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KI15A_XENLA
ID   KI15A_XENLA             Reviewed;        1388 AA.
AC   Q91785;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Kinesin-like protein KIF15-A;
DE   AltName: Full=Kinesin-like protein 2-A;
DE            Short=Xklp2-A;
GN   Name=kif15-a; Synonyms=klp2;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Oocyte;
RX   PubMed=8548825; DOI=10.1016/s0092-8674(00)80992-7;
RA   Boleti H., Karsenti E., Vernos I.;
RT   "Xklp2, a novel Xenopus centrosomal kinesin-like protein required for
RT   centrosome separation during mitosis.";
RL   Cell 84:49-59(1996).
RN   [2]
RP   HOMODIMER, IDENTIFICATION IN A COMPLEX WITH TPX2 AND MICROTUBULES,
RP   MUTAGENESIS OF LEU-1371, AND SUBCELLULAR LOCATION.
RX   PubMed=9813089; DOI=10.1083/jcb.143.3.673;
RA   Wittmann T., Boleti H., Antony C., Karsenti E., Vernos I.;
RT   "Localization of the kinesin-like protein Xklp2 to spindle poles requires a
RT   leucine zipper, a microtubule-associated protein, and dynein.";
RL   J. Cell Biol. 143:673-685(1998).
RN   [3]
RP   IDENTIFICATION IN A COMPLEX WITH TPX2 AND MICROTUBULES, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=10871281; DOI=10.1083/jcb.149.7.1405;
RA   Wittmann T., Wilm M., Karsenti E., Vernos I.;
RT   "TPX2, a novel Xenopus MAP involved in spindle pole organization.";
RL   J. Cell Biol. 149:1405-1418(2000).
CC   -!- FUNCTION: Plus-end directed kinesin-like motor enzyme involved in
CC       mitotic spindle assembly. Required for centrosome separation and
CC       maintenance of spindle bipolarity during mitosis.
CC       {ECO:0000269|PubMed:8548825}.
CC   -!- SUBUNIT: Homodimer. Dimerization is required for targeting to
CC       microtubule minus ends. Found in a complex with tpx2 and microtubules.
CC       Its association with microtubules and targeting to microtubule minus
CC       ends requires tpx2. {ECO:0000269|PubMed:10871281,
CC       ECO:0000269|PubMed:9813089}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome. Cytoplasm, cytoskeleton, spindle.
CC       Cytoplasm, cytoskeleton, spindle pole. Note=Localizes during metaphase
CC       on spindle microtubules, with a strong enrichment at spindle poles.
CC       Localizes to the minus ends of spindle pole and aster microtubules in a
CC       dynein- and dynactin-dependent manner. Detected diffusively in the
CC       cytoplasm. Localized (PubMed:8548825) at the centrosome during the
CC       interphase and throughout mitosis. {ECO:0000269|PubMed:8548825}.
CC   -!- TISSUE SPECIFICITY: Strongly expressed in testis and weakly in lung (at
CC       protein level). {ECO:0000269|PubMed:8548825}.
CC   -!- DEVELOPMENTAL STAGE: Expressed maternally in oocytes and eggs (at
CC       protein level). {ECO:0000269|PubMed:8548825}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. KLP2 subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00283}.
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DR   EMBL; X94082; CAA63826.1; -; mRNA.
DR   PIR; T30335; T30335.
DR   RefSeq; NP_001081543.1; NM_001088074.1.
DR   AlphaFoldDB; Q91785; -.
DR   SMR; Q91785; -.
DR   BioGRID; 99246; 1.
DR   MaxQB; Q91785; -.
DR   PRIDE; Q91785; -.
DR   GeneID; 397909; -.
DR   KEGG; xla:397909; -.
DR   CTD; 397909; -.
DR   OrthoDB; 241787at2759; -.
DR   Proteomes; UP000186698; Chromosome 6L.
DR   Bgee; 397909; Expressed in spleen and 9 other tissues.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:1901673; P:regulation of mitotic spindle assembly; IEA:InterPro.
DR   Gene3D; 3.40.850.10; -; 1.
DR   InterPro; IPR031794; HMMR_C.
DR   InterPro; IPR044986; KIF15/KIN-12E.
