ID   KINH_DORPE              Reviewed;         967 AA.
AC   P21613;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Kinesin heavy chain;
OS   Doryteuthis pealeii (Longfin inshore squid) (Loligo pealeii).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC   Coleoidea; Decapodiformes; Teuthida; Myopsina; Loliginidae; Doryteuthis.
OX   NCBI_TaxID=1051067;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2137456; DOI=10.1016/s0021-9258(19)39764-9;
RA   Kosik K.S., Orecchio L.D., Schnapp B., Inouye H., Neve R.L.;
RT   "The primary structure and analysis of the squid kinesin heavy chain.";
RL   J. Biol. Chem. 265:3278-3283(1990).
RN   [2]
RP   INTERACTION WITH AMYLOID-BETA PRECURSOR-LIKE PROTEIN, AND SUBCELLULAR
RP   LOCATION.
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).
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       Interacts with amyloid-beta precursor-like protein (via cytoplasmic
CC       domain) (PubMed:23011729). {ECO:0000269|PubMed:23011729}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Cell
CC       projection, axon {ECO:0000269|PubMed:23011729}.
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; J05258; AAA29990.1; -; mRNA.
DR   PIR; A35075; A35075.
DR   AlphaFoldDB; P21613; -.
DR   SMR; P21613; -.
DR   GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
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; 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   1: Evidence at protein level;
KW   ATP-binding; Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Microtubule; Motor protein; Nucleotide-binding.
FT   CHAIN           1..967
FT                   /note="Kinesin heavy chain"
FT                   /id="PRO_0000125358"
FT   DOMAIN          8..326
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   REGION          173..314
FT                   /note="Microtubule-binding"
FT   REGION          387..411
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          862..967
FT                   /note="Globular"
FT   REGION          923..967
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          392..861
FT   BINDING         85..92
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   967 AA;  109407 MW;  CC40353FA3F33E35 CRC64;
     MDVASECNIK VICRVRPLNE AEERAGSKFI LKFPTDDSIS IAGKVFVFDK VLKPNVSQEY
     VYNVGAKPIV ADVLSGCNGT IFAYGQTSSG KTHTMEGVLD KPSMHGIIPR IVQDIFNYIY
     GMDENLEFHI KISYYEIYLD KIRDLLDVTK TNLAVHEDKN RVPFVKGATE RFVSSPEEVM
     EVIDEGKNNR HVAVTNMNEH SSRSHSVFLI NVKQENVETQ KKLSGKLYLV DLAGSEKVSK
     TGAEGAVLDE AKNINKSLSA LGNVISALAD GNKSHVPYRD SKLTRILQES LGGNARTTMV
     ICCSPASYNE SETKSTLLFG QRAKTIKNVV SVNEELTADE WKRRYEKEKE RVTKLKATMA
     KLEAELQRWR TGQAVSVEEQ VDLKEDVPAE SPATSTTSLA GGLIASMNEG DRTQLEEERL
     KLYQQLDDKD DEINNQSQLI EKLKEQMMEQ EDLIAQSRRD YENLQQDMSR IQADNESAKD
     EVKEVLQALE ELAMNYDQKS QEVEDKNKEN ENLSEELNQK LSTLNSLQNE LDQLKDSSMH
     HRKRVTDMMI NLLKDLGDIG TIVGGNAAET KPTAGSGEKI EEEFTVARLY ISKMKSEVKT
     LVSRNNQLEN TQQDNFKKIE THEKDLSNCK LLIQQHEAKM ASLQEAIKDS ENKKRMLEDN
     VDSLNEEYAK LKAQEQMHLA ALSEREKETS QASETREVLE KQMEMHREQH QKQLQSLRDE
     ISEKQATVDN LKDDNQRLSL ALEKLQADYD KLKQEEVEKA AKLADLSLQI DRREQAKQDL
     KGLEETVAKE LQTLHNLRKL FVQDLQNKVK KSCSKTEEED EDTGGNAAQK QKISFLENNL
     EQLTKVHKQL VRDNADLRCE LPKLEKRLRA TMERVKSLES ALKDAKEGAM RDRKRYQHEV
     DRIKEAVRQK NLARRGHAAQ IAKPIRPGQH QSVSPAQAAA IRGGGGLSQN GPMITSTPIR
     MAPESKA