ID   FLA10_CHLRE             Reviewed;         786 AA.
AC   P46869;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Kinesin-like protein FLA10;
DE   AltName: Full=Protein KHP1;
GN   Name=FLA10;
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].
RC   STRAIN=137c / CC-125;
RX   PubMed=8027176; DOI=10.1083/jcb.126.1.175;
RA   Walther Z., Vashishtha M., Hall J.L.;
RT   "The Chlamydomonas FLA10 gene encodes a novel kinesin-homologous protein.";
RL   J. Cell Biol. 126:175-188(1994).
RN   [2]
RP   INTERACTION WITH D1BLIC AND DHC1B.
RX   PubMed=17895364; DOI=10.1242/jcs.012773;
RA   Rompolas P., Pedersen L.B., Patel-King R.S., King S.M.;
RT   "Chlamydomonas FAP133 is a dynein intermediate chain associated with the
RT   retrograde intraflagellar transport motor.";
RL   J. Cell Sci. 120:3653-3665(2007).
RN   [3]
RP   INTERACTION WITH DAW1.
RX   PubMed=18852297; DOI=10.1083/jcb.200802025;
RA   Ahmed N.T., Gao C., Lucker B.F., Cole D.G., Mitchell D.R.;
RT   "ODA16 aids axonemal outer row dynein assembly through an interaction with
RT   the intraflagellar transport machinery.";
RL   J. Cell Biol. 183:313-322(2008).
CC   -!- FUNCTION: Probably involved in flagellar assembly and maintenance. May
CC       play a role in flagellar synthesis.
CC   -!- SUBUNIT: Interacts with D1BLIC, DHC1B and DAW1.
CC       {ECO:0000269|PubMed:17895364, ECO:0000269|PubMed:18852297}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Flagellar axoneme.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. Kinesin II subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00283}.
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DR   EMBL; L33697; AAA21738.1; -; mRNA.
DR   PIR; A53939; A53939.
DR   RefSeq; XP_001701510.1; XM_001701458.1.
DR   AlphaFoldDB; P46869; -.
DR   SMR; P46869; -.
DR   STRING; 3055.EDO97387; -.
DR   PRIDE; P46869; -.
DR   EnsemblPlants; PNW70698; PNW70698; CHLRE_17g730950v5.
DR   GeneID; 5727085; -.
DR   Gramene; PNW70698; PNW70698; CHLRE_17g730950v5.
DR   KEGG; cre:CHLRE_17g730950v5; -.
DR   eggNOG; KOG4280; Eukaryota.
DR   HOGENOM; CLU_001485_22_4_1; -.
DR   OMA; LESKMLC; -.
DR   OrthoDB; 862274at2759; -.
DR   GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR   GO; GO:0097014; C:ciliary plasm; IDA:BHF-UCL.
DR   GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0031514; C:motile cilium; IDA:BHF-UCL.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR   GO; GO:0035720; P:intraciliary anterograde transport; IMP:BHF-UCL.
DR   GO; GO:0044458; P:motile cilium assembly; IMP:BHF-UCL.
DR   Gene3D; 3.40.850.10; -; 1.
DR   InterPro; IPR027640; Kinesin-like_fam.
DR   InterPro; IPR019821; Kinesin_motor_CS.
DR   InterPro; IPR001752; Kinesin_motor_dom.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR24115; PTHR24115; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW   Motor protein; Nucleotide-binding.
FT   CHAIN           1..786
FT                   /note="Kinesin-like protein FLA10"
FT                   /id="PRO_0000125403"
FT   DOMAIN          10..353
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   REGION          688..786
FT                   /note="Globular"
FT                   /evidence="ECO:0000255"
FT   REGION          700..786
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          367..687
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        751..786
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         97..104
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   786 AA;  86672 MW;  F90969203EB79F1B CRC64;
     MPPAGGGSES VKVVVRCRPL NGKEKADGRS RIVDMDVDAG QVKVRNPKAD ASEPPKAFTF
     DQVYDWNCQQ RDVFDITARP LIDSCIEGYN GTIFAYGQTG TGKSHTMEGK DEPPELRGLI
     PNTFRYVFEI IARDSGTKEF LVRSSYLEIY NEEVRDLLGK DHSKKMELKE SPDRGVYVKD
     LSQFVCKNYE EMNKVLLAGK DNRQVGATLM NQDSSRSHSI FTITIECIEK LESAAAQKPG
     AKKDDSNHVR VGKLNLVDLA GSERQDKTGA TGDRLKEGIK INLSLTALGN VISALVDGKS
     GHIPYRDSKL TRLLQDSLGG NTKTVMVANI GPADWNYDET MSTLRYANRA KNIQNKPKIN
     EDPKDAMLRQ FQEEIKKLKE QLAARAAGGG GPITMPSGGG SPTQKIVERT EEVDPDIDAI
     KAQMRAELEA KMKSDISTEA LDKAREEAEA AAKKQLQAII DDQGKTEAQK KAARDALKKQ
     AEEARAIAGA IEKEKQEKAV LESRIKEMEG KIVVGGVNML EKVDELKQKS EDIKREAAIR
     KRQEEEAKRR LEELQAAQVD ADAKFASLDE EINVKSRQLK KLFEKYQGKK GELADLQEQF
     QREREGMLED YRILTQQIKL KNLIIACFIP PDYQDKIMQH CHWQDYDSSW NIDCIAYAGN
     AVRTNQELQA QEDKEHDAAA ENERLKNCFF SYEQFEAAGA GSKQGGGGGG GGGGAARPGS
     SAGRAVGSAA RRTGGKAGGK DITDIGSLRD SVNWGDDDDK KKGAIPKAKG LVKDTVDPRL
     RASKLK