ID   KIF25_MACFA             Reviewed;         586 AA.
AC   Q4R918;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Kinesin-like protein KIF25 {ECO:0000305};
GN   Name=KIF25 {ECO:0000250|UniProtKB:Q9UIL4};
GN   ORFNames=QtsA-10923 {ECO:0000303|PubMed:15944441};
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15944441; DOI=10.1093/molbev/msi187;
RA   Osada N., Hirata M., Tanuma R., Kusuda J., Hida M., Suzuki Y., Sugano S.,
RA   Gojobori T., Shen C.K., Wu C.I., Hashimoto K.;
RT   "Substitution rate and structural divergence of 5'UTR evolution:
RT   comparative analysis between human and cynomolgus monkey cDNAs.";
RL   Mol. Biol. Evol. 22:1976-1982(2005).
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX   PubMed=28263957; DOI=10.1038/ncb3486;
RA   Decarreau J., Wagenbach M., Lynch E., Halpern A.R., Vaughan J.C.,
RA   Kollman J., Wordeman L.;
RT   "The tetrameric kinesin Kif25 suppresses pre-mitotic centrosome separation
RT   to establish proper spindle orientation.";
RL   Nat. Cell Biol. 19:384-390(2017).
CC   -!- FUNCTION: Minus-end microtubule-dependent motor protein
CC       (PubMed:28263957). Acts as a negative regulator of centrosome
CC       separation required to prevent premature centrosome separation during
CC       interphase (By similarity). Required to maintain a centered nucleus to
CC       ensure that the spindle is stably oriented at the onset of mitosis (By
CC       similarity). May also act as a negative regulator of amino acid
CC       starvation-induced autophagy (By similarity).
CC       {ECO:0000250|UniProtKB:Q9UIL4, ECO:0000269|PubMed:28263957}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:28263957}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome {ECO:0000269|PubMed:28263957}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}.
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DR   EMBL; AB168279; BAE00403.1; -; mRNA.
DR   AlphaFoldDB; Q4R918; -.
DR   SMR; Q4R918; -.
DR   STRING; 9541.XP_005551480.1; -.
DR   eggNOG; KOG0239; Eukaryota.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005813; C:centrosome; IDA:UniProtKB.
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-KW.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   GO; GO:0008569; F:minus-end-directed microtubule motor activity; IDA:UniProtKB.
DR   GO; GO:0051294; P:establishment of spindle orientation; ISS:UniProtKB.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   GO; GO:0046603; P:negative regulation of mitotic centrosome separation; ISS:UniProtKB.
DR   GO; GO:0051647; P:nucleus localization; ISS:UniProtKB.
DR   GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR   Gene3D; 3.40.850.10; -; 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; PTHR24115; PTHR24115; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW   Motor protein; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..586
FT                   /note="Kinesin-like protein KIF25"
FT                   /id="PRO_0000440626"
FT   DOMAIN          173..565
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   REGION          417..460
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          564..586
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          10..94
FT                   /evidence="ECO:0000255"
FT   BINDING         267..274
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   586 AA;  64008 MW;  698409E374C8531B CRC64;
     MPAGGGRWGS FWEQRTRQLQ SQVRAKEDKI AELETENAVL LLKLAEYKGK IEKSRSEATR
     ISTLYNKQQR LQRNTRSALS QLDGVIQKLN QDIQAFHSSS RALLRDYQDE YQDRVSAIVT
     AVQRTRQSAE TLLACQAKVV HLEQALQDVS ARHQLERQRR KALHNSLVEL RGNIRVHCRI
     RPLLPFDSES DDPVLQSSSI SREVAHAVDD ETVLVKCDRP GHPLINKTYH FERVYGPAES
     QSAVFGDVCP LLTSLLDGYN VCVMAYGQTG SGKSYTMLGP HSDDGPVLPL DPQSDLGIIP
     RAAEELFRLI SENPSRSPKV EVSIVEVYNN DIFDLLAKDT VAAVSGVKRE VMTAKDGRTE
     VALLASEAVG SASKLMELVR GGLQLRAKHP TLVHADSSRS HLIITVTLTT AACSDSTADQ
     ACSATHPGEQ TEAGRAGRSR RTSQGASAPQ PVPGDPAGRA EQVQARLQLV DLAGSECIGV
     SGVTGSALRE TACINRSLAA LADVLGALSE HRSHIPYRNS RLTHLLQDCL GGDAKLLVIL
     CISPSQRHLA QTLQGLGFGI RARQVQRGPA RKRPPSSQME GKRRPD