ID   IF172_CHLRE             Reviewed;        1755 AA.
AC   Q5DM57;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=Intraflagellar transport protein 172;
GN   Name=IFT172; Synonyms=FLA11; ORFNames=CHLREDRAFT_183240;
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], INTERACTION WITH MAPRE1, AND MUTAGENESIS OF
RP   LEU-1615.
RX   PubMed=15694311; DOI=10.1016/j.cub.2005.01.037;
RA   Pedersen L.B., Miller M.S., Geimer S., Leitch J.M., Rosenbaum J.L.,
RA   Cole D.G.;
RT   "Chlamydomonas IFT172 is encoded by FLA11, interacts with CrEB1, and
RT   regulates IFT at the flagellar tip.";
RL   Curr. Biol. 15:262-266(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC-503, and cw92;
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   PROTEIN SEQUENCE OF 1243-1262, AND SUBCELLULAR LOCATION.
RX   PubMed=9585417; DOI=10.1083/jcb.141.4.993;
RA   Cole D.G., Diener D.R., Himelblau A.L., Beech P.L., Fuster J.C.,
RA   Rosenbaum J.L.;
RT   "Chlamydomonas kinesin-II-dependent intraflagellar transport (IFT): IFT
RT   particles contain proteins required for ciliary assembly in Caenorhabditis
RT   elegans sensory neurons.";
RL   J. Cell Biol. 141:993-1008(1998).
RN   [4]
RP   INTERACTION WITH THE INTRAFLAGELLAR TRANSPORT CORE B COMPLEX.
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   SUBCELLULAR LOCATION.
RX   PubMed=17326139; DOI=10.1002/cm.20195;
RA   Sloboda R.D., Howard L.;
RT   "Localization of EB1, IFT polypeptides, and kinesin-2 in Chlamydomonas
RT   flagellar axonemes via immunogold scanning electron microscopy.";
RL   Cell Motil. Cytoskeleton 64:446-460(2007).
CC   -!- FUNCTION: Required for the maintenance and formation of cilia and
CC       participates in the control of flagellar assembly/disassembly at the
CC       tip. Involved in regulating the transition between anterograde and
CC       retrograde intraflagellar transport at the tip.
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 microtubule
CC       end-binding protein 1 (MAPRE1/EB1). {ECO:0000269|PubMed:15694311,
CC       ECO:0000269|PubMed:15955805}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body
CC       {ECO:0000269|PubMed:17326139, ECO:0000269|PubMed:9585417}.
CC   -!- SIMILARITY: Belongs to the IFT172 family. {ECO:0000305}.
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DR   EMBL; AY615520; AAT99263.1; -; mRNA.
DR   EMBL; DS496120; EDP04848.1; -; Genomic_DNA.
DR   RefSeq; XP_001691740.1; XM_001691688.1.
DR   AlphaFoldDB; Q5DM57; -.
DR   STRING; 3055.EDP04848; -.
DR   PaxDb; Q5DM57; -.
DR   PRIDE; Q5DM57; -.
DR   EnsemblPlants; PNW70057; PNW70057; CHLRE_17g703900v5.
DR   GeneID; 5717250; -.
DR   Gramene; PNW70057; PNW70057; CHLRE_17g703900v5.
DR   KEGG; cre:CHLRE_17g703900v5; -.
DR   eggNOG; KOG3616; Eukaryota.
DR   HOGENOM; CLU_002716_0_0_1; -.
DR   InParanoid; Q5DM57; -.
DR   OMA; YQQLGMW; -.
DR   OrthoDB; 30851at2759; -.
DR   GO; GO:0036064; C:ciliary basal body; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0030992; C:intraciliary transport particle B; IDA:BHF-UCL.
DR   GO; GO:0031514; C:motile cilium; IDA:MGI.
DR   Gene3D; 2.130.10.10; -; 2.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR011044; Quino_amine_DH_bsu.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF50969; SSF50969; 1.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Cell projection; Cilium; Cytoplasm; Cytoskeleton; Developmental protein;
KW   Direct protein sequencing; Repeat; TPR repeat; WD repeat.
FT   CHAIN           1..1755
FT                   /note="Intraflagellar transport protein 172"
FT                   /id="PRO_0000328947"
FT   REPEAT          14..53
FT                   /note="WD 1"
FT   REPEAT          63..102
FT                   /note="WD 2"
FT   REPEAT          111..153
FT                   /note="WD 3"
FT   REPEAT          155..194
FT                   /note="WD 4"
FT   REPEAT          198..238
FT                   /note="WD 5"
FT   REPEAT          289..328
FT                   /note="WD 6"
FT   REPEAT          487..525
FT                   /note="WD 7"
FT   REPEAT          526..563
FT                   /note="WD 8"
FT   REPEAT          597..628
FT                   /note="TPR 1"
FT   REPEAT          696..729
FT                   /note="TPR 2"
FT   REPEAT          754..788
FT                   /note="TPR 3"
FT   REPEAT          813..846
FT                   /note="TPR 4"
FT   REPEAT          858..892
FT                   /note="TPR 5"
FT   REPEAT          916..949
FT                   /note="TPR 6"
FT   REPEAT          988..1023
FT                   /note="TPR 7"
FT   REPEAT          1048..1081
FT                   /note="TPR 8"
FT   REPEAT          1219..1252
FT                   /note="TPR 9"
FT   REPEAT          1285..1318
FT                   /note="TPR 10"
FT   REPEAT          1355..1388
FT                   /note="TPR 11"
FT   REPEAT          1455..1489
FT                   /note="TPR 12"
FT   REPEAT          1586..1619
FT                   /note="TPR 13"
FT   MUTAGEN         1615
FT                   /note="L->P: In fla11-ts; temperature-sensitive mutant that
FT                   leads to defects in intraflagellar transport particle
FT                   turnaround at the tip when transferred to nonpermissive
FT                   temperature."
