KINH_STRPU
ID KINH_STRPU Reviewed; 1031 AA.
AC P35978;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Kinesin heavy chain;
OS Strongylocentrotus purpuratus (Purple sea urchin).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC Euechinoidea; Echinacea; Camarodonta; Echinidea; Strongylocentrotidae;
OC Strongylocentrotus.
OX NCBI_TaxID=7668;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1827446; DOI=10.1083/jcb.113.4.817;
RA Wright B.D., Henson J.H., Wedaman K.P., Willy P.J., Morand J.N.,
RA Scholey J.M.;
RT "Subcellular localization and sequence of sea urchin kinesin heavy chain:
RT evidence for its association with membranes in the mitotic apparatus and
RT interphase cytoplasm.";
RL J. Cell Biol. 113:817-833(1991).
CC -!- FUNCTION: Kinesin is a microtubule-associated force-producing protein
CC that may play a role in organelle transport.
CC -!- SUBUNIT: Oligomer composed of two heavy chains and two light chains.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
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 -!- 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; X56844; CAA40175.1; -; mRNA.
DR PIR; A38713; A38713.
DR RefSeq; NP_999628.1; NM_214463.1.
DR AlphaFoldDB; P35978; -.
DR SMR; P35978; -.
DR STRING; 7668.SPU_021656-tr; -.
DR PRIDE; P35978; -.
DR EnsemblMetazoa; NM_214463; NP_999628; LOC373178.
DR GeneID; 373178; -.
DR KEGG; spu:373178; -.
DR eggNOG; KOG0240; Eukaryota.
DR OMA; RMAKMMA; -.
DR OrthoDB; 1334528at2759; -.
DR PhylomeDB; P35978; -.
DR Proteomes; UP000007110; Unassembled WGS sequence.
DR GO; GO:0032839; C:dendrite cytoplasm; IEA:GOC.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; 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:0008574; F:plus-end-directed microtubule motor activity; IBA:GO_Central.
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:0030705; P:cytoskeleton-dependent intracellular transport; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0048489; P:synaptic vesicle transport; IBA:GO_Central.
DR Gene3D; 3.40.850.10; -; 1.
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 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; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW Motor protein; Nucleotide-binding; Reference proteome.
FT CHAIN 1..1031
FT /note="Kinesin heavy chain"
FT /id="PRO_0000125359"
FT DOMAIN 8..325
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 673..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 858..1031
FT /note="Globular"
FT REGION 906..1031
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 393..857
FT COMPBIAS 673..688
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..975
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1031
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 84..91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1031 AA; 117523 MW; AC6462E773449E58 CRC64;
MADPAECNIK VVCRVRPMNA TEQNTSHICT KFISEEQVQI GGKLNMFDRI FKPNTTQEEV
YNKAARQIVK DVLDGYNGTI FAYGQTSSGK TFTMEGVMGN PQYMGIIPRI VQDIFNHIYQ
MDESLEFHIK VSYFEIYMDR IRDLLDVSKT NLSVHEDKNR VPFVKGATER FASSPEEVMD
VIEEGKSNRH IAVTNMNEHS SRSHSIFLIQ VKQENMETKK KLSGKLYLVD LAGSEKVSKT
GAEGTVLDEA KNINKSLSAL GNVISALADG KKSHIPYRDS KMTRILQESL GGNARTTIVI
CCSPSSFNES ESKSTLMFGQ RAKTIKNTVT VNMELTAEEW RNRYEKEKEK NGRLKAQLLI
LENELQRWRA GESVPVKEQG NKNDEILKEM MKPKQMTVHV SEEEKNKWEE EKVKLYEQLD
EKDSEIDNQS RLTEKLKQQM LEQEELLSSM QRDYELLQSQ MGRLEAENAA AKEEAKEVLQ
ALEEMAVNYD EKSKEVEDKN RMNETLSEEV NEKMTALHTT STELQKLQEL EQHQRRRITE
MMASLLKDLG EIGTALGGNA ADMKPNVENI EKVDEEFTMA RLFVSKMKTE VKTMSQRCKI
LEASNAENET KIRTSEDELD SCRMTIQQHE AKMKSLSENI RETEGKKRHL EDSLDMLNEE
IVKLRAAEEI RLTDQEDKKR EEEDKMQSAT EMQASMSEQM ESHRDAHQKQ LANLRTEINE
KEHQMEELKD VNQRMTLQHE KLQLDYEKLK IEEAEKAAKL RELSQQFDRR EQAKQDLKGL
EETVAKELQT LHNLRKLFVS DLQNRVKKAL EGGDRDDDSG GSQAQKQKIS FLENNLEQLT
KVHKQLVRDN ADLRCELPKL ERRLRATSER VKALEMSLKE TKEGAMRDRK RYQQEVDRIR
EAVRQRNFAK RGSSAQIAKA IRAGHPPPSP GGSTGIRGGG YSGIRGGGSP VIRPPSHGSP
EPISHNNSFE KSLNPNDAEN MEKKANKRLP KLPPGGNKLT ESDIAAMKAR SKARNNTPGK
APLTTSGEQG S
