KIF5A_RAT
ID KIF5A_RAT Reviewed; 1027 AA.
AC Q6QLM7;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Kinesin heavy chain isoform 5A;
DE AltName: Full=Kinesin heavy chain neuron-specific 1;
DE AltName: Full=Neuronal kinesin heavy chain;
DE Short=NKHC;
GN Name=Kif5a {ECO:0000312|RGD:1303035};
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] {ECO:0000312|EMBL:AAS45402.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:AAS45402.1};
RA Taylor A.G., Miyashiro K., Eberwine J., Meaney D.F.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=7514426; DOI=10.1016/0896-6273(94)90314-x;
RA Niclas J., Navone F., Hom-Booher N., Vale R.D.;
RT "Cloning and localization of a conventional kinesin motor expressed
RT exclusively in neurons.";
RL Neuron 12:1059-1072(1994).
RN [3]
RP INTERACTION WITH DTNB.
RX PubMed=14600269; DOI=10.1242/jcs.00805;
RA Macioce P., Gambara G., Bernassola M., Gaddini L., Torreri P., Macchia G.,
RA Ramoni C., Ceccarini M., Petrucci T.C.;
RT "Beta-dystrobrevin interacts directly with kinesin heavy chain in brain.";
RL J. Cell Sci. 116:4847-4856(2003).
RN [4]
RP FUNCTION.
RX PubMed=23576431; DOI=10.1074/jbc.m113.464453;
RA Sun T., Yu N., Zhai L.K., Li N., Zhang C., Zhou L., Huang Z., Jiang X.Y.,
RA Shen Y., Chen Z.Y.;
RT "c-Jun NH2-terminal kinase (JNK)-interacting protein-3 (JIP3) regulates
RT neuronal axon elongation in a kinesin- and JNK-dependent manner.";
RL J. Biol. Chem. 288:14531-14543(2013).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 252-351 IN COMPLEX WITH ADP.
RX PubMed=9405049; DOI=10.1021/bi9722498;
RA Sack S., Mueller J., Marx A., Thormaehlen M., Mandelkow E.M., Brady S.T.,
RA Mandelkow E.;
RT "X-ray structure of motor and neck domains from rat brain kinesin.";
RL Biochemistry 36:16155-16165(1997).
CC -!- FUNCTION: Microtubule-dependent motor required for slow axonal
CC transport of neurofilament proteins (NFH, NFM and NFL). Can induce
CC formation of neurite-like membrane protrusions in non-neuronal cells in
CC a ZFYVE27-dependent manner. The ZFYVE27-KIF5A complex contributes to
CC the vesicular transport of VAPA, VAPB, SURF4, RAB11A, RAB11B and RTN3
CC proteins in neurons (By similarity). Required for anterograde axonal
CC transportation of MAPK8IP3/JIP3 which is essential for MAPK8IP3/JIP3
CC function in axon elongation (PubMed:23576431).
CC {ECO:0000250|UniProtKB:P33175, ECO:0000269|PubMed:23576431}.
CC -!- SUBUNIT: Oligomer composed of two heavy chains and two light chains.
CC Interacts with GRIP1. Interacts with FMR1 (via C-terminus); this
CC interaction is increased in a mGluR-dependent manner. Interacts with
CC BORCS5. Interacts with ZFYVE27. Interacts with VAPA, VAPB, SURF4,
CC RAB11A (GDP-bound form), RAB11B (GDP-bound form) and RTN3 in a ZFYVE27-
CC dependent manner. Interacts with BICD2. Interacts with DTNB
CC (PubMed:14600269). {ECO:0000250|UniProtKB:P33175,
CC ECO:0000250|UniProtKB:Q12840, ECO:0000269|PubMed:14600269}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:7514426}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:7514426}. Perikaryon {ECO:0000269|PubMed:7514426}.
CC Note=Concentrated in the cell body of the neurons, particularly in the
CC perinuclear region.
CC -!- TISSUE SPECIFICITY: Expressed in brain. {ECO:0000269|PubMed:7514426}.
