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Protein

SUN domain-containing protein 1

Gene

Sun1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning. Required for interkinetic nuclear migration (INM) and essential for nucleokinesis and centrosome-nucleus coupling during radial neuronal migration in the cerebral cortex and during glial migration. Involved in telomere attachment to nuclear envelope in the prophase of meiosis implicating a SUN1/2:KASH5 LINC complex in which SUN1 and SUN2 seem to act at least partial redundantly. Required for gametogenesis and involved in selective gene expression of coding and non-coding RNAs needed for gametogenesis. Helps to define the distribution of nuclear pore complexes (NPCs). Required for efficient localization of SYNE4 in the nuclear envelope.8 Publications
Isoform 5 may be involved in nuclear remodeling during sperm head formation in spermatogenenis. A probable SUN1 isoform 5:SYNE3 LINC complex may tether spermatid nuclei to anterior cytoskeletal structures such as actin filaments present at membraneous junctions of spermatids and Sertoli cells.1 Publication

GO - Molecular functioni

  • lamin binding Source: UniProtKB
  • protein membrane anchor Source: GO_Central

GO - Biological processi

  • centrosome localization Source: UniProtKB
  • cytoskeletal anchoring at nuclear membrane Source: MGI
  • meiotic attachment of telomere to nuclear envelope Source: UniProtKB
  • nuclear envelope organization Source: MGI
  • nuclear matrix anchoring at nuclear membrane Source: MGI
  • nucleokinesis involved in cell motility in cerebral cortex radial glia guided migration Source: UniProtKB
  • ossification Source: Ensembl
  • response to mechanical stimulus Source: Ensembl
  • spermatogenesis Source: UniProtKB-KW
  • synapsis Source: MGI

Keywordsi

Biological processDifferentiation, Meiosis, Spermatogenesis

Names & Taxonomyi

Protein namesi
Recommended name:
SUN domain-containing protein 1
Alternative name(s):
Protein unc-84 homolog A
Sad1/unc-84 protein-like 1
Gene namesi
Name:Sun1
Synonyms:Unc84a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1924303 Sun1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 415NuclearAdd BLAST415
Transmembranei416 – 436HelicalAdd BLAST21
Topological domaini437 – 913Perinuclear spaceAdd BLAST477

Keywords - Cellular componenti

Cytoplasmic vesicle, Membrane, Nucleus

Pathology & Biotechi

Disruption phenotypei

Mutant mice are viable, but display hearing loss at all frequencies.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002189121 – 913SUN domain-containing protein 1Add BLAST913

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei48PhosphoserineBy similarity1
Modified residuei66PhosphoserineCombined sources1
Modified residuei139PhosphoserineBy similarity1
Disulfide bondi759Interchain (with KASH domain-containing nesprins)By similarity

Post-translational modificationi

The disulfid bond with KASH domain containing nesprins is required for stability of the respective LINC complexes under tensile forces.By similarity

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

EPDiQ9D666
PaxDbiQ9D666
PeptideAtlasiQ9D666
PRIDEiQ9D666

PTM databases

iPTMnetiQ9D666
PhosphoSitePlusiQ9D666

Expressioni

Tissue specificityi

Widely expressed. Expressed in cochlear outer hair cells (at protein level). Seven isoforms are expressed in testis including testis-specific isoform 5. Isoform 5 is the only isoform expressed at the end of sperm differentiation. Six isoforms are expressed in muscle, heart and brain, four isoforms in kidney and three isoforms in liver.4 Publications

Gene expression databases

BgeeiENSMUSG00000036817
CleanExiMM_UNC84A
ExpressionAtlasiQ9D666 baseline and differential
GenevisibleiQ9D666 MM

