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Database: UniProt
Entry: RTP4_MOUSE
LinkDB: RTP4_MOUSE
Original site: RTP4_MOUSE 
ID   RTP4_MOUSE              Reviewed;         249 AA.
AC   Q9ER80; Q9D3D6;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   24-JAN-2024, entry version 134.
DE   RecName: Full=Receptor-transporting protein 4;
DE   AltName: Full=28 kDa interferon-responsive protein;
GN   Name=Rtp4; Synonyms=Ifrg28;
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].
RC   STRAIN=DBA/2J;
RA   Meritet J.F., Dron M., Tovey M.G.;
RT   "Characterization of ifrg15 and ifrg28, two newly identified interferon
RT   responsive gene.";
RL   Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=15550249; DOI=10.1016/j.cell.2004.11.021;
RA   Saito H., Kubota M., Roberts R.W., Chi Q., Matsunami H.;
RT   "RTP family members induce functional expression of mammalian odorant
RT   receptors.";
RL   Cell 119:679-691(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Pancreas, and Thymus;
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   [4]
RP   FUNCTION, AND INTERACTION WITH OPRD1 AND OPRM1.
RX   PubMed=18836069; DOI=10.1073/pnas.0804106105;
RA   Decaillot F.M., Rozenfeld R., Gupta A., Devi L.A.;
RT   "Cell surface targeting of mu-delta opioid receptor heterodimers by RTP4.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:16045-16050(2008).
CC   -!- FUNCTION: Probable chaperone protein which facilitates trafficking and
CC       functional cell surface expression of some G-protein coupled receptors
CC       (GPCRs). Promotes functional expression of the bitter taste receptor
CC       TAS2R16 (By similarity). Also promotes functional expression of the
CC       opioid receptor heterodimer OPRD1-OPRM1 (PubMed:18836069).
CC       {ECO:0000250|UniProtKB:Q96DX8, ECO:0000269|PubMed:18836069}.
CC   -!- SUBUNIT: Interacts with TASR16 (By similarity). Interacts with OPRD1
CC       and OPRM1; the interaction promotes cell surface localization of the
CC       OPDR1-OPRM1 heterodimer (PubMed:18836069).
CC       {ECO:0000250|UniProtKB:Q96DX8, ECO:0000269|PubMed:18836069}.
CC   -!- INTERACTION:
CC       Q9ER80; P32300: Oprd1; NbExp=2; IntAct=EBI-15731539, EBI-2615936;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type III
CC       membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed at low levels in olfactory neurons.
CC       {ECO:0000269|PubMed:15550249}.
CC   -!- INDUCTION: By interferons.
CC   -!- SIMILARITY: Belongs to the TMEM7 family. {ECO:0000305}.
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DR   EMBL; AJ251364; CAC13976.1; -; mRNA.
DR   EMBL; AY562228; AAT70673.1; -; mRNA.
DR   EMBL; AK007477; BAB25057.1; -; mRNA.
DR   EMBL; AK018021; BAB31041.1; -; mRNA.
DR   CCDS; CCDS28079.1; -.
DR   RefSeq; NP_075875.3; NM_023386.5.
DR   RefSeq; XP_006522554.1; XM_006522491.3.
DR   AlphaFoldDB; Q9ER80; -.
DR   DIP; DIP-46418N; -.
DR   IntAct; Q9ER80; 2.
DR   STRING; 10090.ENSMUSP00000147521; -.
DR   iPTMnet; Q9ER80; -.
DR   PhosphoSitePlus; Q9ER80; -.
DR   MaxQB; Q9ER80; -.
DR   PaxDb; 10090-ENSMUSP00000041091; -.
DR   PeptideAtlas; Q9ER80; -.
DR   ProteomicsDB; 260867; -.
DR   Antibodypedia; 46841; 134 antibodies from 18 providers.
DR   DNASU; 67775; -.
DR   Ensembl; ENSMUST00000038423.6; ENSMUSP00000041091.6; ENSMUSG00000033355.7.
