KASH5_MOUSE
ID KASH5_MOUSE Reviewed; 648 AA.
AC Q80VJ8; E9QNS3; E9QQ69;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 3.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Protein KASH5 {ECO:0000305};
DE AltName: Full=Coiled-coil domain-containing protein 155;
DE AltName: Full=KASH domain-containing protein 5;
GN Name=Kash5 {ECO:0000303|PubMed:22826121, ECO:0000312|MGI:MGI:2687329};
GN Synonyms=Ccdc155 {ECO:0000312|MGI:MGI:2687329};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP INTERACTION WITH SUN1, AND MUTAGENESIS OF 645-PRO--PRO-647.
RX PubMed=22826121; DOI=10.1083/jcb.201204085;
RA Morimoto A., Shibuya H., Zhu X., Kim J., Ishiguro K., Han M., Watanabe Y.;
RT "A conserved KASH domain protein associates with telomeres, SUN1, and
RT dynactin during mammalian meiosis.";
RL J. Cell Biol. 198:165-172(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=129/Sv X 129SvCp; TISSUE=Embryonic stem cell;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND TISSUE SPECIFICITY.
RX PubMed=24062341; DOI=10.1083/jcb.201304004;
RA Horn H.F., Kim D.I., Wright G.D., Wong E.S., Stewart C.L., Burke B.,
RA Roux K.J.;
RT "A mammalian KASH domain protein coupling meiotic chromosomes to the
RT cytoskeleton.";
RL J. Cell Biol. 202:1023-1039(2013).
RN [6]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=24586178; DOI=10.1371/journal.pgen.1004099;
RA Link J., Leubner M., Schmitt J., Goeb E., Benavente R., Jeang K.T., Xu R.,
RA Alsheimer M.;
RT "Analysis of meiosis in SUN1 deficient mice reveals a distinct role of SUN2
RT in mammalian meiotic LINC complex formation and function.";
RL PLoS Genet. 10:E1004099-E1004099(2014).
RN [7]
RP FUNCTION.
RX PubMed=25892231; DOI=10.1016/j.celrep.2015.03.045;
RA Lee C.Y., Horn H.F., Stewart C.L., Burke B., Bolcun-Filas E.,
RA Schimenti J.C., Dresser M.E., Pezza R.J.;
RT "Mechanism and regulation of rapid telomere prophase movements in mouse
RT meiotic chromosomes.";
RL Cell Rep. 11:551-563(2015).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=26842404; DOI=10.1038/srep20408;
RA Luo Y., Lee I.W., Jo Y.J., Namgoong S., Kim N.H.;
RT "Depletion of the LINC complex disrupts cytoskeleton dynamics and meiotic
RT resumption in mouse oocytes.";
RL Sci. Rep. 6:20408-20408(2016).
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:0000269|PubMed:24062341,
CC ECO:0000269|PubMed:25892231, ECO:0000269|PubMed:26842404}.
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:Q8WXH0, ECO:0000269|PubMed:22826121,
CC ECO:0000269|PubMed:24062341, ECO:0000305, ECO:0000305|PubMed:24586178}.
CC -!- INTERACTION:
CC Q80VJ8; Q9D666: Sun1; NbExp=4; IntAct=EBI-11666341, EBI-6752574;
CC -!- SUBCELLULAR LOCATION: Nucleus outer membrane
CC {ECO:0000269|PubMed:24062341, ECO:0000269|PubMed:26842404}; Single-pass
CC type IV membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC Nucleus {ECO:0000269|PubMed:22826121}. Chromosome, telomere
CC {ECO:0000269|PubMed:22826121}. 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:0000269|PubMed:24586178, ECO:0000269|PubMed:26842404}.
CC -!- TISSUE SPECIFICITY: Restricted to the testis and the early
CC ootidogenesis ovary. Expressed in spermatocytes and oocytes (at protein
CC level). {ECO:0000269|PubMed:22826121, ECO:0000269|PubMed:24062341,
CC ECO:0000269|PubMed:26842404}.
CC -!- DOMAIN: The C-terminal 22 AA is required and sufficient for
CC localization to telomeres at the nuclear envelope.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH50196.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB725603; BAM28637.1; -; mRNA.
DR EMBL; AC149868; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC050196; AAH50196.1; ALT_INIT; mRNA.
DR CCDS; CCDS21234.2; -.
DR RefSeq; NP_958762.2; NM_201374.2.
DR AlphaFoldDB; Q80VJ8; -.
DR SMR; Q80VJ8; -.
DR DIP; DIP-60733N; -.
DR IntAct; Q80VJ8; 6.
DR STRING; 10090.ENSMUSP00000113616; -.
DR PaxDb; Q80VJ8; -.
DR PRIDE; Q80VJ8; -.
DR ProteomicsDB; 268957; -.
DR Antibodypedia; 9176; 62 antibodies from 17 providers.
DR DNASU; 384619; -.
DR Ensembl; ENSMUST00000121017; ENSMUSP00000113616; ENSMUSG00000038292.
DR GeneID; 384619; -.
DR KEGG; mmu:384619; -.