FT                   /evidence="ECO:0000269|PubMed:15694311"
SQ   SEQUENCE   1755 AA;  197608 MW;  B283B44BE9988545 CRC64;
     MQLRYFKSIL PPADQYQKIT SLTWAPNNSR LAAVSTDKVV YLFDENGEKR DKFKTKAAEA
     NNPNTYIIRA MAFSPDSTKL AIAQSDNIVF IYRLVDPDTG AEKKSICNKF PQACAVTSLV
     WPKDRPNEVV FGLADGKVRL GMLKNNKSYT CYAHPENSYV VALASSLNGQ NVISGHMDGA
     IWKFNFPAEE GGTPTSSQLV VHSCVPYSLG WGSCIAAAGN DNRVVFYDLN GREIRSFDYS
     NNDEVREFTT CAFNPSGDTV VFGTYNRFYM YTFNIQRNDW EEAGHKQIDN FYAVSAASWK
     PDGSKMTVGS MTGAVDMYDA CVKRHMYKGK FEFTYVSKSA VIVKTLKTGM RIVLKSVYGY
     EIEKINIYHD RYLIARTTYT LLMGDLDTCK LSEIPWDSDG SEKFHFENER VCMVHYAGEL
     HIVEYGRNDV LGTCRTEHMN PYLISAVVQE ARGIASESKK LAYLIDLQTV RIQDLMAPVG
     STLATVNHDT KVDWLELNQR GTHLLFRDKK RHLHLFSLSG QERTTLLNYC QYVQWVPGSD
     VIVAQSRNNL CVWYSVNKPD NVTMFPIKGE VVDIERHNHR TEVIVDEGIN TVSYALDEAL
     IYFGAALEDQ DYERAVQTLE PLELTPETEA QWMQLAEQAL ATNQLVIAER CYAALGDIAK
     SRFLHKVVKK AQQAAKEFGG DGTDAWSVRA MMAQLNKQWP VSESLLLAQG KVDDAITLYQ
     DNHRWEDAIR VADSTHHANA AALKQQYLTW LLETGQEEQA GAVKEREGDY LAAIGLYLKG
     GLPGRAAQVV MSVHNVNWDP ALLDSILASL AKAGLYERAG ELYEHMSRSS EAMQSYRRGH
     AYRKAIDLAR REFPAEVIII EEEWGDWLVT QKQMDAAINH FIESGATLKA IKAAIDCRQF
     AKAAGIIEVL DPREAMPYFR RIAQHYETTG ALEEAERYYI RADMARDAVE MYSRAGKWEA
     AQRVARGYLT ESEMRAFYRA KAAEFEAAHK LKEAEKAYLA AGGDDVDKAI AMYKRNKMYD
     QMIRLVTQYR KEKVPEAHTL IAQQLEVEGN LREAEKHFVE AKDWKSAVQM YRQVNQWEDA
     LRVAKVYGGV NASKQVAYAW ALTLGGDDGA QLLKKMGLLD HAIEYAVESG AFAQAFEMTR
     AGAKHKLPEV HLKYAMFLED EGRFAEAEAE FISAGKPKEA CDMYMHNQDW DAAMRIAERY
     DPTMVSEILV SQARVAVERK QWLPAEGLFI KAKRPEAALK MYRDARMWND ALRVAEQYLP
     TKVAEVQMEL LSGQGAGGGS GGASADAVIN KARGFERNND YARAIETYLS LTAQDTSNQD
     QLEHCWGQAA QLAINYQRHR MKDVVNTVSE RLQEIGRHQA AGELHESIDD AQGAIRAYCA
     GRLWDKARTL AGTNPTFSRY IEDQYNNYLL QNQQADELAS RGGQHAQQAI EMYVARDEWA
     KVHELAAQQG PEVASNYALK HAERRFKQGD YAQAAQVFAQ HGITAQPQYF ELYKSIAQGV
     LHASQGDRNP VAEKSLRDMM YRLVNVLRSG GGAGKYKVDT DAFQNYYLAA HYLTCAAAAK
     EQGLKDIAAM NLTSVLRYVG PTIPADRAFY EAGLAWYEAG RKNMAFVMLN RFLDLSDAMD
     EPDSSAAVIE NADFSDTDIP YDFTIPERAY CTESQREDVR NLVLEISMDR SSDQSLALKA
     CEHCGKPTYE ANLTCHFCKK KYDPCVVTGY PIQSYDRVVF KNNGPELNAI RDMWNKWVEA
     FGTDPVTGMQ AAPMY