ID L5K731_PTEAL Unreviewed; 631 AA.
AC L5K731;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=EGF, latrophilin and seven transmembrane domain-containing protein 1 {ECO:0000313|EMBL:ELK06283.1};
GN ORFNames=PAL_GLEAN10023894 {ECO:0000313|EMBL:ELK06283.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK06283.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; KB031032; ELK06283.1; -; Genomic_DNA.
DR AlphaFoldDB; L5K731; -.
DR STRING; 9402.L5K731; -.
DR InParanoid; L5K731; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:InterPro.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR CDD; cd00054; EGF_CA; 2.
DR Gene3D; 2.60.220.50; -; 1.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 2.
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; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR032471; GAIN_dom_N.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR017981; GPCR_2-like_7TM.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR InterPro; IPR000203; GPS.
DR PANTHER; PTHR12011:SF59; ADHESION G PROTEIN-COUPLED RECEPTOR L4; 1.
DR PANTHER; PTHR12011; ADHESION G-PROTEIN COUPLED RECEPTOR; 1.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF07645; EGF_CA; 2.
DR Pfam; PF16489; GAIN; 1.
DR Pfam; PF01825; GPS; 1.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00303; GPS; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR PROSITE; PS50221; GPS; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 438..455
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 493..512
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 518..538
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 559..581
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 587..608
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 13..51
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 64..101
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 432..525
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
SQ SEQUENCE 631 AA; 70964 MW; 082C4534BC6478E1 CRC64;
MGFSGNGITI CEDDNECGNL TQSCGENANC TNTEGSYYCM CAPGFRSSSN QDRFITNDGT
VCIDIDECDE LIACGDHAVC ENMDGGYSCS CKEGYQTSTG EAQFTPNDGT YCQENVNADC
HLDNACITAN IDKTLTKIRR INQPVALLEE VYRNSAKDLS PMDIITYIEI LAESSPLLRY
INSTNSDKDT LSNSTLTEFV KTVNNFVRKD TFIVWNKLPT NRRRTHLTKL IHAAEQATLR
ISQNFEKTTH FDTNSSDVAL KAFFFDSHHM KHIHPHMNVD GDYIEIFPKR KAADDSEGNV
AVVFLYYKSI GPLFSSSDNF IMEPQSYDNS EEEESVISSI ISVSISSNPP TLYELEKITF
TLSHIKTPDK YKSQCAFWNY LPDTMNGNWS LDGCELIYSN ETHTSCSCNH LTHFAILMSS
GTSIGITDYN ILTRITQLGI IISLICLALC IFTFWFFSEI QSTRTTIHKN LCCNLFLAEL
VFLIGINTNS NKLFCSIIAG LLHYFFLAAF AWMCIEGIHL YLIVVNLLAF GVIIYKVFRH
TAGLKPEVSC YENIRSCARG ALALLFLLGT TWIFGVLHVV HASVVTAYLF TISNAFQGMF
IFLFLCVLSR KIQEEYYRLF KNVPCCFGCL R
//
