RFTN2_MOUSE
ID RFTN2_MOUSE Reviewed; 500 AA.
AC Q8CHX7; Q8R306; Q9CXJ5;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Raftlin-2;
DE AltName: Full=Raft-linking protein 2;
GN Name=Rftn2;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Head;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=FVB/N; TISSUE=Colon, and Mammary tumor;
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 [3]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=19414744; DOI=10.4049/jimmunol.0802672;
RA Saeki K., Fukuyama S., Ayada T., Nakaya M., Aki D., Takaesu G., Hanada T.,
RA Matsumura Y., Kobayashi T., Nakagawa R., Yoshimura A.;
RT "A major lipid raft protein raftlin modulates T cell receptor signaling and
RT enhances th17-mediated autoimmune responses.";
RL J. Immunol. 182:5929-5937(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-404; THR-408 AND SER-429, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, and Spleen;
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, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=27022195; DOI=10.4049/jimmunol.1501734;
RA Tatematsu M., Yoshida R., Morioka Y., Ishii N., Funami K., Watanabe A.,
RA Saeki K., Seya T., Matsumoto M.;
RT "Raftlin controls lipopolysaccharide-induced TLR4 internalization and
RT TICAM-1 signaling in a cell type-specific manner.";
RL J. Immunol. 196:3865-3876(2016).
CC -!- FUNCTION: Upon bacterial lipopolysaccharide stimulation, mediates
CC clathrin-dependent internalization of TLR4 in dendritic cells,
CC resulting in activation of TICAM1-mediated signaling and subsequent
CC IFNB1 production (PubMed:27022195). May regulate B-cell antigen
CC receptor-mediated signaling. {ECO:0000269|PubMed:19414744,
CC ECO:0000269|PubMed:27022195}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q14699};
CC Lipid-anchor {ECO:0000250|UniProtKB:Q14699}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8CHX7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CHX7-2; Sequence=VSP_015324, VSP_015325;
CC -!- TISSUE SPECIFICITY: Expressed in B-cells, heart, brain, spleen, large
CC intestine and lung (PubMed:19414744). Expressed in dendritic cells and
CC macrophages (PubMed:27022195). {ECO:0000269|PubMed:19414744,
CC ECO:0000269|PubMed:27022195}.
CC -!- DISRUPTION PHENOTYPE: Double RFTN1 and RFTN2 mutant mice show no
CC visible phenotype under pathogen-free conditions but show greatly
CC reduced interferon beta production in splenic dendritic cells under
CC poly(I:C) or lipopolysaccharide stimulation.
CC {ECO:0000269|PubMed:27022195}.
CC -!- SIMILARITY: Belongs to the raftlin family. {ECO:0000305}.
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DR EMBL; AK014318; BAB29269.1; ALT_TERM; mRNA.
DR EMBL; BC026871; AAH26871.1; -; mRNA.
DR EMBL; BC038341; AAH38341.1; -; mRNA.
DR CCDS; CCDS14962.1; -. [Q8CHX7-1]
DR RefSeq; NP_082989.1; NM_028713.1. [Q8CHX7-1]
DR AlphaFoldDB; Q8CHX7; -.
DR STRING; 10090.ENSMUSP00000027121; -.
DR iPTMnet; Q8CHX7; -.
DR PhosphoSitePlus; Q8CHX7; -.
DR SwissPalm; Q8CHX7; -.
DR jPOST; Q8CHX7; -.
DR MaxQB; Q8CHX7; -.
DR PaxDb; Q8CHX7; -.
DR PeptideAtlas; Q8CHX7; -.
DR PRIDE; Q8CHX7; -.
DR ProteomicsDB; 255013; -. [Q8CHX7-1]
DR ProteomicsDB; 255014; -. [Q8CHX7-2]
DR Antibodypedia; 34069; 131 antibodies from 25 providers.
DR DNASU; 74013; -.
DR Ensembl; ENSMUST00000027121; ENSMUSP00000027121; ENSMUSG00000025978. [Q8CHX7-1]
DR Ensembl; ENSMUST00000114428; ENSMUSP00000110071; ENSMUSG00000025978. [Q8CHX7-2]
DR GeneID; 74013; -.
DR KEGG; mmu:74013; -.
DR UCSC; uc007bag.1; mouse. [Q8CHX7-1]
DR CTD; 130132; -.
DR MGI; MGI:1921263; Rftn2.
DR VEuPathDB; HostDB:ENSMUSG00000025978; -.
DR eggNOG; ENOG502QVRY; Eukaryota.
DR GeneTree; ENSGT00530000063609; -.
DR HOGENOM; CLU_025878_0_0_1; -.
DR InParanoid; Q8CHX7; -.
DR OMA; EENTYSP; -.
DR OrthoDB; 434232at2759; -.
DR PhylomeDB; Q8CHX7; -.
DR TreeFam; TF333285; -.
DR BioGRID-ORCS; 74013; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Rftn2; mouse.
DR PRO; PR:Q8CHX7; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8CHX7; protein.
DR Bgee; ENSMUSG00000025978; Expressed in humerus cartilage element and 195 other tissues.
DR ExpressionAtlas; Q8CHX7; baseline and differential.
DR Genevisible; Q8CHX7; MM.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033227; P:dsRNA transport; IMP:MGI.
DR GO; GO:0043330; P:response to exogenous dsRNA; IMP:MGI.
DR InterPro; IPR028169; Raftlin.
DR PANTHER; PTHR17601; PTHR17601; 1.
DR Pfam; PF15250; Raftlin; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Lipoprotein; Membrane; Myristate;
KW Palmitate; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..500
FT /note="Raftlin-2"
FT /id="PRO_0000089339"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..427
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 404
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 408
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 429
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 309..344
FT /note="GDQLPKSLEGFFIYEEEGSGVPGSNRRGNDAIVVEQ -> VAKLEAFQLSVS
FT DKLPKGKQKYSFQSLSGIPASGLA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015324"
FT VAR_SEQ 345..500
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015325"
SQ SEQUENCE 500 AA; 54972 MW; 1D5DC3727517C68A CRC64;
MGCGLRKLED PDESSPGKIF STLKRPQVET KTEFAYEYAL LDFTLQASTN PDVIKINSVL
DIVAKVEDYY LKGYVVGAIH PVIQPVGQRK HLPASHLYRA VLSRLKLSPK HSAAGGQRRA
RLVMEECPLT CEAQANDAAK ELMDKINAAA KRGMKFVGLV SQCYLPSMHC NGASHDGVAE
SGLHVRQDSQ DNCKGWNEGA LGGHLSESGV EEEPQHESGQ HQTERNSSPS YANPKRGEAP
DGKLYMVFNA FEEDAASWAY QEGVLSMKVT RKGAVISALD ANWLELTTFY YKQGFSLIDS
FVCWETPKGD QLPKSLEGFF IYEEEGSGVP GSNRRGNDAI VVEQWTVIEG CEIKTDYGPL
LHTLAEFGWL LTSVLPTPIL RHDSEGNLAT KQVVFLQRPV TWNSAAQTPE RKGSRLLKGE
DRNKVSSRSL GLDTNASQAA GGRAPLEEGS LSPSRECWTK EERPAQSDSF SGFSSSDSVL
RELDDGQFDQ EEGVTQVTCM