Interactioni

Subunit structurei

Core component of the LINC complex which is composed of inner nuclear membrane SUN domain-containing proteins coupled to outer nuclear membrane KASH domain-containing nesprins. SUN and KASH domain-containing proteins seem to bind each other promiscuously; however, differentially expression of LINC complex constituents is giving rise to specific assemblies. At least SUN1/2-containing core LINC complexes are proposed to be hexameric composed of three protomers of each KASH and SUN domain-containing protein. Interacts with CCDC155/KASH5 (via the last 22 amino acids); this interaction mediates CCDC155 telomere localization by forming a SUN1:KASH5 LINC complex. Isoform 5 is proposed to form a non-nuclear spermatogenesis-specific LINC complex with SYNE3 during sperm head formation. Interacts with SYNE2 and SYNE1; probably forming respective LINC complexes. Interacts with A-type lamin with a strong preference for unprocessed A-type lamin compared with the mature protein. Interaction with lamins B1 and C is hardly detectable. Interacts with NAT10. Interacts with EMD and TSNAX. Associates with the nuclear pore complex (NPC). Interacts with CCDC79/TERB1; promoting the accumulation of the LINC complex complexes at the telomere-nuclear envelope attachment sites.By similarity10 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • lamin binding Source: UniProtKB
  • protein membrane anchor Source: GO_Central

Protein-protein interaction databases

BioGridi218484, 6 interactors
DIPiDIP-60732N
IntActiQ9D666, 8 interactors
MINTiQ9D666
STRINGi10090.ENSMUSP00000056655

Structurei

Secondary structure

1913
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi673 – 698Combined sources26
Helixi704 – 713Combined sources10
Helixi721 – 734Combined sources14
Helixi748 – 750Combined sources3
Helixi756 – 758Combined sources3
Beta strandi766 – 770Combined sources5
Beta strandi774 – 780Combined sources7
Helixi784 – 788Combined sources5
Beta strandi789 – 791Combined sources3
Beta strandi798 – 801Combined sources4
Beta strandi805 – 823Combined sources19
Helixi827 – 829Combined sources3
Beta strandi841 – 849Combined sources9
Beta strandi856 – 862Combined sources7
Beta strandi869 – 874Combined sources6
Beta strandi883 – 890Combined sources8
Beta strandi893 – 895Combined sources3
Beta strandi897 – 902Combined sources6
Beta strandi904 – 911Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5YWZX-ray2.20A672-913[»]
ProteinModelPortaliQ9D666
SMRiQ9D666
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini751 – 912SUNPROSITE-ProRule annotationAdd BLAST162

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 139LMNA-bindingBy similarityAdd BLAST139
Regioni209 – 399SYNE2-bindingBy similarityAdd BLAST191
Regioni310 – 399EMD-bindingBy similarityAdd BLAST90
Regioni703 – 913Sufficient for interaction with SYNE1 and SYNE2By similarityAdd BLAST211

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili491 – 533Sequence analysisAdd BLAST43
Coiled coili563 – 638Sequence analysisAdd BLAST76

Domaini

The coiled coil domains differentially mediate trimerization required for binding to nesprins and are proposed to dynamically regulate the oligomeric state by locking the SUN domain in an inactive confirmation. The coiled coil domains are proposed to be involved in load-bearing and force transmission from the cytoskeleton.By similarity
The SUN domain may play a role in the nuclear anchoring and/or migration.

Keywords - Domaini

Coiled coil, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2687 Eukaryota
ENOG410YM6S LUCA
GeneTreeiENSGT00390000011587
HOVERGENiHBG104132
InParanoidiQ9D666
KOiK19347
OMAiLMKLNYE
OrthoDBiEOG091G0AZ8
PhylomeDBiQ9D666
TreeFamiTF323915

Family and domain databases

Gene3Di2.60.120.260, 1 hit
InterProiView protein in InterPro
IPR008979 Galactose-bd-like_sf
IPR018539 SUN1
IPR032680 SUN1_N
IPR012919 SUN_dom
PANTHERiPTHR12911:SF23 PTHR12911:SF23, 1 hit
PfamiView protein in Pfam
PF09387 MRP, 1 hit
PF07738 Sad1_UNC, 1 hit
PROSITEiView protein in PROSITE
PS51469 SUN, 1 hit

