ID   TEKT_CHLRE              Reviewed;         482 AA.
AC   A8J8F6; Q7Y084;
DT   04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Tektin {ECO:0000305};
GN   ORFNames=CHLREDRAFT_24358 {ECO:0000312|EMBL:EDO99707.1};
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], SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=21gr / CC-1690;
RX   PubMed=14978211; DOI=10.1091/mbc.e03-11-0854;
RA   Yanagisawa H.A., Kamiya R.;
RT   "A tektin homologue is decreased in chlamydomonas mutants lacking an
RT   axonemal inner-arm dynein.";
RL   Mol. Biol. Cell 15:2105-2115(2004).
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   METHYLATION AT ARG-462.
RX   PubMed=24152136; DOI=10.1021/bi4011623;
RA   Werner-Peterson R., Sloboda R.D.;
RT   "Methylation of structural components of the axoneme occurs during
RT   flagellar disassembly.";
RL   Biochemistry 52:8501-8509(2013).
CC   -!- FUNCTION: Structural component of ciliary and flagellar microtubules.
CC       Plays a key role in the assembly or attachment of the inner dynein arm
CC       to microtubules in flagella and cilia. Forms filamentous polymers in
CC       the walls of ciliary and flagellar microtubules.
CC       {ECO:0000305|PubMed:14978211}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum axoneme
CC       {ECO:0000269|PubMed:14978211}. Cytoplasm, cytoskeleton, flagellum basal
CC       body {ECO:0000269|PubMed:14978211}.
CC   -!- PTM: Asymmetrically dimethylated at Arg-462 during flagellum
CC       resorption. Probably methylated by PRMT1.
CC       {ECO:0000269|PubMed:24152136}.
CC   -!- DISRUPTION PHENOTYPE: defects in axonemal inner-arm dynein.
CC       {ECO:0000269|PubMed:14978211}.
CC   -!- SIMILARITY: Belongs to the tektin family. {ECO:0000305}.
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DR   EMBL; AB111498; BAC77347.1; -; mRNA.
DR   EMBL; DS496144; EDO99707.1; -; Genomic_DNA.
DR   RefSeq; XP_001697824.1; XM_001697772.1.
DR   AlphaFoldDB; A8J8F6; -.
DR   SMR; A8J8F6; -.
DR   STRING; 3055.EDO99707; -.
DR   iPTMnet; A8J8F6; -.
DR   PaxDb; A8J8F6; -.
DR   PRIDE; A8J8F6; -.
DR   EnsemblPlants; PNW71473; PNW71473; CHLRE_16g655750v5.
DR   GeneID; 5723451; -.
DR   Gramene; PNW71473; PNW71473; CHLRE_16g655750v5.
DR   KEGG; cre:CHLRE_16g655750v5; -.
DR   eggNOG; KOG2685; Eukaryota.
DR   HOGENOM; CLU_566680_0_0_1; -.
DR   InParanoid; A8J8F6; -.
DR   OMA; RNLEDTH; -.
DR   OrthoDB; 958327at2759; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR   GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW.
DR   GO; GO:0060294; P:cilium movement involved in cell motility; IEA:InterPro.
DR   InterPro; IPR000435; Tektin.
DR   PANTHER; PTHR19960; PTHR19960; 1.
PE   1: Evidence at protein level;
KW   Cell projection; Cilium; Coiled coil; Cytoplasm; Cytoskeleton; Flagellum;
KW   Methylation.
FT   CHAIN           1..482
FT                   /note="Tektin"
FT                   /id="PRO_0000431950"
FT   REGION          311..330
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          100..129
FT                   /evidence="ECO:0000255"
FT   COILED          171..204
FT                   /evidence="ECO:0000255"
FT   COILED          282..324
FT                   /evidence="ECO:0000255"
FT   COILED          376..407
FT                   /evidence="ECO:0000255"
FT   COILED          441..478
FT                   /evidence="ECO:0000255"
FT   MOD_RES         462
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000269|PubMed:24152136"
FT   CONFLICT        77
FT                   /note="S -> N (in Ref. 1; BAC77347)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        224
FT                   /note="T -> A (in Ref. 1; BAC77347)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        464
FT                   /note="A -> V (in Ref. 1; BAC77347)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   482 AA;  52840 MW;  211B8A1AB10E0297 CRC64;
     MPSYNHTSNG VNMANFRALG GKNTGRGGTY RAPYEWTLES VEQMGLGATE NRMSSTLRDA
     SSQLQAVASA TVANDISIVD RALTTKLSQT ESLKNMLETC LAEVISEIAE LLSTKKRLEE
     RNGKVQAKIG VNSNRMQVRS SRPPREMTMD EVEKGLIKQQ GMLGSFSDRV ARAVAQVDRE
     VAQLEAVRAK LEADLRDKTE ALRVDEAVLS IPTDPTVEGT LSPTFRRGAA DCPPKTPHTW
     VRNTEDNLRN AHHWLADSAR LRKAIAHAVA NSRATEHDVA NRLNENMLAK VAATRNLRED
     LQAQLEKVRE EQARAKGQRS ALTSALDDKR GPLAQARERL AVRKARPCRE NVNDEVEAAL
     AKEVAHLAAV TQQLSVKVAA VDREIAALDA TAAQLESNIA DKDDALRVDE RVVLLDGRIN
     LAQRPPSSVA SFAMSDMSAP RTQTLARIRE LEASLTSARR EREAMESSIR QLRDTMGGGG
     AF