KLP20_CAEEL
ID KLP20_CAEEL Reviewed; 646 AA.
AC Q965T6;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Kinesin-like protein klp-20 {ECO:0000305};
GN Name=klp-20 {ECO:0000312|WormBase:Y50D7A.6};
GN ORFNames=Y50D7A.6 {ECO:0000312|WormBase:Y50D7A.6};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN KINESIN II MOTOR COMPLEX, AND SUBUNIT.
RX PubMed=17000880; DOI=10.1083/jcb.200606003;
RA Pan X., Ou G., Civelekoglu-Scholey G., Blacque O.E., Endres N.F., Tao L.,
RA Mogilner A., Leroux M.R., Vale R.D., Scholey J.M.;
RT "Mechanism of transport of IFT particles in C. elegans cilia by the
RT concerted action of kinesin-II and OSM-3 motors.";
RL J. Cell Biol. 174:1035-1045(2006).
RN [3] {ECO:0000305}
RP FUNCTION, AND IDENTIFICATION IN KINESIN II MOTOR COMPLEX.
RX PubMed=20833139; DOI=10.1016/j.bbrc.2010.09.007;
RA Pan X., Acar S., Scholey J.M.;
RT "Torque generation by one of the motor subunits of heterotrimeric kinesin-
RT 2.";
RL Biochem. Biophys. Res. Commun. 401:53-57(2010).
RN [4] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN KINESIN II MOTOR COMPLEX, AND SUBUNIT.
RX PubMed=20498083; DOI=10.1073/pnas.1005177107;
RA Brunnbauer M., Mueller-Planitz F., Koesem S., Ho T.H., Dombi R.,
RA Gebhardt J.C., Rief M., Okten Z.;
RT "Regulation of a heterodimeric kinesin-2 through an unprocessive motor
RT domain that is turned processive by its partner.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:10460-10465(2010).
RN [5] {ECO:0000305}
RP INTERACTION WITH KLP-11.
RX PubMed=21917588; DOI=10.1091/mbc.e11-02-0112;
RA Vukajlovic M., Dietz H., Schliwa M., Oekten Z.;
RT "How kinesin-2 forms a stalk.";
RL Mol. Biol. Cell 22:4279-4287(2011).
RN [6] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN KINESIN II MOTOR COMPLEX, SUBCELLULAR LOCATION,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=28479320; DOI=10.1016/j.cub.2017.04.015;
RA Yi P., Li W.J., Dong M.Q., Ou G.;
RT "Dynein-driven retrograde intraflagellar transport is triphasic in C.
RT elegans sensory cilia.";
RL Curr. Biol. 27:1448-1461(2017).
CC -!- FUNCTION: Component of the kinesin II motor complex (composed of kap-1
CC and the heterodimeric motor proteins klp-11 and klp-20) which is
CC required for intraflagellar transport (IFT) (PubMed:20833139,
CC PubMed:20498083). Heterodimerizes with klp-11 to form a 'processive'
CC molecular motor upon IFT cargo binding, which, within the kinesin II
CC motor complex, binds to and moves along microtubules in a
CC unidirectional manner (without dissociation of the heterodimer), and in
CC turn, is responsible for the IFT of cargo (PubMed:20498083).
CC Specifically, the kinesin II motor complex, together with the kinesin
CC motor protein osm-3 moves along microtubules and is required for
CC anterograde IFT along the middle segment of the sensory neuron cilia
CC (PubMed:17000880, PubMed:20833139, PubMed:28479320). In particular, the
CC kinesin II motor complex delivers specific ciliary cargo proteins such
CC as che-3 which are related to motility to ciliary tips
CC (PubMed:28479320). This is likely mediated by IFT complexes A and B
CC (PubMed:28479320). {ECO:0000269|PubMed:17000880,
CC ECO:0000269|PubMed:20498083, ECO:0000269|PubMed:20833139,
CC ECO:0000269|PubMed:28479320}.
CC -!- SUBUNIT: Component of the kinesin II motor complex, a heterotrimeric
CC complex composed of kap-1, klp-11 and klp-20 (PubMed:17000880,
CC PubMed:20833139, PubMed:20498083, PubMed:28479320). Interacts (via C-
CC terminus) with klp-11 (via C-terminus) to form a heterodimer
CC (PubMed:20498083, PubMed:21917588). Furthermore, within the
CC heterodimer, the C-termini of klp-20 and klp-11 interact to form a
CC coiled coil (stalk) or tail domain, and this is necessary for
CC association with kap-1, and kinesin II motor complex activity upon IFT
CC cargo binding (PubMed:20498083, PubMed:21917588). Prior to cargo
CC binding, the klp-11/klp-20 heterodimer is autoinhibited by the tail
CC domain of the heterodimer, which folds onto the kinesin motor domain
CC (PubMed:20498083). Cargo binding to the heterodimer relieves the
CC autoinhibition, and allows for an extended conformation of the tail
CC domain, and function of the heterodimer (PubMed:20498083).
CC {ECO:0000269|PubMed:17000880, ECO:0000269|PubMed:20498083,
CC ECO:0000269|PubMed:21917588, ECO:0000269|PubMed:28479320,
CC ECO:0000305|PubMed:20833139}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000269|PubMed:28479320}. Cytoplasm, cytoskeleton {ECO:0000305}.