DR   Ensembl; ENSMUST00000209422.2; ENSMUSP00000147521.2; ENSMUSG00000033355.7.
DR   Ensembl; ENSMUST00000210901.2; ENSMUSP00000147442.2; ENSMUSG00000033355.7.
DR   GeneID; 67775; -.
DR   KEGG; mmu:67775; -.
DR   UCSC; uc007ytw.2; mouse.
DR   AGR; MGI:1915025; -.
DR   CTD; 64108; -.
DR   MGI; MGI:1915025; Rtp4.
DR   VEuPathDB; HostDB:ENSMUSG00000033355; -.
DR   eggNOG; ENOG502S085; Eukaryota.
DR   GeneTree; ENSGT00940000162610; -.
DR   HOGENOM; CLU_045693_0_1_1; -.
DR   InParanoid; Q9ER80; -.
DR   OrthoDB; 3020199at2759; -.
DR   PhylomeDB; Q9ER80; -.
DR   TreeFam; TF333246; -.
DR   BioGRID-ORCS; 67775; 5 hits in 80 CRISPR screens.
DR   ChiTaRS; Rtp4; mouse.
DR   PRO; PR:Q9ER80; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   RNAct; Q9ER80; Protein.
DR   Bgee; ENSMUSG00000033355; Expressed in small intestine Peyer's patch and 174 other cell types or tissues.
DR   ExpressionAtlas; Q9ER80; baseline and differential.
DR   Genevisible; Q9ER80; MM.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0031849; F:olfactory receptor binding; IBA:GO_Central.
DR   GO; GO:0051607; P:defense response to virus; ISO:MGI.
DR   GO; GO:0001580; P:detection of chemical stimulus involved in sensory perception of bitter taste; ISO:MGI.
DR   GO; GO:0051205; P:protein insertion into membrane; IBA:GO_Central.
DR   GO; GO:0006612; P:protein targeting to membrane; ISO:MGI.
DR   InterPro; IPR026096; R-trans_p.
DR   InterPro; IPR027377; ZAR1/RTP1-5-like_Znf-3CxxC.
DR   PANTHER; PTHR14402; RECEPTOR TRANSPORTING PROTEIN; 1.
DR   PANTHER; PTHR14402:SF8; RECEPTOR-TRANSPORTING PROTEIN 4; 1.
DR   Pfam; PF13695; zf-3CxxC; 1.
DR   SMART; SM01328; zf-3CxxC; 1.
PE   1: Evidence at protein level;
KW   Membrane; Metal-binding; Reference proteome; Transmembrane;
KW   Transmembrane helix; Zinc; Zinc-finger.
FT   CHAIN           1..249
FT                   /note="Receptor-transporting protein 4"
FT                   /id="PRO_0000181996"
FT   TOPO_DOM        1..227
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        228..248
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         50..162
FT                   /note="3CxxC-type"
FT                   /evidence="ECO:0000255"
FT   REGION          173..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        177..196
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        185
FT                   /note="K -> N (in Ref. 2; AAT70673 and 3; BAB31041)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        209
FT                   /note="F -> L (in Ref. 2; AAT70673 and 3; BAB31041)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   249 AA;  28392 MW;  2C79B36ED6F042D4 CRC64;
     MLFPDDFSTW EQTFQELMQE EKPGAKWSLH LDKNIVPDGA ALGWRQHQQT VLGRFQCSRC
     CRSWTSAQVM ILCHMYPDTL KSQGQARMRI FGQKCQKCFG CQFETPKFST EIIKRILNNL
     VNYILQRYYG HRKIALTSNA SLGEKVTLDG PHDTRNCEAC SLNSHGRCAL AHKVKPPRSP
     SPLPKSSSPS KSCPPPPQTR NTDFGNKTFQ DFGNRTFQGC REPPQREIEP PLFLFLSIAA
     FALFSLFTR
//
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