GP108_HUMAN
ID GP108_HUMAN Reviewed; 543 AA.
AC Q9NPR9; B9EJD7;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Protein GPR108;
DE AltName: Full=Lung seven transmembrane receptor 2;
DE Flags: Precursor;
GN Name=GPR108 {ECO:0000312|HGNC:HGNC:17829}; Synonyms=LUSTR2;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-36.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-543, AND VARIANT ARG-36.
RG The European IMAGE consortium;
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION (MICROBIAL INFECTION), SUBCELLULAR LOCATION, AND DOMAIN (MICROBIAL
RP INFECTION).
RX PubMed=31784416; DOI=10.1016/j.ymthe.2019.11.005;
RA Dudek A.M., Zabaleta N., Zinn E., Pillay S., Zengel J., Porter C.,
RA Franceschini J.S., Estelien R., Carette J.E., Zhou G.L., Vandenberghe L.H.;
RT "GPR108 Is a Highly Conserved AAV Entry Factor.";
RL Mol. Ther. 28:367-381(2020).
RN [6]
RP FUNCTION (MICROBIAL INFECTION), AND SUBCELLULAR LOCATION.
RX PubMed=32280726; DOI=10.1016/j.omtm.2020.03.012;
RA Meisen W.H., Nejad Z.B., Hardy M., Zhao H., Oliverio O., Wang S., Hale C.,
RA Ollmann M.M., Collins P.J.;
RT "Pooled Screens Identify GPR108 and TM9SF2 as Host Cell Factors Critical
RT for AAV Transduction.";
RL Mol. Ther. Methods Clin. Dev. 17:601-611(2020).
CC -!- FUNCTION: May play a role in intracellular immune modulation by
CC activating NF-kappaB response and attenuating Toll-like-receptor
CC response. {ECO:0000250|UniProtKB:Q91WD0}.
CC -!- FUNCTION: (Microbial infection) Plays an essential function in adeno-
CC associated virus (AAV) transduction across multiple serotypes except
CC AAV5. May play a critical role in mediating the endosomal virus escape
CC or in the AAV virions trafficking from endosomes to the nucleus.
CC {ECO:0000269|PubMed:31784416, ECO:0000269|PubMed:32280726}.
CC -!- INTERACTION:
CC Q9NPR9; P19397: CD53; NbExp=3; IntAct=EBI-11343451, EBI-6657396;
CC Q9NPR9; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-11343451, EBI-18304435;
CC Q9NPR9; P48165: GJA8; NbExp=3; IntAct=EBI-11343451, EBI-17458373;
CC Q9NPR9; P43628: KIR2DL3; NbExp=3; IntAct=EBI-11343451, EBI-8632435;
CC Q9NPR9; Q96E29: MTERF3; NbExp=3; IntAct=EBI-11343451, EBI-7825321;
CC Q9NPR9; P15941-11: MUC1; NbExp=3; IntAct=EBI-11343451, EBI-17263240;
CC Q9NPR9; O14524-2: NEMP1; NbExp=3; IntAct=EBI-11343451, EBI-10969203;
CC Q9NPR9; Q9BU79: TMEM243; NbExp=3; IntAct=EBI-11343451, EBI-12887458;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane
CC {ECO:0000250|UniProtKB:Q91WD0}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q91WD0}. Golgi apparatus, trans-Golgi network
CC membrane {ECO:0000269|PubMed:31784416}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q91WD0}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:32280726}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Colocalizes with TLR3, -7, -4, and -9.
CC {ECO:0000250|UniProtKB:Q91WD0}.
CC -!- DOMAIN: (Microbial infection) N- and C-terminal domains are required
CC for AAV transduction. {ECO:0000269|PubMed:31784416}.
CC -!- SIMILARITY: Belongs to the LU7TM family. {ECO:0000305}.
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DR EMBL; CH471139; EAW69067.1; -; Genomic_DNA.
DR EMBL; AC008760; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC146909; AAI46910.1; -; mRNA.
DR EMBL; AL365404; CAB96950.1; -; mRNA.
DR CCDS; CCDS42479.1; -.
DR RefSeq; NP_001073921.1; NM_001080452.1.
DR AlphaFoldDB; Q9NPR9; -.
DR BioGRID; 121254; 30.
DR IntAct; Q9NPR9; 12.
DR STRING; 9606.ENSP00000264080; -.
DR GlyGen; Q9NPR9; 7 sites, 2 O-linked glycans (1 site).
DR iPTMnet; Q9NPR9; -.
DR PhosphoSitePlus; Q9NPR9; -.
DR SwissPalm; Q9NPR9; -.
DR BioMuta; GPR108; -.
DR DMDM; 296439338; -.
