ID   KIF3C_PONAB             Reviewed;         793 AA.
AC   Q5R706;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Kinesin-like protein KIF3C;
GN   Name=KIF3C;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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; CR860317; CAH92454.1; -; mRNA.
DR   RefSeq; NP_001124561.1; NM_001131089.1.
DR   AlphaFoldDB; Q5R706; -.
DR   SMR; Q5R706; -.
DR   STRING; 9601.ENSPPYP00000014056; -.
DR   GeneID; 100169734; -.
DR   KEGG; pon:100169734; -.
DR   CTD; 3797; -.
DR   eggNOG; KOG4280; Eukaryota.
DR   InParanoid; Q5R706; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
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..793
FT                   /note="Kinesin-like protein KIF3C"
FT                   /id="PRO_0000262924"
FT   DOMAIN          10..365
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   REGION          250..288
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          395..423
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          631..793
FT                   /note="Globular"
FT                   /evidence="ECO:0000255"
FT   REGION          756..793
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          376..630
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        253..273
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        758..782
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   793 AA;  89515 MW;  A4DACAF92874B830 CRC64;
     MASKTKASEA LKVVARCRPL SRKEEAAGHE QILTMDVKLG QVTLRNPRAA PGELPKTFTF
     DAVYDASSKQ ADLYDETVRP LIDSVLQGFN GTVFAYGQTG TGKTYTMQGT WVEPELRGVI
     PNAFEHIFTH ISRSQNQQYL VRASYLEIYQ EEIRDLLSKE PGKRLELKEN PETGVYIKDL
     SSFVTKNVKE IEHVMNLGNQ TRAVGSTHMN EVSSRSHAIF IITVECSERG SDGQDHIRVG
     KLNLVDLAGS ERQNKAGPNT AGGASTPSSG GSGGGGGSGG GAGGERPKEA SKINLSLSAL
     GNVIAALAGN RSTHIPYRDS KLTRLLQDSL GGNAKTIMVA TLGPASHSYD ESLSTLRFAN
     RAKNIKNKPR VNEDPKDTLL REFQEEIARL KAQLEKRGML GKRPRRKSSR GKKAVSAPPG
     YPESPVIEAW VAEEEDDNNN NHRPPQPILE SALEKNMENY LQEQKERLEE EKAAIQDDRS
     LVSEEKQKLL EEKEKMLEKD LRREQQATEL LAAKYKAMES KLLIGGRNIM DHTNEQQKML
     ELKRQEIAEQ KRREREMQQE MMLRDEETME LRGTYTSLQQ EVEVKTKKLK KLYAKLQAVK
     AEIQDQHDEY IRVRQDLEEA QNEQTRELKL KYLIIENFIP PEEKNKIMNR LFLDCEEEQW
     KFQPLVPAGV NSQMKKRPTS AVGYKRPISQ YARVAMAMGS HPRYRAENIM FLELDVSPPA
     VFEMEFSHDQ EQDPRALHME RLMRLDSFLE RLSTSKVRKS RSWCQSPQRP PPSTTHASLA
     SASLRPATVA DHE