KIFC2_MOUSE
ID KIFC2_MOUSE Reviewed; 792 AA.
AC O08672; O08613;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Kinesin-like protein KIFC2;
GN Name=Kifc2;
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].
RC STRAIN=ICR; TISSUE=Brain;
RX PubMed=9115736; DOI=10.1016/s0896-6273(00)81243-x;
RA Saito N., Okada Y., Noda Y., Kinoshita Y., Kondo S., Hirokawa N.;
RT "KIFC2 is a novel neuron-specific C-terminal type kinesin superfamily motor
RT for dendritic transport of multivesicular body-like organelles.";
RL Neuron 18:425-438(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RX PubMed=9115737; DOI=10.1016/s0896-6273(00)81244-1;
RA Hanlon D.W., Yang Z., Goldstein L.S.;
RT "Characterization of KIFC2, a neuronal kinesin superfamily member in
RT mouse.";
RL Neuron 18:439-451(1997).
RN [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=11259594; DOI=10.1128/mcb.21.7.2463-2466.2001;
RA Yang Z., Roberts E.A., Goldstein L.S.;
RT "Functional analysis of mouse C-terminal kinesin motor KifC2.";
RL Mol. Cell. Biol. 21:2463-2466(2001).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
CC -!- FUNCTION: May play a role in microtubule-dependent retrograde axonal
CC transport. May function as the motor for the transport of
CC multivesicular body (MVB)-like organelles in dendrites.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Present in axons and dendrites of neurons in the
CC central and peripheral nervous systems.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:11259594}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}.
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DR EMBL; D49545; BAA19677.1; -; mRNA.
DR EMBL; U92949; AAB51397.1; -; mRNA.
DR CCDS; CCDS27583.1; -.
DR AlphaFoldDB; O08672; -.
DR SMR; O08672; -.
DR STRING; 10090.ENSMUSP00000004294; -.
DR iPTMnet; O08672; -.
DR PhosphoSitePlus; O08672; -.
DR PaxDb; O08672; -.
DR PRIDE; O08672; -.
DR ProteomicsDB; 263606; -.
DR MGI; MGI:109187; Kifc2.
DR eggNOG; KOG0239; Eukaryota.
DR InParanoid; O08672; -.
DR PhylomeDB; O08672; -.
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 PRO; PR:O08672; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O08672; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; 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:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0090307; P:mitotic spindle assembly; 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; 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 ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW Motor protein; Nucleotide-binding; Reference proteome.
FT CHAIN 1..792
FT /note="Kinesin-like protein KIFC2"
FT /id="PRO_0000125430"
FT DOMAIN 409..732
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 22..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 734..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 186..347
FT /evidence="ECO:0000255"
FT COMPBIAS 142..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..764
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 486..493
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT CONFLICT 447
FT /note="C -> R (in Ref. 2; AAB51397)"
FT /evidence="ECO:0000305"
FT CONFLICT 618
FT /note="P -> A (in Ref. 2; AAB51397)"
FT /evidence="ECO:0000305"
FT CONFLICT 698
FT /note="W -> C (in Ref. 2; AAB51397)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 792 AA; 85686 MW; F8616F929B1613B6 CRC64;
MYAFYSLLIY IFYSLFRRDG GAAAVSDPGD PTQKSGGQPR GRRRPDQFTS ELWSELNSLA
GCSESEDGQK GAEGGAAEVS LEEALMRLAE FLSVQLGAEE SCGTTPDLGK PGEVPPLLTV
TSQLLALLAW TRSPRGRQAL LQGTQPTCPV QPSTLDGSLS QEESSSQPTP ILDEVPRDET
QEHQPLQLEE EQRVWQRLEQ LILGQLEELR QQLEQQEEEL SRLRLGVGVT DSEKRVQHLT
LENEALKQSL SLTRDLLLHW GPGPLPRLSQ EEAGALLELQ GQLQEAQDTT EALRVQLGAQ
ELQLQGLRGA LRQLQQETEQ NCRQELQQVH GQLAGLRARM ASLRQGCGDL RGLVSTFTQS
CQGSLSEAQG QVSWALGALS AGKAKTQLSE GNQAPPTGCS GRLLELKGNI RVLCRLRPAE
GQPSSLVSVE PGQGGTITTC YRGRQHCFRL DWVFPQDASQ EEVFRQLEPA VLSCLQGYSV
CIFTYGQTGT GKTYSMEGPP EDPGIAPRAL QLLFREMGTG GHHHVTLSMV EIYNEAVRDL
LATGPPERLV VRQGPAGQGG IQVAGLTHWD VPNLETLHQM LSLGRSNRAT AATVMNQHSS
RSHALVTLTL RAASPPRPQG ITGTLHLVDL AGSERVWKAG VASPVQRDPN GARRLREAQA
INRSLLALGG VMAALRARRP HVPFRDSQLT RLLQPALWAG TTAVLLLQIS TRAEDLGETI
CSLKFAERVG QVELGPARRR RAPRSGTPSS LSTDTPLTGT SCTPTPSPGS PPSTSPNSCS
GLTLEPPGDP PP
