IFT46_CHLRE
ID IFT46_CHLRE Reviewed; 344 AA.
AC A2T2X4; A8JIV6;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Intraflagellar transport protein 46;
DE AltName: Full=Flagellar-associated protein 32;
DE AltName: Full=IFT complex B protein {ECO:0000312|EMBL:ABH06907.1};
GN Name=IFT46 {ECO:0000312|EMBL:ABH06907.1}; Synonyms=FAP32;
GN ORFNames=CHLREDRAFT_108954;
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ABH06907.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=17312020; DOI=10.1083/jcb.200608041;
RA Hou Y., Qin H., Follit J.A., Pazour G.J., Rosenbaum J.L., Witman G.B.;
RT "Functional analysis of an individual IFT protein: IFT46 is required for
RT transport of outer dynein arms into flagella.";
RL J. Cell Biol. 176:653-665(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503, and cw92;
RX PubMed=17932292; DOI=10.1126/science.1143609;
RA Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L.,
RA Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H.,
RA Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M.,
RA Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L.,
RA Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H.,
RA Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M.,
RA Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A.,
RA Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L.,
RA Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C.,
RA Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.J.,
RA Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L.,
RA Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L.,
RA Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C.,
RA Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J.,
RA Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P.,
RA Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R.,
RA Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P.,
RA Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y.,
RA Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L.,
RA Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.;
RT "The Chlamydomonas genome reveals the evolution of key animal and plant
RT functions.";
RL Science 318:245-250(2007).
RN [3] {ECO:0000305}
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=15955805; DOI=10.1074/jbc.m505062200;
RA Lucker B.F., Behal R.H., Qin H., Siron L.C., Taggart W.D., Rosenbaum J.L.,
RA Cole D.G.;
RT "Characterization of the intraflagellar transport complex B core: direct
RT interaction of the IFT81 and IFT74/72 subunits.";
RL J. Biol. Chem. 280:27688-27696(2005).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15998802; DOI=10.1083/jcb.200504008;
RA Pazour G.J., Agrin N., Leszyk J., Witman G.B.;
RT "Proteomic analysis of a eukaryotic cilium.";
RL J. Cell Biol. 170:103-113(2005).
RN [5] {ECO:0000305}
RP INTERACTION WITH DAW1, AND SUBCELLULAR LOCATION.
RX PubMed=18852297; DOI=10.1083/jcb.200802025;
RA Ahmed N.T., Gao C., Lucker B.F., Cole D.G., Mitchell D.R.;
RT "ODA16 aids axonemal outer row dynein assembly through an interaction with
RT the intraflagellar transport machinery.";
RL J. Cell Biol. 183:313-322(2008).
RN [6] {ECO:0000305}
RP INTERACTION WITH IFT25, AND SUBCELLULAR LOCATION.
RX PubMed=19382199; DOI=10.1002/cm.20369;
RA Lechtreck K.F., Luro S., Awata J., Witman G.B.;
RT "HA-tagging of putative flagellar proteins in Chlamydomonas reinhardtii
RT identifies a novel protein of intraflagellar transport complex B.";
RL Cell Motil. Cytoskeleton 66:469-482(2009).
RN [7] {ECO:0000305}
RP SUBCELLULAR LOCATION.
RX PubMed=19412537; DOI=10.1371/journal.pone.0005384;
RA Wang Z., Fan Z.C., Williamson S.M., Qin H.;
RT "Intraflagellar transport (IFT) protein IFT25 is a phosphoprotein component
RT of IFT complex B and physically interacts with IFT27 in Chlamydomonas.";
RL PLoS ONE 4:E5384-E5384(2009).
RN [8] {ECO:0000305}
RP FUNCTION, INTERACTION WITH IFT52 AND IFT88, AND DISRUPTION PHENOTYPE.
RX PubMed=20435895; DOI=10.1074/jbc.m110.106997;
RA Lucker B.F., Miller M.S., Dziedzic S.A., Blackmarr P.T., Cole D.G.;
RT "Direct interactions of intraflagellar transport complex B proteins IFT88,
RT IFT52, and IFT46.";
RL J. Biol. Chem. 285:21508-21518(2010).
RN [9] {ECO:0000305}
RP INTERACTION WITH IFT70.
RX PubMed=20534810; DOI=10.1091/mbc.e10-03-0191;
RA Fan Z.C., Behal R.H., Geimer S., Wang Z., Williamson S.M., Zhang H.,
RA Cole D.G., Qin H.;
RT "Chlamydomonas IFT70/CrDYF-1 is a core component of IFT particle complex B
RT and is required for flagellar assembly.";
RL Mol. Biol. Cell 21:2696-2706(2010).
CC -!- FUNCTION: Forms part of a complex involved in intraflagellar transport
CC (IFT), the bi-directional movement of particles required for the
CC assembly, maintenance and functioning of primary cilia. Plays a role in
CC maintaining IFT complex B stability. {ECO:0000269|PubMed:17312020,
CC ECO:0000269|PubMed:20435895}.
