GP108_RAT
ID GP108_RAT Reviewed; 577 AA.
AC Q6P6V6; M0R518;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Protein GPR108;
DE Flags: Precursor;
GN Name=Gpr108;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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).
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 -!- 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:0000250|UniProtKB:Q9NPR9}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q91WD0}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9NPR9}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Colocalizes with TLR3, -7, -4, and -9.
CC {ECO:0000250|UniProtKB:Q91WD0}.
CC -!- SIMILARITY: Belongs to the LU7TM family. {ECO:0000305}.
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DR EMBL; AABR07066499; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC061996; AAH61996.1; -; mRNA.
DR RefSeq; NP_955431.1; NM_199399.1.
DR AlphaFoldDB; Q6P6V6; -.
DR STRING; 10116.ENSRNOP00000064473; -.
DR GlyGen; Q6P6V6; 4 sites.
DR iPTMnet; Q6P6V6; -.
DR PhosphoSitePlus; Q6P6V6; -.
DR PaxDb; Q6P6V6; -.
DR GeneID; 316136; -.
DR KEGG; rno:316136; -.
DR CTD; 56927; -.
DR RGD; 735149; Gpr108.
DR VEuPathDB; HostDB:ENSRNOG00000046128; -.
DR eggNOG; KOG2569; Eukaryota.
DR HOGENOM; CLU_020277_4_1_1; -.
DR InParanoid; Q6P6V6; -.
DR OMA; CKARIHK; -.
DR OrthoDB; 1427067at2759; -.
DR PhylomeDB; Q6P6V6; -.
DR PRO; PR:Q6P6V6; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000046128; Expressed in pancreas and 20 other tissues.
DR GO; GO:0033106; C:cis-Golgi network membrane; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS: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; ISO:RGD.
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 2: Evidence at transcript level;
KW Glycoprotein; Golgi apparatus; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..577
FT /note="Protein GPR108"
FT /id="PRO_0000045085"
FT TRANSMEM 296..316
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..345
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 369..389
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 400..420
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 434..454
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 482..502
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TRANSMEM 506..526
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT REGION 144..224
FT /note="Disordered"
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 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 469
FT /note="V -> M (in Ref. 2; AAH61996)"
SQ SEQUENCE 577 AA; 64689 MW; 986C80BC1314A615 CRC64;
MAVSERRGLS GESPAQCRWE YLSLLVLMLS GCSGRIHRLT LTGEKRADIQ LNSFGFYTNG
SLEVELSLLR LSLQETEDKF PKVGFSLSRV RSGSVRSYSS RNSHECPLER NSSNFLVLFL
INIKDLQVQV RKYGEQKLFI SPGLLPEAPS QSGPPKPDPT GTPKDNHVIH PSPKKMSAVK
EDQAKLTVPQ VSGDKALPAG HRHSSDGQPQ SQPPTRGPSG KEKDLVLGLG HLNDSYNFSF
HIVIGSRAEE GQYSLNFHNC YNTIPGQEQP FDLTVMIREK NPEGFLSAAE IPLFKLYLIM
SACFLAAGIF WVSVLCKNTY SVFKIHWLMA ALAFTKSVSL LFHSINYYFI NSQGHPIEGL
AVMHYITHLL KGALLFITIA LIGSGWAFVK YMLSDKEKKI FGIVIPLQVL ANVAYIVIES
REEGASDYGL WKEILFLVDL ICCGAILFPV VWSIRHLQDA SGTDGKVAVN LAKLKLFRHY
YVMVICYIYF TRIIAILLRV AVPFQWQWLY QLLVESSTLA FFVLTGYKFQ PAGDNPYLQL
PQQEDEEDVQ MEQVMTDSGF REGLSKVNKT ASGRELL
