RFTN1_MOUSE
ID RFTN1_MOUSE Reviewed; 554 AA.
AC Q6A0D4; Q3U654; Q3U8P6; Q80US1;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Raftlin;
DE AltName: Full=Raft-linking protein;
GN Name=Rftn1; Synonyms=Kiaa0084;
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].
RC TISSUE=Embryonic tail;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
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].
RC STRAIN=C57BL/6J;
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 TISSUE SPECIFICITY.
RX PubMed=12805216; DOI=10.1093/emboj/cdg293;
RA Saeki K., Miura Y., Aki D., Kurosaki T., Yoshimura A.;
RT "The B cell-specific major raft protein, Raftlin, is necessary for the
RT integrity of lipid raft and BCR signal transduction.";
RL EMBO J. 22:3015-3026(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183 AND SER-530, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-507, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, 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 [8]
RP FUNCTION, AND TISSUE SPECIFICITY.
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: Involved in protein trafficking via association with clathrin
CC and AP2 complex (By similarity). Upon bacterial lipopolysaccharide
CC stimulation, mediates internalization of TLR4 to endosomes in dendritic
CC cells and macrophages, and internalization of poly(I:C) to TLR3-
CC positive endosomes in myeloid dendritic cells and epithelial cells;
CC resulting in activation of TICAM1-mediated signaling and subsequent
CC IFNB1 production (PubMed:27022195). Involved in T-cell antigen
CC receptor-mediated signaling by regulating tyrosine kinase LCK
CC localization, T-cell dependent antibody production and cytokine
CC secretion (PubMed:19414744). May regulate B-cell antigen receptor-
CC mediated signaling (By similarity). May play a pivotal role in the
CC formation and/or maintenance of lipid rafts (By similarity).
CC {ECO:0000250|UniProtKB:Q14699, ECO:0000269|PubMed:19414744,
CC ECO:0000269|PubMed:27022195}.
CC -!- SUBUNIT: Interacts with TLR4; the interaction occurs in response to
CC lipopolysaccharide stimulation. Interacts with CLTC; the interaction
CC occurs in response to pathogens. Interacts with AP2A1 and AP2B1.
CC {ECO:0000250|UniProtKB:Q14699}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19414744};
CC Lipid-anchor {ECO:0000250|UniProtKB:Q14699}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q14699}. Membrane raft
CC {ECO:0000250|UniProtKB:Q14699}. Endosome
CC {ECO:0000250|UniProtKB:Q14699}. Early endosome
CC {ECO:0000250|UniProtKB:Q14699}. Note=Translocates from cytoplasm to
CC cell membrane where it colocalizes with poly (I:C) and then moves to
CC endosomes where it colocalizes with TLR3. Translocates from cytoplasm
CC to cell membrane where it colocalizes with TLR4 and then together with
CC TLR4 moves to endosomes, upon lipopolysaccharide stimulation
CC (PubMed:27022195). {ECO:0000250|UniProtKB:Q14699}.
CC -!- TISSUE SPECIFICITY: Expressed in T-cells, B-cells, thymus and spleen
CC (at protein level) (PubMed:19414744, PubMed:12805216). Expressed in
CC dendritic cells, macrophages, heart, lung and small intestine
CC (PubMed:19414744). {ECO:0000269|PubMed:12805216,
CC ECO:0000269|PubMed:19414744}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice have smaller spleen, fewer
CC splenocytes, reduced IgM production and secrete less IFNG, during
CC antigen re-stimulation (PubMed:19414744). Double RFTN1 and RFTN2 mutant
CC mice show no visible phenotype under pathogen-free conditions but show
CC greatly reduced IFNB1 production in splenic dendritic cells following
CC poly(I:C) or LPS stimulation (PubMed:27022195).
CC {ECO:0000269|PubMed:19414744, ECO:0000269|PubMed:27022195}.
CC -!- SIMILARITY: Belongs to the raftlin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32162.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE31871.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK172884; BAD32162.1; ALT_INIT; mRNA.
DR EMBL; AK152130; BAE30971.1; -; mRNA.
DR EMBL; AK153288; BAE31871.1; ALT_INIT; mRNA.
DR EMBL; AK155870; BAE33473.1; -; mRNA.
DR EMBL; BC052074; AAH52074.1; -; mRNA.
DR CCDS; CCDS28873.1; -.
DR RefSeq; NP_852062.1; NM_181397.2.
DR AlphaFoldDB; Q6A0D4; -.
DR BioGRID; 218128; 1.
DR IntAct; Q6A0D4; 1.
DR MINT; Q6A0D4; -.
DR STRING; 10090.ENSMUSP00000046524; -.
DR iPTMnet; Q6A0D4; -.
