KIF3C_HUMAN
ID KIF3C_HUMAN Reviewed; 793 AA.
AC O14782; O43544; Q4ZG18; Q53SX5; Q562F7;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 4.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Kinesin-like protein KIF3C;
GN Name=KIF3C;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9480755; DOI=10.1006/geno.1997.5123;
RA Sardella M., Navone F., Rocchi M., Rubartelli A., Viggiano L., Vignali G.,
RA Consalez G.G., Sitia R., Cabibbo A.;
RT "KIF3C, a novel member of the kinesin superfamily: sequence, expression,
RT and mapping to human chromosome 2 at 2p23.";
RL Genomics 47:405-408(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=9446808; DOI=10.1006/bbrc.1997.7977;
RA Telford E.A.R., Wightman P., Leek J., Markham A.F., Lench N.J.,
RA Bonthron D.T.;
RT "cDNA cloning, genomic organization, and chromosomal localization of a
RT novel human gene that encodes a kinesin-related protein highly similar to
RT mouse Kif3C.";
RL Biochem. Biophys. Res. Commun. 242:407-412(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLN-370.
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 7-383 IN COMPLEX WITH ADP.
RG Structural genomics consortium (SGC);
RT "Motor domain of human kinesin family member 3C in complex with ADP.";
RL Submitted (JAN-2008) to the PDB data bank.
RN [6]
RP VARIANT GLN-571.
RX PubMed=26138355; DOI=10.1111/cge.12636;
RA Dimassi S., Labalme A., Ville D., Calender A., Mignot C., Boutry-Kryza N.,
RA de Bellescize J., Rivier-Ringenbach C., Bourel-Ponchel E., Cheillan D.,
RA Simonet T., Maincent K., Rossi M., Till M., Mougou-Zerelli S., Edery P.,
RA Saad A., Heron D., des Portes V., Sanlaville D., Lesca G.;
RT "Whole-exome sequencing improves the diagnosis yield in sporadic infantile
RT spasm syndrome.";
RL Clin. Genet. 89:198-204(2016).
CC -!- FUNCTION: Microtubule-based anterograde translocator for membranous
CC organelles. {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer of KIF3A and KIF3C. {ECO:0000250}.
CC -!- INTERACTION:
CC O14782; Q9NRI5: DISC1; NbExp=3; IntAct=EBI-1104854, EBI-529989;
CC O14782; P23508: MCC; NbExp=3; IntAct=EBI-1104854, EBI-307531;
CC O14782; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-1104854, EBI-1105213;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
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; AF018164; AAC05302.1; -; mRNA.
DR EMBL; AF035621; AAC39562.1; -; mRNA.
DR EMBL; AJ002223; CAA05252.1; -; Genomic_DNA.
DR EMBL; AJ002224; CAA05253.1; -; Genomic_DNA.
DR EMBL; AJ002225; CAA05254.1; -; Genomic_DNA.
DR EMBL; AJ002226; CAA05255.1; -; Genomic_DNA.
DR EMBL; AJ002227; CAA05256.1; -; Genomic_DNA.
DR EMBL; AJ002228; CAA05257.1; -; Genomic_DNA.
DR EMBL; AJ002229; CAA05258.1; -; Genomic_DNA.
DR EMBL; AC013449; AAY24261.1; -; Genomic_DNA.
DR EMBL; AC064847; AAX88877.1; -; Genomic_DNA.
DR EMBL; BC092406; AAH92406.1; -; mRNA.
DR EMBL; BC130423; AAI30424.1; -; mRNA.
DR CCDS; CCDS1719.1; -.
DR PIR; JC5831; JC5831.
DR RefSeq; NP_002245.4; NM_002254.6.
DR PDB; 3B6V; X-ray; 2.70 A; A/B=7-383.
DR PDBsum; 3B6V; -.
DR AlphaFoldDB; O14782; -.
DR SMR; O14782; -.
DR BioGRID; 109998; 20.
DR ComplexPortal; CPX-3199; KIF3 complex variant AC.
DR ComplexPortal; CPX-3200; KIF3 complex variant AC-KAP3.
