ID U3JGN1_FICAL Unreviewed; 1127 AA.
AC U3JGN1;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSFALP00000001935.2};
OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000001935.2, ECO:0000313|Proteomes:UP000016665};
RN [1] {ECO:0000313|Ensembl:ENSFALP00000001935.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; U3JGN1; -.
DR STRING; 59894.ENSFALP00000001935; -.
DR Ensembl; ENSFALT00000001946.2; ENSFALP00000001935.2; ENSFALG00000001851.2.
DR eggNOG; KOG3545; Eukaryota.
DR eggNOG; KOG4193; Eukaryota.
DR eggNOG; KOG4729; Eukaryota.
DR GeneTree; ENSGT00940000159684; -.
DR HOGENOM; CLU_002753_1_1_1; -.
DR Proteomes; UP000016665; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate 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; cd22844; Gal_Rha_Lectin_LPHN1; 1.
DR Gene3D; 1.25.40.610; -; 1.
DR Gene3D; 2.60.120.740; -; 1.
DR Gene3D; 2.60.220.50; -; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 2.
DR InterPro; IPR032471; GAIN_dom_N.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR017981; GPCR_2-like_7TM.
DR InterPro; IPR003924; GPCR_2_latrophilin.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR000203; GPS.
DR InterPro; IPR000922; Lectin_gal-bd_dom.
DR InterPro; IPR043159; Lectin_gal-bd_sf.
DR InterPro; IPR003112; Olfac-like_dom.
DR PANTHER; PTHR12011:SF62; ADHESION G PROTEIN-COUPLED RECEPTOR L1; 1.
DR PANTHER; PTHR12011; ADHESION G-PROTEIN COUPLED RECEPTOR; 1.
DR Pfam; PF00002; 7tm_2; 2.
DR Pfam; PF16489; GAIN; 1.
DR Pfam; PF02140; Gal_Lectin; 1.
DR Pfam; PF01825; GPS; 1.
DR Pfam; PF02191; OLF; 1.
DR PRINTS; PR01444; LATROPHILIN.
DR SMART; SM00303; GPS; 1.
DR SMART; SM00284; OLF; 1.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR PROSITE; PS50221; GPS; 1.
DR PROSITE; PS51132; OLF; 1.
DR PROSITE; PS50228; SUEL_LECTIN; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00446};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000016665};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 734..758
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 770..790
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 802..828
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 848..867
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 888..911
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 917..940
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 7..96
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50228"
FT DOMAIN 101..360
FT /note="Olfactomedin-like"
FT /evidence="ECO:0000259|PROSITE:PS51132"
FT DOMAIN 736..941
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 394..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 102..284
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00446"
SQ SEQUENCE 1127 AA; 121772 MW; C90A2730B28129E2 CRC64;
LARRELACEG YPLELRCPGS DVVLVADANY GRTDDKICDA DPGQMANVQC YLPQAHPIMA
QRCNNRTQCV VVAGSDAFPD PCPGTYKYLE VQYDCVPYIF VCPGVPQRVG PALSTHESPH
QAGGWCRDPL QSGDRLYVLP WVPYRTDTLT EYASWADLVG ARPAATHRLP HRADGTGFVV
YDGAVFYNKE RTRSIVKYDL RTRIKSGETV VGAANYHDTS PYRWGGKTDI DLAVDEEGLW
VIYATEGNGG RLVVSQLNPY TLRLEGTWET GYAKRAASDA FMACGVLYVL RSVYLDDDTE
HLGNALVYAF DTRRGRGAAL ALPFPNPYQF VASVGYNPRD NQLYVWNNHF LLRYESLGPQ
ISVGSPGLIW GCSPRYSGTP QIIGGSPGCS RFLGGIPQTP WGISGSTSPP PPGGGGGGGG
GGGGGGGGGG GGGGGGGGGG GGGGGGGGGG GGGGGGGGGG GGGGGGGGGG GGGEQLLDIL
DAQLQALRPL ERESAGKNYN KMHKRERTCK DYIKAVVEAV DNLLRPEALE SWRDMNGSEQ
APVSHGLFPI SHGLFPVSHV LEVSVLNTEG PLQELVFPQE LGGDGSIQLS ASTLKQNSRN
GVVKVVFILY NNLGLFLPTE NATVRLGGDG GPRAPQLVVN SQVIAASINK ESSRVFLRDP
VVFTLPHLET KNHFGANCSF WNYSERSMAG HWSSQGCRLL RSNGTHSSCA CSHLTNFALL
MARTQSFPGR LNEVLLSVIT WAGILVALLC LGLSISAFCC LRGLPSERTT IHKNLCISLF
LAELLFLVGI DKTQYQVACP IFAGLLHYFF LASFSWLCLE GVHLYLLLLE VFDSDPGRRK
CWLRVDNYFI WSFIGPVTLV FLLVTLHKML RSSAALKPDS SRLDSIRSWA LGAIALLLLL
GLTWAFGLLF VTRESLLTAS LFTACNALQG TFIFLFHCAL QKKVGGRWGN WEGTEGHWGA
HWESLGEYWE GLEGSERYWD TLGTLGGTER RWETPEIRNE ETGRALGGDW EGTGRHWEAL
GGHWEALGGH WEAVAPPPPP RQWEALGGHW ERLGGHWEAL GGDWEGSGRH LEGTGRHWEG
TGRHWEETGR ALGGTFIFLL HCALQKKVWG HWERLGESGT DWDHHRA
//