KIF3A_MACFA
ID KIF3A_MACFA Reviewed; 702 AA.
AC Q4R628;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Kinesin-like protein KIF3A;
DE AltName: Full=Microtubule plus end-directed kinesin motor 3A;
GN Name=KIF3A; ORFNames=QtsA-19288;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Microtubule-based anterograde translocator for membranous
CC organelles. Plus end-directed microtubule sliding activity in vitro.
CC Plays a role in primary cilia formation. Plays a role in centriole
CC cohesion and subdistal appendage organization and function. Regulates
CC the formation of the subdistal appendage via recruitment of DCTN1 to
CC the centriole. Also required for ciliary basal feet formation and
CC microtubule anchoring to mother centriole.
CC {ECO:0000250|UniProtKB:P28741}.
CC -!- SUBUNIT: Heterodimer of KIF3A and KIF3B (By similarity). Interacts with
CC PIFO. Interacts with CLN3 (By similarity). Interacts with DCTN1 (By
CC similarity). Interacts with FLCN. Interacts with AP3B1 (By similarity).
CC {ECO:0000250|UniProtKB:P28741, ECO:0000250|UniProtKB:Q9Y496}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Cell
CC projection, cilium {ECO:0000250|UniProtKB:P28741}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome, centriole
CC {ECO:0000250|UniProtKB:P28741}. Note=Localizes to the subdistal
CC appendage region of the centriole. {ECO:0000250|UniProtKB:P28741}.
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; AB169362; BAE01447.1; -; mRNA.
DR RefSeq; NP_001306382.1; NM_001319453.1.
DR AlphaFoldDB; Q4R628; -.
DR SMR; Q4R628; -.
DR STRING; 9541.XP_005557792.1; -.
DR PRIDE; Q4R628; -.
DR GeneID; 101865142; -.
DR CTD; 11127; -.
DR eggNOG; KOG4280; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0005929; C:cilium; ISS:UniProtKB.
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:0010457; P:centriole-centriole cohesion; ISS:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0034454; P:microtubule anchoring at centrosome; ISS:UniProtKB.
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; 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 2: Evidence at transcript level;
KW ATP-binding; Cell projection; Cilium; Cilium biogenesis/degradation;
KW Coiled coil; Cytoplasm; Cytoskeleton; Microtubule; Motor protein;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..702
FT /note="Kinesin-like protein KIF3A"
FT /id="PRO_0000230790"
FT DOMAIN 14..345
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 372..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..702
FT /note="Globular"
FT REGION 667..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 355..593
FT /evidence="ECO:0000255"
FT COMPBIAS 382..398
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..424
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 100..107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 690
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y496"
SQ SEQUENCE 702 AA; 80341 MW; 4A0C3E7CEDBFAAB4 CRC64;
MPINKSEKPE SCDNVKVVVR CRPLNEREKS MCYKQAVSVD EMRGTITVHK TDSSNEPPKT
FTFDTVFGPE SKQLDVYNLT ARPIIDSVLE GYNGTIFAYG QTGTGKTFTM EGVRAVPELR
GIIPNSFAHI FGHIAKAEGD TRFLVRVSYL EIYNEEVRDL LGKDQTQRLE VKERPDVGVY
IKDLSAYVVN NADDMDRIMT LGHKNRSVGA TNMNEHSSRS HAIFTITIEC SEKGIDGNMH
VRMGKLHLVD LAGSERQAKT GATGQRLKEA TKINLSLSTL GNVISALVDG KSTHVPYRNS
KLTRLLQDSL GGNSKTMMCA NIGPADYNYD ETISTLRYAN RAKNIKNKAR INEDPKDALL
RQFQKEIEEL KKKLEEGEEI SGSDISGSEE DDDEEGEVGE DGEKRKKRRD QAGKKKVSPD
KMIEMQAKID EERKALETKL DMEEEERNKA RAELEKREKD LLKAQQEHQS LLEKLSALEK
KVIVGGVDLL AKAEEQEKLL EESNMELEER RKRAEQLRRE LEEKEQERLD IEEKYTSLQE
EAQGKTKKLK KVWTMLMAAK SEMADLQQEH QREIEGLLEN IRQLSRELRL QMLIIDNFIP
RDYQEMIENY VHWNEDIGEW QLKCVAYTGN NMRKQTPVPD KKEKDPFEVD LSHVYLAYTE
ESLRQSLMKL ERPRTSKGKA RPKTGRRKRS AKPETVIDSL LQ
