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Database: UniProt
Entry: G3TWE5_LOXAF
LinkDB: G3TWE5_LOXAF
Original site: G3TWE5_LOXAF 
ID   G3TWE5_LOXAF            Unreviewed;       584 AA.
AC   G3TWE5;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN   Name=KIF2A {ECO:0000313|Ensembl:ENSLAFP00000019903.1};
OS   Loxodonta africana (African elephant).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX   NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000019903.1, ECO:0000313|Proteomes:UP000007646};
RN   [1] {ECO:0000313|Ensembl:ENSLAFP00000019903.1, ECO:0000313|Proteomes:UP000007646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000019903.1,
RC   ECO:0000313|Proteomes:UP000007646};
RA   Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Loxodonta africana (African elephant).";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLAFP00000019903.1}
RP   IDENTIFICATION.
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000019903.1};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Cytoplasm,
CC       cytoskeleton, spindle {ECO:0000256|ARBA:ARBA00004186}.
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   AlphaFoldDB; G3TWE5; -.
DR   Ensembl; ENSLAFT00000026054.1; ENSLAFP00000019903.1; ENSLAFG00000009967.3.
DR   GeneTree; ENSGT00940000155570; -.
DR   HOGENOM; CLU_001485_19_1_1; -.
DR   Proteomes; UP000007646; Unassembled WGS sequence.
DR   GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005819; C:spindle; 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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   CDD; cd01367; KISc_KIF2_like; 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; PTHR47971:SF22; KINESIN-LIKE PROTEIN; 1.
DR   PANTHER; PTHR47971; KINESIN-RELATED PROTEIN 6; 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}; Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Microtubule {ECO:0000256|RuleBase:RU000394};
KW   Mitosis {ECO:0000256|ARBA:ARBA00022776};
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:UP000007646}.
FT   DOMAIN          204..534
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          45..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..121
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        130..167
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         294..301
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   584 AA;  65632 MW;  5F4B4F7585B87A78 CRC64;
     GRIHQAMVTS LNEDNESVTV EWIENGDTKG KEIDLESIFS LNPDLVPDEE IEPSPETPPP
     PASSAKINKI VKNRRTVASI KNDPPPRDNR VTVVGSARAR PSQLPEQSSS VQQNGSVSDI
     SPVQAAKKEF GPPSRRKSNC VKEVEKLQEK REKRRLQQQE LREKRAQDVD ATNPNYEIMC
     MIRDFRGSLD YRPLTTADPI DEHRICVCVR KRPLNKKETQ MKDLDVITIP SKDVVMVHEP
     KQKVDLTRYL ENQTFRFDYA FDDSAPNEMV YRFTARPLVE TIFERGMATC FAYGQTGSGK
     THTMGGDFSG KNQDCSKGIY ALAARDVFLM LKKPNYKKLE LQVYATFFEI YSGKVFDLLN
     RKTKLRVLED GKQQVQVVGL QEREVKCVED VLKLIDIGNS CRTSGQTSAN AHSSRSHAVF
     QIILRRKGKL HGKFSLIDLA GNERGADTSS ADRQTRLEGA EINKSLLALK ECIRALGRNK
     PHTPFRASKL TQVLRDSFIG ENSRTCMIAT ISPGMASCEN TLNTLRYANR VKELTVDPTA
     AGDVRPVMHH PPSQIDDLET QWGVGSSPQR DDLKLLCEQN VSDI
//
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