GP108_MOUSE
ID GP108_MOUSE Reviewed; 569 AA.
AC Q91WD0; Q8BXE9; Q925B1;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Protein GPR108;
DE AltName: Full=Lung seven transmembrane receptor 2 {ECO:0000303|PubMed:17454009};
DE Flags: Precursor;
GN Name=Gpr108; Synonyms=Lustr2 {ECO:0000303|PubMed:17454009};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=17454009; DOI=10.1080/10425170701207182;
RA Edgar A.J.;
RT "Human GPR107 and murine Gpr108 are members of the LUSTR family of proteins
RT found in both plants and animals, having similar topology to G-protein
RT coupled receptors.";
RL DNA Seq. 18:235-241(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=30332431; DOI=10.1371/journal.pone.0205303;
RA Dong D., Zhou H., Na S.Y., Niedra R., Peng Y., Wang H., Seed B., Zhou G.L.;
RT "GPR108, an NF-kappaB activator suppressed by TIRAP, negatively regulates
RT TLR-triggered immune responses.";
RL PLoS ONE 13:e0205303-e0205303(2018).
RN [6]
RP FUNCTION (MICROBIAL INFECTION), SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
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).
CC -!- FUNCTION: May play a role in intracellular immune modulation by
CC activating NF-kappaB response and attenuating Toll-like-receptor
CC response. {ECO:0000269|PubMed:30332431}.
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}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane
CC {ECO:0000269|PubMed:30332431}; Multi-pass membrane protein. Golgi
CC apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:31784416};
CC Multi-pass membrane protein {ECO:0000305}. Golgi apparatus membrane;
CC Multi-pass membrane protein {ECO:0000255}. Note=Colocalizes with TLR3,
CC -7, -4, and -9. {ECO:0000269|PubMed:30332431}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q91WD0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q91WD0-2; Sequence=VSP_016607;
CC -!- TISSUE SPECIFICITY: High expression in spleen, lung, stomach, large and
CC small intestine, and thymus. {ECO:0000269|PubMed:30332431}.
CC -!- DOMAIN: (Microbial infection) N- and C-terminal domains are essential
CC for mediating AAV transduction. {ECO:0000250|UniProtKB:Q9NPR9}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice are viable and fertile and exhibit
CC normal Mendelian segregation, however deficient mice exhibit increased
CC LPS-induced mortality. TLR-mediated pro-inflammatory signaling are
CC increased in embryonic fibroblasts and macrophages from Gpr108
CC deficient mice (PubMed:30332431). Depending on the AAV serotype used,
CC 10-fold to 100-fold reduced expression for AAV is observed in Gpr108
CC knockout mice following retro-orbital administration (PubMed:31784416).
CC {ECO:0000269|PubMed:30332431, ECO:0000269|PubMed:31784416}.
CC -!- SIMILARITY: Belongs to the LU7TM family. {ECO:0000305}.
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DR EMBL; AF376726; AAK57696.1; -; mRNA.
DR EMBL; AK159313; BAE34981.1; -; mRNA.
DR EMBL; AK047364; BAC33036.1; -; mRNA.
DR EMBL; BC016104; AAH16104.1; -; mRNA.
DR CCDS; CCDS28929.1; -. [Q91WD0-1]
DR CCDS; CCDS89128.1; -. [Q91WD0-2]
DR RefSeq; NP_001295001.1; NM_001308072.1. [Q91WD0-2]
DR RefSeq; NP_001295003.1; NM_001308074.1.
DR RefSeq; NP_084360.2; NM_030084.4. [Q91WD0-1]
DR AlphaFoldDB; Q91WD0; -.
DR BioGRID; 219318; 1.
DR STRING; 10090.ENSMUSP00000005975; -.
DR GlyGen; Q91WD0; 5 sites.
DR iPTMnet; Q91WD0; -.
DR PhosphoSitePlus; Q91WD0; -.
DR SwissPalm; Q91WD0; -.
DR EPD; Q91WD0; -.
