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KASH5_BOVIN
ID   KASH5_BOVIN             Reviewed;         525 AA.
AC   Q2T9R2; F1N496;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2012, sequence version 2.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Protein KASH5 {ECO:0000305};
DE   AltName: Full=Coiled-coil domain-containing protein 155;
GN   Name=KASH5; Synonyms=CCDC155;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford;
RX   PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA   Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA   Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA   Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT   "A whole-genome assembly of the domestic cow, Bos taurus.";
RL   Genome Biol. 10:R42.01-R42.10(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: As a component of the LINC (LInker of Nucleoskeleton and
CC       Cytoskeleton) complex, involved in the connection between the nuclear
CC       lamina and the cytoskeleton. The nucleocytoplasmic interactions
CC       established by the LINC complex play an important role in the
CC       transmission of mechanical forces across the nuclear envelope and in
CC       nuclear movement and positioning. Required for telomere attachment to
CC       nuclear envelope in the prophase of meiosis and for rapid telomere
CC       prophase movements implicating a SUN1/2:KASH5 LINC complex in which
CC       SUN1 and SUN2 seem to act at least partial redundantly. Required for
CC       homolog pairing during meiotic prophase in spermatocytes and probably
CC       oocytes. Essential for male and female gametogenesis. Recruits
CC       cytoplasmic dynein to telomere attachment sites at the nuclear envelope
CC       in spermatocytes. In oocytes is involved in meiotic resumption and
CC       spindle formation. {ECO:0000250|UniProtKB:Q80VJ8}.
CC   -!- SUBUNIT: Core component the LINC complex which is composed of inner
CC       nuclear membrane SUN domain-containing proteins coupled to outer
CC       nuclear membrane KASH domain-containing nesprins. SUN and KASH domain-
CC       containing proteins seem to bind each other promiscuously; however,
CC       differentially expression of LINC complex constituents is giving rise
CC       to specific assemblies. At least SUN1/2-containing core LINC complexes
CC       are proposed to be hexameric composed of three protomers of each KASH
CC       and SUN domain-containing protein. Interacts (via the last 22 AA) with
CC       SUN1; this interaction mediates its telomere localization by forming a
CC       SUN1:KASH5 LINC complex. Component of a probable SUN2:KASH5 LINC
CC       complex. Self-associates. Interacts with DYNC1H1, DCTN1, DYNC1I1/2 and
CC       PAFAH1B1; suggesting the association with the dynein-dynactin motor
CC       complex. {ECO:0000250|UniProtKB:Q80VJ8}.
CC   -!- SUBCELLULAR LOCATION: Nucleus outer membrane
CC       {ECO:0000250|UniProtKB:Q80VJ8, ECO:0000305}; Single-pass type IV
CC       membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Nucleus
CC       {ECO:0000250|UniProtKB:Q80VJ8}. Chromosome, telomere
CC       {ECO:0000250|UniProtKB:Q80VJ8}. Note=Localized exclusively at telomeres
CC       from the leptotene to diplotene stages. Colocalizes with SUN2 at sites
CC       of telomere attachment in meiocytes. At oocyte MI stage localized
CC       around the spindle, at MII stage localized to the spindle poles.
CC       {ECO:0000250|UniProtKB:Q80VJ8}.
CC   -!- DOMAIN: The C-terminal 22 AA is required and sufficient for
CC       localization to telomeres at the nuclear envelope. {ECO:0000250}.
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DR   EMBL; DAAA02047474; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC111305; AAI11306.1; -; mRNA.
DR   RefSeq; NP_001070414.1; NM_001076946.2.
DR   AlphaFoldDB; Q2T9R2; -.
DR   SMR; Q2T9R2; -.
DR   STRING; 9913.ENSBTAP00000040719; -.
DR   PaxDb; Q2T9R2; -.
DR   GeneID; 617651; -.
DR   KEGG; bta:617651; -.