DR PhosphoSitePlus; Q6A0D4; -.
DR SwissPalm; Q6A0D4; -.
DR EPD; Q6A0D4; -.
DR jPOST; Q6A0D4; -.
DR MaxQB; Q6A0D4; -.
DR PaxDb; Q6A0D4; -.
DR PeptideAtlas; Q6A0D4; -.
DR PRIDE; Q6A0D4; -.
DR ProteomicsDB; 255316; -.
DR Antibodypedia; 53317; 119 antibodies from 23 providers.
DR Ensembl; ENSMUST00000044503; ENSMUSP00000046524; ENSMUSG00000039316.
DR GeneID; 76438; -.
DR KEGG; mmu:76438; -.
DR UCSC; uc008cyr.1; mouse.
DR CTD; 23180; -.
DR MGI; MGI:1923688; Rftn1.
DR VEuPathDB; HostDB:ENSMUSG00000039316; -.
DR eggNOG; ENOG502QVP2; Eukaryota.
DR GeneTree; ENSGT00530000063609; -.
DR InParanoid; Q6A0D4; -.
DR OMA; DSKTMQG; -.
DR OrthoDB; 434232at2759; -.
DR PhylomeDB; Q6A0D4; -.
DR TreeFam; TF333285; -.
DR BioGRID-ORCS; 76438; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Rftn1; mouse.
DR PRO; PR:Q6A0D4; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q6A0D4; protein.
DR Bgee; ENSMUSG00000039316; Expressed in mesenteric lymph node and 217 other tissues.
DR ExpressionAtlas; Q6A0D4; baseline and differential.
DR Genevisible; Q6A0D4; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0003725; F:double-stranded RNA binding; ISO:MGI.
DR GO; GO:0050853; P:B cell receptor signaling pathway; ISO:MGI.
DR GO; GO:0033227; P:dsRNA transport; ISO:MGI.
DR GO; GO:0001765; P:membrane raft assembly; ISO:MGI.
DR GO; GO:0040010; P:positive regulation of growth rate; ISO:MGI.
DR GO; GO:0032740; P:positive regulation of interleukin-17 production; IMP:UniProtKB.
DR GO; GO:1903044; P:protein localization to membrane raft; IMP:UniProtKB.
DR GO; GO:0032596; P:protein transport into membrane raft; IMP:UniProtKB.
DR GO; GO:0043330; P:response to exogenous dsRNA; ISO:MGI.
DR GO; GO:0002457; P:T cell antigen processing and presentation; IMP:UniProtKB.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0034138; P:toll-like receptor 3 signaling pathway; ISO:MGI.
DR InterPro; IPR028169; Raftlin.
DR PANTHER; PTHR17601; PTHR17601; 1.
DR Pfam; PF15250; Raftlin; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Endosome; Lipoprotein; Membrane; Myristate;
KW Palmitate; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q14699"
FT CHAIN 2..554
FT /note="Raftlin"
FT /id="PRO_0000251954"
FT REGION 192..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 441..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..462
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14699"
FT MOD_RES 507
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 530
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
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 CONFLICT 236
FT /note="Q -> R (in Ref. 2; BAE30971/BAE31871)"
FT /evidence="ECO:0000305"
FT CONFLICT 472
FT /note="N -> D (in Ref. 1; BAD32162)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 554 AA; 61537 MW; 34AFE53D91861A2C CRC64;
MGCSLNKLEK REEKRPGNIY STLKRPQVET KVDVTYEYCF LEFTTLTAAE LPRSSATRLA
SLRDLPDQLL ELYQQGFSLA ALHPFVQPTR RQEKILLEHI FRAILVKKTN RSQKAELHDE
GYTLELDYCS SLEHLADQKL IPEFIKKVQE AASQGLKFVS VVPQYQPSVS SAGSRRLKPV
ANSVEDARDV KCTLGDRSSL ENDTPKAAET DAATAGVNRR PETKPGSTGD VPSAQQPGIP
SPSAENEAGE FPLRGLQPAL DRSEGDPSNG PEELPSRKME IFAFFNRPKS QQKCRQYYPV
TIPLQVSKNG QTVSSLDASW LEHMSDHFRK GGVLVNAVFQ LGMANDSFYG LTDGVFIFEA
VSTEDNRTTQ GYDAIVVEQW TVLEGTEVQT DYMPLLNSLA AYGWQLTCVL PTPILKTTRE
GNVSTKQIVF LQRPCLPQKT KKRESKFQWR FSRNEIHGRQ TRKSKGKLSA SNKQQAEENE
KNLEDQFSKA GDVGNCVLGA PQWGRASEVR EQRQGSAAVQ NGPAGHNRDS VALRHSNPRA
EAELAAGPTP TEAN
