IFT25_CHLRE
ID IFT25_CHLRE Reviewed; 189 AA.
AC B8LIX8; A8HZT2;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Intraflagellar transport protein 25;
DE AltName: Full=Flagellar-associated protein 232;
GN Name=IFT25; Synonyms=FAP232; ORFNames=CHLREDRAFT_98791;
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], PROTEIN SEQUENCE OF 98-108 AND 129-15,
RP FUNCTION, IDENTIFICATION IN THE IFT COMPLEX B, SUBCELLULAR LOCATION,
RP INTERACTION WITH IFT27, AND PHOSPHORYLATION.
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 [2]
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 [3]
RP IDENTIFICATION IN THE IFT COMPLEX B, 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 [4]
RP X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 1-135 IN COMPLEX WITH CALCIUM AND
RP IFT27, INTERACTION WITH IFT27, AND MUTAGENESIS OF ASP-30; THR-35;
RP 38-VAL--THR-40 AND THR-125.
RX PubMed=21505417; DOI=10.1038/emboj.2011.110;
RA Bhogaraju S., Taschner M., Morawetz M., Basquin C., Lorentzen E.;
RT "Crystal structure of the intraflagellar transport complex 25/27.";
RL EMBO J. 30:1907-1918(2011).
CC -!- FUNCTION: Component of the intraflagellar transport (IFT) complex B.
CC Forms a subcomplex within the IFT complex B with IFT27.
CC {ECO:0000269|PubMed:19412537}.
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 IFT27; the
CC interaction is direct. {ECO:0000269|PubMed:19382199,
CC ECO:0000269|PubMed:19412537, ECO:0000269|PubMed:21505417}.
CC -!- INTERACTION:
CC B8LIX8; A8HN58: IFT27; NbExp=3; IntAct=EBI-8629367, EBI-8629375;
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum. Cytoplasm,
CC cytoskeleton, flagellum basal body. Note=Colocalizes with IFT27 at the
CC distal-most portion of basal bodies, probably the transition zones, and
CC concentrates in the basal body region.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:19412537}.
CC -!- SIMILARITY: Belongs to the IFT25 family. {ECO:0000305}.
CC -!- CAUTION: Was initially classified as a member of the small heat shock
CC family protein. However, it was later shown that it is not the case
CC (PubMed:21505417). {ECO:0000305|PubMed:21505417}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDP08000.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; EF593953; ABU90455.1; -; mRNA.
DR EMBL; DS496111; EDP08000.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001698507.1; XM_001698455.1.
DR PDB; 2YC2; X-ray; 2.59 A; A/B=1-135.
DR PDB; 2YC4; X-ray; 2.80 A; A/B=1-135.
DR PDBsum; 2YC2; -.
DR PDBsum; 2YC4; -.
DR AlphaFoldDB; B8LIX8; -.
DR SMR; B8LIX8; -.
DR IntAct; B8LIX8; 1.
DR MINT; B8LIX8; -.
DR STRING; 3055.EDP08000; -.
DR PaxDb; B8LIX8; -.
DR PRIDE; B8LIX8; -.
DR EnsemblPlants; PNW77755; PNW77755; CHLRE_10g450350v5.
DR GeneID; 5723882; -.
DR Gramene; PNW77755; PNW77755; CHLRE_10g450350v5.
DR KEGG; cre:CHLRE_10g450350v5; -.
DR eggNOG; KOG3437; Eukaryota.
DR HOGENOM; CLU_132151_0_0_1; -.
DR OMA; EHTEGHL; -.
DR OrthoDB; 1454920at2759; -.
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; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042073; P:intraciliary transport; IEA:InterPro.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR033558; IFT25.
DR PANTHER; PTHR33906; PTHR33906; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell projection; Cilium; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Flagellum; Metal-binding.
FT CHAIN 1..189
FT /note="Intraflagellar transport protein 25"
FT /id="PRO_0000424811"
FT REGION 135..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:21505417"
FT BINDING 30
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:21505417"
FT BINDING 32
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:21505417"
FT BINDING 35
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:21505417"
FT BINDING 127
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:21505417"
FT MUTAGEN 30
FT /note="D->A: Does not affect interaction with IFT27."
FT /evidence="ECO:0000269|PubMed:21505417"
FT MUTAGEN 35
FT /note="T->A: Does not affect interaction with IFT27."
FT /evidence="ECO:0000269|PubMed:21505417"
FT MUTAGEN 38..40
FT /note="VTT->RAR: Abolishes interaction with IFT27; when
FT associated with E-125."
FT /evidence="ECO:0000269|PubMed:21505417"
FT MUTAGEN 125
FT /note="T->E: Abolishes interaction with IFT27; when
FT associated with 38-R--R-40."
FT /evidence="ECO:0000269|PubMed:21505417"
FT CONFLICT 101
FT /note="E -> EV (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:2YC4"
FT HELIX 25..29
FT /evidence="ECO:0007829|PDB:2YC2"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:2YC2"
FT STRAND 45..75
FT /evidence="ECO:0007829|PDB:2YC2"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:2YC2"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:2YC2"
FT STRAND 99..122
FT /evidence="ECO:0007829|PDB:2YC2"
FT STRAND 125..134
FT /evidence="ECO:0007829|PDB:2YC2"
SQ SEQUENCE 189 AA; 20360 MW; EAD121E6AAE928EB CRC64;
MKDYAREENG GLVVMASCSD ERFPPENMLD GKDNTFWVTT GMFPQEFVLR LESCIRVSKI
TTLSLNVRKL AVEKCDQDKP DQFEKVFEVE LANRGDRLQT EVHQVNIRAK YLKFILLQGH
GEFATVNRVS VVGGDDDGGG YDEPGGGYGS MQRQPSMGYG GGGGSAATGF AADPGNAAAG
GGGGFEDEF
