVIGRQCN RCDSPFAEVT
ASGCQVVYEG CPKAFDTGIW WPKTKFGRPA AVNCPKGSVG TAIRHCSDEK GWLPPELFNC
TTVTFSQLRR LNEEMHQNET IIDGEKSKSI ARMLRNATEH TDTFYGNDVR TAYHLLSQLL
EYESQQQGFE LAATRDADFN ENIIKAGSAI LDPRNKDHWE HIQRSEGGTA QLLRHFEEYS
DILAQNMKRT YLKPFTIVTD NMIVAVDYLD TSSPDHAKMP RFREIRDAYP KDLESSIQFP
KFTLTASDGK GESTEEPFTQ TDNTGVDFTP SAKKRRHADG NGPLPVAVVI VYRSLGQLLP
QRYDPDRRSL RLPNRPIINT PIVSTAVHSE GVPLTAPLEQ PITLDYTLLE TEERTKPVCV
FWNHSIAIGG TGGWSSKGCE LVFRNNTHIR CQCNHMTSFA VLMDISKREH GDVLPLKIFT
YTAVSASLVA LLLTFILLAI IRKLHSNLHS IHKNLVAALF FSELVFLIGI NQTENPFLCT
VIAILLHYFY MCTFAWMFVE GLHIYRMLTE MRNIDHGQMR FYYAIGWGIP AIITGLAVGL
DPQGYGNPDF CWLSVNIVVF VLAAKASCGR RQRMFEKSGV ISALRTAFLL LLLISATWLL
GLMAVNSDVM TFHYLFAVFS CLQGIFVFFL HCVFNKDVRK NLKNVFMGKK PLPDESSATR
ATLLTRSLNC NNTYTEDGAL YRTPIGESTV SMETSVRSAH SHRSYLTHVF RDDSGLKPSG
SSGTAKVGHA DGETSIFQGN GTKGDDSDSD SELSLDEHSS SYASSHSSDS EEDEVDIKGK
WNPSTPKNNE RQPLHSTPKV DTLSNHVKPY WPTDGMTASD SEDLSRVEKL RVETKVDVEL
HPENKLNHIK DLPEDKELSG KEVSPPSQLN SNHKAEQRKG ILKNKITYPL PLTDKNMKNR
LREKLSDYNP PTITRASSLG SNEGIRPAHG NNGVVIKPPH RLSPTPREQP NGVAMSLRRG
LVNGDDDTDS E
//
