KINH_CAEEL
ID KINH_CAEEL Reviewed; 815 AA.
AC P34540;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Kinesin heavy chain;
DE AltName: Full=Uncoordinated protein 116;
DE Short=Protein unc-116;
GN Name=unc-116 {ECO:0000312|WormBase:R05D3.7};
GN Synonyms=khc-1 {ECO:0000312|WormBase:R05D3.7};
GN ORFNames=R05D3.7 {ECO:0000312|WormBase:R05D3.7};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Bristol N2;
RX PubMed=8105472; DOI=10.1073/pnas.90.19.9181;
RA Patel N., Thierry-Mieg D., Mancillas J.R.;
RT "Cloning by insertional mutagenesis of a cDNA encoding Caenorhabditis
RT elegans kinesin heavy chain.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:9181-9185(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Siddiqui S.S., Ali M.Y., Khan M.A.;
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
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 [5]
RP FUNCTION.
RX PubMed=16236031; DOI=10.1111/j.1471-4159.2005.03490.x;
RA Tsuboi D., Hikita T., Qadota H., Amano M., Kaibuchi K.;
RT "Regulatory machinery of UNC-33 Ce-CRMP localization in neurites during
RT neuronal development in Caenorhabditis elegans.";
RL J. Neurochem. 95:1629-1641(2005).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19605495; DOI=10.1242/dev.038596;
RA Meyerzon M., Fridolfsson H.N., Ly N., McNally F.J., Starr D.A.;
RT "UNC-83 is a nuclear-specific cargo adaptor for kinesin-1-mediated nuclear
RT migration.";
RL Development 136:2725-2733(2009).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21205795; DOI=10.1242/dev.060939;
RA Aguirre-Chen C., Buelow H.E., Kaprielian Z.;
RT "C. elegans bicd-1, homolog of the Drosophila dynein accessory factor
RT Bicaudal D, regulates the branching of PVD sensory neuron dendrites.";
RL Development 138:507-518(2011).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22634595; DOI=10.1038/ncb2508;
RA Winter J.F., Hoepfner S., Korn K., Farnung B.O., Bradshaw C.R., Marsico G.,
RA Volkmer M., Habermann B., Zerial M.;
RT "Caenorhabditis elegans screen reveals role of PAR-5 in RAB-11-recycling
RT endosome positioning and apicobasal cell polarity.";
RL Nat. Cell Biol. 14:666-676(2012).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27697906; DOI=10.1242/dev.141192;
RA Bone C.R., Chang Y.T., Cain N.E., Murphy S.P., Starr D.A.;
RT "Nuclei migrate through constricted spaces using microtubule motors and
RT actin networks in C. elegans hypodermal cells.";
RL Development 143:4193-4202(2016).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=30254025; DOI=10.1242/jcs.223107;
RA Harterink M., Edwards S.L., de Haan B., Yau K.W., van den Heuvel S.,
RA Kapitein L.C., Miller K.G., Hoogenraad C.C.;
RT "Local microtubule organization promotes cargo transport in C. elegans
RT dendrites.";
RL J. Cell Sci. 131:0-0(2018).
CC -!- FUNCTION: Microtubule-dependent motor protein required for organelle
CC transport (PubMed:22634595, PubMed:30254025). Plays a role in endosome
CC transport (PubMed:22634595). Required for the transport of mitochondria
CC along the axon of motor neurons (PubMed:30254025). Involved in the
CC nuclear migration of hyp7 hypodermal precursor cells (PubMed:19605495,
CC PubMed:27697906). Required for the formation of dendritic branches of
CC PVD sensory neurons (PubMed:21205795). In non-ciliated neurons such as
CC the PVD and PHC neurons, required for the organization of minus-end out
CC microtubules in dendrites (PubMed:30254025). Involved in the
CC localization of unc-33 to neurites (PubMed:16236031).
