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KLP19_CAEEL
ID   KLP19_CAEEL             Reviewed;        1083 AA.
AC   O45935;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 170.
DE   RecName: Full=Kinesin-like protein klp-19;
GN   Name=klp-19 {ECO:0000312|WormBase:Y43F4B.6};
GN   ORFNames=Y43F4B.6 {ECO:0000312|WormBase:Y43F4B.6};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN   [1] {ECO:0000312|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2] {ECO:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP   AND DISRUPTION PHENOTYPE.
RX   PubMed=15452142; DOI=10.1083/jcb.200403036;
RA   Powers J., Rose D.J., Saunders A., Dunkelbarger S., Strome S., Saxton W.M.;
RT   "Loss of KLP-19 polar ejection force causes misorientation and
RT   missegregation of holocentric chromosomes.";
RL   J. Cell Biol. 166:991-1001(2004).
CC   -!- FUNCTION: Required for chromosome movement and orientation on spindle
CC       poles in mitosis and meiosis (PubMed:15452142). May play a role in
CC       early anterior-posterior chromosome movement in mitotic embryos
CC       (PubMed:15452142). {ECO:0000269|PubMed:15452142}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC       {ECO:0000269|PubMed:15452142}. Nucleus {ECO:0000269|PubMed:15452142}.
CC       Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:15452142}.
CC       Chromosome {ECO:0000269|PubMed:15452142}. Note=Localizes to nuclei of
CC       the distal mitotic zone (PubMed:15452142). During mitotic prophase in
CC       embryos, localizes to the nucleoplasm (PubMed:15452142). In
CC       prometaphase, localizes to the body of the spindle and the periphery of
CC       chromosomes (PubMed:15452142). In anaphase, localizes to the spindle
CC       interzone (PubMed:15452142). Localizes to early meiotic prophase nuclei
CC       and to the nucleoplasm in late prophase (PubMed:15452142). Localizes to
CC       prophase chromosomes before fertilization (PubMed:15452142). During
CC       metaphase of meiosis I and meiosis II, localizes to the body of the
CC       spindle, around the periphery of chromosomes, and between homologous
CC       chromosomes (PubMed:15452142). {ECO:0000269|PubMed:15452142}.
CC   -!- TISSUE SPECIFICITY: Expressed in the gonad.
CC       {ECO:0000269|PubMed:15452142}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in embryos.
CC       {ECO:0000269|PubMed:15452142}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in embryos that
CC       undergo early mitotic divisions as in wild-type, but which later then
CC       display aberrant patterns of nuclei and arrest before morphogenesis
CC       (PubMed:15452142). RNAi-mediated knockdown results in chromosome
CC       segregation defects in mitotic embryos whereby chromosomes form a
CC       disordered metaphase plate and multiple chromosomes exhibit delays in
CC       segregation resulting in the formation of bridges during anaphase
CC       (PubMed:15452142). The chromosome bridges stretch, break and sometimes
CC       form micronuclei (PubMed:15452142). RNAi-mediated knockdown results in
CC       kinetochore orientation defects in anaphase spindles in embryos in
CC       which kinetochores do not align on the spindle and some kinetochores
CC       stretch across the spindle interzone, parallel to the pole-pole axis
CC       (PubMed:15452142). RNAi-mediated knockdown does not cause defects in
CC       spindle architecture or cytokinesis in embryos (PubMed:15452142).
CC       {ECO:0000269|PubMed:15452142}.
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; BX284603; CAA16335.1; -; Genomic_DNA.
DR   PIR; T26844; T26844.
DR   RefSeq; NP_499742.1; NM_067341.3.
DR   SMR; O45935; -.
DR   DIP; DIP-24548N; -.
DR   IntAct; O45935; 1.
DR   STRING; 6239.Y43F4B.6; -.
DR   EPD; O45935; -.
DR   PaxDb; O45935; -.
DR   PeptideAtlas; O45935; -.
DR   EnsemblMetazoa; Y43F4B.6.1; Y43F4B.6.1; WBGene00002229.
DR   GeneID; 176750; -.
DR   KEGG; cel:CELE_Y43F4B.6; -.
DR   UCSC; Y43F4B.6.1; c. elegans.
DR   CTD; 176750; -.
DR   WormBase; Y43F4B.6; CE16631; WBGene00002229; klp-19.
