KIF3C_RAT
ID KIF3C_RAT Reviewed; 796 AA.
AC O55165; O88657;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Kinesin-like protein KIF3C;
GN Name=Kif3c;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9487132; DOI=10.1091/mbc.9.3.637;
RA Muresan V., Abramson T., Lyass A., Winter D., Porro E., Hong F.,
RA Chamberlin N.L., Schnapp B.J.;
RT "KIF3C and KIF3A form a novel neuronal heteromeric kinesin that associates
RT with membrane vesicles.";
RL Mol. Biol. Cell 9:637-652(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9808286; DOI=10.1016/s0171-9335(98)80099-x;
RA Faire K., Gruber D., Bulinski J.C.;
RT "Identification of kinesin-like molecules in myogenic cells.";
RL Eur. J. Cell Biol. 77:27-34(1998).
CC -!- FUNCTION: Microtubule-based anterograde translocator for membranous
CC organelles.
CC -!- SUBUNIT: Heterodimer of KIF3A and KIF3C.
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; AJ223599; CAA11465.1; -; mRNA.
DR EMBL; AF083330; AAC33291.1; -; mRNA.
DR RefSeq; NP_445938.1; NM_053486.1.
DR AlphaFoldDB; O55165; -.
DR SMR; O55165; -.
DR STRING; 10116.ENSRNOP00000015820; -.
DR iPTMnet; O55165; -.
DR PhosphoSitePlus; O55165; -.
DR jPOST; O55165; -.
DR PaxDb; O55165; -.
DR PRIDE; O55165; -.
DR GeneID; 85248; -.
DR KEGG; rno:85248; -.
DR CTD; 3797; -.
DR RGD; 621538; Kif3c.
DR eggNOG; KOG4280; Eukaryota.
DR InParanoid; O55165; -.
DR OrthoDB; 862274at2759; -.
DR PhylomeDB; O55165; -.
DR Reactome; R-RNO-2132295; MHC class II antigen presentation.
DR Reactome; R-RNO-5620924; Intraflagellar transport.
DR Reactome; R-RNO-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-RNO-983189; Kinesins.
DR PRO; PR:O55165; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0030426; C:growth cone; IDA:RGD.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
DR GO; GO:0035371; C:microtubule plus-end; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0071598; C:neuronal ribonucleoprotein granule; IDA:MGI.
DR GO; GO:0008021; C:synaptic vesicle; IDA:RGD.
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; IPI:RGD.
DR GO; GO:0008017; F:microtubule binding; IDA:RGD.
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:0072384; P:organelle transport along microtubule; ISO:RGD.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:RGD.
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 2: Evidence at transcript level;
KW ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW Motor protein; Nucleotide-binding; Reference proteome.
FT CHAIN 1..796
FT /note="Kinesin-like protein KIF3C"
FT /id="PRO_0000125399"
FT DOMAIN 10..367
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 251..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 633..793
FT /note="Globular"
FT /evidence="ECO:0000255"
FT REGION 754..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 378..632
FT /evidence="ECO:0000255"
FT COMPBIAS 253..291
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 352
FT /note="D -> DD (in Ref. 2; AAC33291)"
FT /evidence="ECO:0000305"
FT CONFLICT 562..563
FT /note="ML -> IV (in Ref. 2; AAC33291)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 796 AA; 89816 MW; 935A79A01F8BDC0D 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 ERQNKAGPNT PGGPATQSTA GGGGGGGGTS GSGSSGERPK EASKINLSLS
ALGNVIAALA GNRSTHIPYR DSKLTRLLQD SLGGNAKTIM VATLGPASHS YDESLSTLRF
ANRAKNIKNK PRVNEDPKDT LLREFQEEIA RLKAQLEKKG MLGKRPRRKS SRRKKAVSAP
AGYPEGAVIE AWVAEEEDDN NNNHRPPQPT LEAALEKNME NYLQEQKERL EEEKAAIQDD
RSLVSEEKQK LLEEKEKMLE DLKREQQATE LLAAKYKAME SKLLIGGRNI MDHTNEQQKM
LELKRQEIAE QKRREREMQQ EMLLRDEETM ELRGTYSSLQ QEVEVKTKKL KKLYAKLQAV
KAEIQDQHEE YIRVRQDLEE AQNEQTRELK LKYLIIENFI PPEEKNKIMN RLFLDCEEEQ
WKFQPLVPAG VNNSQMKKRP TSAVGYKRPI SQYARVAMAM GSHPRYRAEN IMFLELDVSP
PAIFEMEFSH DQEQDPRVLH MERLMRLDSF LERPSTSKVR KSRSWCQSPQ RPPPPSTVHA
SMASAPLHPA TVVDHD