DR MaxQB; Q91WD0; -.
DR PaxDb; Q91WD0; -.
DR PeptideAtlas; Q91WD0; -.
DR PRIDE; Q91WD0; -.
DR ProteomicsDB; 271256; -. [Q91WD0-1]
DR ProteomicsDB; 271257; -. [Q91WD0-2]
DR Antibodypedia; 24252; 209 antibodies from 28 providers.
DR DNASU; 78308; -.
DR Ensembl; ENSMUST00000005975; ENSMUSP00000005975; ENSMUSG00000005823. [Q91WD0-2]
DR Ensembl; ENSMUST00000233568; ENSMUSP00000156910; ENSMUSG00000005823. [Q91WD0-1]
DR GeneID; 78308; -.
DR KEGG; mmu:78308; -.
DR UCSC; uc008deh.1; mouse. [Q91WD0-1]
DR UCSC; uc008dei.1; mouse. [Q91WD0-2]
DR CTD; 56927; -.
DR MGI; MGI:1925558; Gpr108.
DR VEuPathDB; HostDB:ENSMUSG00000005823; -.
DR eggNOG; KOG2569; Eukaryota.
DR GeneTree; ENSGT00940000160446; -.
DR HOGENOM; CLU_020277_4_1_1; -.
DR InParanoid; Q91WD0; -.
DR OMA; CKARIHK; -.
DR PhylomeDB; Q91WD0; -.
DR TreeFam; TF314804; -.
DR BioGRID-ORCS; 78308; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Gpr108; mouse.
DR PRO; PR:Q91WD0; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q91WD0; protein.
DR Bgee; ENSMUSG00000005823; Expressed in granulocyte and 207 other tissues.
DR Genevisible; Q91WD0; MM.
DR GO; GO:0033106; C:cis-Golgi network membrane; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0034122; P:negative regulation of toll-like receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0050776; P:regulation of immune response; IMP: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 Alternative splicing; Glycoprotein; Golgi apparatus;
KW Host-virus interaction; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..569
FT /note="Protein GPR108"
FT /id="PRO_0000045084"
FT TRANSMEM 289..309
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 318..338
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..382
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..413
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 427..447
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 475..495
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TRANSMEM 499..519
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT REGION 144..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 168..174
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:17454009"
FT /id="VSP_016607"
FT CONFLICT 9
FT /note="L -> V (in Ref. 2; BAC33036)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="S -> P (in Ref. 2; BAC33036)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="Q -> H (in Ref. 1; AAK57696)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 569 AA; 63981 MW; 8247D05D3BB18D94 CRC64;
MAVSERRGLS GESPTQCRWG YLSLLVLTLS GCSGRIHRLT LTGEKRADIQ LNSFGFYTNG
SLEVELSLLR LSLQETEKKL PKVGFSLSRV RSGSVRSYSR RNSHECPLDR NSSNFLVLFL
INIKDLQVQV RKYGEQKLFI SPGLLPEAPT QSGPPKPDPA GTPKDNHVIH PSPTEMSAVK
ENQTAPQVSG DKTTPGEHRH SSERQPPTQD PSGKEKDQVL GLGHLNDSYN FSFHIVISSR
AEEGQYSLNF HNCHNSIPGQ EQPFDLTVMI REKNPEGFLS AAEIPLFKLY LIMSACFLAA
DIFWVSVLCK NTYSVFKIHW LMAALAFTKS VSLLFHSINY YFINSQGHPI EGLAVMHYIT
HLLKGALLFI TIALIGSGWA FVKYMLSDKE KKIFGIVIPL QVLANVAYIV IESREEGASD
YGLWKEILFL VDLICCGAIL FPVVWSIRHL QDASGTDGKV AVNLARLKLF RHYYVMVICY
IYFTRIIAIL LQVAVPFQWQ WLYQLLVESS TLAFFVLTGY KFQPAGDNPY LQLPQEDEED
VQMEQVMTDS GFREGLSKVN KTASGRELL
