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CFA91_CHLRE
ID   CFA91_CHLRE             Reviewed;        1029 AA.
AC   A8IH47;
DT   12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Cilia- and flagella-associated protein 91 {ECO:0000305};
DE   AltName: Full=Flagellar-associated protein 91 {ECO:0000305};
GN   Name=CFAP91 {ECO:0000305}; Synonyms=FAP91 {ECO:0000303|PubMed:17967944};
GN   ORFNames=CHLREDRAFT_196748 {ECO:0000312|EMBL:EDP05695.1};
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 [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   [2]
RP   FUNCTION, IDENTIFICATION IN A COMPLEX CONTAINING CFAP61; CFAP91 AND
RP   CFAP251, SUBCELLULAR LOCATION, INTERACTION WITH RSP3, AND INTERACTION WITH
RP   CALMODULIN.
RX   PubMed=17967944; DOI=10.1083/jcb.200703107;
RA   Dymek E.E., Smith E.F.;
RT   "A conserved CaM- and radial spoke associated complex mediates regulation
RT   of flagellar dynein activity.";
RL   J. Cell Biol. 179:515-526(2007).
CC   -!- FUNCTION: As component of a spoke-associated complex, regulates
CC       flagellar dynein activity by mediating regulatory signals between the
CC       radial spokes and dynein arms. {ECO:0000269|PubMed:17967944}.
CC   -!- SUBUNIT: Identified in a spoke-associated complex containing CFAP61,
CC       CFAP91 and CFAP251; the complex is associated with the radial spokes of
CC       the axoneme (PubMed:17967944). The complex associates with Calmodulin;
CC       the association is calcium sensitive (PubMed:17967944). Interacts with
CC       RSP3 (PubMed:17967944). {ECO:0000269|PubMed:17967944}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum axoneme
CC       {ECO:0000269|PubMed:17967944}.
CC   -!- SIMILARITY: Belongs to the CFAP91 family.
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DR   EMBL; DS496117; EDP05695.1; -; Genomic_DNA.
DR   RefSeq; XP_001690436.1; XM_001690384.1.
DR   AlphaFoldDB; A8IH47; -.
DR   STRING; 3055.EDP05695; -.
DR   PaxDb; A8IH47; -.
DR   PRIDE; A8IH47; -.
DR   EnsemblPlants; PNW80814; PNW80814; CHLRE_07g330700v5.
DR   GeneID; 5716169; -.
DR   Gramene; PNW80814; PNW80814; CHLRE_07g330700v5.
DR   eggNOG; ENOG502QRFI; Eukaryota.
DR   HOGENOM; CLU_294633_0_0_1; -.
DR   InParanoid; A8IH47; -.
DR   OrthoDB; 707324at2759; -.
DR   GO; GO:0005930; C:axoneme; IDA:UniProtKB.
DR   GO; GO:0031514; C:motile cilium; IDA:UniProtKB.
DR   GO; GO:0003341; P:cilium movement; IDA:UniProtKB.
DR   InterPro; IPR026720; CFAP91.
DR   InterPro; IPR032840; CFAP91_dom.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   PANTHER; PTHR22455; PTHR22455; 1.
DR   Pfam; PF14738; CFAP91; 1.
DR   Pfam; PF00612; IQ; 2.
DR   SMART; SM00015; IQ; 3.
DR   PROSITE; PS50096; IQ; 2.
PE   1: Evidence at protein level;
KW   Cell projection; Cilium; Coiled coil; Cytoplasm; Cytoskeleton; Flagellum.
FT   CHAIN           1..1029
FT                   /note="Cilia- and flagella-associated protein 91"
FT                   /id="PRO_0000439535"
FT   REGION          72..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          117..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          837..861
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          876..1029
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          272..299
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        838..856
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        894..908
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        980..998
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1029 AA;  107241 MW;  BDEB18B8FCC4906E CRC64;
     MAQPQRPYDA LYDPNFTVAG PRDHYRQQTM AGGFNIERAP VYNNFFSELP HHPPSTLRLK
     NADRVPAFVD RNYRPAANDP NDTRQRSDAL AVSGPNRPKY FRRPMLAAAE IHIKQAPPSQ
     LPPLPSHQDL NATAPAAMGG AGGLGEPRSK TIGTQSDYRE NEAQTAPWEP GYVLPAPGAL
     TAKQAALMRR YHTDVPEVLQ LKDLAFPDGL PAGLQEVTRI DKMRAKRAFE ASLPPIDDVA
     RLPLRQRMIE EWEAKEWEER EQEILSIQDK RLELLDNALQ VREEELDDEN RLRVEARKEA
     MLAGRAGKFA DVQATRIKTM RQLIENRKYV EKHRKLHKPT IVERYANYGS GTYAPLQREG
     RFPESKPLGK EIETEGYAPV TLKGVVDLES FLPSRLLNPR VAAPQKPARL DYHQRKEAAV
     QRDLKAINDL LDTAKGTAGR GFGDCWPAPL QDDGGAGMGN GTLGRATSTV GKGTLGAGGS
     AGGAAPGGAS MALLGGPSTA AASAMGPLAS GVSGSPSRRV VRAIERPPTP ELPQPPAVTA
     PQHAAVVLLQ RLLRGRAAQN IMYEGRVRRQ ELIDELRLEE VVSADGTKID GQPIRRPEHR
     DTATLRIDAL VGSAVAEVAA ILAETDPERR ETLLAGLDVS RAHATAAAVA AAAADINASA
     RAEAEEAAAT AMAEAAAAAA AAAAAAAAAE DGGAEGAAES AAEAAAAAEA AASAAEEAYA
     GAVAAAAAPA RAAALNLEAL GISPEEAEEA AVRIQAAFKG HKARKEVAAM RARGEMLRNI
     MANGDEAKVV TCQAAIRGHL ARKRVRQLRA SQAGNEGFAG APSASPEPAA PLPALAENQD
     QQEPQPQPQP SSSSGALDLA DYDDHHGEAS AAMLGGEPSL AVGGSREGEQ QLEADAEAEA
     EAEAEAEAGA EAEASAQAGA EAEAEAGVEA EAEASAGAEA SVGAGAEGDA EAETEAGAQA
     EPGPEAEAEA EAGAEAEAEN GAEAEARLGG EEEGFREGEG QGGAAAGEAG PGGELAEGEG
     EAGEGEAAE
 
 
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