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; PTHR37739; PTHR37739; 1.
DR   Pfam; PF15908; HMMR_C; 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..1388
FT                   /note="Kinesin-like protein KIF15-A"
FT                   /id="PRO_0000328688"
FT   DOMAIN          26..364
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   REGION          1127..1156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1139..1388
FT                   /note="Necessary for its targeting to microtubule minus
FT                   ends"
FT                   /evidence="ECO:0000250"
FT   COILED          369..1383
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1131..1145
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         110..117
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   MUTAGEN         1371
FT                   /note="L->K: Inhibits its targeting to microtubule minus
FT                   ends."
FT                   /evidence="ECO:0000269|PubMed:9813089"
SQ   SEQUENCE   1388 AA;  159141 MW;  1F8825558B9AE28E CRC64;
     MPPGTKGDPS NVTQPLPCLP SAEEDAIKVF VRIRPPVEGT LTGVDGEQGL CLTALSSTTI
     RLHSKPEPKM FTFDHVANVD TNQESVFSSV AKNIVESCMN GYNGTIFAYG QTGSGKTFTM
     LGPSESDNFT HNLRGVIPRS FEYLFFLINR EKEKAGEGKS FLCKCSFIEI YNEQIFDLLD
     SASAGLFLRE HIKKGVFVVG AVEQVVTSAA EAYQVLSMGW RNRRVASTSM NRESSRSHAV
     FTVTIESMEK TNDLVNIRSS QLNLVDLAGS ERQKDTQTEG VRLKEAGSIN RSLSCLGQVI
     TALVDVANGR QRHICYRDSK LTFLLRDSLG GNAKTFYIAN VHPGSKCFGE TLSTLQFAQR
     AKLIKNKAVV NEDTQGNVSQ LQAEVKKLKE QLSQLLSGQM PGDISVARVP SVGDNNMDYM
     NNFIEAMMIL EKSDREKKVL LQKVVQLEDL CNKKEKFIQS NKMIVKFRED HISRLEKAHK
     EGRISLSNNE QDDFIAELKE EIRTLKEQVE HHPRVAKYAL ENHSLREENK RLHSLQSVKR
     AQEVTAQMIA ELEKAFLEVS VSEKDRQVAP MHSTPIQLDN NSLMSAARMR ERMLQLESEL
     ATSKQEYEEF KELTKKKQVE QESELQSLIK SNQHLENILE AIKANKRHEV SQLNRMHAAE
     TIKNMTTPTK SYNLRSRLVP RLSPDAMPNG LMDTPKSGDV MDDIINEPIP PEMSEQAYEA
     IAEELRIVQE QVTALQAKLD EEEGKNIRLQ QQVNKLELCS TQIQELFNSE RSNWNKEQQD
     LIAQIKSLEK QKQENKSQED VLKSEVHDLR VVLQSADREL GAVKGEYSLY REKQEKELSQ
     LSARHMDVQL QLDNVRLEHE TLLEEKRSLQ DAFDNLEEVM KFEIDQLKQE ISDSKHENET
     LRAEFSNLLE LLETEKERRQ KLTSQLEEDK ENKTKELLQV VDENMHLRKQ CSELMTKCEQ
     QVTELHGLEH SLTSSKEMIA DLEKKNTADK EVVADLMNQI QVHRTTIIHK TESIDLLTRE
     LEDIHSKYSI VLLAKEESKT VIEEQEKQIE ELRECLERKQ SADNIEKELL CDDLAHATEE
     LEKLTEAFNK QEALLHTHEK ELVEKEQQIS ELTNQVKLMT DLEISREQEK IRPASSNSSS
     PVVLPETPRT PEGNPYDSEI ANLQKRNTNL EILVSELNEE RTSKNEEIIR LKMQLCETEN
     MRLEIQNLQG MCKELKSQLE NCNNVMKDSN DQKPSDMQDL KREIEKEVSE RMEKGKATEH
     ILKLQAELEE TRNILCTKDH SLNELSKEIE RTRSLEAKAF TEKEEIRSIL EGKYEETEKL
     SHELDMLRKQ VLFLAEENGK ILGHQNPNQK IQYLVKLKKE NNKLLEEAEK LRIENLFLKE
     SKKCEHCN
 
 
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