IFT74_CHLRE
ID IFT74_CHLRE Reviewed; 641 AA.
AC Q6RCE1; Q84P51;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Intraflagellar transport protein 74;
DE AltName: Full=Intraflagellar transport protein 71;
DE Short=IFT-71;
DE AltName: Full=Intraflagellar transport protein 72;
DE Short=IFT74/72;
GN Name=IFT74; Synonyms=IFT71; ORFNames=CHLREDRAFT_136521;
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15024030; DOI=10.1083/jcb.200312133;
RA Iomini C., Tejada K., Mo W., Vaananen H., Piperno G.;
RT "Primary cilia of human endothelial cells disassemble under laminar shear
RT stress.";
RL J. Cell Biol. 164:811-817(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND IDENTIFICATION IN THE IFT COMPLEX
RP B.
RX PubMed=14718520; DOI=10.1083/jcb.200308132;
RA Qin H., Diener D.R., Geimer S., Cole D.G., Rosenbaum J.L.;
RT "Intraflagellar transport (IFT) cargo: IFT transports flagellar precursors
RT to the tip and turnover products to the cell body.";
RL J. Cell Biol. 164:255-266(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503;
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 [4]
RP IDENTIFICATION IN THE IFT COMPLEX B.
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE IFT COMPLEX B, AND
RP INTERACTION WITH BETA-TUBULIN AND IFT81.
RX PubMed=23990561; DOI=10.1126/science.1240985;
RA Bhogaraju S., Cajanek L., Fort C., Blisnick T., Weber K., Taschner M.,
RA Mizuno N., Lamla S., Bastin P., Nigg E.A., Lorentzen E.;
RT "Molecular basis of tubulin transport within the cilium by IFT74 and
RT IFT81.";
RL Science 341:1009-1012(2013).
CC -!- FUNCTION: Component of the intraflagellar transport (IFT) complex B:
CC together with IFT81, forms a tubulin-binding module that specifically
CC mediates transport of tubulin within the cilium. Binds beta-tubulin via
CC its basic region. Required for ciliogenesis.
CC {ECO:0000269|PubMed:14718520, ECO:0000269|PubMed:23990561}.
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 IFT81; the
CC interaction is direct: within the IFT complex B, IFT74 and IFT81
CC mediate the transport of tubulin within the cilium. Interacts (via
CC basic region) with beta-tubulin (via acidic region); interaction is
CC direct. {ECO:0000269|PubMed:14718520, ECO:0000269|PubMed:15955805,
CC ECO:0000269|PubMed:23990561}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000305|PubMed:23990561}.
CC -!- SIMILARITY: Belongs to the IFT74 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO92260.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY505143; AAS48648.1; -; mRNA.
DR EMBL; AY245434; AAO92260.1; ALT_FRAME; mRNA.
DR EMBL; DS496108; EDP09301.1; -; Genomic_DNA.
DR RefSeq; XP_001689563.1; XM_001689511.1.
DR AlphaFoldDB; Q6RCE1; -.
DR SMR; Q6RCE1; -.
DR STRING; 3055.EDP09301; -.
DR PaxDb; Q6RCE1; -.
DR PRIDE; Q6RCE1; -.
DR EnsemblPlants; PNW88405; PNW88405; CHLRE_01g027950v5.
DR GeneID; 5715315; -.
DR Gramene; PNW88405; PNW88405; CHLRE_01g027950v5.
DR KEGG; cre:CHLRE_01g027950v5; -.
DR eggNOG; ENOG502QS4E; Eukaryota.
DR HOGENOM; CLU_027673_0_0_1; -.
DR InParanoid; Q6RCE1; -.
DR OrthoDB; 622935at2759; -.
DR GO; GO:0030992; C:intraciliary transport particle B; IDA:UniProtKB.
DR GO; GO:0031514; C:motile cilium; IDA:BHF-UCL.
DR GO; GO:0048487; F:beta-tubulin binding; IDA:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0035735; P:intraciliary transport involved in cilium assembly; IMP:UniProtKB.
DR InterPro; IPR029602; IFT74.
DR PANTHER; PTHR31432; PTHR31432; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cilium; Cilium biogenesis/degradation; Coiled coil.
FT CHAIN 1..641
FT /note="Intraflagellar transport protein 74"
FT /id="PRO_0000424813"
FT REGION 1..132
FT /note="Basic region"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 139..633
FT /evidence="ECO:0000255"
FT CONFLICT 328
FT /note="E -> G (in Ref. 2; AAO92260)"
FT /evidence="ECO:0000305"
FT CONFLICT 394
FT /note="A -> V (in Ref. 2; AAO92260)"
FT /evidence="ECO:0000305"
FT CONFLICT 414
FT /note="D -> H (in Ref. 2; AAO92260)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 641 AA; 71540 MW; D13329EC5929DC82 CRC64;
MDRPSSRGAL ALGAGGLGKA PTGGAVQQPD RPMTGQRGAA PAGPMRAPAG ASIIGAGPPG
TAMRGGPGPA GGPPGTAYKR MGTASQRPGT GQQAAAAAAA ARAGQQLQVE NRPITNHGVS
GMKTAAAGVG RQVLDKNYFM NELRQKRMEI AQVTSNMKSD LEALERKQAQ YNSMDKRASD
LSKEVKILQE ALADYNTVLD KVGSQAPVYV IQQEFAALKD RNEQQRKRVD EVLTERLNLE
SKAKQAESKM SEIQASMDQR LNSMPPSQRN EYTTLVAEQQ QLQADSKRFE EVLDELDKAL
QASEGELARN PFKQRSLQLQ EQIRALTEKK YELTEEERQS KRSPEELRAD LMAKIKRDNT
EVEQMTQQIR ELQDQIKKME ERVKSLGGAT SGAAAAEEKA NREKFEELLA KERDLNNFMD
GFPSRKAAKM QEKQQKEDGI VGVLEKMVKM QGIIGSNLPS QKKYKEMQDE LEYKKMQLEN
TQTTQERLKE ELTMRRTELE KIDTLEDKIK LELTQLAERQ EAMEKEMGEF GSVEDIQRKA
NAARERMEGL RSVLLKRKDL LRSIVAERGL KFQAKRAQLQ DHNLQVQLEK MEAKLKNLSA
GVFEMDEFIK AKESETNYRQ LASNIAALVD DLNVHVKKAV V
