KIF1C_MOUSE
ID KIF1C_MOUSE Reviewed; 1100 AA.
AC O35071; Q5SX62;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Kinesin-like protein KIF1C;
GN Name=Kif1c;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 94-253.
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-674; SER-676 AND SER-1089,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, and
RC Testis;
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).
RN [4]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1039, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Motor required for the retrograde transport of Golgi vesicles
CC to the endoplasmic reticulum. Has a microtubule plus end-directed
CC motility (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. Unc-104 subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00283}.
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DR EMBL; AL596117; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB001456; BAA22398.1; -; mRNA.
DR CCDS; CCDS24965.1; -.
DR RefSeq; NP_694743.2; NM_153103.2.
DR RefSeq; XP_006532383.1; XM_006532320.3.
DR RefSeq; XP_006532384.1; XM_006532321.3.
DR RefSeq; XP_006532385.1; XM_006532322.3.
DR AlphaFoldDB; O35071; -.
DR SMR; O35071; -.
DR BioGRID; 200937; 21.
DR IntAct; O35071; 20.
DR STRING; 10090.ENSMUSP00000092075; -.
DR iPTMnet; O35071; -.
DR PhosphoSitePlus; O35071; -.
DR EPD; O35071; -.
DR jPOST; O35071; -.
DR MaxQB; O35071; -.
DR PaxDb; O35071; -.
DR PeptideAtlas; O35071; -.
DR PRIDE; O35071; -.
DR ProteomicsDB; 269218; -.
DR Antibodypedia; 11469; 156 antibodies from 29 providers.
DR DNASU; 16562; -.
DR Ensembl; ENSMUST00000094499; ENSMUSP00000092075; ENSMUSG00000020821.
DR Ensembl; ENSMUST00000102554; ENSMUSP00000099614; ENSMUSG00000020821.
DR Ensembl; ENSMUST00000137119; ENSMUSP00000123242; ENSMUSG00000020821.
DR GeneID; 16562; -.
DR KEGG; mmu:16562; -.
DR UCSC; uc007jwl.1; mouse.
DR CTD; 10749; -.
DR MGI; MGI:1098260; Kif1c.
DR VEuPathDB; HostDB:ENSMUSG00000020821; -.
DR eggNOG; KOG0245; Eukaryota.
DR GeneTree; ENSGT00940000159295; -.
DR InParanoid; O35071; -.
DR OMA; GGFHYNQ; -.
DR OrthoDB; 76316at2759; -.
DR PhylomeDB; O35071; -.
DR TreeFam; TF105221; -.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-MMU-983189; Kinesins.
DR BioGRID-ORCS; 16562; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Kif1c; mouse.
DR PRO; PR:O35071; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; O35071; protein.
DR Bgee; ENSMUSG00000020821; Expressed in hindlimb stylopod muscle and 256 other tissues.
DR ExpressionAtlas; O35071; baseline and differential.
DR Genevisible; O35071; MM.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
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: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; IBA:GO_Central.
DR GO; GO:1990048; P:anterograde neuronal dense core vesicle transport; ISO:MGI.
DR GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:1990049; P:retrograde neuronal dense core vesicle transport; ISO:MGI.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IDA:MGI.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR CDD; cd00060; FHA; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR027640; Kinesin-like_fam.
DR InterPro; IPR032405; Kinesin_assoc.
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 InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR24115; PTHR24115; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF16183; Kinesin_assoc; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF49879; SSF49879; 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 ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; Methylation;
KW Microtubule; Motor protein; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1100
FT /note="Kinesin-like protein KIF1C"
FT /id="PRO_0000125411"
FT DOMAIN 5..348
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT DOMAIN 523..590
FT /note="FHA"
FT REGION 393..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 894..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 951..1100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 359..381
FT /evidence="ECO:0000255"
FT COILED 438..479
FT /evidence="ECO:0000255"
FT COILED 634..671
FT /evidence="ECO:0000255"
FT COILED 827..871
FT /evidence="ECO:0000255"
FT COMPBIAS 401..423
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1003..1018
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1034..1063
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1064..1080
FT /note="Pro 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 MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43896"
FT MOD_RES 494
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43896"
FT MOD_RES 674
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 676
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 914
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43896"
FT MOD_RES 1031
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43896"
FT MOD_RES 1039
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1080
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O43896"
FT MOD_RES 1089
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 1100 AA; 122434 MW; E92CFFECE6D0F0DA CRC64;
MAGASVKVAV RVRPFNARET SQDAKCVVSM QGNTTSIINP KQSKDAPKSF TFDYSYWSHT
SVEDPQFASQ QQVYRDIGEE MLLHAFEGYN VCIFAYGQTG AGKSYTMMGR QEPGQQGIVP
QLCEDLFSRV NVNQSAQLSY SVEVSYMEIY CERVRDLLNP KSRGSLRVRE HPILGPYVQD
LSKLAVTSYA DIADLMDCGN KARTVAATNM NETSSRSHAV FTIVFTQRSH DQLTGLDSEK
VSKISLVDLA GSERADSSGA RGMRLKEGAN INKSLTTLGK VISALADLQS KKRKSDFIPY
RDSVLTWLLK ENLGGNSRTA MIAALSPADI NYEETLSTLR YADRTKQIRC NAVINEDPNA
RLIRELQEEV ARLRDLLMAQ GLSASALGGL KVEEGSPGGV LPPASSPPAP ASPSSPPPHN
GELEPSFSPS AEPQIGPEEA MERLQETEKI IAELNETWEE KLRKTEALRM EREALLAEMG
VAVREDGGTV GVFSPKKTPH LVNLNEDPLM SECLLYHIKD GVTRVGQVDV DIKLTGQFIR
EQHCLFRSIP QPDGEVMVTL EPCEGAETYV NGKLVTEPLV LKSGNRIVMG KNHVFRFNHP
EQARLERERG VPPPPGPPSE PVDWNFAQKE LLEQQGIDIK LEMEKRLQDL ENQYRKEKEE
ADLLLEQQRL YADSDSGEDS DKRSCEESWR LISSLREQLP PTTVQNIVKR CGLPSSGKRR
APRRVYQIPQ RRRLQGKDPR WATMADLKMQ AVKEICYEVA LADFRHGRAE IEALAALKMR
ELCRTYGKPE GPGDAWRAVA RDVWDTVGEE EGCGGGGGGS EEGARGAEVE DLRAHIDKLT
GILQEVKLQN SSKDRELQAL RDRMLRMERV IPLTQDLEDD NDESGLVTWA PPEGPEAVEE
TVPNDHSPAV RPTSPPLSSW ERVSRLMEED PAFRRGRLRW LKQEQLRLQG LQGAGGRGGG
LRRPPARFVP PHDCKLRFPF KSNPQHRESW PGMGSGEAPA PQPPEEVTVP PAPPNRRPPS
PRRPHRSRRN SLDGGSRSRG GGSTQPEPQH LRPQKHNGYP QQPQPSPAQR PGPRYPPYTT
PPRMRRQRSA PDLKESGAAV
