RFTN1_HUMAN
ID RFTN1_HUMAN Reviewed; 578 AA.
AC Q14699; Q0D2G0; Q496Y2; Q4QQI7; Q5JB48; Q7Z7P2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Raftlin;
DE AltName: Full=Cell migration-inducing gene 2 protein;
DE AltName: Full=Raft-linking protein;
GN Name=RFTN1; Synonyms=KIAA0084; ORFNames=MIG2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-421.
RA Kim J.W.;
RT "Identification of a human cell migration gene 2.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow;
RX PubMed=7788527; DOI=10.1093/dnares/2.1.37;
RA Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S.,
RA Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. III. The
RT coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 2:37-43(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph;
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, FUNCTION, TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-2 AND CYS-3, MYRISTOYLATION AT
RP GLY-2, AND PALMITOYLATION AT CYS-3.
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [6]
RP MYRISTOYLATION AT GLY-2.
RX PubMed=20213681; DOI=10.1002/pmic.200900783;
RA Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E.,
RA Tsunasawa S., Utsumi T.;
RT "Strategy for comprehensive identification of human N-myristoylated
RT proteins using an insect cell-free protein synthesis system.";
RL Proteomics 10:1780-1793(2010).
RN [7]
RP FUNCTION, INTERACTION WITH CLTC, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=21266579; DOI=10.1074/jbc.m110.185793;
RA Watanabe A., Tatematsu M., Saeki K., Shibata S., Shime H., Yoshimura A.,
RA Obuse C., Seya T., Matsumoto M.;
RT "Raftlin is involved in the nucleocapture complex to induce poly(I:C)-
RT mediated TLR3 activation.";
RL J. Biol. Chem. 286:10702-10711(2011).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [11]
RP FUNCTION, INTERACTION WITH TLR4; CLTC; AP2A1 AND AP2B1, SUBCELLULAR
RP LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
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 (PubMed:27022195, PubMed:21266579). Upon bacterial
CC lipopolysaccharide stimulation, mediates internalization of TLR4 to
CC endosomes in dendritic cells and macrophages; and internalization of
CC poly(I:C) to TLR3-positive endosomes in myeloid dendritic cells and
CC epithelial cells; resulting in activation of TICAM1-mediated signaling
CC and subsequent IFNB1 production (PubMed:27022195, PubMed:21266579).
CC Involved in T-cell antigen receptor-mediated signaling by regulating
CC tyrosine kinase LCK localization, T-cell dependent antibody production
CC and cytokine secretion (By similarity). May regulate B-cell antigen
CC receptor-mediated signaling (PubMed:12805216). May play a pivotal role
CC in the formation and/or maintenance of lipid rafts (PubMed:12805216).
CC {ECO:0000250|UniProtKB:Q6A0D4, ECO:0000269|PubMed:12805216,
CC ECO:0000269|PubMed:21266579, ECO:0000269|PubMed:27022195}.
CC -!- SUBUNIT: Interacts with TLR4; the interaction occurs in response to
CC lipopolysaccharide stimulation (PubMed:27022195). Interacts with CLTC;
CC the interaction occurs in response to pathogens (PubMed:27022195,
CC PubMed:21266579). Interacts with AP2A1 and AP2B1 (PubMed:27022195).
CC {ECO:0000269|PubMed:21266579, ECO:0000269|PubMed:27022195}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12805216,
CC ECO:0000269|PubMed:21266579, ECO:0000269|PubMed:27022195}; Lipid-anchor
CC {ECO:0000269|PubMed:12805216}. Cytoplasm {ECO:0000269|PubMed:21266579,
CC ECO:0000269|PubMed:27022195}. Membrane raft
CC {ECO:0000269|PubMed:12805216}. Endosome {ECO:0000269|PubMed:21266579,
CC ECO:0000269|PubMed:27022195}. Early endosome
CC {ECO:0000269|PubMed:21266579}. Note=Translocates from cytoplasm to cell
CC membrane where it colocalizes with poly (I:C) and then moves to
CC endosomes where it colocalizes with TLR3 (PubMed:21266579).
