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KIF2A_CHICK
ID   KIF2A_CHICK             Reviewed;         706 AA.
AC   Q5ZKV8;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 2.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Kinesin-like protein KIF2A;
GN   Name=KIF2A {ECO:0000250|UniProtKB:O00139}; ORFNames=RCJMB04_9a7;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1] {ECO:0000312|EMBL:CAG31635.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB {ECO:0000312|EMBL:CAG31635.1};
RC   TISSUE=Bursa of Fabricius {ECO:0000312|EMBL:CAG31635.1};
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
CC   -!- FUNCTION: Plus end-directed microtubule-dependent motor required for
CC       normal brain development. May regulate microtubule dynamics during
CC       axonal growth. Required for normal progression through mitosis.
CC       Required for normal congress of chromosomes at the metaphase plate.
CC       Required for normal spindle dynamics during mitosis. Promotes spindle
CC       turnover. Implicated in formation of bipolar mitotic spindles. Has
CC       microtubule depolymerization activity (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P28740}.
CC       Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC       {ECO:0000250|UniProtKB:P28740}. Cytoplasm, cytoskeleton, spindle pole
CC       {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}.
CC       Note=Localized to the spindle microtubules and spindle poles from
CC       prophase to metaphase. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. MCAK/KIF2 subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00283}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAG31635.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AJ719976; CAG31635.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001034401.2; NM_001039312.2.
DR   AlphaFoldDB; Q5ZKV8; -.
DR   SMR; Q5ZKV8; -.
DR   STRING; 9031.ENSGALP00000023720; -.
DR   PaxDb; Q5ZKV8; -.
DR   GeneID; 427156; -.
DR   KEGG; gga:427156; -.
DR   CTD; 3796; -.
DR   VEuPathDB; HostDB:geneid_427156; -.
DR   eggNOG; KOG0246; Eukaryota.
DR   InParanoid; Q5ZKV8; -.
DR   PhylomeDB; Q5ZKV8; -.
DR   PRO; PR:Q5ZKV8; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR   GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR   GO; GO:0005819; C:spindle; IBA:GO_Central.
DR   GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
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:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR   GO; GO:0007052; P:mitotic spindle organization; ISS:UniProtKB.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   ATP-binding; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW   Cytoskeleton; Developmental protein; Differentiation; Microtubule; Mitosis;
KW   Motor protein; Neurogenesis; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..706
FT                   /note="Kinesin-like protein KIF2A"
FT                   /id="PRO_0000306274"
FT   DOMAIN          223..553
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   REGION          64..187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          154..187
FT                   /evidence="ECO:0000255"
FT   COILED          662..699
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        115..140
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        149..187
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         313..320
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   706 AA;  79864 MW;  6C5CA4DAE3DA1EC8 CRC64;
     MAAANFGKIQ IGIYVEIKRS DGRIHQAMVT SLNEDNESVT VEWIENGDTK GKEIDLESIF
     SLNPDLAPDE DIEPSPETQP LPAPSAKVNK IVKGRRTVAP VKNDTPARDN RVASSARARP
     TQLPEQSSSS QQNGTVSGIS PVQAAKKEFG PPSRRKSNCV KEVEKLQEKR EKRRLQQQEL
     REKRAQDVDA TNPNYEIMCM IRDFRGNLDY RPLTTADPID EHRICVCVRK RPLNRKETLM
     KDLDVITIPS KDVVMVHEPK QKVDLTRYLE NQTFRFDYAF DETAPNEMVY RFTARPLVET
     IFERGMATCF AYGQTGSGKT HTMGGDFSGK NQDCSKGIYA LAARDVFLML KKPNYKKLEL
     QVYATFFEIY SGKVFDLLNR KTKLRVLEDG KQQVQVVGLQ EREVKCVEDV LKLIEIGNSC
     RTSGQTSANA HSSRSHAVFQ IILRRKGKLH GKFSLIDLAG NERGADTSSA DRQTRLEGAE
     INKSLLALKE CIRALGRNKP HTPFRASKLT QVLRDSFIGE NSRTCMIATI SPGMASCENT
     LNTLRYANRV KELTIDPSAA GDIRPIIHHT PSQIDDLDTQ WGVGSSPQRD DLKLLCEQNE
     EEVSPQLFTF HEAVSQMVEM EEQVVEDHRT VFQESIRWLE DEKALLEMTE EVDYDVDSYA
     TQLEAILDQK IDILTELRDK VKSFRAALQE EEQASKQINP KRPRAV
 
 
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