IFT81_CHLRE
ID IFT81_CHLRE Reviewed; 683 AA.
AC Q68RJ5;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Intraflagellar transport protein 81;
GN Name=IFT81; ORFNames=CHLREDRAFT_138649;
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], AND IDENTIFICATION IN THE IFT COMPLEX B.
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 [2]
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 [3]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-225, FUNCTION, SUBCELLULAR
RP LOCATION, IDENTIFICATION IN THE IFT COMPLEX B, AND INTERACTION WITH TUBULIN
RP AND IFT74.
RX PubMed=23990561; DOI=10.1126/science.1240985;
RA Bhogaraju S., Cajanek L., Fort C., Blisnick T., Weber K., Taschner M.,
RA Mizuno N., Lamla S., Bastin P., Nigg E.A., Lorentzen E.;
RT "Molecular basis of tubulin transport within the cilium by IFT74 and
RT IFT81.";
RL Science 341:1009-1012(2013).
CC -!- FUNCTION: Component of the intraflagellar transport (IFT) complex B:
CC together with IFT74, forms a tubulin-binding module that specifically
CC mediates transport of tubulin within the cilium. Binds tubulin via its
CC CH (calponin-homology)-like region. Required for ciliogenesis.
CC {ECO:0000269|PubMed:23990561}.
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 IFT81; the
CC interaction is direct: within the IFT complex B, IFT74 and IFT81
CC mediate the transport of tubulin within the cilium. Interacts with
CC tubulin; interaction is direct. {ECO:0000269|PubMed:15955805,
CC ECO:0000269|PubMed:23990561}.
CC -!- INTERACTION:
CC Q68RJ5; Q68K27: IFT140; NbExp=2; IntAct=EBI-958528, EBI-958534;
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000305|PubMed:23990561}.
CC -!- DOMAIN: The CH (calponin-homology)-like region shows high similarity to
CC a CH (calponin-homology) domain and mediated binding to the globular
CC domain of tubulin. {ECO:0000269|PubMed:23990561}.
CC -!- SIMILARITY: Belongs to the IFT81 family. {ECO:0000305}.
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DR EMBL; AY615519; AAT99262.1; -; mRNA.
DR EMBL; DS496139; EDP00479.1; -; Genomic_DNA.
DR RefSeq; XP_001697224.1; XM_001697172.1.
DR PDB; 4LVP; X-ray; 2.32 A; A=1-126.
DR PDB; 4LVR; X-ray; 2.60 A; A=1-124.
DR PDBsum; 4LVP; -.
DR PDBsum; 4LVR; -.
DR AlphaFoldDB; Q68RJ5; -.
DR SMR; Q68RJ5; -.
DR IntAct; Q68RJ5; 2.
DR STRING; 3055.EDP00479; -.
DR PaxDb; Q68RJ5; -.
DR PRIDE; Q68RJ5; -.
DR EnsemblPlants; PNW70526; PNW70526; CHLRE_17g723600v5.
DR GeneID; 5722735; -.
DR Gramene; PNW70526; PNW70526; CHLRE_17g723600v5.
DR KEGG; cre:CHLRE_17g723600v5; -.
DR eggNOG; ENOG502QSBR; Eukaryota.
DR HOGENOM; CLU_017012_1_0_1; -.
DR InParanoid; Q68RJ5; -.
DR OMA; WILTHME; -.
DR OrthoDB; 301582at2759; -.
DR GO; GO:0045177; C:apical part of cell; IDA:BHF-UCL.
DR GO; GO:0030992; C:intraciliary transport particle B; IDA:UniProtKB.
DR GO; GO:0031514; C:motile cilium; IDA:BHF-UCL.
DR GO; GO:0015631; F:tubulin binding; IDA:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0035735; P:intraciliary transport involved in cilium assembly; IMP:UniProtKB.
DR Gene3D; 1.10.418.70; -; 1.
DR InterPro; IPR029600; IFT81.
DR InterPro; IPR041146; IFT81_CH.
DR InterPro; IPR043016; IFT81_N_sf.
DR PANTHER; PTHR15614; PTHR15614; 1.
DR Pfam; PF18383; IFT81_CH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell projection; Cilium; Cilium biogenesis/degradation;
KW Coiled coil.
FT CHAIN 1..683
FT /note="Intraflagellar transport protein 81"
FT /id="PRO_0000424814"
FT REGION 1..122
FT /note="CH (calponin-homology)-like region"
FT COILED 134..387
FT /evidence="ECO:0000255"
FT COILED 587..618
FT /evidence="ECO:0000255"
FT HELIX 1..11
FT /evidence="ECO:0007829|PDB:4LVP"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:4LVP"
FT HELIX 22..26
FT /evidence="ECO:0007829|PDB:4LVP"
FT HELIX 30..44
FT /evidence="ECO:0007829|PDB:4LVP"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:4LVP"
FT HELIX 58..71
FT /evidence="ECO:0007829|PDB:4LVP"
FT HELIX 81..90
FT /evidence="ECO:0007829|PDB:4LVP"
FT HELIX 93..103
FT /evidence="ECO:0007829|PDB:4LVP"
FT HELIX 107..114
FT /evidence="ECO:0007829|PDB:4LVP"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:4LVP"
SQ SEQUENCE 683 AA; 77073 MW; 767A22450BCF3B1A CRC64;
MGDVSYIVDS LGLPPFSYQM SLLSFTEKGP QELLQLLSDV FSTISPKHQK VDVAKEVPDQ
TADRLIGFLK IIKYRPNVQD PLLFRQLVAA GDRETLYQIL RWVVPQAQLL EKRAFVGYYL
SFPDMPEEFN FDPDIMELKE EIKAMQQEFI ELHKSSDAIK TLSKDTQALK NKIKSLEEEK
ERLGEKVERA KGAVDKLPDR SSYMEVCTNL RKQQDEEVNL STAIQTQRAL QEKAEASYHR
AAARLRELQT SYQEGSAGKL LETLNEDVKN LRAQVNERYP KEVEKRQKRQ AALSEALASG
ISTEMDLQRL QHQATALHNQ ITEIQERKVA QDKARQGDKA YLQLRQAQQM ATVSARKKEE
LGAKQERLQE KKTALTAQLD KLNAEGGGSG AVFSEEEWRT KYESMKSKLP IYKKMKKELG
DLEAEVFVLA HTEELLASQE GGLLEKVKRL EKQQGISGFT ETAQHLEKVS EAKSQMDEEK
GMTLIEISRT VEEINNAINQ RKQQLAPQIK KLRSVRQDFA EFEAKYLEKK TAYDNVVATF
EARTSALEGE VSGLKAEVSE NETKYHMLHC QLHITDQNIK KVTSGPAAER LRDKYEAKVK
EAEDSTKALR DRQREIKDTH STGLSQIDIM NDMLRLLQLK LNLARGIAVD MSQYGGGGGA
AGGANGGMAG QTYDTGSANV LQL
