ID   IFT22_CHLRE             Reviewed;         192 AA.
AC   A8HME3;
DT   11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Intraflagellar transport protein 22;
DE   AltName: Full=Flagellar-associated protein 9;
GN   Name=FAP9; ORFNames=CHLREDRAFT_195877;
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   NUCLEOTIDE SEQUENCE [MRNA].
RA   Qin H., Rosenbaum J.L.;
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE IFT COMPLEX B.
RX   PubMed=22076686; DOI=10.1002/cm.20546;
RA   Silva D.A., Huang X., Behal R.H., Cole D.G., Qin H.;
RT   "The RABL5 homolog IFT22 regulates the cellular pool size and the amount of
RT   IFT particles partitioned to the flagellar compartment in Chlamydomonas
RT   reinhardtii.";
RL   Cytoskeleton 69:33-48(2012).
CC   -!- FUNCTION: Component of the intraflagellar transport (IFT) complex B.
CC       Functions in regulating the cellular pool size of both complex A and
CC       complex B and thus plays a critical role in determining the cellular
CC       availability of IFT particles. {ECO:0000269|PubMed:22076686}.
CC   -!- SUBUNIT: Component of the IFT complex B, composed of IFT88, IFT70,
CC       IFT52, IFT46, IFT27, IFT25 and IFT22. {ECO:0000269|PubMed:22076686}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum
CC       {ECO:0000269|PubMed:22076686}.
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 67 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:22076686) and
CC       unlikely to associate directly with membranes.
CC       {ECO:0000305|PubMed:22076686}.
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DR   EMBL; DS496108; EDP09407.1; -; Genomic_DNA.
DR   EMBL; EF593954; ABU90456.1; -; mRNA.
DR   RefSeq; XP_001689669.1; XM_001689617.1.
DR   AlphaFoldDB; A8HME3; -.
DR   SMR; A8HME3; -.
DR   STRING; 3055.EDP09407; -.
DR   PaxDb; A8HME3; -.
DR   PRIDE; A8HME3; -.
DR   EnsemblPlants; PNW88659; PNW88659; CHLRE_01g039200v5.
DR   GeneID; 5715530; -.
DR   Gramene; PNW88659; PNW88659; CHLRE_01g039200v5.
DR   KEGG; cre:CHLRE_01g039200v5; -.
DR   eggNOG; ENOG502RXD4; Eukaryota.
DR   HOGENOM; CLU_1416996_0_0_1; -.
DR   InParanoid; A8HME3; -.
DR   OrthoDB; 1428809at2759; -.
DR   GO; GO:0031514; C:motile cilium; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   1: Evidence at protein level;
KW   Cell projection; Cilium; Flagellum; GTP-binding; Nucleotide-binding.
FT   CHAIN           1..192
FT                   /note="Intraflagellar transport protein 22"
FT                   /id="PRO_0000429420"
FT   BINDING         12..19
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         62..69
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   192 AA;  21343 MW;  138EEC1B70A9C700 CRC64;
     MAEHGLKIAV VGPQRTGKTL LCRALAEQPI LLGEMSYQPT AAVRIQEISR VLGIDRVKVQ
     FWDVSGSVQY QSYWPVLAKE VDGLLMVIDP NRPEQERDLE TFYRNFAEPN NLYTRQCMVM
     AIQVQKEGGG LGGWQGLQGG LKKLSQSYVA INPANPAAGV QEAYSHLDVL FQGALQSKKE
     ALESSYMNQE DQ