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Database: UniProt
Entry: L8YAI4_TUPCH
LinkDB: L8YAI4_TUPCH
Original site: L8YAI4_TUPCH 
ID   L8YAI4_TUPCH            Unreviewed;      1760 AA.
AC   L8YAI4;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Kinesin-like protein KIF13A {ECO:0000313|EMBL:ELV12074.1};
DE   Flags: Fragment;
GN   ORFNames=TREES_T100012594 {ECO:0000313|EMBL:ELV12074.1};
OS   Tupaia chinensis (Chinese tree shrew).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Scandentia; Tupaiidae; Tupaia.
OX   NCBI_TaxID=246437 {ECO:0000313|EMBL:ELV12074.1, ECO:0000313|Proteomes:UP000011518};
RN   [1] {ECO:0000313|Proteomes:UP000011518}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Zhang G., Fan Y., Yao Y., Huang Z.;
RT   "Genome of the Chinese tree shrew, a rising model animal genetically
RT   related to primates.";
RL   Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000011518}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23385571; DOI=10.1038/ncomms2416;
RA   Fan Y., Huang Z.Y., Cao C.C., Chen C.S., Chen Y.X., Fan D.D., He J.,
RA   Hou H.L., Hu L., Hu X.T., Jiang X.T., Lai R., Lang Y.S., Liang B.,
RA   Liao S.G., Mu D., Ma Y.Y., Niu Y.Y., Sun X.Q., Xia J.Q., Xiao J.,
RA   Xiong Z.Q., Xu L., Yang L., Zhang Y., Zhao W., Zhao X.D., Zheng Y.T.,
RA   Zhou J.M., Zhu Y.B., Zhang G.J., Wang J., Yao Y.G.;
RT   "Genome of the Chinese tree shrew.";
RL   Nat. Commun. 4:1426-1426(2013).
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR   EMBL; KB364734; ELV12074.1; -; Genomic_DNA.
DR   STRING; 246437.L8YAI4; -.
DR   eggNOG; KOG0241; Eukaryota.
DR   InParanoid; L8YAI4; -.
DR   Proteomes; UP000011518; Unassembled WGS sequence.
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-UniRule.
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   CDD; cd22729; FHA_KIF13A; 1.
DR   Gene3D; 2.60.200.20; -; 1.
DR   Gene3D; 6.10.250.2520; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR022164; Kinesin-like.
DR   InterPro; IPR022140; Kinesin-like_KIF1-typ.
DR   InterPro; IPR032405; Kinesin_assoc.
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   InterPro; IPR008984; SMAD_FHA_dom_sf.
DR   PANTHER; PTHR47117:SF5; -; 1.
DR   PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR   Pfam; PF12473; DUF3694; 2.
DR   Pfam; PF00498; FHA; 1.
DR   Pfam; PF12423; KIF1B; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   Pfam; PF16183; Kinesin_assoc; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF49879; SMAD/FHA domain; 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};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW   Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00283}; Reference proteome {ECO:0000313|Proteomes:UP000011518}.
