ID G3H4T6_CRIGR Unreviewed; 2868 AA.
AC G3H4T6;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Kinesin-like protein KIF1B {ECO:0000313|EMBL:EGV95317.1};
GN ORFNames=I79_005302 {ECO:0000313|EMBL:EGV95317.1};
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029 {ECO:0000313|EMBL:EGV95317.1, ECO:0000313|Proteomes:UP000001075};
RN [1] {ECO:0000313|Proteomes:UP000001075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075};
RX PubMed=21804562; DOI=10.1038/nbt.1932;
RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA Famili I., Palsson B.O., Wang J.;
RT "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line.";
RL Nat. Biotechnol. 29:735-741(2011).
CC -!- SUBCELLULAR LOCATION: Cell projection, axon
CC {ECO:0000256|ARBA:ARBA00004489}.
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; JH000147; EGV95317.1; -; Genomic_DNA.
DR STRING; 10029.G3H4T6; -.
DR PaxDb; 10029-XP_007621172-1; -.
DR eggNOG; KOG0245; Eukaryota.
DR InParanoid; G3H4T6; -.
DR Proteomes; UP000001075; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; cd22726; FHA_KIF1A; 1.
DR CDD; cd01365; KISc_KIF1A_KIF1B; 1.
DR CDD; cd01233; PH_KIFIA_KIFIB; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 6.10.250.2520; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 3.
DR Gene3D; 2.20.110.10; Histone H3 K4-specific methyltransferase SET7/9 N-terminal domain; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR049779; FHA_KIF1A.
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; IPR003409; MORN.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR049780; PH_KIFIA_KIFIB.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR InterPro; IPR002893; Znf_MYND.
DR PANTHER; PTHR47117:SF2; KINESIN-LIKE PROTEIN KIF1A ISOFORM X1; 1.
DR PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF12473; DUF3694; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF12423; KIF1B; 1.
DR Pfam; PF00225; Kinesin; 2.
DR Pfam; PF16183; Kinesin_assoc; 1.
DR Pfam; PF02493; MORN; 3.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF01753; zf-MYND; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00248; ANK; 5.
DR SMART; SM00240; FHA; 1.
DR SMART; SM00129; KISc; 1.
DR SMART; SM00698; MORN; 3.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF82185; Histone H3 K4-specific methyltransferase SET7/9 N-terminal domain; 1.
DR SUPFAM; SSF144232; HIT/MYND zinc finger-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 3.
DR PROSITE; PS50088; ANK_REPEAT; 3.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS01360; ZF_MYND_1; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00283}; Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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:UP000001075};
KW Synapse {ECO:0000256|ARBA:ARBA00023018};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00134}.
FT DOMAIN 113..483
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 671..727
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT DOMAIN 1784..1882
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REPEAT 2218..2250
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 2570..2607
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 2607..2639
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 2800..2840
FT /note="MYND-type"
FT /evidence="ECO:0000259|PROSITE:PS50865"
FT REGION 1030..1072
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1621..1662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1735..1766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1886..1907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 585..612
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 783..817