CC Translocates from cytoplasm to cell membrane where it colocalizes with
CC TLR4 and then together with TLR4 moves to endosomes, upon
CC lipopolysaccharide stimulation (PubMed:27022195).
CC {ECO:0000269|PubMed:21266579, ECO:0000269|PubMed:27022195}.
CC -!- TISSUE SPECIFICITY: Expressed in B-cells (at protein level)
CC (PubMed:12805216). Expressed in dendritic cells and macrophages
CC (PubMed:27022195, PubMed:21266579). {ECO:0000269|PubMed:12805216,
CC ECO:0000269|PubMed:21266579, ECO:0000269|PubMed:27022195}.
CC -!- SIMILARITY: Belongs to the raftlin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH51336.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH69209.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA07644.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY237654; AAO91814.1; -; mRNA.
DR EMBL; D42043; BAA07644.1; ALT_INIT; mRNA.
DR EMBL; BC051336; AAH51336.1; ALT_INIT; mRNA.
DR EMBL; BC069209; AAH69209.1; ALT_INIT; mRNA.
DR EMBL; BC098270; AAH98270.2; -; mRNA.
DR EMBL; BC100667; AAI00668.2; -; mRNA.
DR EMBL; BC100669; AAI00670.2; -; mRNA.
DR EMBL; BC121795; AAI21796.1; -; mRNA.
DR CCDS; CCDS33712.1; -.
DR RefSeq; NP_055965.1; NM_015150.1.
DR RefSeq; XP_005265042.1; XM_005264985.1.
DR RefSeq; XP_005265043.1; XM_005264986.2.
DR RefSeq; XP_006713132.1; XM_006713069.1.
DR RefSeq; XP_011531832.1; XM_011533530.1.
DR AlphaFoldDB; Q14699; -.
DR BioGRID; 116792; 36.
DR ELM; Q14699; -.
DR IntAct; Q14699; 25.
DR MINT; Q14699; -.
DR STRING; 9606.ENSP00000334153; -.
DR iPTMnet; Q14699; -.
DR PhosphoSitePlus; Q14699; -.
DR SwissPalm; Q14699; -.
DR BioMuta; RFTN1; -.
DR DMDM; 115502444; -.
DR CPTAC; CPTAC-1000; -.
DR EPD; Q14699; -.
DR jPOST; Q14699; -.
DR MassIVE; Q14699; -.
DR MaxQB; Q14699; -.
DR PaxDb; Q14699; -.
DR PeptideAtlas; Q14699; -.
DR PRIDE; Q14699; -.
DR ProteomicsDB; 60140; -.
DR Antibodypedia; 53317; 119 antibodies from 23 providers.
DR DNASU; 23180; -.
DR Ensembl; ENST00000334133.9; ENSP00000334153.4; ENSG00000131378.14.
DR GeneID; 23180; -.
DR KEGG; hsa:23180; -.
DR MANE-Select; ENST00000334133.9; ENSP00000334153.4; NM_015150.2; NP_055965.1.
DR UCSC; uc003cay.4; human.
DR CTD; 23180; -.
DR DisGeNET; 23180; -.
DR GeneCards; RFTN1; -.
DR HGNC; HGNC:30278; RFTN1.
DR HPA; ENSG00000131378; Tissue enhanced (lymphoid).
DR MIM; 618210; gene.
DR neXtProt; NX_Q14699; -.
DR OpenTargets; ENSG00000131378; -.
DR PharmGKB; PA162401206; -.
DR VEuPathDB; HostDB:ENSG00000131378; -.
DR eggNOG; ENOG502QVP2; Eukaryota.
DR GeneTree; ENSGT00530000063609; -.
DR HOGENOM; CLU_025878_1_0_1; -.
DR InParanoid; Q14699; -.
DR OMA; DSKTMQG; -.
DR OrthoDB; 434232at2759; -.
DR PhylomeDB; Q14699; -.
DR TreeFam; TF333285; -.
DR PathwayCommons; Q14699; -.
DR SignaLink; Q14699; -.
DR BioGRID-ORCS; 23180; 9 hits in 1067 CRISPR screens.