CC -!- DOMAIN: Composed of three structural domains: a large globular N-
CC terminal domain which is responsible for the motor activity of kinesin
CC (it hydrolyzes ATP and binds microtubule), a central alpha-helical
CC coiled coil domain that mediates the heavy chain dimerization; and a
CC small globular C-terminal domain which interacts with other proteins
CC (such as the kinesin light chains), vesicles and membranous organelles.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. Kinesin subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00283}.
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DR EMBL; AY535015; AAS45402.1; -; mRNA.
DR RefSeq; NP_997688.1; NM_212523.1.
DR PDB; 2KIN; X-ray; 2.00 A; B=252-351.
DR PDB; 3KIN; X-ray; 3.10 A; B/D=256-372.
DR PDBsum; 2KIN; -.
DR PDBsum; 3KIN; -.
DR AlphaFoldDB; Q6QLM7; -.
DR SMR; Q6QLM7; -.
DR BioGRID; 260858; 4.
DR CORUM; Q6QLM7; -.
DR DIP; DIP-46364N; -.
DR IntAct; Q6QLM7; 7.
DR MINT; Q6QLM7; -.
DR STRING; 10116.ENSRNOP00000007721; -.
DR jPOST; Q6QLM7; -.
DR PaxDb; Q6QLM7; -.
DR PRIDE; Q6QLM7; -.
DR GeneID; 314906; -.
DR KEGG; rno:314906; -.
DR UCSC; RGD:1303035; rat.
DR CTD; 3798; -.
DR RGD; 1303035; Kif5a.
DR eggNOG; KOG0240; Eukaryota.
DR InParanoid; Q6QLM7; -.
DR OrthoDB; 1334528at2759; -.
DR PhylomeDB; Q6QLM7; -.
DR Reactome; R-RNO-2132295; MHC class II antigen presentation.
DR Reactome; R-RNO-5625970; RHO GTPases activate KTN1.
DR Reactome; R-RNO-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-RNO-983189; Kinesins.
DR EvolutionaryTrace; Q6QLM7; -.
DR PRO; PR:Q6QLM7; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0097440; C:apical dendrite; IDA:RGD.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0090724; C:central region of growth cone; IDA:RGD.
DR GO; GO:0035253; C:ciliary rootlet; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0032839; C:dendrite cytoplasm; IEA:GOC.
DR GO; GO:0005871; C:kinesin complex; IDA:RGD.
DR GO; GO:0005874; C:microtubule; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR GO; GO:0000932; C:P-body; IDA:RGD.
DR GO; GO:0043204; C:perikaryon; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0019894; F:kinesin binding; ISO:RGD.
DR GO; GO:0008017; F:microtubule binding; ISO:RGD.
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:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0097110; F:scaffold protein binding; IDA:RGD.
DR GO; GO:0099641; P:anterograde axonal protein transport; IMP:UniProtKB.
DR GO; GO:0098971; P:anterograde dendritic transport of neurotransmitter receptor complex; ISO:RGD.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0071361; P:cellular response to ethanol; IEP:RGD.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEP:RGD.
DR GO; GO:0021987; P:cerebral cortex development; IEP:RGD.
DR GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IBA:GO_Central.
DR GO; GO:0021766; P:hippocampus development; IEP:RGD.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0007017; P:microtubule-based process; TAS:RGD.
DR GO; GO:0048666; P:neuron development; IEP:RGD.
DR GO; GO:1904647; P:response to rotenone; IEP:RGD.
DR GO; GO:1990049; P:retrograde neuronal dense core vesicle transport; IGI:ARUK-UCL.
DR GO; GO:0048489; P:synaptic vesicle transport; IBA:GO_Central.
DR GO; GO:0021794; P:thalamus development; IEP:RGD.
DR GO; GO:0016192; P:vesicle-mediated transport; ISS:UniProtKB.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR027640; Kinesin-like_fam.