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1030..1046
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1047..1071
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1625..1652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1889..1907
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 205..212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 2868 AA; 322132 MW; 8262EE0E1F37CC1D CRC64;
MFPRAWAKPG LLDPKDRASG CWYQSTKAVL SPYRKRSRDT PAPPNVVVLL LYVPPPPPFP
PSQGPGSTLG LTDCSSPRVW LSQACRDAGD SALSGATAAA ELPTHSTDMA GASVKVAVRV
RPFNSREMSR DSKCIIQMSG STTTIVNPKQ PKETPKSFSF DYSYWSHTSP EDINYASQKQ
VYRDIGEEML QHAFEGYNVC IFAYGQTGAG KSYTMMGKQE KDQQGIIPQA CLGLERIVGG
GLRGGRGRAW DGLQEGLCED LFSRINDTTN DNMSYSVEVS YMEIYCERVR DLLNPKNKGN
LRVREHPLLG PYVEDLSKLA VTSYNDIQDL MDSGNKARTV AATNMNETSS RSHAVFNIIF
TQKRHDAETN ITTEKVSKIS LVDLAGSERA DSTGAKGTRL KEGANINKSL TTLGKVISAL
AEMNKKKKKT DFIPYRDSVL TWLLRENLGG NSRTAMVAAL SPADINYDET LSTLRYADRA
KQIRCNAIIN EDPNNKLIRE LKDEVTRLRD LLYAQGLGDI TDNVFDLENS NRNCGGAELS
QAPNNLSTVT NALVGMSPSS SLSALSSRAA SVSSLHERIL FAPGSEEAIE RLKETEKIIA
ELNETWEEKL RRTEAIRMER EALLAEMGVA MREDGGTLGV FSPKKTPHLV NLNEDPLMSE
CLLYYIKDGV TRVGREDAER RQDIVLSGHF IKEEHCIFRS DSRGGGEAVV TLEPCEGADT
YVNGKKVTEP SILRSGNRII MGKSHVFRFN HPEQARQERE RTPCAETPAE PVDWAFAQRE
LLEKQGIDMK QEMEQRLQEL EDQYRREREE ATYLLEQQRL DYESKLEALQ KQMDSRYYPE
VNEEEEEPED EVQWTERECE LALWAFRKWK WYQFTSLRDL LWGNAIFLKE ANAISVELKK
KVQFQFVLLT DTLYSPLPPD LLPPEAAKDR ETRPFPRTIV AVEVQDQKNG ATHYWTLEKL
RQRLDLMREM YDRAAEVPSS VVEDCDNVVT GGDPFYDRFP WFRLVGSSVI SGCNSYPLLN
TCMSERMAAL TPSPTFSSPD SDTTEPAEEQ SVGEEEEEEE EEEEDLEDDV FPEHTLCDGR
DPFYDRPPLF SLVGRAFVYL SNLLYPVPLV HRVAIVSEKG EVKGFLRVAV QAISADEEAP
DYGSGVRQSG TAKISFDDQH FEKFQSESCP VVGMSRSGTS QEELRIVEGQ GQGADSGPSA
DEVNNNTCSA VTPEGLLDSP EKTALDGPLD TALDHLRLGS TFTFRVTVLQ ASSISAEYAD
IFCQFNFIHR HDEAFSTEPL KNTGRGPPLG FYHVQNIAVE VTKSFIEYIK SQPIVFEVFG
HYQQHPFPPL CKDVLSPLRP SRRHFPRVMP LSKPVPATKL STMTRPSPGP CHCKYDLLVY
FEICELEANG DYIPAVVDHR GGMPCMGTFL LHQGIQRRIT VTLLHETGSH IRWKEVRELV
VGRIRNTPET DESLIDPNIL SLNILSSGYV HPAQDDRSPK LWDARRNPQV TLKSGETVIT
KDFCMVFYSR DAKLPASRSI RNLFGSGSLR ATEGNRVTGV YELSLCHVAD AGSPGMQRRR
RRVLDTSVAY VRGEENLAGW RPRSDSLILD HQWELEKLSL LQEVEKTRHY LLLREKLETT
QRPGPEALSL ASSEDSESRS SSGASSPLSA EGQPSPLEAP NERQRELAVK CLRLLMHTFN
REYTHSHVCI SASESKLSEM SVTLMRDPSM SPLGAATLTP SSTCPSLIEG RYGATDVRPA
SPEPELLPEI DSKKTPSPAR ATEVDKEPQR LLVPDIQEIR VSPIVSKKGY LHFLEPHTAG
WAKRFVVVRR PYAYMYNSDK DSVERFVLNL STAQVEYSED QQAMLKTPNT FAVCTEHRGI
LLQANSDKDM HDWLYAFNPL LAGTIRNSSS DPREDEEESE GSQRKQDLKE TYIRITQGVQ
EWQDGSVYKG DFGLDMKLGF GEFSWPTGET YRGQFYRDHC HGVGTYTWPN GSSFTGLFYL
SQREGYGTMF MKTKLFQGLY KDDQRFGPGI ETYPDGSQDV GLWFREHLLK LGTEVPSSFS
LLNYPEFLDF LTSSRGRISL SDEENKMWGL PEDQDPFFYE YKRFLLNDDI TLPPEMHIYS
TDNSHLPMTG SLRRELEGRI FMNEIPPFIE DEEPWLITNE TPLLVKIQKQ TYKFRNKSAH
TSWNIAAILE GNRSCFGPSG PKELISREMI LKAEEGDYDW IFGILRDNLA CADVADSKGY
TVLAAAAVHS HRNIVNLLLD YGADVNKRSD EGLTPLSMCF LQYYPSKSFH PNIAERTLPQ
ELPKSLITPK ISFLFGEPNV DYFYDMGVST PVGEEYKSSP PLSSILEDAL ILGTVQSRES
ISWKSSVTHK RDTPSVKSVS SDIEKEPEDM AENMDASTLY SVNTDFESNM CLRNYSIHVS
KDILEKSAQA YSSLLHIPAL SDKGTVRKMA QTMAERRNRW LTITLLLHRG ADPNLCQVPM
QALFLAVKAG DVDGVRLLLE SGARTDIQFP AQLLSLTPLH IAASLPGEEG VKITELLLHA
VTDVDAKAAD QDDLYKTGKV DLLPSSLKLN NETGPPRSYY NVSTFIPEEG GRTPLHVACE
REDNKKCARD IVRLLLSHRA NPNMLWSGHS PLSLSIASGN DLVVKELLSQ GADPNLPLTK
GLGTALCVVC DLAYEQQRST ENKIALIDRL ISYGADILKP VALVQGERTA VGTAVDYGYF
KFYQDRKIAH CPFHALMPAE REIFLARKRL LEYMGLQLRR AVLNKENQLD MKSLYLSKRG
ADSDLSTAEL SPSHRLKRRS SSILKTSPTE KQHLPFYKFC YQCGRSIGVR LTPCPRCYGI
LTCSKYCKTK AWTEFHKKDC NDIMILSRFG CHVGVGWRGA NCCCLGQR
//
