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 02-NOV-2016, entry version 55.
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; Chlorophyceae;
OC 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.,
RA Marechal-Drouard L., Marshall W.F., Qu L.H., Nelson D.R.,
RA Sanderfoot A.A., Spalding M.H., Kapitonov V.V., Ren Q., Ferris P.,
RA Lindquist E., Shapiro H., Lucas S.M., Grimwood J., Schmutz J.,
RA Cardol P., Cerutti H., Chanfreau G., Chen C.L., Cognat V., Croft M.T.,
RA Dent R., Dutcher S., Fernandez E., Fukuzawa H., Gonzalez-Ballester D.,
RA Gonzalez-Halphen D., Hallmann A., Hanikenne M., Hippler M., Inwood W.,
RA Jabbari K., Kalanon M., Kuras R., Lefebvre P.A., Lemaire S.D.,
RA Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L., Mittag M.,
RA Mittelmeier T., Moroney J.V., Moseley J., Napoli C., Nedelcu A.M.,
RA Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.J., Purton S.,
RA Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L., Schroda M.,
RA Stern D., Umen J., Willows R., Wilson N., Zimmer S.L., Allmer J.,
RA 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.,
RA Jorgensen R., Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T.,
RA Brokstein P., Dubchak I., Goodstein D., Hornick L., Huang Y.W.,
RA Jhaveri J., Luo Y., Martinez D., Ngau W.C., Otillar B., Poliakov A.,
RA Porter A., Szajkowski L., Werner G., Zhou K., Grigoriev I.V.,
RA Rokhsar D.S., Grossman A.R.;
RT "The Chlamydomonas genome reveals the evolution of key animal and
RT plant 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
RT cell-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
RT component of IFT complex B and physically interacts with IFT27 in
RT Chlamydomonas.";
RL PLoS ONE 4:E5384-E5384(2009).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) IN COMPLEX WITH IFT27,
RP GTP-BINDING, 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
CC transport (IFT) complex B. Forms a subcomplex within the IFT
CC complex B with IFT25. Has very low GTPase activity either because
CC it lacks the conserved catalytic Gln in position 79 or because it
CC requires some GTPase-activating protein (GAP) for GTP turnover.
CC {ECO:0000269|PubMed:21505417}.
CC -!- SUBUNIT: Component of the IFT complex B, the core composed of
CC IFT25, IFT27, IFT46, IFT52, IFT74, IFT81 and IFT88 as well as
CC associated subunits IFT20, IFT57, IFT80 and IFT172. Interacts with
CC IFT25; the interaction is direct. {ECO:0000269|PubMed:17276912,
CC ECO:0000269|PubMed:19412537, ECO:0000269|PubMed:21505417}.
CC -!- INTERACTION:
CC B8LIX8:IFT25; NbExp=3; IntAct=EBI-8629375, EBI-8629367;
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum
CC {ECO:0000269|PubMed:17276912}. Cytoplasm, cytoskeleton, flagellum
CC basal body {ECO:0000269|PubMed:17276912}. Note=Colocalizes with
CC IFT25 at the distal-most portion of basal bodies, probably the
CC transition zones, and 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
CC the conserved catalytic Gln in position 79 which is replaced by a
CC Ser residue, possibly explaining the weak GTPase activity. In
CC contrast to other members of the family, it is not prenylated
CC (PubMed:21505417). {ECO:0000305|PubMed:21505417}.
DR EMBL; DS496108; EDP09483.1; -; Genomic_DNA.
DR RefSeq; XP_001689745.1; XM_001689693.1.
DR UniGene; Cre.3218; -.
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 ProteinModelPortal; A8HN58; -.
DR SMR; A8HN58; -.
DR IntAct; A8HN58; 1.
DR MINT; MINT-8184259; -.
DR STRING; 3055.EDP09483; -.
DR PaxDb; A8HN58; -.
DR EnsemblPlants; EDP09483; EDP09483; CHLREDRAFT_129193.
DR GeneID; 5715694; -.
DR Gramene; EDP09483; EDP09483; CHLREDRAFT_129193.
DR KEGG; cre:CHLREDRAFT_129193; -.
DR eggNOG; KOG0079; Eukaryota.
DR eggNOG; ENOG4111IWZ; LUCA.
DR InParanoid; A8HN58; -.
DR KO; K07934; -.
DR OMA; FHCLAKQ; -.
DR Proteomes; UP000006906; Unassembled WGS sequence.
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:0007264; P:small GTPase mediated signal transduction; 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 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; Complete proteome; Cytoplasm;
KW Cytoskeleton; GTP-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1 204 Intraflagellar transport protein 27.
FT /FTId=PRO_0000424812.
FT NP_BIND 23 30 GTP. {ECO:0000250}.
FT NP_BIND 75 79 GTP. {ECO:0000250}.
FT NP_BIND 136 139 GTP. {ECO:0000250}.
FT MUTAGEN 30 30 S->N: Impaired GTP-binding.
FT {ECO:0000269|PubMed:21505417}.
FT MUTAGEN 79 79 S->Q: Shows higher GTPase activity.
FT {ECO:0000269|PubMed:21505417}.
FT MUTAGEN 194 194 V->R: Does not affect interaction with
FT IFT25. {ECO:0000269|PubMed:21505417}.
FT HELIX 8 10 {ECO:0000244|PDB:2YC2}.
FT STRAND 12 21 {ECO:0000244|PDB:2YC2}.
FT HELIX 25 27 {ECO:0000244|PDB:2YC4}.
FT HELIX 29 37 {ECO:0000244|PDB:2YC4}.
FT STRAND 58 61 {ECO:0000244|PDB:2YC2}.
FT STRAND 65 75 {ECO:0000244|PDB:2YC2}.
FT TURN 76 79 {ECO:0000244|PDB:2YC2}.
FT HELIX 80 86 {ECO:0000244|PDB:2YC2}.
FT STRAND 95 101 {ECO:0000244|PDB:2YC2}.
FT HELIX 105 121 {ECO:0000244|PDB:2YC2}.
FT STRAND 130 136 {ECO:0000244|PDB:2YC2}.
FT HELIX 149 158 {ECO:0000244|PDB:2YC2}.
FT STRAND 162 165 {ECO:0000244|PDB:2YC2}.
FT HELIX 177 200 {ECO:0000244|PDB:2YC2}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 18 184 ipfam:Ras [T]
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
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