GP158_HUMAN
ID GP158_HUMAN Reviewed; 1215 AA.
AC Q5T848; Q6QR81; Q9ULT3;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Probable G-protein coupled receptor 158;
DE Flags: Precursor;
GN Name=GPR158; Synonyms=KIAA1136;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLY-425.
RC TISSUE=Brain;
RA Bonner T.I., Nagle J.W., Kauffman D.;
RT "Complete coding sequence of GPR158.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 620-1215.
RC TISSUE=Brain;
RX PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT "Characterization of cDNA clones selected by the GeneMark analysis from
RT size-fractionated cDNA libraries from human brain.";
RL DNA Res. 6:329-336(1999).
RN [4]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [5]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-774, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=18655026; DOI=10.1002/pmic.200700887;
RA Tan F., Lu L., Cai Y., Wang J., Xie Y., Wang L., Gong Y., Xu B.-E., Wu J.,
RA Luo Y., Qiang B., Yuan J., Sun X., Peng X.;
RT "Proteomic analysis of ubiquitinated proteins in normal hepatocyte cell
RT line Chang liver cells.";
RL Proteomics 8:2885-2896(2008).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAS18315.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY528411; AAS18315.1; ALT_INIT; mRNA.
DR EMBL; AL161654; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL355587; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL139821; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB032962; BAA86450.2; -; mRNA.
DR CCDS; CCDS31166.1; -.
DR RefSeq; NP_065803.2; NM_020752.2.
DR PDB; 7EWL; EM; 3.52 A; A/B=24-710.
DR PDB; 7EWP; EM; 4.30 A; A/B=1-863.
DR PDB; 7EWR; EM; 4.70 A; A/B=1-863.
DR PDB; 7SHE; EM; 3.40 A; A/B=1-775.
DR PDB; 7SHF; EM; 3.40 A; A/B=1-775.
DR PDBsum; 7EWL; -.
DR PDBsum; 7EWP; -.
DR PDBsum; 7EWR; -.
DR PDBsum; 7SHE; -.
DR PDBsum; 7SHF; -.
DR AlphaFoldDB; Q5T848; -.
DR SMR; Q5T848; -.
DR BioGRID; 121576; 4.
DR IntAct; Q5T848; 2.
DR STRING; 9606.ENSP00000365529; -.
DR ChEMBL; CHEMBL4523874; -.
DR GlyGen; Q5T848; 5 sites.
DR iPTMnet; Q5T848; -.
DR PhosphoSitePlus; Q5T848; -.
DR BioMuta; GPR158; -.
DR DMDM; 67461010; -.
DR MassIVE; Q5T848; -.
DR PaxDb; Q5T848; -.
DR PeptideAtlas; Q5T848; -.
DR PRIDE; Q5T848; -.
DR ProteomicsDB; 64705; -.
DR ABCD; Q5T848; 2 sequenced antibodies.
DR Antibodypedia; 2922; 101 antibodies from 19 providers.
DR DNASU; 57512; -.
DR Ensembl; ENST00000376351.4; ENSP00000365529.3; ENSG00000151025.11.
DR GeneID; 57512; -.
DR KEGG; hsa:57512; -.
DR MANE-Select; ENST00000376351.4; ENSP00000365529.3; NM_020752.3; NP_065803.2.
DR UCSC; uc001isj.4; human.
DR CTD; 57512; -.
DR DisGeNET; 57512; -.
DR GeneCards; GPR158; -.
DR HGNC; HGNC:23689; GPR158.
DR HPA; ENSG00000151025; Tissue enriched (brain).
DR MIM; 614573; gene.
DR neXtProt; NX_Q5T848; -.
DR OpenTargets; ENSG00000151025; -.
DR PharmGKB; PA134939018; -.
DR VEuPathDB; HostDB:ENSG00000151025; -.
DR eggNOG; KOG4418; Eukaryota.
DR GeneTree; ENSGT00940000155918; -.
DR HOGENOM; CLU_006832_1_0_1; -.
DR InParanoid; Q5T848; -.
DR OMA; THVCLPC; -.
DR OrthoDB; 63351at2759; -.
DR PhylomeDB; Q5T848; -.
DR TreeFam; TF319114; -.
DR PathwayCommons; Q5T848; -.
DR SignaLink; Q5T848; -.
DR BioGRID-ORCS; 57512; 8 hits in 1071 CRISPR screens.
