KIF3C_MOUSE
ID KIF3C_MOUSE Reviewed; 796 AA.
AC O35066; O35229; Q3UH55;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Kinesin-like protein KIF3C;
GN Name=Kif3c;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9450952; DOI=10.1091/mbc.9.2.249;
RA Yang Z., Goldstein L.S.B.;
RT "Characterization of the KIF3C neural kinesin-like motor from mouse.";
RL Mol. Biol. Cell 9:249-261(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 NUCLEOTIDE SEQUENCE [MRNA] OF 93-157.
RC STRAIN=ICR;
RX PubMed=9275178; DOI=10.1073/pnas.94.18.9654;
RA Nakagawa T., Tanaka Y., Matsuoka E., Kondo S., Okada Y., Noda Y., Kanai Y.,
RA Hirokawa N.;
RT "Identification and classification of 16 new kinesin superfamily (KIF)
RT proteins in mouse genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:9654-9659(1997).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Microtubule-based anterograde translocator for membranous
CC organelles. {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer of KIF3A and KIF3C. {ECO:0000250}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF013116; AAC39965.1; -; mRNA.
DR EMBL; AK147572; BAE28002.1; -; mRNA.
DR EMBL; CH466623; EDL01397.1; -; Genomic_DNA.
DR EMBL; BC127063; AAI27064.1; -; mRNA.
DR EMBL; AB001433; BAA22393.1; -; mRNA.
DR CCDS; CCDS25783.1; -.
DR RefSeq; NP_032471.2; NM_008445.2.
DR PDB; 5JVM; X-ray; 1.57 A; A/B=374-402.
DR PDBsum; 5JVM; -.
DR AlphaFoldDB; O35066; -.
DR SMR; O35066; -.
DR BioGRID; 200943; 19.
DR ComplexPortal; CPX-3202; KIF3 complex variant AC.
DR ComplexPortal; CPX-3205; KIF3 complex variant AC-KAP3.
DR IntAct; O35066; 13.
DR STRING; 10090.ENSMUSP00000020999; -.
DR iPTMnet; O35066; -.
DR PhosphoSitePlus; O35066; -.
DR EPD; O35066; -.
DR MaxQB; O35066; -.
DR PaxDb; O35066; -.
DR PeptideAtlas; O35066; -.
DR PRIDE; O35066; -.
DR ProteomicsDB; 263537; -.
DR Antibodypedia; 13243; 90 antibodies from 22 providers.
DR DNASU; 16570; -.
DR Ensembl; ENSMUST00000020999; ENSMUSP00000020999; ENSMUSG00000020668.
DR Ensembl; ENSMUST00000220210; ENSMUSP00000151286; ENSMUSG00000020668.
DR GeneID; 16570; -.
DR KEGG; mmu:16570; -.
DR UCSC; uc007mwm.1; mouse.
DR CTD; 3797; -.
DR MGI; MGI:107979; Kif3c.
DR VEuPathDB; HostDB:ENSMUSG00000020668; -.
DR eggNOG; KOG4280; Eukaryota.
DR GeneTree; ENSGT00940000153739; -.
DR HOGENOM; CLU_001485_22_4_1; -.
DR InParanoid; O35066; -.
DR OMA; GLDGQDH; -.
DR OrthoDB; 862274at2759; -.
DR PhylomeDB; O35066; -.
DR TreeFam; TF105223; -.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-5620924; Intraflagellar transport.
DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-MMU-983189; Kinesins.
DR BioGRID-ORCS; 16570; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Kif3c; mouse.
DR PRO; PR:O35066; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; O35066; protein.
DR Bgee; ENSMUSG00000020668; Expressed in cortical plate and 252 other tissues.
DR ExpressionAtlas; O35066; baseline and differential.
DR Genevisible; O35066; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0030426; C:growth cone; ISO:MGI.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0035371; C:microtubule plus-end; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0071598; C:neuronal ribonucleoprotein granule; ISO:MGI.
DR GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0019894; F:kinesin binding; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; ISO:MGI.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
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 Microtubule; Motor protein; Nucleotide-binding; Reference proteome.
FT CHAIN 1..796
FT /note="Kinesin-like protein KIF3C"
FT /id="PRO_0000125398"
FT DOMAIN 10..367
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 252..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 633..793
FT /note="Globular"
FT /evidence="ECO:0000255"
FT REGION 758..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 378..632
FT /evidence="ECO:0000255"
FT COMPBIAS 269..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..784
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT CONFLICT 93
FT /note="V -> I (in Ref. 4; BAA22393)"
FT /evidence="ECO:0000305"
FT CONFLICT 564
FT /note="L -> V (in Ref. 1; AAC39965)"
FT /evidence="ECO:0000305"
FT HELIX 377..402
FT /evidence="ECO:0007829|PDB:5JVM"
SQ SEQUENCE 796 AA; 89973 MW; 5CC5A5EB12958166 CRC64;
MASKTKASEA LKVVARCRPL SRKEEAAGHE QILTMDVKLG QVTLRNPRAA PGELPKTFTF
DAVYDASSKQ ADLYDETVRP LIDSVLQGFN GTVFAYGQTG TGKTYTMQGT WVEPELRGVI
PNAFEHIFTH ISRSQNQQYL VRASYLEIYQ EEIRDLLSKE PGKRLELKEN PETGVYIKDL
SSFVTKNVKE IEHVMNLGNQ ARAVGSTHMN EVSSRSHAIF VITVECSERG SDGQDHIRVG
KLNLVDLAGS ERQNKAGPNA AGGPATQPTA GGGSGSGSAS GSASSGERPK EASKINLSLS
ALGNVIAALA GNRSTHIPYR DSKLTRLLQD SLGGNAKTIM VATLGPASHS YDESLSTLRF
ANRAKNIKNK PRVNEDPKDT LLREFQEEIA RLKAQLEKKG MLGKRPRRKS SRRKKAVSAP
AGYPEGSVIE AWVAEEEDDN NNNHHPPQPI LEAALEKNME NYLQDQKERL EEEKAAIQDD
RSLVSEEKQK LLEEKEKMLE DLRREQQATE LLAAKYKAME SKLLIGGRNI MDHTNEQQKM
LELKRQEIAE QKRREREMQQ EMLLRDEETM ELRGTYSSLQ QEVEVKTKKL KKLYAKLQAV
KAEIQDQHEE YIRVRQDLEE AQNEQTRELK LKYLIIENFI PPEEKNKIMN RLFLDCEEEQ
WRFQPLVPAG VNNSQMKKRP TSAVGYKRPI SQYARVAMAM GSHPRYRAEN IMFLELDVSP
PAIFEMEFSH DQEQDPRVLH MERLMRLDSF LERPSTTKVR KSRSWCQSPQ RMPPPSTAHA
SMTSVPLHPA TVVDHD
