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 18-JAN-2017, entry version 77.
DE RecName: Full=Intraflagellar transport protein 172;
GN Name=IFT172; Synonyms=FLA11; ORFNames=CHLREDRAFT_183240;
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; Chlorophyceae;
OC Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH MAPRE1, AND MUTAGENESIS
RP OF 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.,
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 [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):
RT IFT particles contain proteins required for ciliary assembly in
RT Caenorhabditis 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.,
RA Rosenbaum J.L., Cole D.G.;
RT "Characterization of the intraflagellar transport complex B core:
RT direct 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
CC the tip. Involved in regulating the transition between anterograde
CC and retrograde intraflagellar transport at the tip.
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 microtubule end-binding protein 1 (MAPRE1/EB1).
CC {ECO:0000269|PubMed:15694311, 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}.
CC -!- SIMILARITY: Contains 13 TPR repeats. {ECO:0000305}.
CC -!- SIMILARITY: Contains 8 WD repeats. {ECO:0000255|PROSITE-
CC ProRule:PRU00221}.
DR EMBL; AY615520; AAT99263.1; -; mRNA.
DR EMBL; DS496120; EDP04848.1; -; Genomic_DNA.
DR RefSeq; XP_001691740.1; XM_001691688.1.
DR UniGene; Cre.13782; -.
DR ProteinModelPortal; Q5DM57; -.
DR STRING; 3055.EDP04848; -.
DR PaxDb; Q5DM57; -.
DR EnsemblPlants; EDP04848; EDP04848; CHLREDRAFT_183240.
DR GeneID; 5717250; -.
DR Gramene; EDP04848; EDP04848; CHLREDRAFT_183240.
DR KEGG; cre:CHLREDRAFT_183240; -.
DR eggNOG; KOG3616; Eukaryota.
DR eggNOG; ENOG410XR2C; LUCA.
DR InParanoid; Q5DM57; -.
DR KO; K19676; -.
DR OMA; EDIHLKN; -.
DR Proteomes; UP000006906; Unassembled WGS sequence.
DR GO; GO:0005930; C:axoneme; IBA:GO_Central.
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 GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
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.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR017986; WD40_repeat_dom.
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; Complete proteome; Cytoplasm; Cytoskeleton;
KW Developmental protein; Direct protein sequencing; Reference proteome;
KW Repeat; TPR repeat; WD repeat.
FT CHAIN 1 1755 Intraflagellar transport protein 172.
FT /FTId=PRO_0000328947.
FT REPEAT 14 53 WD 1.
FT REPEAT 63 102 WD 2.
FT REPEAT 111 153 WD 3.
FT REPEAT 155 194 WD 4.
FT REPEAT 198 238 WD 5.
FT REPEAT 289 328 WD 6.
FT REPEAT 487 525 WD 7.
FT REPEAT 526 563 WD 8.
FT REPEAT 597 628 TPR 1.
FT REPEAT 696 729 TPR 2.
FT REPEAT 754 788 TPR 3.
FT REPEAT 813 846 TPR 4.
FT REPEAT 858 892 TPR 5.
FT REPEAT 916 949 TPR 6.
FT REPEAT 988 1023 TPR 7.
FT REPEAT 1048 1081 TPR 8.
FT REPEAT 1219 1252 TPR 9.
FT REPEAT 1285 1318 TPR 10.
FT REPEAT 1355 1388 TPR 11.
FT REPEAT 1455 1489 TPR 12.
FT REPEAT 1586 1619 TPR 13.
FT MUTAGEN 1615 1615 L->P: In fla11-ts; temperature-sensitive
FT mutant that leads to defects in
FT intraflagellar transport particle
FT turnaround at the tip when transferred to
FT nonpermissive temperature.
FT {ECO:0000269|PubMed:15694311}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 12 102 iprf:WD_REPEATS_REGION [T]
FT MYHIT 55 93 ismart:WD40 [T]
FT MYHIT 103 142 ismart:WD40 [T]
FT MYHIT 284 319 ismart:WD40 [T]
FT MYHIT 826 855 iprf:IQ [T]
FT MYHIT 230 272 ismart:WD40 [T]
FT MYHIT 144 185 ismart:WD40 [T]
FT MYHIT 9 44 ismart:WD40 [T]
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
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