SYNE4_RAT
ID SYNE4_RAT Reviewed; 340 AA.
AC Q5M844;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Nesprin-4;
DE AltName: Full=KASH domain-containing protein 4;
DE Short=KASH4;
DE AltName: Full=Nuclear envelope spectrin repeat protein 4;
GN Name=Syne4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
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).
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. Behaves as a kinesin cargo, providing
CC a functional binding site for kinesin-1 at the nuclear envelope. Hence
CC may contribute to the establishment of secretory epithelial morphology,
CC by promoting kinesin-dependent apical migration of the centrosome and
CC Golgi apparatus and basal localization of the nucleus (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Core component of LINC complexes which are 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 can give rise to
CC specific assemblies. Probably part of a SUN1-containing LINC complex.
CC Interacts with kinesins KIF5B and KLC1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus outer membrane {ECO:0000250}; Single-pass
CC type IV membrane protein {ECO:0000250}. Note=Localization at the
CC nucleus outer membrane location requires the presence of SUN1.
CC {ECO:0000250}.
CC -!- DOMAIN: The KASH domain, which contains a transmembrane domain,
CC mediates the nuclear envelope targeting and is involved in the binding
CC to SUN1 and SUN2 through recognition of their SUN domains.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the nesprin family. {ECO:0000305}.
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DR EMBL; BC088237; AAH88237.1; -; mRNA.
DR RefSeq; NP_001009283.1; NM_001009283.1.
DR RefSeq; XP_017443924.1; XM_017588435.1.
DR AlphaFoldDB; Q5M844; -.
DR STRING; 10116.ENSRNOP00000028265; -.
DR PaxDb; Q5M844; -.
DR Ensembl; ENSRNOT00000051422; ENSRNOP00000044396; ENSRNOG00000049277.
DR GeneID; 292781; -.
DR KEGG; rno:292781; -.
DR UCSC; RGD:1304580; rat.
DR CTD; 163183; -.
DR RGD; 1304580; Syne4.
DR eggNOG; ENOG502SZGW; Eukaryota.
DR GeneTree; ENSGT00510000049061; -.
DR HOGENOM; CLU_034166_1_0_1; -.
DR InParanoid; Q5M844; -.
DR OMA; WTPGSPC; -.
DR PRO; PR:Q5M844; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000020830; Expressed in pancreas and 19 other tissues.
DR ExpressionAtlas; Q5M844; baseline.
DR Genevisible; Q5M844; RN.
DR GO; GO:0031309; C:integral component of nuclear outer membrane; ISS:UniProtKB.
DR GO; GO:0034993; C:meiotic nuclear membrane microtubule tethering complex; IEA:InterPro.
DR GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; ISS:UniProtKB.
DR InterPro; IPR012315; KASH.
DR InterPro; IPR030268; SYNE4.
DR PANTHER; PTHR21640; PTHR21640; 2.
DR Pfam; PF10541; KASH; 1.
DR SMART; SM01249; KASH; 1.
DR PROSITE; PS51049; KASH; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Membrane; Nucleus; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..340
FT /note="Nesprin-4"
FT /id="PRO_0000306266"
FT TOPO_DOM 1..291
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00385"
FT TRANSMEM 292..312
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00385"
FT TOPO_DOM 313..340
FT /note="Perinuclear space"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00385"
FT DOMAIN 283..340
FT /note="KASH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00385"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 317
FT /note="Interchain (with SUN1)"
FT /evidence="ECO:0000250|UniProtKB:Q8WXH0"
FT DISULFID 317
FT /note="Interchain (with SUN2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8WXH0"
SQ SEQUENCE 340 AA; 36515 MW; 6A902E1B950B4346 CRC64;
MAQFPLLGHG FPPEPVNHPL GGPRGLDVAG PTICPAPEEE PSRPEQVQAS LDAPEHFMDE
PKSTESATSP SKLPLASSHE HQDGGKPCEA LQAELQGAAE RVDALLVFGE GLAERSEPRA
WTSLEQVLRA LGTHRDTIFQ RLWQLQAQLI SYSLVLEKAN LLDQDLEVEG DSDGPAAGGV
WGPWAPSIFP TPAELEWDPA GDVGGLGPSG QKISRIPGAP CELCGYRGSQ SSGQGFEDLL
SLGLGHRKHL AAHHRRRLQK PQDKKRQGPP SLPDAMLEVD RGVPAPASRR PLTFLLLLLF
LLLVGATLLL PLSGVPCCSH TRLARTPYLV LSYVNGLPPI
