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   27-MAR-2024, entry version 139.
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   TCDB; 9.A.14.22.6; the g-protein-coupled receptor (gpcr) family.
DR   GlyCosmos; Q9NPR9; 7 sites, 2 glycans.
DR   GlyGen; Q9NPR9; 11 sites, 4 O-linked glycans (5 sites).
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; 9606-ENSP00000264080; -.
DR   PeptideAtlas; Q9NPR9; -.
DR   ProteomicsDB; 82047; -.
DR   Antibodypedia; 24252; 225 antibodies from 29 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   AGR; HGNC:17829; -.
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; RRGLGCW; -.
DR   OrthoDB; 25639at2759; -.
DR   PhylomeDB; Q9NPR9; -.
DR   TreeFam; TF314804; -.
DR   PathwayCommons; Q9NPR9; -.
DR   SignaLink; Q9NPR9; -.
DR   BioGRID-ORCS; 56927; 11 hits in 1155 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 175 other cell types or tissues.
DR   ExpressionAtlas; Q9NPR9; baseline and differential.
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: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; LUNG SEVEN TRANSMEMBRANE RECEPTOR; 1.
DR   PANTHER; PTHR21229:SF11; PROTEIN GPR108; 1.
DR   Pfam; PF06814; Lung_7-TM_R; 1.
DR   Genevisible; Q9NPR9; HS.
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
//