CC -!- SUBUNIT: Component of the IFT complex B, the core composed of IFT25,
CC IFT27, IFT46, IFT52, IFT74, IFT81 and IFT88 as well as associated
CC subunits IFT20, IFT57, IFT80 and IFT172. Interacts with IFT25, IFT52,
CC IFT70, IFT88 AND DAW1. {ECO:0000269|PubMed:15955805,
CC ECO:0000269|PubMed:18852297, ECO:0000269|PubMed:19382199,
CC ECO:0000269|PubMed:20435895, ECO:0000269|PubMed:20534810}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000269|PubMed:15955805, ECO:0000269|PubMed:17312020,
CC ECO:0000269|PubMed:18852297, ECO:0000269|PubMed:19382199,
CC ECO:0000269|PubMed:19412537}. Cell projection, cilium
CC {ECO:0000269|PubMed:15955805, ECO:0000269|PubMed:17312020,
CC ECO:0000269|PubMed:18852297, ECO:0000269|PubMed:19382199,
CC ECO:0000269|PubMed:19412537}. Note=Expression is concentrated at the
CC cilium basal body but is also detected along the length of the cilium.
CC {ECO:0000269|PubMed:15955805, ECO:0000269|PubMed:17312020,
CC ECO:0000269|PubMed:18852297, ECO:0000269|PubMed:19382199,
CC ECO:0000269|PubMed:19412537}.
CC -!- DISRUPTION PHENOTYPE: Individuals have short, non-motile flagellae.
CC {ECO:0000269|PubMed:17312020, ECO:0000269|PubMed:20435895}.
CC -!- SIMILARITY: Belongs to the IFT46 family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDO96191.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DQ787426; ABH06907.1; -; mRNA.
DR EMBL; DS496218; EDO96191.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001691140.1; XM_001691088.1.
DR AlphaFoldDB; A2T2X4; -.
DR SMR; A2T2X4; -.
DR STRING; 3055.EDO96191; -.
DR PaxDb; A2T2X4; -.
DR PRIDE; A2T2X4; -.
DR EnsemblPlants; PNW83496; PNW83496; CHLRE_05g241637v5.
DR GeneID; 5716734; -.
DR Gramene; PNW83496; PNW83496; CHLRE_05g241637v5.
DR KEGG; cre:CHLRE_05g241637v5; -.
DR eggNOG; ENOG502QPNA; Eukaryota.
DR HOGENOM; CLU_039364_3_0_1; -.
DR InParanoid; A2T2X4; -.
DR OMA; AYNAQEY; -.
DR OrthoDB; 878878at2759; -.
DR GO; GO:0097546; C:ciliary base; IDA:MGI.
DR GO; GO:0060170; C:ciliary membrane; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0030992; C:intraciliary transport particle B; IDA:UniProtKB.
DR GO; GO:0031514; C:motile cilium; IDA:BHF-UCL.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:BHF-UCL.
DR GO; GO:0035082; P:axoneme assembly; IMP:MGI.
DR GO; GO:0060271; P:cilium assembly; IMP:BHF-UCL.
DR GO; GO:0044782; P:cilium organization; IMP:MGI.
DR GO; GO:0060285; P:cilium-dependent cell motility; IMP:MGI.
DR GO; GO:0042073; P:intraciliary transport; IDA:UniProtKB.
DR GO; GO:0036158; P:outer dynein arm assembly; IMP:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IDA:BHF-UCL.
DR GO; GO:0015031; P:protein transport; IMP:MGI.
DR GO; GO:1902017; P:regulation of cilium assembly; IMP:MGI.
DR GO; GO:0031647; P:regulation of protein stability; IMP:MGI.
DR InterPro; IPR022088; Intraflagellar_transp_cmplxB.
DR PANTHER; PTHR13376; PTHR13376; 1.
DR Pfam; PF12317; IFT46_B_C; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cilium; Cytoplasm; Cytoskeleton.
FT CHAIN 1..344
FT /note="Intraflagellar transport protein 46"
FT /id="PRO_0000399500"
FT REGION 1..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 344 AA; 37935 MW; 33D1C0837A17D62E CRC64;
MDDSMDYPDR DGDDLDQFQG TARSQVVQNQ PHDEEVNLSE SESFAGADEP PAAPRDASLI
ESHDMDEGPA APARTLSPTG YEAGKHAPGG IANSDEAPPG AYNAQEYKHL NVGEDVRELF
SYIGRYKPQT VELDTRIKPF IPDYIPAVGG IDEFIKVPRP DTKPDYLGLK VLDEPAAKQS
DPTVLTLQLR QLSKEAPGAK ADMVGRLEHT DENKAKKIQQ WIASINDIHK AKPAATVNYS
KRMPEIEALM QEWPPEVETF LKTMHMPSGD VELDIKTYAR LVCTLLDIPV YDDPVESLHV
LFTLYLEFKN NPIFRQHMEM ENKLDGMSGG GGGMMGGGAD VLGL
