KINH_RAT
ID KINH_RAT Reviewed; 963 AA.
AC Q2PQA9; Q9WV65;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Kinesin-1 heavy chain;
DE AltName: Full=Conventional kinesin heavy chain;
DE AltName: Full=Ubiquitous kinesin heavy chain;
DE Short=UKHC;
GN Name=Kif5b {ECO:0000312|EMBL:ABC25059.1};
GN Synonyms=Khc {ECO:0000303|PubMed:10573845};
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:0000305, ECO:0000312|EMBL:ABC25059.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RA Allan V.J., McKenzie E.A., Wozniak M.J.;
RT "Sequencing of rat KIF5B from rat testis cDNA library.";
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAD39239.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 551-803.
RC TISSUE=Brain {ECO:0000312|EMBL:AAD39239.1};
RX PubMed=10573845; DOI=10.2307/1542638;
RA Gould R., Freund C., Palmer F., Knapp P.E., Huang J., Morrison H.,
RA Feinstein D.L.;
RT "Messenger RNAs for kinesins and dynein are located in neural processes.";
RL Biol. Bull. 197:259-260(1999).
RN [3] {ECO:0000305}
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-933, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [5]
RP INTERACTION WITH APP, AND TISSUE SPECIFICITY.
RX PubMed=23011729; DOI=10.1088/1478-3975/9/5/055005;
RA Seamster P.E., Loewenberg M., Pascal J., Chauviere A., Gonzales A.,
RA Cristini V., Bearer E.L.;
RT "Quantitative measurements and modeling of cargo-motor interactions during
RT fast transport in the living axon.";
RL Phys. Biol. 9:055005-055005(2012).
RN [6]
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 [7]
RP INTERACTION WITH OGT; RHOT1; RHOT2 AND TRAK1.
RX PubMed=24995978; DOI=10.1016/j.cell.2014.06.007;
RA Pekkurnaz G., Trinidad J.C., Wang X., Kong D., Schwarz T.L.;
RT "Glucose regulates mitochondrial motility via Milton modification by O-
RT GlcNAc transferase.";
RL Cell 158:54-68(2014).
CC -!- FUNCTION: Microtubule-dependent motor required for normal distribution
CC of mitochondria and lysosomes. Can induce formation of neurite-like
CC membrane protrusions in non-neuronal cells in a ZFYVE27-dependent
CC manner (By similarity). Regulates centrosome and nuclear positioning
CC during mitotic entry. During the G2 phase of the cell cycle in a BICD2-
CC dependent manner, antagonizes dynein function and drives the separation
CC of nuclei and centrosomes (By similarity). Required for anterograde
CC axonal transportation of MAPK8IP3/JIP3 which is essential for
CC MAPK8IP3/JIP3 function in axon elongation (PubMed:23576431). Through
CC binding with PLEKHM2 and ARL8B, directs lysosome movement toward
CC microtubule plus ends. Involved in NK cell-mediated cytotoxicity.
CC Drives the polarization of cytolytic granules and microtubule-
CC organizing centers (MTOCs) toward the immune synapse between effector
CC NK lymphocytes and target cells (By similarity).
CC {ECO:0000250|UniProtKB:P33176, ECO:0000250|UniProtKB:Q61768,
CC ECO:0000269|PubMed:23576431}.
CC -!- SUBUNIT: Oligomer composed of two heavy chains and two light chains.
CC Interacts with GRIP1 and PPP1R42 (By similarity). Interacts with SYBU.
CC Interacts with JAKMIP1. Interacts with PLEKHM2. Interacts with ECPAS
CC (By similarity). Interacts with ZFYVE27 (By similarity). Found in a
CC complex with OGT, RHOT1, RHOT2 and TRAK1 (PubMed:24995978). Interacts
CC with APP (via cytoplasmic domain) (PubMed:23011729).
CC {ECO:0000250|UniProtKB:P33176, ECO:0000250|UniProtKB:Q61768,
CC ECO:0000269|PubMed:23011729, ECO:0000269|PubMed:24995978}.
