ID A0A3Q1LRB7_BOVIN Unreviewed; 1153 AA.
AC A0A3Q1LRB7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Kinesin family member 1B {ECO:0008006|Google:ProtNLM};
GN Name=KIF1B {ECO:0000313|Ensembl:ENSBTAP00000059670.1};
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:ENSBTAP00000059670.1, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000059670.1, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000059670.1,
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:ENSBTAP00000059670.1}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000059670.1};
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 RefSeq; XP_005194866.1; XM_005194809.3.
DR RefSeq; XP_005217055.1; XM_005216998.3.
DR AlphaFoldDB; A0A3Q1LRB7; -.
DR Ensembl; ENSBTAT00000083891.1; ENSBTAP00000059670.1; ENSBTAG00000054239.1.
DR GeneID; 100337161; -.
DR CTD; 23095; -.
DR VEuPathDB; HostDB:ENSBTAG00000054239; -.
DR GeneTree; ENSGT00940000157445; -.
DR OrthoDB; 126886at2759; -.
DR Proteomes; UP000009136; Chromosome 16.
DR Bgee; ENSBTAG00000054239; Expressed in longissimus muscle and 110 other cell types or tissues.
DR ExpressionAtlas; A0A3Q1LRB7; baseline and differential.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
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; cd22727; FHA_KIF1B; 1.
DR CDD; cd01365; KISc_KIF1A_KIF1B; 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; 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:SF6; KINESIN-LIKE PROTEIN KIF1C ISOFORM X1; 1.
DR PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF16183; Kinesin_assoc; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00240; FHA; 1.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS50006; 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 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 5..348
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 510..566
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT REGION 859..911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 949..1079
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1116..1153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 629..656
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 816..850
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 864..889
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 982..1010
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1020..1079
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1116..1135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 97..104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1153 AA; 130367 MW; 6BBE0698571EE383 CRC64;
MSGASVKVAV RVRPFNSRET SKESKCIIQM QGNSTSIINP KNPKEAPKSF SFDYSYWSHT
SPEDPCFASQ NRVYNDIGKE MLLHAFEGYN VCIFAYGQTG AGKSYTMMGK QEESQAGIIP
QLCEELFEKI NDNCNEEMSY SVEVSYMEIY CERVRDLLNP KNKGHLRVRE HPLLGPYVED
LSKLAVTSYT DIADLMDAGN KARTVAATNM NETSSRSHAV FTIVFTQKKH DTETNLSTEK
VSKISLVDLA GSERADSTGA KGTRLKEGAN INKSLTTLGK VISALAEVSK KKKKTDFIPY
RDSVLTWLLR ENLGGNSRTA MVAALSPADI NYDETLSTLR YADRAKQIKC NAVINEDPNA
KLVRELKEEV TRLKDLLRAQ GLGDIIDTSM GSLTSSPSSC SLNSQVGLTS VTSIQERIMS
TPGGEEAIER LKESEKIIAE LNETWEEKLR KTEAIRMERE ALLAEMGVAI REDGGTLGVF
SPKKTPHLVN LNEDPLMSEC LLYYIKDGIT RVGQADAERR QDIVLSGAHI KEEHCIFRSE
RNNSGDVIVT LEPCERSETY VNGKRVTQPV QLRSGNRIIM GKNHVFRFNH PEQARAEREK
TPSAETPSEP VDWTFAQREL LEKQGIDMKQ EMEKRLQEME ILYKKEKEEA DLLLEQQRLD
ADSDSGDDSD KRSCEESWKL ITSLREKLPP SKLQTIVKKC GLPSSGKKRE PIKMYQIPQR
RRLSKDSKWV TISDLKIQAV KEICYEVALN DFRHSRQEIE ALAIVKMKEL CAMYGKKDPN
ERDSWRAVAR DVWDTVGVGD EKIEDVMASS KGGTDVDDLK VHIDKLEDIL QEVKKQNNMK
DEEIKVLRNK MLKMEKVLPL IGSPEQKTQG NQKSKEPSGA GASSKPENDV SKGDSGDLGK
EERVSQLMNG DPAFRRGRLR WMRQEQIRFK NLQQQEITKQ LRRQNVPHRF IPPENRKPRF
PFKSNPKHRN SWSPGTHIII TEDEVIELRI PKEEDGRKGN KPENQEKGTR AASKDPQLPW
GPQGTRSQDH IQVSKQHINN QQQPPQLRWR SNSLNNGQPK STRCQASASP EVLASHSGHP
TADLQTFQAK RHMHQHRQAY CSYNTGAQLE GSAATSCQKQ TDRPNHCSQF VTPPRMRRQF
SAPNLKTGRE TTV
//
