KINH_NEUCR
ID KINH_NEUCR Reviewed; 928 AA.
AC P48467; Q7RVK5;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Kinesin heavy chain;
GN Name=kin; ORFNames=NCU09730;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=74A;
RX PubMed=8589459; DOI=10.1091/mbc.6.11.1605;
RA Steinberg G., Schliwa M.;
RT "The Neurospora organelle motor: a distant relative of conventional kinesin
RT with unconventional properties.";
RL Mol. Biol. Cell 6:1605-1618(1995).
RN [2]
RP SEQUENCE REVISION.
RA Kirchner J.;
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-355 IN COMPLEX WITH ADP.
RX PubMed=11707393; DOI=10.1093/emboj/20.22.6213;
RA Song Y.-H., Marx A., Muller J., Woehlke G., Schliwa M., Krebs A.,
RA Hoenger A., Mandelkow E.;
RT "Structure of a fast kinesin: implications for ATPase mechanism and
RT interactions with microtubules.";
RL EMBO J. 20:6213-6225(2001).
CC -!- FUNCTION: Kinesin is a microtubule-associated force-producing protein
CC that may play a role in organelle transport. Its motor activity is
CC directed toward the microtubule's plus end.
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; L47106; AAB52961.1; -; mRNA.
DR EMBL; CM002239; EAA35196.2; -; Genomic_DNA.
DR PIR; T10164; T10164.
DR RefSeq; XP_964432.2; XM_959339.3.
DR PDB; 1GOJ; X-ray; 2.30 A; A=1-355.
DR PDBsum; 1GOJ; -.
DR AlphaFoldDB; P48467; -.
DR SMR; P48467; -.
DR STRING; 5141.EFNCRP00000009482; -.
DR PRIDE; P48467; -.
DR EnsemblFungi; EAA35196; EAA35196; NCU09730.
DR GeneID; 3880594; -.
DR KEGG; ncr:NCU09730; -.
DR VEuPathDB; FungiDB:NCU09730; -.
DR HOGENOM; CLU_001485_3_1_1; -.
DR InParanoid; P48467; -.
DR OMA; RMAKMMA; -.
DR EvolutionaryTrace; P48467; -.
DR Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:CAFA.
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:0099609; F:microtubule lateral binding; IMP:CAFA.
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:0030705; P:cytoskeleton-dependent intracellular transport; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
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; 2.
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; ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Microtubule; Motor protein; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..928
FT /note="Kinesin heavy chain"
FT /id="PRO_0000125362"
FT DOMAIN 7..330
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 395..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 893..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 343..866
FT /evidence="ECO:0000255"
FT COMPBIAS 395..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..928
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 88..95
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 238..245
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT STRAND 9..14
FT /evidence="ECO:0007829|PDB:1GOJ"
FT HELIX 19..22
FT /evidence="ECO:0007829|PDB:1GOJ"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:1GOJ"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:1GOJ"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:1GOJ"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:1GOJ"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:1GOJ"
FT HELIX 61..68
FT /evidence="ECO:0007829|PDB:1GOJ"
FT HELIX 70..76
FT /evidence="ECO:0007829|PDB:1GOJ"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:1GOJ"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:1GOJ"
FT HELIX 94..98
FT /evidence="ECO:0007829|PDB:1GOJ"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:1GOJ"
FT HELIX 111..124
FT /evidence="ECO:0007829|PDB:1GOJ"
FT STRAND 130..142
FT /evidence="ECO:0007829|PDB:1GOJ"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:1GOJ"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:1GOJ"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:1GOJ"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:1GOJ"
FT HELIX 180..200
FT /evidence="ECO:0007829|PDB:1GOJ"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:1GOJ"
FT STRAND 209..220
FT /evidence="ECO:0007829|PDB:1GOJ"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:1GOJ"
FT STRAND 226..235
FT /evidence="ECO:0007829|PDB:1GOJ"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:1GOJ"
FT TURN 252..255
FT /evidence="ECO:0007829|PDB:1GOJ"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:1GOJ"
FT HELIX 261..274
FT /evidence="ECO:0007829|PDB:1GOJ"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:1GOJ"
FT HELIX 286..290
FT /evidence="ECO:0007829|PDB:1GOJ"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:1GOJ"
FT STRAND 300..307
FT /evidence="ECO:0007829|PDB:1GOJ"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:1GOJ"
FT HELIX 314..328
FT /evidence="ECO:0007829|PDB:1GOJ"
FT STRAND 338..341
FT /evidence="ECO:0007829|PDB:1GOJ"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:1GOJ"
SQ SEQUENCE 928 AA; 102411 MW; 2E2475195F674C02 CRC64;
MSSSANSIKV VARFRPQNRV EIESGGQPIV TFQGPDTCTV DSKEAQGSFT FDRVFDMSCK
QSDIFDFSIK PTVDDILNGY NGTVFAYGQT GAGKSYTMMG TSIDDPDGRG VIPRIVEQIF
TSILSSAANI EYTVRVSYME IYMERIRDLL APQNDNLPVH EEKNRGVYVK GLLEIYVSSV
QEVYEVMRRG GNARAVAATN MNQESSRSHS IFVITITQKN VETGSAKSGQ LFLVDLAGSE
KVGKTGASGQ TLEEAKKINK SLSALGMVIN ALTDGKSSHV PYRDSKLTRI LQESLGGNSR
TTLIINCSPS SYNDAETLST LRFGMRAKSI KNKAKVNAEL SPAELKQMLA KAKTQITSFE
NYIVNLESEV QVWRGGETVP KEKWVPPLEL AITPSKSAST TARPSTPSRL LPESRAETPA
ISDRAGTPSL PLDKDEREEF LRRENELQDQ IAEKESIAAA AERQLRETKE ELIALKDHDS
KLGKENERLI SESNEFKMQL ERLAFENKEA QITIDGLKDA NSELTAELDE VKQQMLDMKM
SAKETSAVLD EKEKKKAEKM AKMMAGFDLS GDVFSDNERA VADAIAQLDA LFEISSAGDA
IPPEDIKALR EKLVETQGFV RQAELSSFSA ASSDAEARKR AELEARLEAL QQEHEELLSR
NLTEADKEEV KALLAKSLSD KSAVQVELVE QLKADIALKN SETEHLKALV DDLQRRVKAG
GAGVAMANGK TVQQQLAEFD VMKKSLMRDL QNRCERVVEL EISLDETREQ YNNVLRSSNN
RAQQKKMAFL ERNLEQLTQV QRQLVEQNSA LKKEVAIAER KLMARNERIQ SLESLLQESQ
EKMAQANHKF EVQLAAVKDR LEAAKAGSTR GLGTDAGLGG FSIGSRIAKP LRGGGDAVAG
ATATNPTIAT LQQNPPENKR SSWFFQKS
