Entry sw: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   02-NOV-2016, entry version 37.
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; Chlorophyceae;
OC   Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH FAP73,
RP   SUBCELLULAR 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
RT   for 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.,
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).
CC   -!- FUNCTION: As part of MIA, a complex associated with the outer
CC       doublet microtubules of the axoneme, may play a role in
CC       ciliary/flagellar motility by regulating the assembly and the
CC       activity of axonemal inner dynein arm.
CC       {ECO:0000269|PubMed:23569216}.
CC   -!- SUBUNIT: Interacts with FAP73; form the modifier of inner arm
CC       (MIA) 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
CC       mutants do not express the protein in the axoneme and display
CC       slightly jerky, slow swimming phenotypes, reduced flagellar beat
CC       frequencies and defective phototaxis.
CC       {ECO:0000269|PubMed:23569216}.
CC   -!- SIMILARITY: Belongs to the CFAP100 family. {ECO:0000305}.
DR   EMBL; AB692780; BAM95825.1; -; mRNA.
DR   EMBL; DS496112; EDP07473.1; -; Genomic_DNA.
DR   RefSeq; XP_001699777.1; XM_001699725.1.
DR   UniGene; Cre.114; -.
DR   STRING; 3055.EDP07473; -.
DR   EnsemblPlants; EDP07473; EDP07473; CHLREDRAFT_186878.
DR   GeneID; 5725540; -.
DR   Gramene; EDP07473; EDP07473; CHLREDRAFT_186878.
DR   KEGG; cre:CHLREDRAFT_186878; -.
DR   eggNOG; ENOG410IFH9; Eukaryota.
DR   eggNOG; ENOG410YEAI; LUCA.
DR   OMA; SPKEWLE; -.
DR   Proteomes; UP000006906; Unassembled WGS sequence.
DR   GO; GO:0097545; C:axonemal outer doublet; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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   GO; GO:2000574; P:regulation of microtubule motor activity; IMP:UniProtKB.
DR   InterPro; IPR025252; DUF4200.
DR   Pfam; PF13863; DUF4200; 1.
PE   1: Evidence at protein level;
KW   Cell projection; Cilium; Coiled coil; Complete proteome; Cytoplasm;
KW   Cytoskeleton; Flagellum; Reference proteome.
FT   CHAIN         1    576       Cilia- and flagella-associated protein
FT                                100.
FT                                /FTId=PRO_0000437480.
FT   COILED      125    226       {ECO:0000255}.
FT   COILED      254    311       {ECO:0000255}.
FT   COILED      342    408       {ECO:0000255}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       118    235       ipfam:DUF4200 [T]
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
//