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Database: UniProt
Entry: F6U7E5_ORNAN
LinkDB: F6U7E5_ORNAN
Original site: F6U7E5_ORNAN 
ID   F6U7E5_ORNAN            Unreviewed;       837 AA.
AC   F6U7E5;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   02-DEC-2020, sequence version 2.
DT   27-MAR-2024, entry version 82.
DE   RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN   Name=KIF18B {ECO:0000313|Ensembl:ENSOANP00000016703.2};
OS   Ornithorhynchus anatinus (Duckbill platypus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Monotremata; Ornithorhynchidae; Ornithorhynchus.
OX   NCBI_TaxID=9258 {ECO:0000313|Ensembl:ENSOANP00000016703.2, ECO:0000313|Proteomes:UP000002279};
RN   [1] {ECO:0000313|Ensembl:ENSOANP00000016703.2, ECO:0000313|Proteomes:UP000002279}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000016703.2,
RC   ECO:0000313|Proteomes:UP000002279};
RX   PubMed=18464734; DOI=10.1038/nature06936;
RA   Warren W.C., Hillier L.W., Marshall Graves J.A., Birney E., Ponting C.P.,
RA   Grutzner F., Belov K., Miller W., Clarke L., Chinwalla A.T., Yang S.P.,
RA   Heger A., Locke D.P., Miethke P., Waters P.D., Veyrunes F., Fulton L.,
RA   Fulton B., Graves T., Wallis J., Puente X.S., Lopez-Otin C., Ordonez G.R.,
RA   Eichler E.E., Chen L., Cheng Z., Deakin J.E., Alsop A., Thompson K.,
RA   Kirby P., Papenfuss A.T., Wakefield M.J., Olender T., Lancet D.,
RA   Huttley G.A., Smit A.F., Pask A., Temple-Smith P., Batzer M.A.,
RA   Walker J.A., Konkel M.K., Harris R.S., Whittington C.M., Wong E.S.,
RA   Gemmell N.J., Buschiazzo E., Vargas Jentzsch I.M., Merkel A., Schmitz J.,
RA   Zemann A., Churakov G., Kriegs J.O., Brosius J., Murchison E.P.,
RA   Sachidanandam R., Smith C., Hannon G.J., Tsend-Ayush E., McMillan D.,
RA   Attenborough R., Rens W., Ferguson-Smith M., Lefevre C.M., Sharp J.A.,
RA   Nicholas K.R., Ray D.A., Kube M., Reinhardt R., Pringle T.H., Taylor J.,
RA   Jones R.C., Nixon B., Dacheux J.L., Niwa H., Sekita Y., Huang X., Stark A.,
RA   Kheradpour P., Kellis M., Flicek P., Chen Y., Webber C., Hardison R.,
RA   Nelson J., Hallsworth-Pepin K., Delehaunty K., Markovic C., Minx P.,
RA   Feng Y., Kremitzki C., Mitreva M., Glasscock J., Wylie T., Wohldmann P.,
RA   Thiru P., Nhan M.N., Pohl C.S., Smith S.M., Hou S., Nefedov M.,
RA   de Jong P.J., Renfree M.B., Mardis E.R., Wilson R.K.;
RT   "Genome analysis of the platypus reveals unique signatures of evolution.";
RL   Nature 453:175-183(2008).
RN   [2] {ECO:0000313|Ensembl:ENSOANP00000016703.2}
RP   IDENTIFICATION.
RC   STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000016703.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283,
CC       ECO:0000256|RuleBase:RU000394}.
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DR   AlphaFoldDB; F6U7E5; -.
DR   STRING; 9258.ENSOANP00000016703; -.
DR   Ensembl; ENSOANT00000016706.3; ENSOANP00000016703.2; ENSOANG00000010540.3.
DR   eggNOG; KOG0242; Eukaryota.
DR   GeneTree; ENSGT00940000161200; -.
DR   InParanoid; F6U7E5; -.
DR   OMA; HQEEKRF; -.
DR   OrthoDB; 239968at2759; -.
DR   TreeFam; TF105231; -.
DR   Proteomes; UP000002279; Chromosome 11.
DR   Bgee; ENSOANG00000010540; Expressed in fibroblast and 3 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR   GO; GO:0035371; C:microtubule plus-end; IEA:Ensembl.
DR   GO; GO:0061673; C:mitotic spindle astral microtubule; IBA:GO_Central.
DR   GO; GO:1990023; C:mitotic spindle midzone; IBA:GO_Central.
DR   GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR   GO; GO:0019894; F:kinesin binding; IEA:Ensembl.
DR   GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR   GO; GO:0008574; F:plus-end-directed microtubule motor activity; IBA:GO_Central.
DR   GO; GO:0007019; P:microtubule depolymerization; IBA:GO_Central.
DR   GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR   GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
DR   GO; GO:0051302; P:regulation of cell division; IEA:Ensembl.
DR   CDD; cd01370; KISc_KIP3_like; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 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; PTHR47968; CENTROMERE PROTEIN E; 1.
DR   PANTHER; PTHR47968:SF13; KINESIN-LIKE PROTEIN; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00283}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Microtubule {ECO:0000256|RuleBase:RU000394};
KW   Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283,
KW   ECO:0000256|RuleBase:RU000394};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00283}; Reference proteome {ECO:0000313|Proteomes:UP000002279}.
FT   DOMAIN          9..353
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          43..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          412..512
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          551..669
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          779..837
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          368..395
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        416..433
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        484..499
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        809..828
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         111..118
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   837 AA;  90335 MW;  53B8515E2679858B CRC64;
     MVTDEEEGTV TVVVRVRPPT PRELEGRRRP VVQVADGRVL VFDPEGPEAG LPGPWGAGGQ
     DGPRRKGKDL RFVFDRVFGE AATQQEVFQH TTRDILDGVL RGHNCSVFAY GATGAGKTHT
     MLGSEADPGI MYLTTRELYR RLDDCREEKP SQVLVSYQEV YNEQIHDLLE PKGPLAIRED
     PDKGVVVQGL SYHQPASAEQ LLEMLARGNR QRTQHPTDAN ATSSRSHAVF QIYMRQQAQG
     AGGGQVLQLA KMSLIDLAGS ERASHTRARG QRLREGANIN RSLLALINVL NALADSKGRK
     SHVPYRDSKL TRLLKDSIGG NCRTVMIAAV SPSALAYEDT YNTLKYADRA KEIKFSLKGN
     VISLDGPAGQ YAAACEQLKA EVAALREKLR AYEGIPAPAP CLPAGSTQIC LPASSPSPIP
     AGPGTPDSSR HPQPNPAAPR EEEGETEPQP EGDAEGTGLS GPQASVRTED EDAGEQDQAP
     GPGPISPLTR PPEPAAENPV SPRPSGADRT RRLAQTVLRL ARRQYALLKA AELLTPDVIS
     EFAALRRLVR EEKTVPWGEE DEEEEERDGN ADPSQEGLPE IGEDLRPAPS QENPTASGHP
     GPVTRTAARQ LGGLPSTPGP SPADPCPPRK KRRWQSGPSP PERTRAPAPT RQAKRQRQSL
     LPCLGRGPLP RPAPAAEHCL ATSTPVGKAN PPHCSLRICP ATVTKTRPPL GPSAAQNCSV
     PWALPCQDLN ATFDLPEGGR VPAPASACKP CAPEFPGWEN VPRNQDRLGG PFIPRGPVAV
     FTTKGPSAPP GRPPRTGPVP LQRCLSEEET LGQRVRRPLL TRPRRPEPHR PPARQHR
//
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