ID A0A493TPY5_ANAPP Unreviewed; 1338 AA.
AC A0A493TPY5;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Adhesion G protein-coupled receptor F5 {ECO:0000313|Ensembl:ENSAPLP00000027645.1};
GN Name=ADGRF5 {ECO:0000313|Ensembl:ENSAPLP00000027645.1};
OS Anas platyrhynchos platyrhynchos (Northern mallard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000027645.1, ECO:0000313|Proteomes:UP000016666};
RN [1] {ECO:0000313|Ensembl:ENSAPLP00000027645.1, ECO:0000313|Proteomes:UP000016666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT "A new Pekin duck reference genome.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPLP00000027645.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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}.
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DR STRING; 8840.ENSAPLP00000027645; -.
DR Ensembl; ENSAPLT00000019507.1; ENSAPLP00000027645.1; ENSAPLG00000004634.2.
DR GeneTree; ENSGT00940000154603; -.
DR OMA; NIDRVTW; -.
DR Proteomes; UP000016666; Chromosome 3.
DR GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 GO; GO:0006112; P:energy reserve metabolic process; IEA:Ensembl.
DR GO; GO:0048821; P:erythrocyte development; IEA:Ensembl.
DR GO; GO:0045444; P:fat cell differentiation; IEA:Ensembl.
DR GO; GO:0003094; P:glomerular filtration; IEA:Ensembl.
DR GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
DR GO; GO:0042116; P:macrophage activation; IEA:Ensembl.
DR GO; GO:0043031; P:negative regulation of macrophage activation; IEA:Ensembl.
DR GO; GO:0061626; P:pharyngeal arch artery morphogenesis; IEA:Ensembl.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:Ensembl.
DR GO; GO:0071073; P:positive regulation of phospholipid biosynthetic process; IEA:Ensembl.
DR GO; GO:0043129; P:surfactant homeostasis; IEA:Ensembl.
DR Gene3D; 2.60.220.50; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR InterPro; IPR032471; GAIN_dom_N.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR017981; GPCR_2-like_7TM.
DR InterPro; IPR008078; GPCR_2_Ig-hepta-like_rcpt.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR000203; GPS.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013151; Immunoglobulin.
DR InterPro; IPR000082; SEA_dom.
DR InterPro; IPR036364; SEA_dom_sf.
DR PANTHER; PTHR45813; EF-HAND DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR45813:SF8; EF-HAND DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF16489; GAIN; 1.
DR Pfam; PF01825; GPS; 1.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF13927; Ig_3; 1.
DR PRINTS; PR01695; IGHEPTARCPTR.
DR SMART; SM00303; GPS; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SMART; SM00200; SEA; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 2.
DR SUPFAM; SSF82671; SEA domain; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR PROSITE; PS50221; GPS; 1.
DR PROSITE; PS50835; IG_LIKE; 2.
DR PROSITE; PS50024; SEA; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000016666};
KW Signal {ECO:0000256|SAM:SignalP};
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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1338
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019839452"
FT TRANSMEM 1007..1026
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1047..1068
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1088..1110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1122..1144
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1164..1192
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1213..1233
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1239..1262
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 170..294
FT /note="SEA"
FT /evidence="ECO:0000259|PROSITE:PS50024"
FT DOMAIN 267..363
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 479..572
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1005..1263
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 1317..1338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1338 AA; 149953 MW; 8BF7302B374152E3 CRC64;
MPSLLTAALH CLFLLVTAYC HTTQTSNFYP ITQYVGVEEE STHSEPQRQK PNVLLFYLLP
PEHTIEIEIT LRNPDLFSLV TQYYKCQNLQ NSTNISGVEM NISSINVTAV CPPSDENVSC
CYCEAGAYNE SKACSQLSLP SNQSCGYIKD MPFYRFHCDP EPCIGDPHCT GEPVDIHMSV
TLDQAFSDDL RNSSSVLYKK YKDDFENAFL QSYTCLSGFL SVTIIGFRPG GISVDYNVKG
RAVTFSEIHY SNSRVPKFLN QSYHLIPSSF TTEITNERNI TVSPEEIFEG DTVTLMCEIN
AKSGDAIWYH SNQTISNSSQ HLLKTEPTTG VLKSNLTITN VTTKDSGSYT CVFSKISDYY
RLTYKNIQDI TVSSLSITSY SNDMKISCNS PDFQATSNLL FCCLNIYSTS IKSVWKLNGI
NPTTGASNDT KNCTEYEFNI TESLCLPESA TVMTYTCEFQ TGHGARASQN ITVTYSRTDY
VRISPSVNIS VSEGKEFNLT CKGDVKNYDS IIWEIQSGDK IQTVECASCI TTNKSIATSV
LSVNVSTQDW NGTYICTFSN KSSNTSANVT VNVIPLPLTT NIWLDPIKTS IQCKKSQHFN
CCISANTMED YTVTFVVQGK EFQPERKNYG NFLCYSYNYN ETECGKQQNF EVYYRFVNGM
KQEVKSQNIQ LKLTPESSIS CTENFYGAEE DRLIKPCRLL SNTFIRGNEI YKCYNKLWIL
ERNNCVSEQI NSLLIRAESL VNSPVAKTEL PIFLWQLQNV TELQQNVNSP ADLAAIVNIL
YNISAIPADA SKPIIEAFFS TVDNTVNDSK MEFWTELNNE NASSSSLLLY SVERFSENLQ
PVNNTFPNVS TKTLELQGMV VTENRSTDYN KDFNKVGNLS ANVLIEKSVT LPPNSTIVSV
ACSAIGQILP RNDNEYVNSL VVITTLSSER PQNFYINMTF QKANMSLKSP QCVFWNFSFN
GNRGKWDNYS CISTDKEGNV TCSCNHLTPF SILMSLENPS SNAASAYITY SGLAISIVSL
VVCIIIESLV WKNVTNNTTS YMRHICILNI STSLLVADIW FIVTAVISEQ KLQKNREICI
VATFFIHLFY LCGLFWMLSL GLILFYRLVF IFHNTSKTIQ KVLAFCLGYG CPFVFAVITI
AVTLPQKNYI NKDVCWLNWK DSKALLAFII PALAIVVMNL FITGVVIIKI LRPNIGDKTN
KQERKTLFQI GKSLAILTPL LGLTWGFGVA TIMDNKNEAF HILFALLNTL QGLFILVFGT
LWDKKITEAL LKRNSLSRWS SQQTKSTSLI LVSPMFSMGY PLSRTFNNLC GKTGKYTVSS
SEPSSSSENT SKSYSLLN
//