DR   eggNOG; KOG0244; Eukaryota.
DR   GeneTree; ENSGT00940000169248; -.
DR   HOGENOM; CLU_285326_0_0_1; -.
DR   InParanoid; O45935; -.
DR   OMA; CEPELQK; -.
DR   OrthoDB; 248933at2759; -.
DR   PhylomeDB; O45935; -.
DR   Reactome; R-CEL-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR   Reactome; R-CEL-983189; Kinesins.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00002229; Expressed in adult organism and 3 other tissues.
DR   GO; GO:0005694; C:chromosome; IDA:WormBase.
DR   GO; GO:0000794; C:condensed nuclear chromosome; IDA:WormBase.
DR   GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR   GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; IDA:WormBase.
DR   GO; GO:0005819; C:spindle; IDA:WormBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR   GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR   GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR   GO; GO:0010032; P:meiotic chromosome condensation; IMP:UniProtKB.
DR   GO; GO:0051257; P:meiotic spindle midzone assembly; IMP:UniProtKB.
DR   GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
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; 2.
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   2: Evidence at transcript level;
KW   ATP-binding; Cell cycle; Cell division; Chromosome; Coiled coil; Cytoplasm;
KW   Cytoskeleton; Meiosis; Mitosis; Nucleotide-binding; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..1083
FT                   /note="Kinesin-like protein klp-19"
FT                   /id="PRO_0000455829"
FT   DOMAIN          6..328
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   COILED          408..435
FT                   /evidence="ECO:0000255"
FT   COILED          487..650
FT                   /evidence="ECO:0000255"
FT   BINDING         85..92
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1083 AA;  123139 MW;  2410A98C7C142D81 CRC64;
     MSSDASLRVV VRARPMNGRE TKEGASRCVQ FYENTKQIVI NESATFTFDA VFADTSDQES
     VYETTALPLL DRIFAGFNAT VLAYGQTGSG KTYTMGTEDN VGTDEMRRGI IPRLVSALFQ
     RIMNTEAPES FAVTVSMFEV YGDNVYDLLR PDKVKLNVHG DEKNCTVVNL TAVPVIDLKG
     ALKQLAVGCH YRTKAETAMN AMSSRSHAVF TVFVEKTATA ECDSAFSAKL QLVDLAGSER
     LKKTEAEGNR MKEGININGG LLILSQVIAA LATKQKHIPY RNSVITRVLQ DSLGGNSFTV
     FLACISPADS NSQETLNTLR YADRAKQIKN KPIVNKNPKA EEIAILQAQL KRLQKENADL
     KQGIAPAEVR FNDANNSAEI LSLKEEVVRK TEQLKERAMK QSECIIRMSA LTQKNSRLEE
     DKAKLQSMLT DVRNTVLNEE MLDAAEVVRS IQQVVGDTEE STTLADDDND ETALGGQDDT
     IYDTERLPEL QAELDDLEKQ IAMKDENRQK ALDEQRAFIE AMQQRESEKT QLVVRISELE
     TEMNKLRQEG KKVTTAAKLA EERRQKLKDL ERQHAEDKKV LNDMKKLQET RRRMEETLKK
     TEDELKNLKT QRLRLLREQR AEASKFQAFK QKHEREMAQM KSKLQKREND VAIQKRMTDQ
     KLTVLQMRLT EANRANKTLR ELNLKRANRK SSPTNASALQ NMIEEELEHE MCAQRSHWLC
     EDLRRQRHDL MQNINTVESM KFEGGKRRRI SASADPNVSV VIEGEEEFEV KRQKELTFLR
     ASLETLNEEI KDSLRNETIA GNEERANSRW EKVPAEMRPA FEAVYAQAVA HIRKEIELEF
     KLARTKSEFT AKIASKASHE EKRKKEDEEM RAKYRELAQC LEDAKSGLHE KIAFLLCLIK
     ENRVDENAIQ QFESLKNQFC DVEQKVKKAS RRKTTNFMGG LTPKPELQRN ERARRAVKYY
     GNVVNSEDVT MDDSRHQKRK DHSLLAVEMN RTTDDNVKRR VAMSPIKCDD DTRLTEEDED
     IENEAMNNAT FVKDSFNSAT IVLDDSQPSP SNSTFVIGAA PTSEADGVPP IKRKSRRTDL
     GPL
 
 
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