ID M3YXC7_MUSPF Unreviewed; 1028 AA.
AC M3YXC7;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Kinesin family member 17 {ECO:0000313|Ensembl:ENSMPUP00000015987.1};
GN Name=KIF17 {ECO:0000313|Ensembl:ENSMPUP00000015987.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000015987.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000015987.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-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 EMBL; AEYP01008366; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01008367; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M3YXC7; -.
DR STRING; 9669.ENSMPUP00000015987; -.
DR Ensembl; ENSMPUT00000016231.1; ENSMPUP00000015987.1; ENSMPUG00000016094.1.
DR eggNOG; KOG0239; Eukaryota.
DR GeneTree; ENSGT00940000158776; -.
DR HOGENOM; CLU_001485_22_0_1; -.
DR InParanoid; M3YXC7; -.
DR OMA; AKNRMVG; -.
DR GO; GO:0005930; C:axoneme; IEA:Ensembl.
DR GO; GO:0036064; C:ciliary basal body; IEA:Ensembl.
DR GO; GO:0032839; C:dendrite cytoplasm; IEA:GOC.
DR GO; GO:0005871; C:kinesin complex; IEA:Ensembl.
DR GO; GO:1990075; C:periciliary membrane compartment; IEA:Ensembl.
DR GO; GO:0032391; C:photoreceptor connecting cilium; IEA:Ensembl.
DR GO; GO:0001917; C:photoreceptor inner segment; IEA:Ensembl.
DR GO; GO:0001750; C:photoreceptor outer segment; IEA:Ensembl.
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:Ensembl.
DR GO; GO:0098971; P:anterograde dendritic transport of neurotransmitter receptor complex; IEA:Ensembl.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:Ensembl.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR027640; Kinesin-like_fam.
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 PANTHER; PTHR47969; CHROMOSOME-ASSOCIATED KINESIN KIF4A-RELATED; 1.
DR PANTHER; PTHR47969:SF32; KINESIN-LIKE PROTEIN; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00283}.
FT DOMAIN 5..335
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 520..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 633..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 909..932
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 962..1028
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 800..841
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 532..552
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 977..993
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1009..1028
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 91..98
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1028 AA; 113769 MW; 9FD312A5B978D281 CRC64;
MASESVKVVV RCRPMNQRER ELNCQLVVTV DSARGQCFIQ NPGAADEPPK QFTFDGAYYM
DHFTEQIYNE IAYPLVEGVT EGYNGTIFAY GQTGSGKSFT MQGLPDPPSQ RGIIPRAFEH
VFESVQCAEN TKFLVRASYL EIYNEDVRDL LGTDTKQKLE LKEHPERGVY VKGLSMHTVH
SVAQCERIME TGWKNRSVGY TLMNKDSSRS HSIFTISIEI YAVDERGQDH LRAGKLNLVD
LAGSERQSKT GATGERLKEA TKINLSLSAL GNVISALVDG RCKHIPYRDS KLTRLLQDSL
GGNTKTLMVA CLSPADNNYD ETLSTLRYAN RAKNIKNKPR INEDPKDALL REYQEEIKKL
KEILAQQMSP GNLADLLSSQ TPLNAVQTEE KLAPPPVIQP DTEAEKQLIR EEVTQRVAWL
HRVCPLSQED EELLQVDLQV VGKPWDSRAS QSSLNVRPSA EAVLKAEVLK AEVLKAQGTS
RAESVSWPEP SPAFHCELAT KPEIHSMPCA LPGEDVSKTE VSPAFEELPT AETSKSEASL
GSDESSMLED TSMSEACPAP QEPSNVEFSA PETEAVGSSL PDHDLSWEAA GAPRWAGSVP
EDEQPQLAAL GLLPSLHDPF AEVEAKLARL SSAMGGTEAP QAATPRLPTQ HPSLTDLPGP
RSEAEAADFL LPGTEVDLGP EVAEEVVPAA EPGVGAETEA QMALEAQPQP LLATTTVRRD
SVEVAVLTDD LLPVVDQQQV LARLQLLEQQ VVGGEQAKNK DLKEKHKRRK RYADERKKQL
VAALQNSDED GGDWVLLNVY DSIQEEVRAK SKLLERMQRK LRAAEVEIKD LQSEFQLEKI
DYLATIRRQE RDSMLLQQLL EQVQPLIRRD CNYSNLEKIR REACWDEDNG FWKIPEPIII
KTSLPVAVPT GPQNKAVRKA STADNGEPGT EEDRYRLMLS RSDSENIASN YFRSKRASQI
LSTDPMKSLA HHSSPPGLGS PLSNTSAMSP TQAPEMPQPR PFRLESLDIP FSKAKRKKSK
SSFGSEPL
//