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Seven isoforms have been found to be expressed.
Isoform 1 (identifier: Q9D666-1) [UniParc]FASTAAdd to basket
Also known as: alpha

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDFSRLHTYT PPQCVPENTG YTYALSSSYS SDALDFETEH KLEPVFDSPR
60 70 80 90 100
MSRRSLRLVT TASYSSGDSQ AIDSHISTSR ATPAKGRETR TVKQRRSASK
110 120 130 140 150
PAFSINHLSG KGLSSSTSHD SSCSLRSATV LRHPVLDESL IREQTKVDHF
160 170 180 190 200
WGLDDDGDLK GGNKAATQGN GELAAEVASS NGYTCRDCRM LSARTDALTA
210 220 230 240 250
HSAIHGTTSR VYSRDRTLKP RGVSFYLDRT LWLAKSTSSS FASFIVQLFQ
260 270 280 290 300
VVLMKLNFET YKLKGYESRA YESQSYETKS HESEAHLGHC GRMTAGELSR
310 320 330 340 350
VDGESLCDDC KGKKHLEIHT ATHSQLPQPH RVAGAMGRLC IYTGDLLVQA
360 370 380 390 400
LRRTRAAGWS VAEAVWSVLW LAVSAPGKAA SGTFWWLGSG WYQFVTLISW
410 420 430 440 450
LNVFLLTRCL RNICKVFVLL LPLLLLLGAG VSLWGQGNFF SLLPVLNWTA
460 470 480 490 500
MQPTQRVDDS KGMHRPGPLP PSPPPKVDHK ASQWPQESDM GQKVASLSAQ
510 520 530 540 550
CHNHDERLAE LTVLLQKLQI RVDQVDDGRE GLSLWVKNVV GQHLQEMGTI
560 570 580 590 600
EPPDAKTDFM TFHHDHEVRL SNLEDVLRKL TEKSEAIQKE LEETKLKAGS
610 620 630 640 650
RDEEQPLLDR VQHLELELNL LKSQLSDWQH LKTSCEQAGA RIQETVQLMF
660 670 680 690 700
SEDQQGGSLE WLLEKLSSRF VSKDELQVLL HDLELKLLQN ITHHITVTGQ
710 720 730 740 750
APTSEAIVSA VNQAGISGIT EAQAHIIVNN ALKLYSQDKT GMVDFALESG
760 770 780 790 800
GGSILSTRCS ETYETKTALL SLFGVPLWYF SQSPRVVIQP DIYPGNCWAF
810 820 830 840 850
KGSQGYLVVR LSMKIYPTTF TMEHIPKTLS PTGNISSAPK DFAVYGLETE
860 870 880 890 900
YQEEGQPLGR FTYDQEGDSL QMFHTLERPD QAFQIVELRV LSNWGHPEYT
910
CLYRFRVHGE PIQ
Length:913
Mass (Da):101,976
Last modified:February 2, 2004 - v2
Checksum:iB9872C8F2E044964
GO
Isoform 2 (identifier: Q9D666-2) [UniParc]FASTAAdd to basket
Also known as: zeta

The sequence of this isoform differs from the canonical sequence as follows:
     222-344: Missing.

Show »
Length:790
Mass (Da):88,203
Checksum:i127979E6640F2CD4
GO
Isoform 3 (identifier: Q9D666-3) [UniParc]FASTAAdd to basket
Also known as: beta

The sequence of this isoform differs from the canonical sequence as follows:
     308-344: Missing.

Show »
Length:876
Mass (Da):97,924
Checksum:i09357E280A0B8392
GO
Isoform 4 (identifier: Q9D666-4) [UniParc]FASTAAdd to basket
Also known as: delta

The sequence of this isoform differs from the canonical sequence as follows:
     221-285: RGVSFYLDRTLWLAKSTSSSFASFIVQLFQVVLMKLNFETYKLKGYESRAYESQSYETKSHESEA → P

Show »
Length:849
Mass (Da):94,507
Checksum:i7810982DFA292D25
GO
Isoform 5 (identifier: Q9D666-5) [UniParc]FASTAAdd to basket
Also known as: eta

The sequence of this isoform differs from the canonical sequence as follows:
     222-377: Missing.

