SUN1_CAEEL
ID SUN1_CAEEL Reviewed; 473 AA.
AC Q20924;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Sun domain-containing protein 1;
GN Name=sun-1 {ECO:0000312|WormBase:F57B1.2};
GN Synonyms=mtf-1 {ECO:0000312|WormBase:F57B1.2};
GN ORFNames=F57B1.2 {ECO:0000312|WormBase:F57B1.2};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=14697201; DOI=10.1016/s0092-8674(03)00985-1;
RA Malone C.J., Misner L., Le Bot N., Tsai M.-C., Campbell J.M., Ahringer J.,
RA White J.G.;
RT "The C. elegans hook protein, ZYG-12, mediates the essential attachment
RT between the centrosome and nucleus.";
RL Cell 115:825-836(2003).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=24297748; DOI=10.1083/jcb.201307181;
RA Ferreira H.C., Towbin B.D., Jegou T., Gasser S.M.;
RT "The shelterin protein POT-1 anchors Caenorhabditis elegans telomeres
RT through SUN-1 at the nuclear periphery.";
RL J. Cell Biol. 203:727-735(2013).
CC -!- FUNCTION: Involved in centrosome attachment to the nucleus. Required
CC for zyg-12 localization to the nuclear envelope. Together with pot-1,
CC it is required to anchor telomeres to the nuclear envelope in embryos
CC (PubMed:24297748). {ECO:0000269|PubMed:14697201,
CC ECO:0000269|PubMed:24297748}.
CC -!- INTERACTION:
CC Q20924; P30429: ced-4; NbExp=3; IntAct=EBI-15599048, EBI-494118;
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000305|PubMed:14697201};
CC Single-pass membrane protein {ECO:0000305|PubMed:14697201}. Nucleus
CC envelope {ECO:0000269|PubMed:24297748}.
CC -!- DOMAIN: The SUN domain may play a role in nuclear anchoring.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown disrupts both the
CC localization of pot-1 and the anchoring of telomeres to the nuclear
CC envelope in early embryos. {ECO:0000269|PubMed:24297748}.
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DR EMBL; BX284605; CAB01511.1; -; Genomic_DNA.
DR PIR; T22830; T22830.
DR RefSeq; NP_506281.1; NM_073880.4.
DR AlphaFoldDB; Q20924; -.
DR SMR; Q20924; -.
DR BioGRID; 44820; 10.
DR DIP; DIP-52612N; -.
DR IntAct; Q20924; 2.
DR STRING; 6239.F57B1.2; -.
DR iPTMnet; Q20924; -.
DR EPD; Q20924; -.
DR PaxDb; Q20924; -.
DR PeptideAtlas; Q20924; -.
DR EnsemblMetazoa; F57B1.2.1; F57B1.2.1; WBGene00006311.
DR GeneID; 179802; -.
DR KEGG; cel:CELE_F57B1.2; -.
DR UCSC; F57B1.2; c. elegans.
DR CTD; 179802; -.
DR WormBase; F57B1.2; CE11288; WBGene00006311; sun-1.
DR eggNOG; KOG2687; Eukaryota.
DR HOGENOM; CLU_029733_1_0_1; -.
DR InParanoid; Q20924; -.
DR OMA; VPNHAPK; -.
DR OrthoDB; 1090088at2759; -.
DR PRO; PR:Q20924; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00006311; Expressed in germ line (C elegans) and 3 other tissues.
DR GO; GO:0005639; C:integral component of nuclear inner membrane; IEA:InterPro.
DR GO; GO:0034993; C:meiotic nuclear membrane microtubule tethering complex; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; IDA:WormBase.
DR GO; GO:0043495; F:protein-membrane adaptor activity; IBA:GO_Central.
DR GO; GO:0051642; P:centrosome localization; IMP:WormBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0006998; P:nuclear envelope organization; IBA:GO_Central.
DR GO; GO:0008104; P:protein localization; IMP:WormBase.
DR GO; GO:0010824; P:regulation of centrosome duplication; IGI:WormBase.
DR InterPro; IPR045119; SUN1-5.
DR InterPro; IPR012919; SUN_dom.
DR PANTHER; PTHR12911; PTHR12911; 1.
DR Pfam; PF07738; Sad1_UNC; 1.
DR PROSITE; PS51469; SUN; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Membrane; Nucleus; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..473
FT /note="Sun domain-containing protein 1"
FT /id="PRO_0000218921"
FT TRANSMEM 262..282
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 279..443
FT /note="SUN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00802"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 163..191
FT /evidence="ECO:0000255"
FT COILED 204..235
FT /evidence="ECO:0000255"
FT COMPBIAS 450..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 473 AA; 54132 MW; 99BBFCB48695C7FB CRC64;
MALRHTISPQ FSNRHSPPVT RSVSRTGVHQ PLDTSTPVTR RDSQPGTITG TIQRFHESAD
DSEIDLNSSK FIYKEHFSYK EITSMKKEMW YDWLEYRIRM VRRRFVPTWA QFKRTLMAVV
LFAMLYKYAR DCLFDGTHHN SEGSYADKDA NWASEKQKFH QTISNLRAEF SAHDKQLDFK
TDHLEKLLEN VLEHSKGWKE SAIEELKQIK LWQAEISDAL QQMKKEIDDA KSTKIIHSTP
EKAPETAPTA SLPPSSQLQP MHITRRALLG VNVANSLIGA SIDHSCSSRP VSAKDGFFYD
FMSYFGTFQE GYALLDRDVL SPGEAWCTYD KRATLTVKLA RFVIPKSVSY QHVRWSGIVP
NHAPKLYDVV ACTDSCCTKW QPLVANCEYK ERDGSYDEQE QFCSVPTIQN HSPINHVQFR
FRENHGDMPK TCAYLIRVYG EPVDPPKETQ PMTDNGTESK LESAIVNSVS ETA