CC {ECO:0000269|PubMed:16236031, ECO:0000269|PubMed:19605495,
CC ECO:0000269|PubMed:21205795, ECO:0000269|PubMed:22634595,
CC ECO:0000269|PubMed:27697906, ECO:0000269|PubMed:30254025}.
CC -!- SUBUNIT: Oligomer composed of two heavy chains and two light chains.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Cytoplasm
CC {ECO:0000269|PubMed:19605495}.
CC -!- DOMAIN: Composed of three structural domains: a large globular N-
CC terminal domain which is responsible for the motor activity of kinesin
CC (it hydrolyzes ATP and binds microtubule), a central alpha-helical
CC coiled coil domain that mediates the heavy chain dimerization; and a
CC small globular C-terminal domain which interacts with other proteins
CC (such as the kinesin light chains), vesicles and membranous organelles.
CC -!- DISRUPTION PHENOTYPE: Conditional knockout in PVD neuron results in a
CC complete microtubule polarity reversal in the anterior dendrite
CC (PubMed:30254025). Conditional knockout in motor neuron reduces the
CC number of mitochondria in the axon (PubMed:30254025). RNAi-mediated
CC knockdown results in reduced dendritic branch formation in PVD sensory
CC neurons (PubMed:21205795). RNAi-mediated knockdown results in an
CC altered distribution of recycling and late endosomes (PubMed:22634595).
CC RNAi-mediated knockdown results in defects in nuclear migration in hyp7
CC hypodermal precursor cells (PubMed:27697906). RNAi-mediated knockdown
CC in a dhc-1 (js319) mutant background results in defective nuclei
CC migrations in larval hypodermal P-cells (PubMed:27697906).
CC {ECO:0000269|PubMed:21205795, ECO:0000269|PubMed:22634595,
CC ECO:0000269|PubMed:27697906, ECO:0000269|PubMed:30254025}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. Kinesin subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00283}.
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DR EMBL; AB017163; BAA32594.1; -; mRNA.
DR EMBL; L19120; AAA28155.1; -; Genomic_DNA.
DR EMBL; BX284603; CCD73193.1; -; Genomic_DNA.
DR PIR; S44868; S44868.
DR RefSeq; NP_498842.1; NM_066441.6.
DR AlphaFoldDB; P34540; -.
DR SMR; P34540; -.
DR BioGRID; 41383; 9.
DR ComplexPortal; CPX-1390; Kinesin I motor complex, klc-2 variant.
DR ComplexPortal; CPX-1416; Kinesin I motor complex, klc-1 variant.
DR IntAct; P34540; 3.
DR STRING; 6239.R05D3.7; -.
DR iPTMnet; P34540; -.
DR EPD; P34540; -.
DR PaxDb; P34540; -.
DR PeptideAtlas; P34540; -.
DR EnsemblMetazoa; R05D3.7.1; R05D3.7.1; WBGene00006840.
DR GeneID; 176179; -.
DR UCSC; R05D3.7; c. elegans.
DR CTD; 176179; -.
DR WormBase; R05D3.7; CE26945; WBGene00006840; unc-116.
DR eggNOG; KOG0240; Eukaryota.
DR GeneTree; ENSGT00940000175167; -.
DR HOGENOM; CLU_001485_11_1_1; -.
DR InParanoid; P34540; -.
DR OMA; NHMRIGV; -.
DR OrthoDB; 1334528at2759; -.
DR PhylomeDB; P34540; -.
DR Reactome; R-CEL-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-CEL-983189; Kinesins.
DR PRO; PR:P34540; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00006840; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0032839; C:dendrite cytoplasm; IEA:GOC.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0016938; C:kinesin I complex; IPI:WormBase.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IDA:WormBase.
DR GO; GO:0005635; C:nuclear envelope; IDA:WormBase.
DR GO; GO:0045202; C:synapse; IDA:WormBase.
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; IBA:GO_Central.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IDA:WormBase.
