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CP100_CHLRE
ID   CP100_CHLRE             Reviewed;         576 AA.
AC   A8I4E9;
DT   05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Cilia- and flagella-associated protein 100 {ECO:0000305};
DE   AltName: Full=Flagella-associated protein 100 {ECO:0000305|PubMed:23569216};
DE   AltName: Full=Modifier of inner arms 1 protein {ECO:0000303|PubMed:23569216};
DE            Short=Mia1p {ECO:0000303|PubMed:23569216};
GN   Name=FAP100 {ECO:0000303|PubMed:23569216};
GN   Synonyms=MIA1 {ECO:0000303|PubMed:23569216};
GN   ORFNames=CHLREDRAFT_186878 {ECO:0000312|EMBL:EDP07473.1};
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], FUNCTION, INTERACTION WITH FAP73, 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].
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).
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 axonemal inner
CC       dynein arm. {ECO:0000269|PubMed:23569216}.
CC   -!- SUBUNIT: Interacts with FAP73; 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 mia1-1, mia1-2, mia1-3 and mia1-4 mutants do
CC       not express the protein in the axoneme and display slightly jerky, slow
CC       swimming phenotypes, reduced flagellar beat frequencies and defective
CC       phototaxis. {ECO:0000269|PubMed:23569216}.
CC   -!- SIMILARITY: Belongs to the CFAP100 family. {ECO:0000305}.
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DR   EMBL; AB692780; BAM95825.1; -; mRNA.
DR   EMBL; DS496112; EDP07473.1; -; Genomic_DNA.
DR   RefSeq; XP_001699777.1; XM_001699725.1.
DR   AlphaFoldDB; A8I4E9; -.
DR   SMR; A8I4E9; -.
DR   STRING; 3055.EDP07473; -.
DR   PaxDb; A8I4E9; -.
DR   PRIDE; A8I4E9; -.
DR   EnsemblPlants; PNW86981; PNW86981; CHLRE_02g103950v5.
DR   GeneID; 5725540; -.
DR   Gramene; PNW86981; PNW86981; CHLRE_02g103950v5.
DR   KEGG; cre:CHLRE_02g103950v5; -.
DR   eggNOG; ENOG502QSDI; Eukaryota.
DR   HOGENOM; CLU_026271_0_0_1; -.
DR   InParanoid; A8I4E9; -.
DR   OMA; YKIYKDF; -.
DR   OrthoDB; 1092113at2759; -.
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..576
FT                   /note="Cilia- and flagella-associated protein 100"
FT                   /id="PRO_0000437480"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          417..439
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          495..519
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          538..563
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          125..226
FT                   /evidence="ECO:0000255"
FT   COILED          254..311
FT                   /evidence="ECO:0000255"
FT   COILED          342..408
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        417..436
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   576 AA;  65169 MW;  FD5CF6AE975E6C8D CRC64;
     MPIYDEASVP GTAAGRSTTD VGATAGANPF NIPADEEIFR FREEERARKE QDKLIAQTMR
     VADKTTFAAQ MQATATADAR TLLRELRPPK GPKATTTLAA SSVGTLDRRK EKENMADFIA
     KKREIFLLQM SLDTKRAEIK KLEERARQRE EALKKSEQML EEDALRFDAF LKENDEKVQE
     AIKKAEAEAK AKQDKVLEIK RLNTATAALR SELNKYEEQL EDCRRYKEFL DSITPPEWFE
     QQAAKLQRRK DALVAEWQSQ CEALKQRREA ALAAKTAAES DYANARTQQQ AERAERAIKE
     SVAALKEIMK EKEPQPPNLD FEMDPEDEEM YFQEPGQLLA VYKQLEESNL FYIQNAQETE
     EALEELRQKL RDTKTRMDAE AQGLQGQVST LQASIVAARE KAKRLKDRTL ENEGAFTLSM
     GSSNAPTSSV TGSSGPGGPV NLKELGDKVR EVYVRCGFDA DASISTLQML TNIEMKLEEY
     LNLAEGMTPD YVDGAEKARE KDRRKVARDE KLSTQHREHE ARMARALERA AAPVFKKTGK
     PLMFRSAPPQ RKKVVQADDR NDEEAELEAY LAQDMI
 
 
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