KIFC3_MOUSE
ID KIFC3_MOUSE Reviewed; 824 AA.
AC O35231; O35072; Q1WNZ8; Q3UX36; Q3V0U4; Q6NS71; Q8R3Y4; Q91YQ2; Q99KP7;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Kinesin-like protein KIFC3;
GN Name=Kifc3;
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] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND INTERACTION WITH ANNEXIN XIIIB.
RC STRAIN=ICR; TISSUE=Brain;
RX PubMed=11581287; DOI=10.1083/jcb.200108042;
RA Noda Y., Okada Y., Saito N., Setou M., Xu Y., Zhang Z., Hirokawa N.;
RT "KIFC3, a microtubule minus end-directed motor for the apical transport of
RT annexin XIIIb-associated Triton-insoluble membranes.";
RL J. Cell Biol. 155:77-88(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=11154264; DOI=10.1128/mcb.21.3.765-770.2001;
RA Yang Z., Xia C.H., Roberts E.A., Bush K., Nigam S.K., Goldstein L.S.;
RT "Molecular cloning and functional analysis of mouse C-terminal kinesin
RT motor KifC3.";
RL Mol. Cell. Biol. 21:765-770(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, Czech II, and FVB/N; TISSUE=Brain, and Mammary tumor;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 66-824 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 522-678.
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).
CC -!- FUNCTION: Minus-end microtubule-dependent motor protein. Involved in
CC apically targeted transport. Required for zonula adherens maintenance.
CC {ECO:0000269|PubMed:11581287}.
CC -!- SUBUNIT: Interacts with annexin XIIIB. {ECO:0000269|PubMed:11581287}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:11581287}. Cytoplasmic vesicle membrane
CC {ECO:0000305|PubMed:11581287}; Peripheral membrane protein
CC {ECO:0000305|PubMed:11581287}. Cell junction, adherens junction
CC {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center,
CC centrosome {ECO:0000250}. Note=Localizes along zonula adherens only at
CC mature cell-cell contacts (By similarity). Apical cell membrane. On
CC membrane organelles immediately beneath the apical plasma membrane of
CC renal tubular epithelial cells. Localized in the distal tubules and
CC loops of Henle in the kidney, but not in the proximal tubules or the
CC glomeruli, with stronger staining in the apical area of these
CC epithelial cells. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O35231-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O35231-2; Sequence=VSP_022363, VSP_022364;
CC -!- TISSUE SPECIFICITY: Predominant expression in the kidney, testis and
CC ovary. Also expressed in brain, heart, liver, lung and uterus.
CC {ECO:0000269|PubMed:11581287}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH70429.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE21409.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D49546; BAE92567.1; -; mRNA.
DR EMBL; AF013118; AAC39967.2; -; mRNA.
DR EMBL; BC004069; AAH04069.1; -; mRNA.
DR EMBL; BC016118; AAH16118.1; -; mRNA.
DR EMBL; BC023374; AAH23374.1; -; mRNA.
DR EMBL; BC070429; AAH70429.1; ALT_INIT; mRNA.
DR EMBL; AK132895; BAE21409.1; ALT_INIT; mRNA.
DR EMBL; AK135926; BAE22727.1; -; mRNA.
DR EMBL; AB001457; BAA22399.1; -; mRNA.
DR CCDS; CCDS52640.1; -. [O35231-1]
DR RefSeq; NP_001139303.1; NM_001145831.1.
DR RefSeq; NP_001139304.1; NM_001145832.1.
DR RefSeq; NP_034761.3; NM_010631.2. [O35231-1]
DR AlphaFoldDB; O35231; -.
DR SMR; O35231; -.
DR BioGRID; 200954; 5.
DR IntAct; O35231; 3.
DR MINT; O35231; -.
DR STRING; 10090.ENSMUSP00000034240; -.
DR iPTMnet; O35231; -.
DR PhosphoSitePlus; O35231; -.
DR MaxQB; O35231; -.
DR PaxDb; O35231; -.
DR PRIDE; O35231; -.
DR ProteomicsDB; 263607; -. [O35231-1]
DR ProteomicsDB; 263608; -. [O35231-2]
DR Antibodypedia; 15192; 98 antibodies from 25 providers.
DR DNASU; 16582; -.
DR Ensembl; ENSMUST00000034240; ENSMUSP00000034240; ENSMUSG00000031788. [O35231-1]
DR Ensembl; ENSMUST00000169353; ENSMUSP00000127427; ENSMUSG00000031788. [O35231-2]
DR GeneID; 16582; -.
DR KEGG; mmu:16582; -.
DR UCSC; uc009mxu.1; mouse. [O35231-2]
DR UCSC; uc009mxv.1; mouse. [O35231-1]
DR CTD; 3801; -.
DR MGI; MGI:109202; Kifc3.
DR VEuPathDB; HostDB:ENSMUSG00000031788; -.
DR eggNOG; KOG0239; Eukaryota.
DR GeneTree; ENSGT00940000154022; -.
DR InParanoid; O35231; -.
DR OMA; RHDMQKC; -.