CC -!- INTERACTION:
CC Q2PQA9; Q9UPV9: TRAK1; Xeno; NbExp=3; IntAct=EBI-920191, EBI-1105048;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:7514426}. Cytolytic granule membrane
CC {ECO:0000250|UniProtKB:P33176}. Lysosome membrane
CC {ECO:0000250|UniProtKB:P33176}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P33176}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P33176}. Note=Uniformly distributed between soma
CC and neurites in hippocampal neurons. {ECO:0000269|PubMed:7514426}.
CC -!- TISSUE SPECIFICITY: Expressed in the brain (at protein level)
CC (PubMed:23011729). Expressed in the brain, liver, kidney, spleen,
CC heart, lung and sciatic nerve (PubMed:7514426).
CC {ECO:0000269|PubMed:23011729, ECO:0000269|PubMed:7514426}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the brain in the newborn.
CC {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; DQ309275; ABC25059.1; -; mRNA.
DR EMBL; AF155822; AAD39239.1; -; mRNA.
DR RefSeq; NP_476550.1; NM_057202.1.
DR RefSeq; XP_006254067.1; XM_006254005.1.
DR PDB; 4ATX; EM; 8.20 A; C=1-340.
DR PDBsum; 4ATX; -.
DR AlphaFoldDB; Q2PQA9; -.
DR SMR; Q2PQA9; -.
DR BioGRID; 250763; 5.
DR CORUM; Q2PQA9; -.
DR DIP; DIP-37054N; -.
DR IntAct; Q2PQA9; 11.
DR MINT; Q2PQA9; -.
DR STRING; 10116.ENSRNOP00000023860; -.
DR iPTMnet; Q2PQA9; -.
DR PhosphoSitePlus; Q2PQA9; -.
DR jPOST; Q2PQA9; -.
DR PaxDb; Q2PQA9; -.
DR PRIDE; Q2PQA9; -.
DR GeneID; 117550; -.
DR KEGG; rno:117550; -.
DR UCSC; RGD:621559; rat.
DR CTD; 3799; -.
DR RGD; 621559; Kif5b.
DR VEuPathDB; HostDB:ENSRNOG00000017466; -.
DR eggNOG; KOG0240; Eukaryota.
DR HOGENOM; CLU_001485_11_1_1; -.
DR InParanoid; Q2PQA9; -.
DR OMA; RMAKMMA; -.
DR OrthoDB; 1334528at2759; -.
DR PhylomeDB; Q2PQA9; -.
DR TreeFam; TF105225; -.
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 PRO; PR:Q2PQA9; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Bgee; ENSRNOG00000017466; Expressed in heart and 18 other tissues.
DR Genevisible; Q2PQA9; RN.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0044295; C:axonal growth cone; IDA:RGD.
DR GO; GO:0035253; C:ciliary rootlet; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0032839; C:dendrite cytoplasm; IEA:GOC.
DR GO; GO:0030139; C:endocytic vesicle; ISO:RGD.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043227; C:membrane-bounded organelle; ISO:RGD.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:CAFA.
DR GO; GO:0043005; C:neuron projection; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:HGNC-UCL.
DR GO; GO:0045335; C:phagocytic vesicle; ISO:RGD.
DR GO; GO:0031982; C:vesicle; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0008432; F:JUN kinase binding; IPI:RGD.
DR GO; GO:0008017; F:microtubule binding; IDA:HGNC-UCL.
DR GO; GO:0099609; F:microtubule lateral binding; IMP:CAFA.
DR GO; GO:0003777; F:microtubule motor activity; IDA:HGNC-UCL.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR GO; GO:0099641; P:anterograde axonal protein transport; IMP:UniProtKB.
DR GO; GO:0098971; P:anterograde dendritic transport of neurotransmitter receptor complex; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0071346; P:cellular response to interferon-gamma; ISO:RGD.
DR GO; GO:0051642; P:centrosome localization; ISS:UniProtKB.
DR GO; GO:0007028; P:cytoplasm organization; ISO: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:0032418; P:lysosome localization; ISS:UniProtKB.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0042267; P:natural killer cell mediated cytotoxicity; ISS:UniProtKB.
