ID W6V2A4_ECHGR Unreviewed; 1490 AA.
AC W6V2A4;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Kinesin-like protein KIFC3 {ECO:0000313|EMBL:EUB60019.1};
GN ORFNames=EGR_05180 {ECO:0000313|EMBL:EUB60019.1};
OS Echinococcus granulosus (Hydatid tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus;
OC Echinococcus granulosus group.
OX NCBI_TaxID=6210 {ECO:0000313|EMBL:EUB60019.1, ECO:0000313|Proteomes:UP000019149};
RN [1] {ECO:0000313|EMBL:EUB60019.1, ECO:0000313|Proteomes:UP000019149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24013640; DOI=10.1038/ng.2757;
RA Zheng H., Zhang W., Zhang L., Zhang Z., Li J., Lu G., Zhu Y., Wang Y.,
RA Huang Y., Liu J., Kang H., Chen J., Wang L., Chen A., Yu S., Gao Z.,
RA Jin L., Gu W., Wang Z., Zhao L., Shi B., Wen H., Lin R., Jones M.K.,
RA Brejova B., Vinar T., Zhao G., McManus D.P., Chen Z., Zhou Y., Wang S.;
RT "The genome of the hydatid tapeworm Echinococcus granulosus.";
RL Nat. Genet. 45:1168-1175(2013).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-
CC pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
CC -!- SIMILARITY: Belongs to the X(+)/potassium ATPases subunit beta family.
CC {ECO:0000256|ARBA:ARBA00005876}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EUB60019.1}.
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DR EMBL; APAU02000036; EUB60019.1; -; Genomic_DNA.
DR STRING; 6210.W6V2A4; -.
DR EnsemblMetazoa; XM_024494429.1; XP_024351215.1; GeneID_36340895.
DR OrthoDB; 2880589at2759; -.
DR Proteomes; UP000019149; Unassembled WGS sequence.
DR GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; IEA:InterPro.
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 GO; GO:0006813; P:potassium ion transport; IEA:InterPro.
DR GO; GO:0006814; P:sodium ion transport; IEA:InterPro.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 2.60.40.1660; Na, k-atpase alpha subunit; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR000402; Na/K_ATPase_sub_beta.
DR InterPro; IPR038702; Na/K_ATPase_sub_beta_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11523:SF28; AT04468P-RELATED; 1.
DR PANTHER; PTHR11523; SODIUM/POTASSIUM-DEPENDENT ATPASE BETA SUBUNIT; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF00287; Na_K-ATPase; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
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:UP000019149};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1230..1250
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 268..647
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 1104..1125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 126..153
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 352..359
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1490 AA; 167855 MW; 9F494DB8A018BD37 CRC64;
MYMVSGNFCT ILAKVGQVKV YVTNTLSLFC FNPTTTVTAT VIATTVRVED EMIMMEPEPV
QDVECGGVTL DVNNANSAPR MISSCTPIQK TLEAGATTTN PASTEGLMTS PEFGRHLDVG
RLMEFNRELT TRYANLQAQF AELVSEHNRL QYRHNMMELA TLQNSQGDGP QRGKCGEDTL
LAAQYRADLR KMTSEKETVC HQATQLREDL RQTAARLGFL QTYVSQLQQR LVQRDRVIQK
LMQERALNVI RDVHTRMLHN ELLETRGGIR VVVRYLPTAE EFSNIEIVNS NVILIRKPLF
NFAHLKGKAQ AEHLSVFNIH SNATRNAVIF GDVRDYIEAC VDGNTAAIIA NGPKGTGKTH
TMVGPADDAG IIPRALSLIS QLCTDRSPLW EFKISLSAIQ AIQKIVDEEI YDLLTDMDDK
YELRRGWFAA DTLERPSKIT LHDNGSSIVL KNVTELEANT EDRLIQIFCY PSVISDAWQT
HSKSSHIDSA HFIVLVRIKA YGKVPLSKPT KMGTVAGTQA LETRVRCHQI VSHGFLILCD
LVSFDRPRTK RITNTAAWVG KTERQSINVN DIAGTVLGRV FEALRHNATH PQSPIPVPYR
DSKLTHLLKP ALLSEAKCAV ISTISLRTSM FKSTYRVRPM WTNIQFRMGE TSSVPEDLSM
VFRKWARTNL TGSMRKSGTL RSTGKGVAED VEEIIKCIRQ SKLTDPSSTW SERNKEWWDA
ATAGNLHNMK RLLNDDPNIL HWKNPLDGVS CETFKYFTQR FYSDFTLFGS WQKLINPVSF
PRSSTMESHS RLLTALHYVA KSGNLRCLDL LAKQYGASVD TQCKGSTPLH IAVMYSQRLL
ARSLVQIYHA RTDIMDYTGR FPRDLISTPE IKEDLEELLT SGRLAIIRKQ LEILKKPQKT
SFTSRKSHLH VGSGEETLNK VSKSRPIKMD FYTRLLLSAL SRDRGYVNTL VRRLRHAIFI
SPSDLFDDIA DNELSRHRGR DNSQKRGSVF AGGIGEGERR FTVFKVPHLP HPPRNLSAGT
LMTGGLWKRN TLEAGEKGRR WWREQKTAQK VIRKTSTSTL SMLRGGVKRG GASAFERHSF
VGIEHLTARL DAVTVAKDGG AVEEDGRFSR HPSDVSDCIT KSSSDDDDVV FDSVSSSPSP
DGAGSGGVRR TSNLSSLVAC TEDLFTTVDM SVRSRPHSPV SLPSPHEAEF EPLQAFLLKN
TTVYAYPRQR RCPRNRTEDV DSVKAICQRL LYFLTFYTVL ALFFVGYLNW YMYFQVPRDH
PALTGMQSAL QMNPGLSYIP NPDLFSTLLY FRTREPLPYY KKSDEMAAFL HAYQDNTGST
EYEDCVQEGG YKQNPERPCT YDINAGGPCN IMNGYGFDTA QACFVLKMGR IYGWLPDPID
EFATGVLVKC SGVTEDDTFN LGIIRYYDMD YKFSAIAPGK NPGKLDNGSF HSMYFPYTGQ
LAYLQPLVFV LFDGVKRNTF IRVRCWLIAK NIKVDFEKRE GSTEFEIIYD
//
