KIF1C_RAT
ID KIF1C_RAT Reviewed; 1097 AA.
AC O35787;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Kinesin-like protein KIF1C;
DE AltName: Full=Kinesin-like protein KIF1D;
GN Name=Kif1c; Synonyms=Kif1d;
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].
RC STRAIN=Wistar;
RX PubMed=9582454; DOI=10.1016/s0169-328x(98)00022-9;
RA Rogers K.R., Griffin M., Brophy P.J.;
RT "The secretory epithelial cells of the choroid plexus employ a novel
RT kinesin-related protein.";
RL Brain Res. Mol. Brain Res. 55:355-355(1998).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-671; SER-673 AND SER-1028,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Probable motor protein.
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; AJ000696; CAA04248.1; -; mRNA.
DR RefSeq; NP_665884.1; NM_145877.1.
DR AlphaFoldDB; O35787; -.
DR SMR; O35787; -.
DR IntAct; O35787; 1.
DR MINT; O35787; -.
DR STRING; 10116.ENSRNOP00000045754; -.
DR iPTMnet; O35787; -.
DR PhosphoSitePlus; O35787; -.
DR jPOST; O35787; -.
DR PaxDb; O35787; -.
DR PRIDE; O35787; -.
DR GeneID; 113886; -.
DR KEGG; rno:113886; -.
DR UCSC; RGD:70928; rat.
DR CTD; 10749; -.
DR RGD; 70928; Kif1c.
DR eggNOG; KOG0245; Eukaryota.
DR InParanoid; O35787; -.
DR OrthoDB; 76316at2759; -.
DR PhylomeDB; O35787; -.
DR Reactome; R-RNO-2132295; MHC class II antigen presentation.
DR Reactome; R-RNO-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-RNO-983189; Kinesins.
DR PRO; PR:O35787; -.
DR Proteomes; UP000002494; Unplaced.
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; ISO:RGD.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005875; C:microtubule associated complex; TAS: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:0003774; F:cytoskeletal motor activity; TAS:RGD.
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; IGI:ARUK-UCL.
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:0007017; P:microtubule-based process; TAS:RGD.
DR GO; GO:1990049; P:retrograde neuronal dense core vesicle transport; IGI:ARUK-UCL.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; ISO:RGD.
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..1097
FT /note="Kinesin-like protein KIF1C"
FT /id="PRO_0000125412"
FT DOMAIN 5..347
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT DOMAIN 520..587
FT /note="FHA"
FT REGION 397..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 897..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 946..1097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 358..380
FT /evidence="ECO:0000255"
FT COILED 437..478
FT /evidence="ECO:0000255"
FT COILED 630..671
FT /evidence="ECO:0000255"
FT COILED 824..868
FT /evidence="ECO:0000255"
FT COMPBIAS 402..422
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 904..918
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1000..1015
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1033..1060
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1061..1077
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 96..103
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43896"
FT MOD_RES 491
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43896"
FT MOD_RES 671
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 673
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 911
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43896"
FT MOD_RES 1028
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1036
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O43896"
FT MOD_RES 1077
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O43896"
FT MOD_RES 1086
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43896"
SQ SEQUENCE 1097 AA; 122334 MW; 8EF40B1C7579BA5B CRC64;
MAGASVKVAV RVRPFNARET SQDAKCVVSM QGNTTSIINP KQSRMFLKAS FDYSYWSHTS
VEDPQFASQQ QVYRDIGEEM LLHAFEGYNV CIFAYGQTGA GKSYTMMGRQ EPGQQGIVPQ
LCEDLFSRVN VNQSAQLSYS VEVSYMEIYC ERVRDLLNPK SRGSLRVREH PILGPYVQDL
SKLAVTSYAD IADLMDCGNK ARTVAATNMN ETSSRSHAVF TIVFTQRSHD QLTGLDSEKV
SKISLVNLAG SERADSSGAR GMRLKEGANI NKSLTTLGKV ISALADLQSK KRKSDFIPYR
DSVLTWLLKE NLGGNSRTAM IAALSPADIN YEETLSTLRY ADRTKQIRCN AVINEDPNAR
LIRELQEEVA RLRELLMAQG LSASALGGLK VEEGSPGGVL PAASSPPAPA SPSSPPPHNG
ELEPSFSPSA EPQIGPEEAM ERLQETEKII AELNETWEEK LRKTEALRME REALLAEMGS
PGGWRTVGVF SPKKTPHLVN LNEDPLMSEC LLYHIKDGVT RVGQVDVDIK LTGQFIREQH
CLFRSIPQPD GEVMVTLEPC EGAETYVNGK LVTEPLVLKS GNRIVMGKNH VFRFNHPEQA
RLERERGVPP PPGPPSEPVD WNFAQKDWLE QQGIDIKLEM EKRLQDLENQ YRKEKEEADL
LLEQQRLYAD SDSGEDSDKR SCEESWRLIS SLRDELPPNT VQTIVKRCGL PSSGKRRAPR
RVYQIPQRRR LQGKDPRWAT MADLKMQAVK EICYEVALAD FRHGRAEIEA LAALKMRELC
RTYGKPEGPG DAWRAVARDV WDTVGEEEGC GGGGGGGEEG ARGAEVEDLR AHIDKLTGIL
QEVKLQNSSK DRELQALRDR MLRMERVIPL TQDLEDDNEE SGLVTWAPPE GSEAVEEAVS
NDHSPAVRPS SPPQSSWERV SRLMEEDPAF RRGRLRWLKQ EQLRLQGLQG SGGRGGGLRR
PPARFVPPHD CKLRFPFKSN PQHRESWPGM GSGEAPGPQP PEEVTAPPPP PNRRPPSPRR
PHRPRRNSLD GGSRSRGGGS TQPEPQHLRP QKHNSYPQQP QPYPAQRPGP RYPPYTTPPR
MRRQRSAPDL KESGAAV