DR OrthoDB; 364605at2759; -.
DR PhylomeDB; O35231; -.
DR TreeFam; TF105238; -.
DR BioGRID-ORCS; 16582; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Kifc3; mouse.
DR PRO; PR:O35231; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; O35231; protein.
DR Bgee; ENSMUSG00000031788; Expressed in right kidney and 230 other tissues.
DR ExpressionAtlas; O35231; baseline and differential.
DR Genevisible; O35231; MM.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0005871; C:kinesin complex; IDA:MGI.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0005915; C:zonula adherens; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0008569; F:minus-end-directed microtubule motor activity; TAS:MGI.
DR GO; GO:0090136; P:epithelial cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IMP:MGI.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0007017; P:microtubule-based process; IDA:MGI.
DR GO; GO:0045218; P:zonula adherens maintenance; ISS:UniProtKB.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR027325; KIFC3-like.
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; PTHR47972:SF5; PTHR47972:SF5; 1.
DR Pfam; PF00225; Kinesin; 1.
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 Alternative splicing; ATP-binding; Cell junction; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; Cytoskeleton; Membrane; Microtubule; Motor protein;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..824
FT /note="Kinesin-like protein KIFC3"
FT /id="PRO_0000125432"
FT DOMAIN 443..766
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 27..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 771..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 100..360
FT /evidence="ECO:0000255"
FT COILED 393..430
FT /evidence="ECO:0000255"
FT COMPBIAS 775..789
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..824
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 526..533
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 811
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVG8"
FT MOD_RES 815
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVG8"
FT VAR_SEQ 1..115
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11154264"
FT /id="VSP_022363"
FT VAR_SEQ 116..125
FT /note="QEVSRLRSEL -> MPPLGPGSPQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11154264"
FT /id="VSP_022364"
FT CONFLICT 67..74
FT /note="EDSTSRTA -> HCQPTFPT (in Ref. 4; BAE21409)"
FT /evidence="ECO:0000305"
FT CONFLICT 76..83
FT /note="RPSLAQCR -> GLRAQHQP (in Ref. 4; BAE21409)"
FT /evidence="ECO:0000305"
FT CONFLICT 86..103
FT /note="SVDWPGPRSPHRLYLTVQ -> ETAKVRTSALGVVRRCGE (in Ref. 4;
FT BAE21409)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="R -> Q (in Ref. 1; BAE92567)"
FT /evidence="ECO:0000305"
FT CONFLICT 214..215
FT /note="EL -> DV (in Ref. 2; AAC39967)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="D -> Y (in Ref. 1; BAE92567)"
FT /evidence="ECO:0000305"
FT CONFLICT 573
FT /note="A -> R (in Ref. 2; AAC39967)"
FT /evidence="ECO:0000305"
FT CONFLICT 659
FT /note="S -> R (in Ref. 2; AAC39967)"
FT /evidence="ECO:0000305"
FT CONFLICT 690
FT /note="R -> Q (in Ref. 1; BAE92567)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 824 AA; 92556 MW; EE7EF66140725547 CRC64;
MVPSRRTWNL GATPSLRGLW RVGRVQEPKP GMARPAPASP AARPFPHTGQ GRLRTGRGKD
ILPSGEEDST SRTAARPSLA QCRALSVDWP GPRSPHRLYL TVQVENLKEK LISQAQEVSR
LRSELGGTDA EKHRDRLMVE NEQLRQELRR CEVELQELRA QPVVPCEGCE HSQESSQLRD
KLSQLQLEVA ENKGMLSELN LEVQQKTDRL AEVELRLKDC LAEKAQEEER LSRRLRDSHE
TIASLRAQSP PVKYVIKTVE VESSKTKQAL SESQTRNQHL QEQVAMQRQV LKEMEQQLQN
SHQLTVQLRA QIAMYEAELE RAHGQMLEEM QSLEEDKNRA IEEAFARAQV EMKAVHENLA
GVRTNLLTLQ PALRTLTNDY NGLKRQVRGF PLLLQEALRS VKAEIGQAIE EVNSNNQELL
RKYRRELQLR KKCHNELVRL KGNIRVIARV RPVTKEDGEG PEATNAVTFD PDDDSIIHLL
HKGKPVSFEL DKVFSPWASQ QDVFQEVQAL ITSCIDGFNV CIFAYGQTGA GKTYTMEGTP
ENPGINQRAL QLLFSEVQEK ASDWQYNITV SAAEIYNEVL RDLLGKEPQE KLEIRLCPDG
SGQLYVPGLT EFQVQSVDDI NKVFEFGYNN RTTEFTNLNE HSSRSHALLI VTVRGVDCST
GLRTTGKLNL VDLAGSERVG KSGAEGNRLR EAQHINRSLS ALGDVIAALR SRQGHVPFRN
SKLTYLLQDS LSGDSKTLMV VQVSPVEKNT SETLYSLRFA ERVRSVELGP GSRRTELGSW
SSQEHLEWEP ACQTPQPTAR AHSAPGSGTS SRPGSIRRKL QPSA