DR GO; GO:0098957; P:anterograde axonal transport of mitochondrion; IMP:UniProtKB.
DR GO; GO:0098971; P:anterograde dendritic transport of neurotransmitter receptor complex; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IBA:GO_Central.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0051295; P:establishment of meiotic spindle localization; IMP:WormBase.
DR GO; GO:0051296; P:establishment of meiotic spindle orientation; IMP:WormBase.
DR GO; GO:0030951; P:establishment or maintenance of microtubule cytoskeleton polarity; IMP:UniProtKB.
DR GO; GO:0040011; P:locomotion; IMP:WormBase.
DR GO; GO:0033206; P:meiotic cytokinesis; IMP:WormBase.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0030473; P:nuclear migration along microtubule; IMP:UniProtKB.
DR GO; GO:0040038; P:polar body extrusion after meiotic divisions; IMP:WormBase.
DR GO; GO:0010940; P:positive regulation of necrotic cell death; IGI:WormBase.
DR GO; GO:0008104; P:protein localization; IMP:ComplexPortal.
DR GO; GO:0048814; P:regulation of dendrite morphogenesis; IMP:WormBase.
DR GO; GO:0048489; P:synaptic vesicle transport; IMP:WormBase.
DR Gene3D; 3.40.850.10; -; 1.
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 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 2: Evidence at transcript level;
KW ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW Motor protein; Nucleotide-binding; Reference proteome; Transport.
FT CHAIN 1..815
FT /note="Kinesin heavy chain"
FT /id="PRO_0000125349"
FT DOMAIN 11..329
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 788..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 335..374
FT /evidence="ECO:0000255"
FT COILED 422..554
FT /evidence="ECO:0000255"
FT COILED 695..785
FT /evidence="ECO:0000255"
FT COMPBIAS 799..815
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 88..95
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 815 AA; 91894 MW; 1B32718C3A7C254C CRC64;
MEPRTDGAEC GVQVFCRIRP LNKTEEKNAD RFLPKFPSED SISLGGKVYV FDKVFKPNTT
QEQVYKGAAY HIVQDVLSGY NGTVFAYGQT SSGKTHTMEG VIGDNGLSGI IPRIVADIFN
HIYSMDENLQ FHIKVSYYEI YNEKIRDLLD PEKVNLSIHE DKNRVPYVKG ATERFVGGPD
EVLQAIEDGK SNRMVAVTNM NEHSSRSHSV FLITVKQEHQ TTKKQLTGKL YLVDLAGSEK
VSKTGAQGTV LEEAKNINKS LTALGIVISA LAEGTKSHVP YRDSKLTRIL QESLGGNSRT
TVIICASPSH FNEAETKSTL LFGARAKTIK NVVQINEELT AEEWKRRYEK EKEKNTRLAA
LLQAAALELS RWRAGESVSE VEWVNLSDSA QMAVSEVSGG STPLMERSIA PAPPMLTSTT
GPITDEEKKK YEEERVKLYQ QLDEKDDEIQ KVSQELEKLR QQVLLQEEAL GTMRENEELI
REENNRFQKE AEDKQQEGKE MMTALEEIAV NLDVRQAECE KLKRELEVVQ EDNQSLEDRM
NQATSLLNAH LDECGPKIRH FKEGIYNVIR EFNIADIASQ NDQLPDHDLL NHVRIGVSKL
FSEYSAAKES STAAEHDAEA KLAADVARVE SGQDAGRMKQ LLVKDQAAKE IKPLTDRVNM
ELTTLKNLKK EFMRVLVARC QANQDTEGED SLSGPAQKQR IQFLENNLDK LTKVHKQLVR
DNADLRVELP KMEARLRGRE DRIKILETAL RDSKQRSQAE RKKYQQEVER IKEAVRQRNM
RRMNAPQIVK PIRPGQVYTS PSAGMSQGAP NGSNA