Show »
Length:757
Mass (Da):84,671
Checksum:i764BD7C53D24CCA3
GO

Sequence cautioni

The sequence AAH30330 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti6L → V in AAT90501 (PubMed:17132086).Curated1
Sequence conflicti108L → P in BAE39733 (PubMed:16141072).Curated1
Sequence conflicti439F → L in AAT90501 (PubMed:17132086).Curated1
Sequence conflicti479H → N in BAE35723 (PubMed:16141072).Curated1
Sequence conflicti505D → G in BAE39733 (PubMed:16141072).Curated1
Sequence conflicti593E → A in BAE39733 (PubMed:16141072).Curated1
Sequence conflicti704S → F in BAE39733 (PubMed:16141072).Curated1
Sequence conflicti856 – 857QP → AA in AAK13526 (PubMed:12036294).Curated2

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_039552221 – 285RGVSF…HESEA → P in isoform 4. 1 PublicationAdd BLAST65
Alternative sequenceiVSP_058699222 – 377Missing in isoform 5. 1 PublicationAdd BLAST156
Alternative sequenceiVSP_009346222 – 344Missing in isoform 2. 1 PublicationAdd BLAST123
Alternative sequenceiVSP_009347308 – 344Missing in isoform 3. 1 PublicationAdd BLAST37

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY682989 mRNA Translation: AAT90501.1
HQ402597 mRNA Translation: ADP89697.1
AK014585 mRNA Translation: BAB29445.1
AK036187 mRNA Translation: BAC29339.1
AK160281 mRNA Translation: BAE35723.1
AK167686 mRNA Translation: BAE39733.1
AC125065 Genomic DNA No translation available.
BC030330 mRNA Translation: AAH30330.1 Different initiation.
BC047928 mRNA Translation: AAH47928.1
BC048156 mRNA Translation: AAH48156.1
AF343752 mRNA Translation: AAK13526.1
CCDSiCCDS19804.1 [Q9D666-1]
CCDS57395.1 [Q9D666-3]
CCDS57396.1 [Q9D666-4]
CCDS57397.1 [Q9D666-2]
CCDS57398.1 [Q9D666-5]
RefSeqiNP_001243044.1, NM_001256115.1 [Q9D666-3]
NP_001243045.1, NM_001256116.1 [Q9D666-4]
NP_001243046.1, NM_001256117.1 [Q9D666-2]
NP_001243047.1, NM_001256118.1 [Q9D666-5]
NP_077771.1, NM_024451.2 [Q9D666-1]
UniGeneiMm.210845

Genome annotation databases

EnsembliENSMUST00000058716; ENSMUSP00000056655; ENSMUSG00000036817 [Q9D666-1]
ENSMUST00000078690; ENSMUSP00000077756; ENSMUSG00000036817 [Q9D666-4]
ENSMUST00000110882; ENSMUSP00000106506; ENSMUSG00000036817 [Q9D666-5]
ENSMUST00000110883; ENSMUSP00000106507; ENSMUSG00000036817 [Q9D666-2]
ENSMUST00000110884; ENSMUSP00000106508; ENSMUSG00000036817 [Q9D666-3]
GeneIDi77053
KEGGimmu:77053
UCSCiuc009agb.2 mouse [Q9D666-1]
uc009agc.2 mouse [Q9D666-3]
uc009agd.2 mouse [Q9D666-2]
uc009age.2 mouse [Q9D666-4]
uc012efr.2 mouse

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiSUN1_MOUSE
AccessioniPrimary (citable) accession number: Q9D666
Secondary accession number(s): D3Z0V9
, Q3TIW3, Q3TV96, Q6B4H0, Q80SU8, Q8BZ99, Q99P23
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: February 2, 2004
Last modified: May 23, 2018
This is version 153 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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