DR   CTD; 147872; -.
DR   eggNOG; ENOG502RXNC; Eukaryota.
DR   HOGENOM; CLU_039584_1_0_1; -.
DR   InParanoid; Q2T9R2; -.
DR   OrthoDB; 335596at2759; -.
DR   TreeFam; TF337560; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0000781; C:chromosome, telomeric region; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000800; C:lateral element; IBA:GO_Central.
DR   GO; GO:0034993; C:meiotic nuclear membrane microtubule tethering complex; IBA:GO_Central.
DR   GO; GO:0090619; C:meiotic spindle pole; IBA:GO_Central.
DR   GO; GO:0005640; C:nuclear outer membrane; IBA:GO_Central.
DR   GO; GO:0070840; F:dynein complex binding; IBA:GO_Central.
DR   GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR   GO; GO:0090220; P:chromosome localization to nuclear envelope involved in homologous chromosome segregation; IBA:GO_Central.
DR   GO; GO:0007129; P:homologous chromosome pairing at meiosis; IBA:GO_Central.
DR   GO; GO:0090172; P:microtubule cytoskeleton organization involved in homologous chromosome segregation; IBA:GO_Central.
DR   GO; GO:0051225; P:spindle assembly; IBA:GO_Central.
DR   GO; GO:0051653; P:spindle localization; IBA:GO_Central.
DR   GO; GO:0034397; P:telomere localization; IBA:GO_Central.
DR   InterPro; IPR028170; KASH5.
DR   InterPro; IPR028168; KASH5_coiled-coil.
DR   InterPro; IPR039508; KASH5_EF-hand-like_dom.
DR   PANTHER; PTHR47300; PTHR47300; 1.
DR   Pfam; PF14658; EF-hand_9; 1.
DR   Pfam; PF14662; KASH_CCD; 1.
PE   2: Evidence at transcript level;
KW   Chromosome; Coiled coil; Meiosis; Membrane; Nucleus; Reference proteome;
KW   Telomere; Transmembrane; Transmembrane helix.
FT   CHAIN           1..525
FT                   /note="Protein KASH5"
FT                   /id="PRO_0000331526"
FT   TOPO_DOM        1..483
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        484..504
FT                   /note="Helical; Anchor for type IV membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        505..525
FT                   /note="Perinuclear space"
FT                   /evidence="ECO:0000255"
FT   REGION          127..156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          384..409
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          423..444
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          164..360
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        389..409
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        324
FT                   /note="E -> G (in Ref. 2; AAI11306)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   525 AA;  58598 MW;  97C0E856CFA4E57E CRC64;
     MDMPEDQAGG PTAKMYLWDQ AEDRSLGTLL SLEEQILNST FEACDPQRTG TVAVTHLLAY
     LEAVTGRGPQ DARLQTLACS LDPSGEGPQA TVDLDTFLVV MRDWITACQL DGGLELEEET
     AFEGALTSQQ LPSGCPEVED PANLESFGGE DPRPELPATA DLLSSLEDLE LSNRRLAGEN
     AKLQRSVETA EEGSARLGEE ISALRKQLRS TQQALQLARG VDEELEDLKT LAKSLEEQNR
     SLLAQARHTE KEQQRLVAEM ETLQEENGKL LAERDGVKRR SEELASEKDI LKRQLYECEH
     LICQRDAILS ERTRHAESLT KTLEEYRATT QELRLEISHL EEQLSQTQEG LDELSEGAQV
     RRVDCTNLLP PSLGVELQAI QQRNLQEESA HPQEGREEPS TRLPRREEED GAEIQVMVDL
     PLHPEDSHPG DILGNPPESS PSEPELQQAL VPMVKELVPV RRPVWGQLCL WPLHLRRLRV
     TRHLLIPAPL LGLLLLLLLS VLLLGQSPPP TWPHLQLCYL QPPPV
 
 
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