ID   CFA73_CHLRE             Reviewed;         308 AA.
AC   M1V4Y8; A8JB86;
DT   05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2013, sequence version 1.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=Cilia- and flagella-associated protein 73 {ECO:0000305};
DE   AltName: Full=Flagella-associated protein 73 {ECO:0000305|PubMed:23569216};
DE   AltName: Full=Modifier of inner arms 2 protein {ECO:0000303|PubMed:23569216};
DE            Short=Mia2p {ECO:0000303|PubMed:23569216};
GN   Name=FAP73 {ECO:0000303|PubMed:23569216};
GN   Synonyms=MIA2 {ECO:0000303|PubMed:23569216};
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], FUNCTION, INTERACTION WITH FAP100, SUBCELLULAR
RP   LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=23569216; DOI=10.1083/jcb.201211048;
RA   Yamamoto R., Song K., Yanagisawa H., Fox L., Yagi T., Wirschell M.,
RA   Hirono M., Kamiya R., Nicastro D., Sale W.S.;
RT   "The MIA complex is a conserved and novel dynein regulator essential for
RT   normal ciliary motility.";
RL   J. Cell Biol. 201:263-278(2013).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 14-253.
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).
CC   -!- FUNCTION: As part of MIA, a complex associated with the outer doublet
CC       microtubules of the axoneme, may play a role in ciliary/flagellar
CC       motility by regulating the assembly and the activity of inner dynein
CC       arm. {ECO:0000269|PubMed:23569216}.
CC   -!- SUBUNIT: Interacts with FAP100; form the modifier of inner arm (MIA)
CC       complex. {ECO:0000269|PubMed:23569216}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum axoneme
CC       {ECO:0000269|PubMed:23569216}. Note=Localizes to the outer doublet
CC       microtubules of the axoneme. {ECO:0000269|PubMed:23569216}.
CC   -!- DISRUPTION PHENOTYPE: The mia2 mutants do not express the protein in
CC       the axoneme and display slightly jerky, slow swimming phenotypes,
CC       reduced flagellar beat frequencies and defective phototaxis.
CC       {ECO:0000269|PubMed:23569216}.
CC   -!- SIMILARITY: Belongs to the CFAP73 family. {ECO:0000305}.
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DR   EMBL; AB692781; BAM95826.1; -; mRNA.
DR   EMBL; DS496152; EDO98890.1; -; Genomic_DNA.
DR   RefSeq; XP_001699250.1; XM_001699198.1.
DR   AlphaFoldDB; M1V4Y8; -.
DR   SMR; M1V4Y8; -.
DR   STRING; 3055.EDO98890; -.
DR   EnsemblPlants; PNW71820; PNW71820; CHLRE_16g689600v5.
DR   GeneID; 5724743; -.
DR   Gramene; PNW71820; PNW71820; CHLRE_16g689600v5.
DR   KEGG; cre:CHLRE_16g689600v5; -.
DR   eggNOG; ENOG502QRZS; Eukaryota.
DR   OMA; QYYKFIQ; -.
DR   OrthoDB; 1528754at2759; -.
DR   GO; GO:0097545; C:axonemal outer doublet; IDA:UniProtKB.
DR   GO; GO:0031514; C:motile cilium; IDA:UniProtKB.
DR   GO; GO:0070840; F:dynein complex binding; IDA:UniProtKB.
DR   GO; GO:0048870; P:cell motility; IMP:UniProtKB.
DR   GO; GO:0003341; P:cilium movement; IMP:UniProtKB.
DR   GO; GO:0036159; P:inner dynein arm assembly; IMP:UniProtKB.
DR   InterPro; IPR025252; DUF4200.
DR   Pfam; PF13863; DUF4200; 1.
PE   1: Evidence at protein level;
KW   Cell projection; Cilium; Coiled coil; Cytoplasm; Cytoskeleton; Flagellum.
FT   CHAIN           1..308
FT                   /note="Cilia- and flagella-associated protein 73"
FT                   /id="PRO_0000437482"
FT   COILED          103..134
FT                   /evidence="ECO:0000255"
FT   COILED          164..227
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   308 AA;  35614 MW;  BA283C7AA8A67DD2 CRC64;
     MDEEGSATAR AKMMPQTLVL DHVSPATRLL EKRRQMFEVQ EALEAQKQDF NRKEEVFKRR
     EEALKLKDLE LQESLIRFSK FLQENDSKRA RAEKKANDEI KARIQKEKEI EQLTEVLEEL
     KSEKERILEV LEKNMRYQHY LESVLEVADE YQEVADLLLR HATLSATNAD LKDHQRKCSE
     LAEKVRTELQ IYVKQKTDEI LNLNNQVAKL KTELEGYEAE AMVQEAKKDS SLQIASQRTL
     EYGQVVLSAD NIFNRCRSKS SIGHPAESNP LHQLDVIGNF VSDLGSIIKQ FKQEQAKRAS
     LASRAEIE