DR IntAct; O14782; 13.
DR STRING; 9606.ENSP00000264712; -.
DR ChEMBL; CHEMBL1075196; -.
DR GlyGen; O14782; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O14782; -.
DR PhosphoSitePlus; O14782; -.
DR BioMuta; KIF3C; -.
DR EPD; O14782; -.
DR jPOST; O14782; -.
DR MassIVE; O14782; -.
DR MaxQB; O14782; -.
DR PaxDb; O14782; -.
DR PeptideAtlas; O14782; -.
DR PRIDE; O14782; -.
DR ProteomicsDB; 48232; -.
DR Antibodypedia; 13243; 90 antibodies from 22 providers.
DR DNASU; 3797; -.
DR Ensembl; ENST00000264712.8; ENSP00000264712.3; ENSG00000084731.15.
DR Ensembl; ENST00000405914.1; ENSP00000385030.1; ENSG00000084731.15.
DR GeneID; 3797; -.
DR KEGG; hsa:3797; -.
DR MANE-Select; ENST00000264712.8; ENSP00000264712.3; NM_002254.8; NP_002245.4.
DR UCSC; uc002rgu.3; human.
DR CTD; 3797; -.
DR DisGeNET; 3797; -.
DR GeneCards; KIF3C; -.
DR HGNC; HGNC:6321; KIF3C.
DR HPA; ENSG00000084731; Tissue enriched (brain).
DR MIM; 602845; gene.
DR neXtProt; NX_O14782; -.
DR OpenTargets; ENSG00000084731; -.
DR PharmGKB; PA30104; -.
DR VEuPathDB; HostDB:ENSG00000084731; -.
DR eggNOG; KOG4280; Eukaryota.
DR GeneTree; ENSGT00940000153739; -.
DR InParanoid; O14782; -.
DR OrthoDB; 862274at2759; -.
DR PhylomeDB; O14782; -.
DR TreeFam; TF105223; -.
DR PathwayCommons; O14782; -.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR Reactome; R-HSA-5620924; Intraflagellar transport.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-HSA-983189; Kinesins.
DR SignaLink; O14782; -.
DR BioGRID-ORCS; 3797; 16 hits in 1075 CRISPR screens.
DR ChiTaRS; KIF3C; human.
DR EvolutionaryTrace; O14782; -.
DR GeneWiki; KIF3C; -.
DR GenomeRNAi; 3797; -.
DR Pharos; O14782; Tbio.
DR PRO; PR:O14782; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O14782; protein.
DR Bgee; ENSG00000084731; Expressed in cortical plate and 136 other tissues.
DR ExpressionAtlas; O14782; baseline and differential.
DR Genevisible; O14782; HS.
DR GO; GO:0097542; C:ciliary tip; TAS:Reactome.
DR GO; GO:0005929; C:cilium; TAS:Reactome.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
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:0003774; F:cytoskeletal motor activity; TAS:ProtInc.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
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; 2.