DR EPD; Q9NPR9; -.
DR jPOST; Q9NPR9; -.
DR MassIVE; Q9NPR9; -.
DR MaxQB; Q9NPR9; -.
DR PaxDb; Q9NPR9; -.
DR PeptideAtlas; Q9NPR9; -.
DR PRIDE; Q9NPR9; -.
DR ProteomicsDB; 82047; -.
DR Antibodypedia; 24252; 209 antibodies from 28 providers.
DR DNASU; 56927; -.
DR Ensembl; ENST00000264080.12; ENSP00000264080.5; ENSG00000125734.16.
DR GeneID; 56927; -.
DR KEGG; hsa:56927; -.
DR MANE-Select; ENST00000264080.12; ENSP00000264080.5; NM_001080452.2; NP_001073921.1.
DR UCSC; uc002mfp.4; human.
DR CTD; 56927; -.
DR GeneCards; GPR108; -.
DR HGNC; HGNC:17829; GPR108.
DR HPA; ENSG00000125734; Low tissue specificity.
DR MIM; 618491; gene.
DR neXtProt; NX_Q9NPR9; -.
DR PharmGKB; PA28855; -.
DR VEuPathDB; HostDB:ENSG00000125734; -.
DR eggNOG; KOG2569; Eukaryota.
DR GeneTree; ENSGT00940000160446; -.
DR HOGENOM; CLU_020277_4_1_1; -.
DR InParanoid; Q9NPR9; -.
DR OMA; CKARIHK; -.
DR OrthoDB; 1427067at2759; -.
DR PhylomeDB; Q9NPR9; -.
DR TreeFam; TF314804; -.
DR PathwayCommons; Q9NPR9; -.
DR SignaLink; Q9NPR9; -.
DR BioGRID-ORCS; 56927; 8 hits in 1077 CRISPR screens.
DR ChiTaRS; GPR108; human.
DR GenomeRNAi; 56927; -.
DR Pharos; Q9NPR9; Tbio.
DR PRO; PR:Q9NPR9; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9NPR9; protein.
DR Bgee; ENSG00000125734; Expressed in lower esophagus mucosa and 173 other tissues.
DR ExpressionAtlas; Q9NPR9; baseline and differential.
DR Genevisible; Q9NPR9; HS.
DR GO; GO:0033106; C:cis-Golgi network membrane; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0034122; P:negative regulation of toll-like receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0050776; P:regulation of immune response; ISS:UniProtKB.
DR InterPro; IPR009637; GPR107/GPR108-like.
DR PANTHER; PTHR21229; PTHR21229; 1.
DR Pfam; PF06814; Lung_7-TM_R; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Golgi apparatus; Host-virus interaction; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..543
FT /note="Protein GPR108"
FT /id="PRO_0000045083"
FT TRANSMEM 263..283
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..356
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..387
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 401..421
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 449..469
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TRANSMEM 473..493
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT REGION 149..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 534
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 36
FT /note="Q -> R (in dbSNP:rs340138)"
FT /evidence="ECO:0000269|Ref.2, ECO:0000269|Ref.4"
FT /id="VAR_060483"
FT VARIANT 79
FT /note="L -> P (in dbSNP:rs4807897)"
FT /id="VAR_056112"
SQ SEQUENCE 543 AA; 60633 MW; 72B853EA61DEF58A CRC64;
MAVSERRGLG RGSPAEWGQR LLLVLLLGGC SGRIHQLALT GEKRADIQLN SFGFYTNGSL
EVELSVLRLG LREAEEKSLL VGFSLSRVRS GRVRSYSTRD FQDCPLQKNS SSFLVLFLIN
TKDLQVQVRK YGEQKTLFIF PGLLPEAPSK PGLPKPQATV PRKVDGGGTS AASKPKSTPA
VIQGPSGKDK DLVLGLSHLN NSYNFSFHVV IGSQAEEGQY SLNFHNCNNS VPGKEHPFDI
TVMIREKNPD GFLSAAEMPL FKLYMVMSAC FLAAGIFWVS ILCRNTYSVF KIHWLMAALA
FTKSISLLFH SINYYFINSQ GHPIEGLAVM YYIAHLLKGA LLFITIALIG SGWAFIKYVL
SDKEKKVFGI VIPMQVLANV AYIIIESREE GASDYVLWKE ILFLVDLICC GAILFPVVWS
IRHLQDASGT DGKVAVNLAK LKLFRHYYVM VICYVYFTRI IAILLQVAVP FQWQWLYQLL
VEGSTLAFFV LTGYKFQPTG NNPYLQLPQE DEEDVQMEQV MTDSGFREGL SKVNKTASGR
ELL
