GP158_BOVIN
ID GP158_BOVIN Reviewed; 1216 AA.
AC E1BBQ2;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 2.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Probable G-protein coupled receptor 158;
DE Flags: Precursor;
GN Name=GPR158;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
CC -!- FUNCTION: Orphan receptor.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
CC {ECO:0000305}.
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DR EMBL; DAAA02035487; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02035488; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; E1BBQ2; -.
DR SMR; E1BBQ2; -.
DR STRING; 9913.ENSBTAP00000032818; -.
DR PaxDb; E1BBQ2; -.
DR PRIDE; E1BBQ2; -.
DR eggNOG; KOG4418; Eukaryota.
DR HOGENOM; CLU_006832_1_0_1; -.
DR InParanoid; E1BBQ2; -.
DR TreeFam; TF319114; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR InterPro; IPR017978; GPCR_3_C.
DR InterPro; IPR043458; GPR158/179.
DR PANTHER; PTHR32546; PTHR32546; 1.
DR Pfam; PF00003; 7tm_3; 1.
DR PROSITE; PS50259; G_PROTEIN_RECEP_F3_4; 1.
PE 3: Inferred from homology;
KW Cell membrane; G-protein coupled receptor; Glycoprotein; Isopeptide bond;
KW Membrane; Phosphoprotein; Receptor; Reference proteome; Signal; Transducer;
KW Transmembrane; Transmembrane helix; Ubl conjugation.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..1216
FT /note="Probable G-protein coupled receptor 158"
FT /id="PRO_0000418361"
FT TOPO_DOM 24..417
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 439..451
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 452..472
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 473..480
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 481..501
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 502..528
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 529..549
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 550..579
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 580..600
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 601..613
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 614..634
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 635..643
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 644..664
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 665..1216
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 25..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 757..875
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 911..1000
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1038..1072
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1128..1167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..780
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..823
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 931..947
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 948..965
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 978..995
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1151..1166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 694
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C419"
FT MOD_RES 705
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C419"
FT MOD_RES 708
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C419"
FT MOD_RES 866
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C419"
FT MOD_RES 947
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C419"
FT MOD_RES 1066
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C419"
FT MOD_RES 1081
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D4A6L0"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CROSSLNK 774
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q5T848"
SQ SEQUENCE 1216 AA; 135363 MW; 5B83D2CCA66D6ED1 CRC64;
MGVMAYPFLF CLLLVHFGLG AIGASREAPS RPDPPRERTL RAKQHAQQPA RASASDPSAP
WSRSTDGTIL AQKLAEEVPM DVASYLYTGD SHKLKRANCS SRYELAGLPG KSPALASSHP
SLHGALDTLT HATNFLNMML QSNKSREQNL QDDLEWYQAL VRSLLEGEPS ISRAAITFST
ESLSAPAPQV FLQATREESR ILLQDLSSSA HHLANATLET EWFHGLRRKW RTHLHRRGSN
QGPRGLGHSW RRRDGLSGDK SHVKWSPPYL ECENGSYKPG WLVTLSAAFY GLQPNLVPEF
RGVMKVDINL QKVDIDQCSS DGWFSGTHKC HLNNSECMPI KGLGFVLGAY QCICKAGFYH
PRDFSFNNFQ RRGPDHHFVE SAKDVSEEVH VCLPCSEGCP YCADDSPCFV QEDKYLRLAI
ISFQALCMLL DFLSMLVVYR FRKAKSIRAS GLILLETILF GSLLLYFPVV ILYFEPSTFR
CILLRWVRLL GFATVYGTVT LKLHRVLKVF LSRTAQRIPY MTGGRVMRML AVILLVVFWF
LVGWTSSVCQ NLERHISLIG QGRTSDHLIF SMCLVERWDY MTAAAEFLFL LWGVYLCYAV
RTVPSAFHEP RYMAVAVHNE LIISAIFHTI RFVLASRLQS DWMLMLYFAH THLTVTVTIG
LLLIPKFSHS SNNPRDDIAT EAYEDELDMG RSGSYLNSSI NSAWSEHSLD PEDIRDELKK
LYAQLEIYKR KKMITNNPHL QKKRCSKKGL GRSIMRRITE IPETVSRQCS KEDKDGGEHG
SAKGSSAGRK NPQETAGGSG KPKEESLRSR VFSLKKSHST YEHVREQPGG PGSPPAQSRE
EEEATDNSVL GSPVGANRPR PLQEDSQAVS TESVPLVCKS ASAHNLSSEK KPGPTRTSVL
QKSLSVIASA KEKTLGLAGK TQAACVEERA KAQKALPRER ETNRKYSNSD NAETQDSAPP
NSSHSEEPRK PQKLGIMKQQ RANPTTANSD LSPGATHMKD NFDIGEVCPW EIYDLAPGPG
PLESKVQKHV SIAASEMERN PTFSLKEKSH PKPKAADLCQ QSNPKSVDKA EVCPWESQGQ
SLFEEEKYLM SKTQVPLGRA QGENSGQHCA TGVCAGQCEE LPPKAVASKV ENENLNQLGE
QEKKTSSSER NVPDSHNSSN NFQPPLMSRA EVCPWEFETP DKPNAERSVA FPASSALSAN
KIAGPRNEEV RLARKV
