KIF3C_BOVIN
ID KIF3C_BOVIN Reviewed; 792 AA.
AC A0JN40;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Kinesin-like protein KIF3C;
GN Name=KIF3C;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; BC126505; AAI26506.1; -; mRNA.
DR RefSeq; NP_001071623.1; NM_001078155.1.
DR AlphaFoldDB; A0JN40; -.
DR SMR; A0JN40; -.
DR STRING; 9913.ENSBTAP00000025475; -.
DR PaxDb; A0JN40; -.
DR PRIDE; A0JN40; -.
DR Ensembl; ENSBTAT00000025475; ENSBTAP00000025475; ENSBTAG00000019138.
DR GeneID; 777770; -.
DR KEGG; bta:777770; -.
DR CTD; 3797; -.
DR VEuPathDB; HostDB:ENSBTAG00000019138; -.
DR VGNC; VGNC:30604; KIF3C.
DR eggNOG; KOG4280; Eukaryota.
DR GeneTree; ENSGT00940000153739; -.
DR HOGENOM; CLU_001485_22_4_1; -.
DR InParanoid; A0JN40; -.
DR OrthoDB; 862274at2759; -.
DR TreeFam; TF105223; -.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000019138; Expressed in prefrontal cortex and 104 other tissues.
DR ExpressionAtlas; A0JN40; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005876; C:spindle microtubule; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
DR GO; GO:0090307; P:mitotic spindle assembly; IBA:GO_Central.
DR GO; GO:0051231; P:spindle elongation; 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 2: Evidence at transcript level;
KW ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW Motor protein; Nucleotide-binding; Reference proteome.
FT CHAIN 1..792
FT /note="Kinesin-like protein KIF3C"
FT /id="PRO_0000284074"
FT DOMAIN 10..363
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 249..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 628..792
FT /note="Globular"
FT /evidence="ECO:0000255"
FT REGION 749..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 374..627
FT /evidence="ECO:0000255"
FT COMPBIAS 253..268
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"
SQ SEQUENCE 792 AA; 89487 MW; 786FE3FEB3F36098 CRC64;
MASKTKASEA LKVVARCRPL SRKEEAAGHE QILTMDVKLG QVTLRNPRAA LGELPKTFTF
DAVYDASSKQ ADLYDETVRP LVDSVLQGFN GTVFAYGQTG TGKTYTMQGT WVEPEQRGVI
PNAFEHIFTH ISRSQNQQYL VRASYLEIYQ EEIRDLVSKE PGKRLELKEN PETGVYIKDL
SSFVTKNVKE IEHVMNLGNQ TRAVGSTHMN EVSSRSHAIF VITVECSERG SDGQDHIRVG
KLNLVDLAGS ERQNKAGPNT TGGTATQPTG GGGGGGGGGG GGERPKEASK INLSLSALGN
VIAALSGNRS THIPYRDSKL TRLLQDSLGG NAKTIMVATL GPASHSYDES LSTLRFANRA
KNIKNKPRVN EDPKDTLLRE FQEEIARLKA QLEKKGMLGK RLRRKSSRRK KAVSAPAGYP
EGPVIEAWVA EEEDDNNNNH RPPQPILETA LDKNMENYLQ EQKERLEEEK AAIQDDRSLV
SEEKKKLLEE KEKMLEDLRR EQEATELLAA KYKAMESKLL IGGRNIMDHT NEQQKMLELK
RQEIAEQKRR EREMQQEMML RDEETMELRG TYTSLQQEVE VKTKKLKKLY AKLQAVKAEI
QDQHDEYIRV RQDLEEAQNE QTRELKLKYL IIENFIPPEE KNKIMNRLFL DCEEEQWKFQ
PLVPSGANSS QMKKRPTSAV GYKRPISQYA RVAMAMGSHP RYRAENIMFL ELDVSPPAVF
EMEFSHDQDQ DPRALHMERL MRLDSFLERP STSKVRKSRS WCQSPQRPPP PTAHASLAAS
AALRPTTVLD HE