CC Note=In particular, localizes to the base and transition zone of cilia.
CC {ECO:0000269|PubMed:28479320}.
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; BX284603; CCD73793.1; -; Genomic_DNA.
DR RefSeq; NP_497178.1; NM_064777.4.
DR AlphaFoldDB; Q965T6; -.
DR SMR; Q965T6; -.
DR ComplexPortal; CPX-1208; Kinesin II motor complex.
DR STRING; 6239.Y50D7A.6; -.
DR EPD; Q965T6; -.
DR PaxDb; Q965T6; -.
DR PeptideAtlas; Q965T6; -.
DR EnsemblMetazoa; Y50D7A.6.1; Y50D7A.6.1; WBGene00002230.
DR EnsemblMetazoa; Y50D7A.6.2; Y50D7A.6.2; WBGene00002230.
DR EnsemblMetazoa; Y50D7A.6.3; Y50D7A.6.3; WBGene00002230.
DR EnsemblMetazoa; Y50D7A.6.4; Y50D7A.6.4; WBGene00002230.
DR GeneID; 3565057; -.
DR KEGG; cel:CELE_Y50D7A.6; -.
DR UCSC; Y50D7A.6; c. elegans.
DR CTD; 3565057; -.
DR WormBase; Y50D7A.6; CE26143; WBGene00002230; klp-20.
DR eggNOG; KOG4280; Eukaryota.
DR GeneTree; ENSGT00940000156386; -.
DR HOGENOM; CLU_001485_22_3_1; -.
DR InParanoid; Q965T6; -.
DR OMA; NMRKHIE; -.
DR OrthoDB; 862274at2759; -.
DR PhylomeDB; Q965T6; -.
DR Reactome; R-CEL-5620924; Intraflagellar transport.
DR Reactome; R-CEL-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-CEL-983189; Kinesins.
DR PRO; PR:Q965T6; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00002230; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0030993; C:axonemal heterotrimeric kinesin-II complex; IPI:WormBase.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0016939; C:kinesin II complex; IC:ComplexPortal.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IDA:WormBase.
DR GO; GO:0008089; P:anterograde axonal transport; IBA:GO_Central.
DR GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
DR GO; GO:0035720; P:intraciliary anterograde transport; IC:ComplexPortal.
DR GO; GO:0007018; P:microtubule-based movement; IDA:WormBase.
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; Cell projection; Cilium; Coiled coil; Cytoplasm; Cytoskeleton;
KW Microtubule; Motor protein; Nucleotide-binding; Reference proteome.
FT CHAIN 1..646
FT /note="Kinesin-like protein klp-20"
FT /evidence="ECO:0000305"
FT /id="PRO_0000442219"
FT DOMAIN 6..331
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 525..550
FT /note="Interaction with klp-11"
FT /evidence="ECO:0000269|PubMed:21917588"
FT REGION 623..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 342..552
FT /evidence="ECO:0000255"
FT BINDING 91..98
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT SITE 444
FT /note="May be required for autoinhibition within the klp-
FT 11/klp-20 heterodimer"
FT /evidence="ECO:0000269|PubMed:20498083"
FT SITE 445
FT /note="May be required for autoinhibition within the klp-
FT 11/klp-20 heterodimer"
FT /evidence="ECO:0000269|PubMed:20498083"
SQ SEQUENCE 646 AA; 73537 MW; 105A9E3BB27AEAE5 CRC64;
MEGAEKVKVV VRCRPISTTE KLQGHKIAVT CNDEEKAVNI KSLSQEDPPR TFYFDAVFSP
NTDQMTVYNV AARPIVENVL KGYNGTIFAY GQTGTGKTFT MAGDLEPVEM RGIIPNSFAH
IFDHIAKCQH DTTFLVRVSY LEIYNEEIRD LLSKDHNGNL EIKERPDVGV YVRNLSNPTV
ENASKMQALM EFGSKNRKVG ATAMNLESSR SHAMFTVTIE SCRNGLVTQG KLQLVDLAGS
ERQSKTGAQG ERLKEAAKIN LSLSTLGNVI SSLVDGKSTH IPYRNSKLTR LLQDSLGGNS
KTVMIANVGP ATYNYDETLS TLRYANRAKN IQNVAKINED PKDAQLRKFQ LEIEALRKIL
DEENPGDDEN QEEAWEAKMQ EREVEMEKKR KILEERVNSA VNDEETHRLV KEMMENEAEL
KKARSEHEKL RSKLEKIEKK LIVGGENLLE KVEEQAKLLE VNNKELEQSK FQEAHLRTQL
EERTAVKVEI EERYSSLQEE AFVKSKKIKK VSNELKDARA ELKDLEEDHQ RQVEAMLDDI
RQLRKELLLN IAIIDEYIPV EHVELIEKYV SWSEEHGDWQ LKAIAYTGNN MRASAPPAKK
EFSNNNQTVP MYYSYRADLG ASTAEHRPRT SSKKHRASIR LQQLLT