DR ChiTaRS; RFTN1; human.
DR GenomeRNAi; 23180; -.
DR Pharos; Q14699; Tbio.
DR PRO; PR:Q14699; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q14699; protein.
DR Bgee; ENSG00000131378; Expressed in decidua and 191 other tissues.
DR ExpressionAtlas; Q14699; baseline and differential.
DR Genevisible; Q14699; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IDA:MGI.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:MGI.
DR GO; GO:0050853; P:B cell receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0033227; P:dsRNA transport; IMP:MGI.
DR GO; GO:0001765; P:membrane raft assembly; IMP:UniProtKB.
DR GO; GO:0040010; P:positive regulation of growth rate; IMP:UniProtKB.
DR GO; GO:0032740; P:positive regulation of interleukin-17 production; ISS:UniProtKB.
DR GO; GO:1903044; P:protein localization to membrane raft; ISS:CAFA.
DR GO; GO:0032596; P:protein transport into membrane raft; ISS:CAFA.
DR GO; GO:0043330; P:response to exogenous dsRNA; IMP:MGI.
DR GO; GO:0002457; P:T cell antigen processing and presentation; ISS:CAFA.
DR GO; GO:0050852; P:T cell receptor signaling pathway; ISS:CAFA.
DR GO; GO:0034138; P:toll-like receptor 3 signaling pathway; IMP: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 CHAIN 2..578
FT /note="Raftlin"
FT /id="PRO_0000050718"
FT REGION 169..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..485
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..503
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..578
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6A0D4"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 505
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6A0D4"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:12805216,
FT ECO:0000269|PubMed:20213681"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:12805216"
FT VARIANT 248
FT /note="E -> K (in dbSNP:rs34276015)"
FT /id="VAR_051317"
FT VARIANT 421
FT /note="V -> I (in dbSNP:rs11554130)"
FT /evidence="ECO:0000269|Ref.1"
FT /id="VAR_061699"
FT MUTAGEN 2
FT /note="G->A: Loss of association with membranes. Same
FT effect; when associated with S-3."
FT /evidence="ECO:0000269|PubMed:12805216"
FT MUTAGEN 3
FT /note="C->S: Partially affects association with membranes.
FT Loss of association with membranes; when associated with A-
FT 2."
FT /evidence="ECO:0000269|PubMed:12805216"
FT CONFLICT 86
FT /note="V -> A (in Ref. 3; AAH98270)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="C -> S (in Ref. 3; AAH51336/AAH69209)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="A -> V (in Ref. 3; AAH51336/AAH69209)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 578 AA; 63146 MW; 889928D62A62F189 CRC64;
MGCGLNKLEK RDEKRPGNIY STLKRPQVET KIDVSYEYRF LEFTTLSAAE LPGSSAVRLA
SLRDLPAQLL ELYQQGFSLA ALHPFVQPTH EREKTPLEHI FRAILIKKTD RSQKTDLHNE
GYILELDCCS SLDHPTDQKL IPEFIKKIQE AASQGLKFVG VIPQYHSSVN SAGSSAPVST
ANSTEDARDA KNARGDHASL ENEKPGTGDV CSAPAGRNQS PEPSSGPRGE VPLAKQPSSP
SGEGDGGELS PQGVSKTLDG PESNPLEVHE EPLSGKMEIF TLFNKPKSHQ KCRQYYPVTI
PLHVSKNGQT VSGLDANWLE HMSDHFRKGG MLVNAVFYLG IVNDSLHGLT DGVFIFEAVS
TEDSKTIQGY DAIVVEQWTV LEGVEVQTDY VPLLNSLAAY GWQLTCVLPT PVVKTTSEGS
VSTKQIVFLQ RPCLPQKIKK KESKFQWRFS REEMHNRQMR KSKGKLSARD KQQAEENEKN
LEDQSSKAGD MGNCVSGQQQ EGGVSEEMKG PVQEDKGEQL SPGGLLCGVG VEGEAVQNGP
ASHSRALVGI CTGHSNPGED ARDGDAEEVR ELGTVEEN