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 3D-structure; ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton;
KW Disease variant; Microtubule; Motor protein; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..793
FT /note="Kinesin-like protein KIF3C"
FT /id="PRO_0000125397"
FT DOMAIN 10..365
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 251..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..793
FT /note="Globular"
FT /evidence="ECO:0000255"
FT REGION 750..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 376..629
FT /evidence="ECO:0000255"
FT COMPBIAS 758..782
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 97..104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT VARIANT 370
FT /note="R -> Q (in dbSNP:rs1465878)"
FT /evidence="ECO:0000269|PubMed:15815621"
FT /id="VAR_055120"
FT VARIANT 571
FT /note="R -> Q (probable disease-associated variant found in
FT a patient with early infantile epileptic encephalopathy;
FT dbSNP:rs772693472)"
FT /evidence="ECO:0000269|PubMed:26138355"
FT /id="VAR_078709"
FT CONFLICT 77..79
FT /note="TVR -> RE (in Ref. 1; AAC05302)"
FT /evidence="ECO:0000305"
FT CONFLICT 110..111
FT /note="TW -> DL (in Ref. 1; AAC05302)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="K -> R (in Ref. 1; AAC05302)"
FT /evidence="ECO:0000305"
FT CONFLICT 471
FT /note="E -> D (in Ref. 1; AAC05302)"
FT /evidence="ECO:0000305"
FT CONFLICT 630
FT /note="K -> G (in Ref. 1; AAC05302)"
FT /evidence="ECO:0000305"
FT STRAND 12..17
FT /evidence="ECO:0007829|PDB:3B6V"
FT HELIX 22..26
FT /evidence="ECO:0007829|PDB:3B6V"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:3B6V"
FT TURN 37..40
FT /evidence="ECO:0007829|PDB:3B6V"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:3B6V"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:3B6V"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:3B6V"
FT HELIX 70..77
FT /evidence="ECO:0007829|PDB:3B6V"
FT HELIX 79..86
FT /evidence="ECO:0007829|PDB:3B6V"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:3B6V"
FT HELIX 103..107
FT /evidence="ECO:0007829|PDB:3B6V"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:3B6V"
FT HELIX 119..133
FT /evidence="ECO:0007829|PDB:3B6V"
FT STRAND 138..151
FT /evidence="ECO:0007829|PDB:3B6V"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:3B6V"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:3B6V"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:3B6V"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:3B6V"
FT HELIX 188..201
FT /evidence="ECO:0007829|PDB:3B6V"
FT STRAND 215..227
FT /evidence="ECO:0007829|PDB:3B6V"
FT STRAND 237..246
FT /evidence="ECO:0007829|PDB:3B6V"
FT HELIX 295..307
FT /evidence="ECO:0007829|PDB:3B6V"
FT HELIX 317..319
FT /evidence="ECO:0007829|PDB:3B6V"
FT HELIX 321..325
FT /evidence="ECO:0007829|PDB:3B6V"
FT HELIX 326..329
FT /evidence="ECO:0007829|PDB:3B6V"
FT STRAND 332..342
FT /evidence="ECO:0007829|PDB:3B6V"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:3B6V"
FT HELIX 349..362
FT /evidence="ECO:0007829|PDB:3B6V"
SQ SEQUENCE 793 AA; 89454 MW; 04CB96C5F6BED45E CRC64;
MASKTKASEA LKVVARCRPL SRKEEAAGHE QILTMDVKLG QVTLRNPRAA PGELPKTFTF
DAVYDASSKQ ADLYDETVRP LIDSVLQGFN GTVFAYGQTG TGKTYTMQGT WVEPELRGVI
PNAFEHIFTH ISRSQNQQYL VRASYLEIYQ EEIRDLLSKE PGKRLELKEN PETGVYIKDL
SSFVTKNVKE IEHVMNLGNQ TRAVGSTHMN EVSSRSHAIF IITVECSERG SDGQDHIRVG
KLNLVDLAGS ERQNKAGPNT AGGAATPSSG GGGGGGGSGG GAGGERPKEA SKINLSLSAL
GNVIAALAGN RSTHIPYRDS KLTRLLQDSL GGNAKTIMVA TLGPASHSYD ESLSTLRFAN
RAKNIKNKPR VNEDPKDTLL REFQEEIARL KAQLEKRGML GKRPRRKSSR RKKAVSAPPG
YPEGPVIEAW VAEEEDDNNN NHRPPQPILE SALEKNMENY LQEQKERLEE EKAAIQDDRS
LVSEEKQKLL EEKEKMLEDL RREQQATELL AAKYKAMESK LLIGGRNIMD HTNEQQKMLE
LKRQEIAEQK RREREMQQEM MLRDEETMEL RGTYTSLQQE VEVKTKKLKK LYAKLQAVKA
EIQDQHDEYI RVRQDLEEAQ NEQTRELKLK YLIIENFIPP EEKNKIMNRL FLDCEEEQWK
FQPLVPAGVS SSQMKKRPTS AVGYKRPISQ YARVAMAMGS HPRYRAENIM FLELDVSPPA
VFEMEFSHDQ EQDPRALHME RLMRLDSFLE RPSTSKVRKS RSWCQSPQRP PPSTTHASLA
SASLRPATVA DHE
