IFT27_CHLRE
ID IFT27_CHLRE Reviewed; 204 AA.
AC A8HN58;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Intraflagellar transport protein 27;
DE AltName: Full=Flagellar-associated protein 156;
GN Name=IFT27; Synonyms=FAP156; ORFNames=CHLREDRAFT_129193;
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 [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 [2]
RP IDENTIFICATION IN THE IFT COMPLEX B, AND SUBCELLULAR LOCATION.
RX PubMed=17276912; DOI=10.1016/j.cub.2006.12.040;
RA Qin H., Wang Z., Diener D., Rosenbaum J.;
RT "Intraflagellar transport protein 27 is a small G protein involved in cell-
RT cycle control.";
RL Curr. Biol. 17:193-202(2007).
RN [3]
RP INTERACTION WITH IFT25.
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 [4]
RP X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) IN COMPLEX WITH IFT27, GTP-BINDING,
RP FUNCTION, AND MUTAGENESIS OF SER-30; SER-79 AND VAL-194.
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: Small GTPase-like component of the intraflagellar transport
CC (IFT) complex B. Forms a subcomplex within the IFT complex B with
CC IFT25. Has very low GTPase activity either because it lacks the
CC conserved catalytic Gln in position 79 or because it requires some
CC GTPase-activating protein (GAP) for GTP turnover.
CC {ECO:0000269|PubMed:21505417}.
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; the
CC interaction is direct. {ECO:0000269|PubMed:17276912,
CC ECO:0000269|PubMed:19412537, ECO:0000269|PubMed:21505417}.
CC -!- INTERACTION:
CC A8HN58; B8LIX8: IFT25; NbExp=3; IntAct=EBI-8629375, EBI-8629367;
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum
CC {ECO:0000269|PubMed:17276912}. Cytoplasm, cytoskeleton, flagellum basal
CC body {ECO:0000269|PubMed:17276912}. Note=Colocalizes with IFT25 at the
CC distal-most portion of basal bodies, probably the transition zones, and
CC concentrates in the basal body region.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
CC -!- CAUTION: Although similar to the small GTPase superfamily, lacks the
CC conserved catalytic Gln in position 79 which is replaced by a Ser
CC residue, possibly explaining the weak GTPase activity. In contrast to
CC other members of the family, it is not prenylated (PubMed:21505417).
CC {ECO:0000305|PubMed:21505417}.
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DR EMBL; DS496108; EDP09483.1; -; Genomic_DNA.
DR RefSeq; XP_001689745.1; XM_001689693.1.
DR PDB; 2YC2; X-ray; 2.59 A; C/D=1-204.
DR PDB; 2YC4; X-ray; 2.80 A; C/D=1-204.
DR PDBsum; 2YC2; -.
DR PDBsum; 2YC4; -.
DR AlphaFoldDB; A8HN58; -.
DR SMR; A8HN58; -.
DR IntAct; A8HN58; 1.
DR MINT; A8HN58; -.
DR STRING; 3055.EDP09483; -.
DR PaxDb; A8HN58; -.
DR PRIDE; A8HN58; -.
DR EnsemblPlants; PNW88859; PNW88859; CHLRE_01g047950v5.
DR GeneID; 5715694; -.
DR Gramene; PNW88859; PNW88859; CHLRE_01g047950v5.
DR KEGG; cre:CHLRE_01g047950v5; -.
DR eggNOG; KOG0079; Eukaryota.
DR HOGENOM; CLU_041217_10_6_1; -.
DR InParanoid; A8HN58; -.
DR OMA; EMSVKEM; -.
DR OrthoDB; 1585129at2759; -.
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:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51419; RAB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell projection; Cilium; Cytoplasm; Cytoskeleton; Flagellum;
KW GTP-binding; Nucleotide-binding.
FT CHAIN 1..204
FT /note="Intraflagellar transport protein 27"
FT /id="PRO_0000424812"
FT BINDING 23..30
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 75..79
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 136..139
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MUTAGEN 30
FT /note="S->N: Impaired GTP-binding."
FT /evidence="ECO:0000269|PubMed:21505417"
FT MUTAGEN 79
FT /note="S->Q: Shows higher GTPase activity."
FT /evidence="ECO:0000269|PubMed:21505417"
FT MUTAGEN 194
FT /note="V->R: Does not affect interaction with IFT25."
FT /evidence="ECO:0000269|PubMed:21505417"
FT HELIX 8..10
FT /evidence="ECO:0007829|PDB:2YC2"
FT STRAND 12..21
FT /evidence="ECO:0007829|PDB:2YC2"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:2YC4"
FT HELIX 29..37
FT /evidence="ECO:0007829|PDB:2YC4"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:2YC2"
FT STRAND 65..75
FT /evidence="ECO:0007829|PDB:2YC2"
FT TURN 76..79
FT /evidence="ECO:0007829|PDB:2YC2"
FT HELIX 80..86
FT /evidence="ECO:0007829|PDB:2YC2"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:2YC2"
FT HELIX 105..121
FT /evidence="ECO:0007829|PDB:2YC2"
FT STRAND 130..136
FT /evidence="ECO:0007829|PDB:2YC2"
FT HELIX 149..158
FT /evidence="ECO:0007829|PDB:2YC2"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:2YC2"
FT HELIX 177..200
FT /evidence="ECO:0007829|PDB:2YC2"
SQ SEQUENCE 204 AA; 22760 MW; 2FA9BECF50CC0876 CRC64;
MVKKEVKPID ITATLRCKVA VVGEATVGKS ALISMFTSKG SKFLKDYAMT SGVEVVVAPV
TIPDTTVSVE LFLLDTAGSD LYKEQISQYW NGVYYAILVF DVSSMESFES CKAWFELLKS
ARPDRERPLR AVLVANKTDL PPQRHQVRLD MAQDWATTNT LDFFDVSANP PGKDADAPFL
SIATTFYRNY EDKVAAFQDA CRNY