DR GO; GO:0072383; P:plus-end-directed vesicle transport along microtubule; ISO:RGD.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:RGD.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; IMP:RGD.
DR GO; GO:0043268; P:positive regulation of potassium ion transport; ISO:RGD.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0032230; P:positive regulation of synaptic transmission, GABAergic; ISO:RGD.
DR GO; GO:0031340; P:positive regulation of vesicle fusion; IMP:RGD.
DR GO; GO:1905152; P:positive regulation of voltage-gated sodium channel activity; IMP:RGD.
DR GO; GO:0042391; P:regulation of membrane potential; ISO:RGD.
DR GO; GO:1990049; P:retrograde neuronal dense core vesicle transport; IGI:ARUK-UCL.
DR GO; GO:0035617; P:stress granule disassembly; ISO:RGD.
DR GO; GO:0048489; P:synaptic vesicle transport; IBA:GO_Central.
DR GO; GO:0047496; P:vesicle transport along microtubule; IDA:HGNC-UCL.
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 3D-structure; Acetylation; ATP-binding; Coiled coil; Cytoplasm;
KW Cytoskeleton; Isopeptide bond; Lysosome; Membrane; Methylation;
KW Microtubule; Motor protein; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P33176"
FT CHAIN 2..963
FT /note="Kinesin-1 heavy chain"
FT /id="PRO_0000244485"
FT DOMAIN 8..325
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 908..963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 915..963
FT /note="Globular"
FT /evidence="ECO:0000255"
FT COILED 330..913
FT /evidence="ECO:0000255"
FT BINDING 85..92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P33176"
FT MOD_RES 933
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 945
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61768"
FT MOD_RES 956
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P33176"
FT CROSSLNK 213
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P33176"
SQ SEQUENCE 963 AA; 109531 MW; 0A460B2CBA47EC30 CRC64;
MADPAECNIK VMCRFRPLNE SEVNRGDKYV AKFQGEDTVM IASKPYAFDR VFQSSTSQEQ
VYNDCAKKIV KDVLEGYNGT IFAYGQTSSG KTHTMEGKLH DPEGMGIIPR IVQDIFNYIY
SMDENLEFHI KVSYFEIYLD KIRDLLDVSK TNLSVHEDKN RVPYVKGCTE RFVCSPDEVM
DTIDEGKSNR HVAVTNMNEH SSRSHSIFLI NVKQENTQTE QKLSGKLYLV DLAGSEKVSK
TGAEGAVLDE AKNINKSLSA LGNVISALAE GSTYVPYRDS KMTRILQDSL GGNCRTTIVI
CCSPSSYNES ETKSTLLFGQ RAKTIKNTVC VNVELTAEQW KKKYEKEKEK NKTLRNTIQW
LENELNRWRN GETVPIDEQF DKEKANLEAF TADKDVAITN DKPAAAIGMA GSFTDAERRK
CEEEIAKLYK QLDDKDEEIN QQSQLVEKLK TQMLDQEELL ASTRRDQDNM QAELNRLQAE
NDASKEEVKE VLQALEELAV NYDQKSQEVE DKTKEYELLS DELNQKSATL ASIDAELQKL
KEMTNHQKKR AAEMMASLLK DLAEIGIAVG NNDVKQPEGT GMIDEEFTVA RLYISKMKSE
VKTMVKRCKQ LESTQTESNK KMEENEKELA ACQLRISQHE AKIKSLTEYL QNVEQKKRQL
EESVDSLGEE LVQLRAQEKV HEMEKEHLNK VQTANEVKQA VEQQIQSHRE THQKQISSLR
DEVEAKEKLI TDLQDQNQKM VLEQERLRVE HERLKAVDQE KSRKLHELTV MQDRREQARQ
DLKGLEETVA KELQTLHNLR KLFVQDLATR VKKSAEVDSD DTGGSAAQKQ KISFLENNLE
QLTKVHKQLV RDNADLRCEL PKLEKRLRAT AERVKALESA LKEAKENASR DRKRYQQEVD
RIKEAVRSKN MARRGHSAQI AKPIRPGQHP AASPTHPGAV RGGGSFVQNN QPVGLRGGGG
KQA