FT   DOMAIN          1..358
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          13..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          641..664
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1386..1406
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1532..1557
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1570..1669
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1696..1741
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          370..415
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          613..640
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1090..1117
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        18..33
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1541..1557
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1570..1591
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1696..1721
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         108..115
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ELV12074.1"
SQ   SEQUENCE   1760 AA;  195121 MW;  8AF04EF96379DD56 CRC64;
     ELELNTKCVV EMEGNQTVLH PPPSNSKQGE SPSDEDSGCA PPASGSRLLC PALKRARLTQ
     PHAVTGGAPV WVSHSGRAAG QEVVFKCLGE GILEKAFQGY NACIFAYGQT GSGKSFSMMG
     HAEQLGLIPR LCCALFRRIS LEQNESQTFK VEVSYMEIYN EKVRDLLDPK GSRQSLKVRE
     HKVLGPYVDG LSQLAVTSFE DIESLMSEGN KSRTVAATNM NEESSRSHAV FNIIITQTLY
     DLQSGNSGEK VSKVSLVDLA GSERVSKTGA AGERLKEGSN INKSLTTLGL VISSLADQAA
     GKGKNKFVPY RDSVLTWLLK DNLGGNSQTS MIATISPAAD NYEETLSTLR YADRAKRIVN
     HAVVNEDPNA KVIRELREEV EKLREQLSRA EAMKAPELKE KLEESEKLIK ELTVTWEEKL
     RKTEEIAQER QRQLESMGIS LETSGIKVGE DKCYLVNLNA DPALNELLVY YLKDHTRVGA
     DTSQDIQLFG IGIQPEHCEI AIASDGDVTL TPKENARSCV NGAQVCSGTQ LWHGDRILWG
     NNHFFRINLP KRKRRDWLKD LEKETGPPEH DLDAASEASS EPDYNYEFAQ MEVIMKTLNS
     NDPVQNVVQV LEKQYLEEKR SALEEQRLMY ERELEQLRQQ LSPERQAPAP PPAGPTAARR
     HSSKDELFRQ SLAKLREQLV KANTLVREAN FLAEEMRKLT DYQVTLQIPA TNLSANRKRG
     VIVSEPAIQV RRKGKSTQVW TIEKLENKLI DMRDLYQEWK EKVPEAKRLY GKRGDPFYEA
     QENHNLIGVA NVFLECLFCD VKLQYAVPII SQQGEVAGRL HVEVMRVTGA VPERVVEDDS
     SENSSESGSL EVVDSSGEIA HRVKKLTCRV KIKEATGLPL NLSNFVFCQY TFWDQCESTV
     AAPVVDPDVP SPQSKDARYS VTFSHCKDYV VNVTEEFLEF ISEGALAIEV WGHRCAGNGS
     SIWEVDSLHA KTRTLHDRWN EVTRRIEMWI SILELNELGE YAAVELHQAK DVNTGGIFQL
     RQGHSRRVQV TVKPVQHSGT LPLMVEAILS VSIGCVTARS TKLQRGLDSY QEEDLNCVRE
     RWSDALIKRR EYLDEQIKKV SNKKEKTEDD VEREARLVGQ WVGLTEERNA VLVPAPGSGI
     PGAPADWVPP PGMETHIPVL FLDLNADDLS ANEQLVGPHA SGVNSILPKE HGSQFFYLPI
     IKHSDEEVSA TASWDSSVHD SVHLNRVTPQ NERIYLIVKA TVQLSHPAAM ELVLRKRIAA
     NIYNKQATEE IEDRETLALL AARSDSEGTC DGETYIEKYT RGVLQLENIL SLERLRPGSH
     PAVTVKEALS AKARHIRRSV STPNVHNVSS SRGDLSGFDE DDKGWLENQL DVSDYSSSYQ
     DVACYGTLPR DSPRRSKEGS GCAAESPHAL TVSPFKAFSP QPPKFFKPLM PVKEEHKKRT
     ALEARPLLSQ ESVLPPQAPS PGCIVPPGSN GSCMPLEHDS KREKKIDSEE EEGELEALNR
     TLMSSQPYVP VEFADFSVYN AGLESREWFS KADLSSSRAL EKEVSRSPTA SSITSGYFSH
     SASNATLSDV AVPTSDSSDQ LAVQTRDADS SEHGGPSLGP EFRPSPHREL TEGERGSGQE
     KVTAGPQQED SALPGASLAW QSPPEKSADV PGRTGPRLGL SSRPARELCP REVTVEHTTD
     VLEDHAFTEF MGVADGKDLD GVRDSAGALL SRRDRPNKAE STRVPDGPQP PGRPCSELEN
     DQVIRVPEAA LRFRAVREHV
//
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