ID G1QSQ2_NOMLE Unreviewed; 866 AA.
AC G1QSQ2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN Name=KIFC3 {ECO:0000313|Ensembl:ENSNLEP00000003970.2};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000003970.2, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000003970.2, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000003970.2}
RP IDENTIFICATION.
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,
CC ECO:0000256|RuleBase:RU000394}.
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DR EMBL; ADFV01013117; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01013118; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01013119; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01013120; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01013121; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1QSQ2; -.
DR STRING; 61853.ENSNLEP00000003970; -.
DR Ensembl; ENSNLET00000004167.2; ENSNLEP00000003970.2; ENSNLEG00000003191.2.
DR GeneTree; ENSGT00940000154022; -.
DR InParanoid; G1QSQ2; -.
DR OMA; RHDMQKC; -.
DR TreeFam; TF105238; -.
DR Proteomes; UP000001073; Chromosome 2.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0005871; C:kinesin complex; IEA:Ensembl.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005915; C:zonula adherens; 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:InterPro.
DR GO; GO:0090136; P:epithelial cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0007030; P:Golgi organization; IEA:Ensembl.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0045218; P:zonula adherens maintenance; IEA:Ensembl.
DR CDD; cd01366; KISc_C_terminal; 1.
DR Gene3D; 1.10.287.1490; -; 1.
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; PTHR47972:SF5; KINESIN-LIKE PROTEIN KIFC3; 1.
DR PANTHER; PTHR47972; KINESIN-LIKE PROTEIN KLP-3; 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 Microtubule {ECO:0000256|RuleBase:RU000394};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283,
KW ECO:0000256|RuleBase:RU000394};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00283}; Reference proteome {ECO:0000313|Proteomes:UP000001073}.
FT DOMAIN 447..770
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 19..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 790..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 108..234
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 281..347
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 406..433
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 30..48
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 800..820
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 530..537
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 866 AA; 96132 MW; 1FD04EB05722A978 CRC64;
MVPSRRTWNL GATPSLRGLW RVGRAPEPEP GMARPAPAPA PASPAARPFP HTGPGRLRTG
RGKDTPVCGD EDSSARSAAR PALAQCRALS VDWAGPGSPH GLYLTLQVEH LKEKLISQAQ
EVSRLRSELG GTDLEKHRDL LMVENERLRQ EMRRCEAELQ ELRTKPAGPC PGCEHSQESA
QLRDKLSQLQ LEMAESKGML SELNLEVQQK TDRLAEVELR LKDCLAEKAQ EEERLSRRLR
DSHETIASLR AQSPPVKYVI KTVEVESSKT KQALSESQAR NQHLQEQVAM QRQVLKEMEQ
QLQSSHQLTA RLRAQIAMYE SELERAHGQM LEEMQSLEED KNRAIEEAFA RAQVEMKAVH
ENLAGVRTNL LTLQPALRTL TNDYNGLKRQ VRGFPLLLQE ALRSVKAEIG QAIEEVNSNN
QELLRKYRRE LQLRKKCHNE LVRLKGNIRV IARVRPVTKE DGEGPEATNA VTFDADDDSI
IHLLHKGKPV SFELDKVFSP QASQHDVFQE VQALVTSCID GFNVCIFAYG QTGAGKTYTM
EGTAENPGIN QRALQLLFSE VQEKASDWEY TITVSAAEIY NEVLRDLLGK EPQEKLEIRL
CPDGSGQLYV PGLTEFQVQS VDDINKVFEF GHTNRTTEFT NLNEHSSRSH ALLIVTVRGV
DCSTGLRTTG KLNLVDLAGS ERVGKSGAEG SRLREAQHIN KSLSALGDVI AALRSRQGHV
PFRNSKLTYL LQDSLSGDSK TLMVVQVSPV EKNTSETLYS LKFAERVRSV ELGPGLRRAE
LGSWSSQEHL EWEPACQTPQ PSARAHSAPS SGTSSRPGSI RRKLQPLDSA VSVLQVGNGR
SVGRGQCKKT PASQLGVLTL PWDPAL
//
