ID A0A3Q1M799_BOVIN Unreviewed; 1796 AA.
AC A0A3Q1M799;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Kinesin family member 13B {ECO:0000313|Ensembl:ENSBTAP00000066240.1};
GN Name=KIF13B {ECO:0000313|Ensembl:ENSBTAP00000066240.1,
GN ECO:0000313|VGNC:VGNC:30582};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000066240.1, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000066240.1, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000066240.1,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000066240.1}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000066240.1};
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}.
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DR Ensembl; ENSBTAT00000081795.1; ENSBTAP00000066240.1; ENSBTAG00000017232.6.
DR VEuPathDB; HostDB:ENSBTAG00000017232; -.
DR VGNC; VGNC:30582; KIF13B.
DR GeneTree; ENSGT00940000155500; -.
DR Proteomes; UP000009136; Chromosome 8.
DR Bgee; ENSBTAG00000017232; Expressed in spiral colon and 108 other cell types or tissues.
DR ExpressionAtlas; A0A3Q1M799; baseline.
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; cd22730; FHA_KIF13B; 1.
DR CDD; cd01365; KISc_KIF1A_KIF1B; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 6.10.250.2520; -; 1.
DR Gene3D; 2.30.30.190; CAP Gly-rich-like domain; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
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; PF01302; CAP_GLY; 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; SM01052; CAP_GLY; 1.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF74924; Cap-Gly domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS00845; CAP_GLY_1; 1.
DR PROSITE; PS50245; CAP_GLY_2; 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|ARBA:ARBA00023054};
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:UP000009136}.
FT DOMAIN 1..331
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 1683..1725
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT REGION 526..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 620..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1345..1392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1467..1532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1548..1597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1731..1796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..541
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..558
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1352..1392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1499..1520
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1753..1770
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 81..88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1796 AA; 198277 MW; 797880C071F75A9F CRC64;
GRKIDLHTKC VVDVDANKVI LNPVNTDLSK GDVFAYDHCF WSMDESVRDK YAGQDDVFKC
LGENILQNAF DGYNACVFAY GQTGSGKSYT MMGTADQPGL IPRLCSGLFE RTQKEENEEQ
SFKVEVSYME IYNEKVRDLL DPKGSRQTLK VREHSVLGPY VDGLSKLAVT SYKDIESLMS
EGNKSRTVAA TNMNEESSRS HAVFKITLTH TLYDVKSGTS GEKVGKLSLV DLAGSERATK
TGAAGDRLKE GSNINKSLTT LGLVISALAD QGAGKSKNKF VPYRDSVLTW LLKDSLGGNS
KTAMVATVSP AADNYDETLS TLRYADRAKH IVNHAVVNED PNARIIRDLR EEVEKLREQL
TKAEAMKSPE LKDRLEESEK LIQEMTVTWE EKLRKTEEIA QERQKQLESL GISLQSSGIK
VGDDKCFLVN LNADPALNEL LVYYLKEHTL IGSANSQDIQ LCGMGILPEH CIIDITPEGQ
VMLTPQKNTR TFVNGSSVSS PIQLHHGDRI LWGNNHFFRL NLPKKKKNAD RDDEEQDISM
KNDTSSEQLD VDGDSSSEVS SEINFNYEYA QMEVTMKALG SNDPMQSILN SLEQQHEEEK
RSALERQRLM YEHELEQLRR RLSPEKQSGR TSDRFSFHSP SAQQRLRQWT EEREATLNNS
LMRLREQIVK ANLLVREASY IAEELDKRTE YKVTLQIPAS SLDANRKRGS LLSEPAIQVR
RKGKGKQIWS LEKLDNRLLD MRDLYQEWKE CEEDTPVIRS YFRRADPFYD EQENHSLIGV
ANVFLESLFY DVKLQYAVPI INQKGEVAGR LHVEVMRLSG DVGERIAGGD EPVDASSDKE
PQENRLVCMV KILQATGLPQ HLSHFVFCKY DFWDQQEPVT VAPEVDTSSS PVSKEPQCMV
VFDHCSEFSV SITEDFIEHL SEGALAIEVY GHKMNDPRKN PALWDLGIIQ AKTRSLRDRW
SEVTRKVEFW VQILEQNENG EYCPVEVIPA KDVPTGGIFQ LRQGQSRRVQ VEVKSVQESG
TLPLMEERIL SVGIGCVRVR APRSPKTHET VHEEEEDMDS YQDRDLERLR RKWLNALTKR
QEYLDQQLQK LVSKHDKTED DADREAQLLE MRLTLTEERN AVMVPSAGSG IPGAPAEWTP
VPGMETHIPV IFLDLNADDF SSQDNLDDPE AGGWDATLTG EEEDEFFELQ IVRQHDGEVK
AEASWDSAVH GCPQLSKGTP VDERVFLIVR VTVQLSHPAD MQLVLRKRIC VNVHGRQGFA
QSLLKKMSHR SSIPGCGVTF EIVSNIPEDA QGVEERETLA RMAANVENTA SADSEAYIEK
YLRSVLAVEN LLTLDRLRQE VAVKEQLTGK GKLSRRSISS PNVNRLSGSR QDLIPPSSLG
SNKGRWESQQ DVSQIAVSKG ITPALRSPQS NHSPDPGHLA ASYLNPVKSL VPQMPKLLKS
LFPVRDEKRG KQLSPLVHQV KALGGRTCSQ RVAGPAQQEN GGLRVAPSMP VALPATPAPR
TCDGPPRVTP TSPAPEGGDG PPSPLSEASS GYFSHSVSTA TLSDACGPGL DAMASTPPGP
GLAALEPPAA SVEGKTVGSG AALAPAGASP PAPTSPFRIK KVRTSELKSF TRMLGGDPGG
PLGTAEDPLA SRDLGDGSAG AQALGKLEVS SDSEEASEVP EWLKEGEYVT VGTNKTGIVR
YVGPTDFQEG TWVGVELDLP SGKNDGSIGG KQYFKCNPGY GLLVRPGRVR RAAGAGRRRS
AGLRLQGAPE PRRSGPLSSS ATNLASLTAA LAKTEGTALR AERGHGNPEN RKSWAS
//