DR UCSC; uc009gub.1; mouse.
DR CTD; 147872; -.
DR MGI; MGI:2687329; Kash5.
DR VEuPathDB; HostDB:ENSMUSG00000038292; -.
DR eggNOG; ENOG502RXNC; Eukaryota.
DR GeneTree; ENSGT00420000029926; -.
DR HOGENOM; CLU_039584_1_0_1; -.
DR InParanoid; Q80VJ8; -.
DR OMA; RQLCECE; -.
DR OrthoDB; 335596at2759; -.
DR PhylomeDB; Q80VJ8; -.
DR TreeFam; TF337560; -.
DR BioGRID-ORCS; 384619; 3 hits in 110 CRISPR screens.
DR ChiTaRS; Ccdc155; mouse.
DR PRO; PR:Q80VJ8; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q80VJ8; protein.
DR Bgee; ENSMUSG00000038292; Expressed in testis and 44 other tissues.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000800; C:lateral element; IDA:MGI.
DR GO; GO:0034993; C:meiotic nuclear membrane microtubule tethering complex; IDA:UniProtKB.
DR GO; GO:0090619; C:meiotic spindle pole; IDA:UniProtKB.
DR GO; GO:0005640; C:nuclear outer membrane; IDA:MGI.
DR GO; GO:0070840; F:dynein complex binding; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IDA:MGI.
DR GO; GO:0007015; P:actin filament organization; IMP:UniProtKB.
DR GO; GO:0090220; P:chromosome localization to nuclear envelope involved in homologous chromosome segregation; IMP:MGI.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:MGI.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; IMP:MGI.
DR GO; GO:0090172; P:microtubule cytoskeleton organization involved in homologous chromosome segregation; IPI:MGI.
DR GO; GO:0048477; P:oogenesis; IMP:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR GO; GO:0051225; P:spindle assembly; IDA:UniProtKB.
DR GO; GO:0051653; P:spindle localization; IDA:UniProtKB.
DR GO; GO:0034397; P:telomere localization; IMP:UniProtKB.
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 1: Evidence at protein level;
KW Chromosome; Coiled coil; Meiosis; Membrane; Nucleus; Reference proteome;
KW Telomere; Transmembrane; Transmembrane helix.
FT CHAIN 1..648
FT /note="Protein KASH5"
FT /id="PRO_0000331528"
FT TOPO_DOM 1..606
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 607..627
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 628..648
FT /note="Perinuclear space"
FT /evidence="ECO:0000255"
FT REGION 206..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 230..420
FT /evidence="ECO:0000255"
FT COMPBIAS 474..494
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 645..647
FT /note="PPP->AAA: Abolishes interaction with SUN1. Fails to
FT localize at telomere."
FT /evidence="ECO:0000269|PubMed:22826121"
FT MUTAGEN 645..647
FT /note="Missing: Abolishes interaction with SUN1. Fails to
FT localize at telomere."
FT /evidence="ECO:0000269|PubMed:22826121"
FT CONFLICT 9
FT /note="L -> R (in Ref. 3; AAH50196)"
FT /evidence="ECO:0000305"
FT CONFLICT 29
FT /note="G -> R (in Ref. 3; AAH50196)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="G -> E (in Ref. 3; AAH50196)"
FT /evidence="ECO:0000305"
FT CONFLICT 334
FT /note="Q -> P (in Ref. 3; AAH50196)"
FT /evidence="ECO:0000305"
FT CONFLICT 469
FT /note="W -> R (in Ref. 3; AAH50196)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 648 AA; 72444 MW; 65CC342EB6F9DA51 CRC64;
MHSILRSSLS SREALRMRQL KGLRKERPGR HPLGVRLRAI WTSFLFPNPP HSGGKLRAST
AAVEEHQEWS MDLPEGQAGG PTAQMYLWEQ PEEASSRPLL SLEEQILNST FEACDPHKTG
TVTVAHLLAY LEAVTGQGPQ DVRLQTLARS LDPYGEGAGA TVELDTFLVV MRDWIAACQL
QGGLERAEET AYEGALASPH LPSVCPEAEE SANLESFGGE DPRPEGPATA ELLSNLEDLE
LSNRRLAGEN AKLQRSVETA EEGSARLGEE ITALRKQLRS TQQALQVAKA LDEELEDLKT
LAKSLEEQNR SLMAQARHTE KEQQHLAAEV ETLQEENEKL LAERDGVKRR SEELATEKDA
LKRQLCECER LICQREAVLS ERTRHAESLA RTLEEYRTTT QELRQEISNL EEQLSQSQEG
PEELLEGAEA GRVGWIMALP PSLDLEIQAI RQEQDVASAG LSSPLYGVWQ WEEVEPEPEP
EPEPEPEPEP QEVEFPSEDP ARQQTDLQRE PVRALEGSRA PCLRLSRSQE EEEEEEESWV
LADPSSPLGT YHHKLAPGSS RESCHIVPEM HQALMPVVRD LVPVERSRTQ HCLHPQHSPG
IRISQHPLVP TPVLGLLLLL LLSILLFSQS PPPTWPHLQL YYLQPPPV