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; PS50067; KINESIN_MOTOR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Coiled coil; Cytoplasm;
KW Cytoskeleton; Microtubule; Motor protein; Nucleotide-binding;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q12840"
FT CHAIN 2..1027
FT /note="Kinesin heavy chain isoform 5A"
FT /id="PRO_0000251143"
FT DOMAIN 9..327
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 174..315
FT /note="Microtubule-binding"
FT /evidence="ECO:0000255"
FT REGION 271..361
FT /note="Necessary for interaction with ZFYVE27"
FT /evidence="ECO:0000250|UniProtKB:P33175"
FT REGION 353..1027
FT /note="Interaction with BICD2"
FT /evidence="ECO:0000250|UniProtKB:Q12840"
FT REGION 906..936
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 907..1027
FT /note="Globular"
FT /evidence="ECO:0000255"
FT COILED 331..905
FT /evidence="ECO:0000255"
FT BINDING 86..93
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q12840"
FT MOD_RES 397
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P33175"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:2KIN"
FT HELIX 257..271
FT /evidence="ECO:0007829|PDB:2KIN"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:2KIN"
FT HELIX 283..287
FT /evidence="ECO:0007829|PDB:2KIN"
FT HELIX 289..293
FT /evidence="ECO:0007829|PDB:2KIN"
FT STRAND 294..304
FT /evidence="ECO:0007829|PDB:2KIN"
FT HELIX 308..310
FT /evidence="ECO:0007829|PDB:2KIN"
FT HELIX 311..325
FT /evidence="ECO:0007829|PDB:2KIN"
FT STRAND 328..331
FT /evidence="ECO:0007829|PDB:2KIN"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:2KIN"
FT HELIX 339..350
FT /evidence="ECO:0007829|PDB:2KIN"
SQ SEQUENCE 1027 AA; 116916 MW; 2068CCC4E05A24CB CRC64;
MAETNNECSI KVLCRFRPLN QAEILRGDKF IPIFQGDDSV IIGGKPYVFD RVFPPNTTQE
QVYHACAMQI VKDVLAGYNG TIFAYGQTSS GKTHTMEGKL HDPQLMGIIP RIARDIFNHI
YSMDENLEFH IKVSYFEIYL DKIRDLLDVT KTNLSVHEDK NRVPFVRGCT ERFVSSPEEI
LDVIDEGKSN RHVAVTNMNE HSSRSHSIFL INIKQENIET EQKLSGKLYL ADLAGSEKVS
KTGAEGAVLD EAKNINKSLS ALGNVISALA EGTKSYVPYR DSKMTRILQD SLGGNCRTTM
FICCSPSSYN DAETKSTLMF GQRAKTIKNT ASVNLELTAE QWKKKYEKEK EKTKAQKETI
AKLEAELSRW RNGENVPETE RLAGEDSALA AEICEETPVN DNSSIVVRIA PEERQKYEEE
IRRLYKQLDD KDDEINQQSQ LIEKLKQQML DQEELLVSTR GDNEKVQREL SHLQSENDAA
KEEVKEVLQA LEELAVNYDQ KSQEVEEKSQ QNQLLVDELS QKVATMLSLE SEPQRLQEVS
GHQRKRIAEV LNGLMKDLSE FSVIVGNGEI KLPVEISGAI EEEFTVARLY ISKIKSEVKS
VVKRCRQLEN LQVECHRKME VTGRELSSCQ LLISQHEAKI RSLTEYMQTV ELKKRHLEES
YDSLSDELAK LQAQETVHEV ALKDKEPDTQ DAEEVKKALE LQMENHREAH HRQLARLRDE
INEKQKTIDE LKDLDQKLQL ELEKLQADYE RLKNEENEKS AKLQELTFLY ERHEQSKQDL
KGLEETVARE LQTLHNLRKL FVQDVTTRVK KSAEMEPEDS GGIHSQKQKI SFLENNLEQL
TEVHKQLVRD NADLRCELPK LEKRLRATAE RVKALEGALK EAKEGAMKDK RRYQQEVDRI
KEAVRYKSSG KRGHSAQIAK PVRPGHYPAS SPTNPYGTRS PECISYTNNL FQNYQNLHLQ
AAPSSTSDVY FASNGATSVA PLASYQKANT DNGNATDIND NRSDLPCGYE AEDPAKLFPL
HQETAAS