DR ChiTaRS; GPR158; human.
DR GeneWiki; GPR158; -.
DR GenomeRNAi; 57512; -.
DR Pharos; Q5T848; Tbio.
DR PRO; PR:Q5T848; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q5T848; protein.
DR Bgee; ENSG00000151025; Expressed in endothelial cell and 97 other tissues.
DR ExpressionAtlas; Q5T848; baseline and differential.
DR Genevisible; Q5T848; HS.
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 GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; G-protein coupled receptor; Glycoprotein;
KW Isopeptide bond; Membrane; Phosphoprotein; Receptor; Reference proteome;
KW Signal; Transducer; Transmembrane; Transmembrane helix; Ubl conjugation.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..1215
FT /note="Probable G-protein coupled receptor 158"
FT /id="PRO_0000012969"
FT TOPO_DOM 24..417
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 439..451
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 452..472
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 473..483
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 484..506
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 507..528
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 529..549
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 550..579
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 580..600
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 601..613
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 614..634
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 635..643
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 644..664
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 665..1215
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 23..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 757..999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1117..1164
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 50..66
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..830
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..855
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..907
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..950
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 951..967
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 975..998
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1164
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 865
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C419"
FT MOD_RES 946
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C419"
FT MOD_RES 1080
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:0000269|PubMed:18655026"
FT VARIANT 425
FT /note="A -> G (in dbSNP:rs2480345)"
FT /evidence="ECO:0000269|Ref.1"
FT /id="VAR_049285"
FT VARIANT 1209
FT /note="I -> V (in dbSNP:rs10828833)"
FT /id="VAR_049286"
FT CONFLICT 620..630
FT /note="ELIISAIFHTI -> SWIVNSMNSHF (in Ref. 3)"
FT /evidence="ECO:0000305"
FT HELIX 67..75
FT /evidence="ECO:0007829|PDB:7SHE"
FT HELIX 82..86
FT /evidence="ECO:0007829|PDB:7SHE"
FT HELIX 88..92
FT /evidence="ECO:0007829|PDB:7SHE"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:7SHE"
FT HELIX 121..136
FT /evidence="ECO:0007829|PDB:7SHE"
FT TURN 143..146
FT /evidence="ECO:0007829|PDB:7SHE"
FT HELIX 151..166
FT /evidence="ECO:0007829|PDB:7SHE"
FT STRAND 169..176
FT /evidence="ECO:0007829|PDB:7SHE"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:7SHE"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:7SHE"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:7SHE"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:7SHE"
FT TURN 277..279
FT /evidence="ECO:0007829|PDB:7SHE"
FT STRAND 281..288
FT /evidence="ECO:0007829|PDB:7SHE"
FT STRAND 303..309
FT /evidence="ECO:0007829|PDB:7SHE"
FT STRAND 318..323
FT /evidence="ECO:0007829|PDB:7SHE"
FT TURN 324..327
FT /evidence="ECO:0007829|PDB:7SHE"
FT HELIX 334..336
FT /evidence="ECO:0007829|PDB:7SHE"
FT STRAND 337..343
FT /evidence="ECO:0007829|PDB:7SHE"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:7SHE"
FT STRAND 397..400
FT /evidence="ECO:0007829|PDB:7SHE"
FT HELIX 406..408
FT /evidence="ECO:0007829|PDB:7SHE"
FT HELIX 414..440
FT /evidence="ECO:0007829|PDB:7SHE"
FT TURN 441..443
FT /evidence="ECO:0007829|PDB:7SHE"
FT HELIX 445..448
FT /evidence="ECO:0007829|PDB:7SHE"
FT HELIX 452..464
FT /evidence="ECO:0007829|PDB:7SHE"
FT HELIX 470..473
FT /evidence="ECO:0007829|PDB:7SHE"
FT HELIX 480..495
FT /evidence="ECO:0007829|PDB:7SHE"
FT TURN 496..498
FT /evidence="ECO:0007829|PDB:7SHE"
FT HELIX 499..513
FT /evidence="ECO:0007829|PDB:7SHE"
FT TURN 523..525
FT /evidence="ECO:0007829|PDB:7SHE"
FT TURN 527..529
FT /evidence="ECO:0007829|PDB:7SHE"
FT HELIX 530..548
FT /evidence="ECO:0007829|PDB:7SHE"
FT STRAND 549..551
FT /evidence="ECO:0007829|PDB:7SHE"
FT TURN 552..554
FT /evidence="ECO:0007829|PDB:7SHE"
FT STRAND 558..563
FT /evidence="ECO:0007829|PDB:7SHE"
FT STRAND 565..567
FT /evidence="ECO:0007829|PDB:7SHE"
FT STRAND 569..573
FT /evidence="ECO:0007829|PDB:7SHE"
FT HELIX 581..583
FT /evidence="ECO:0007829|PDB:7SHE"
FT HELIX 584..599
FT /evidence="ECO:0007829|PDB:7SHE"
FT STRAND 601..603
FT /evidence="ECO:0007829|PDB:7SHE"
FT HELIX 609..633
FT /evidence="ECO:0007829|PDB:7SHE"
FT STRAND 635..637
FT /evidence="ECO:0007829|PDB:7SHE"
FT HELIX 641..650
FT /evidence="ECO:0007829|PDB:7SHE"
FT TURN 651..654
FT /evidence="ECO:0007829|PDB:7SHE"
FT HELIX 655..661
FT /evidence="ECO:0007829|PDB:7SHE"
FT HELIX 664..667
FT /evidence="ECO:0007829|PDB:7SHE"
FT HELIX 713..729
FT /evidence="ECO:0007829|PDB:7SHF"
SQ SEQUENCE 1215 AA; 135489 MW; E0B565E573B3ADE1 CRC64;
MGAMAYPLLL CLLLAQLGLG AVGASRDPQG RPDSPRERTP KGKPHAQQPG RASASDSSAP
WSRSTDGTIL AQKLAEEVPM DVASYLYTGD SHQLKRANCS GRYELAGLPG KWPALASAHP
SLHRALDTLT HATNFLNVML QSNKSREQNL QDDLDWYQAL VWSLLEGEPS ISRAAITFST
DSLSAPAPQV FLQATREESR ILLQDLSSSA PHLANATLET EWFHGLRRKW RPHLHRRGPN
QGPRGLGHSW RRKDGLGGDK SHFKWSPPYL ECENGSYKPG WLVTLSSAIY GLQPNLVPEF
RGVMKVDINL QKVDIDQCSS DGWFSGTHKC HLNNSECMPI KGLGFVLGAY ECICKAGFYH
PGVLPVNNFR RRGPDQHISG STKDVSEEAY VCLPCREGCP FCADDSPCFV QEDKYLRLAI
ISFQALCMLL DFVSMLVVYH FRKAKSIRAS GLILLETILF GSLLLYFPVV ILYFEPSTFR
CILLRWARLL GFATVYGTVT LKLHRVLKVF LSRTAQRIPY MTGGRVMRML AVILLVVFWF
LIGWTSSVCQ NLEKQISLIG QGKTSDHLIF NMCLIDRWDY MTAVAEFLFL LWGVYLCYAV
RTVPSAFHEP RYMAVAVHNE LIISAIFHTI RFVLASRLQS DWMLMLYFAH THLTVTVTIG
LLLIPKFSHS SNNPRDDIAT EAYEDELDMG RSGSYLNSSI NSAWSEHSLD PEDIRDELKK
LYAQLEIYKR KKMITNNPHL QKKRCSKKGL GRSIMRRITE IPETVSRQCS KEDKEGADHG
TAKGTALIRK NPPESSGNTG KSKEETLKNR VFSLKKSHST YDHVRDQTEE SSSLPTESQE
EETTENSTLE SLSGKKLTQK LKEDSEAEST ESVPLVCKSA SAHNLSSEKK TGHPRTSMLQ
KSLSVIASAK EKTLGLAGKT QTAGVEERTK SQKPLPKDKE TNRNHSNSDN TETKDPAPQN
SNPAEEPRKP QKSGIMKQQR VNPTTANSDL NPGTTQMKDN FDIGEVCPWE VYDLTPGPVP
SESKVQKHVS IVASEMEKNP TFSLKEKSHH KPKAAEVCQQ SNQKRIDKAE VCLWESQGQS
ILEDEKLLIS KTPVLPERAK EENGGQPRAA NVCAGQSEEL PPKAVASKTE NENLNQIGHQ
EKKTSSSEEN VRGSYNSSNN FQQPLTSRAE VCPWEFETPA QPNAGRSVAL PASSALSANK
IAGPRKEEIW DSFKV
