ID  Q20745;
PN  Nuclear migration and anchoring protein unc-84;
GN  unc;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:10375507, ECO:0000269|PubMed:11748140, ECO:0000269|PubMed:11907270, ECO:0000269|PubMed:16481402, ECO:0000269|PubMed:27956467, ECO:0000305|PubMed:21411627}; Single-pass type II membrane protein {ECO:0000305}. Cytoplasm, cytoskeleton {ECO:0000305}. Note=Associated with nuclei during interphase, prophase, prometaphase, metaphase and early anaphase (PubMed:11907270). Released from nuclear membrane in the same time that the nuclear envelope disassembly, during late anaphase, and begins to reaccumulate in early telophase (PubMed:11907270). Localization at the nuclear envelope depends on lmn-1 (PubMed:11748140, PubMed:11907270). Co-localizes with unc-83 at the nuclear envelope, but its localization at the nuclear envelope does not depend on unc-83 (PubMed:11748140, PubMed:11907270). {ECO:0000269|PubMed:11748140, ECO:0000269|PubMed:11907270}.
DR  UNIPROT: Q20745;
DR  UNIPROT: Q9U475;
DR  UNIPROT: Q9U476;
DR  Pfam: PF07738;
DR  PROSITE: PS51469;
DE  Function: Involved in nuclear migration and anchoring in hypodermal precursor cells (PubMed:10375507, PubMed:11748140, PubMed:12169658, PubMed:11907270, PubMed:16481402, PubMed:20921138, PubMed:21411627, PubMed:23150597, PubMed:25023515, PubMed:25057012). Most likely recruits anc-1 to the nuclear envelope where anc-1 functions to tether the nucleus to the actin cytoskeleton (PubMed:12169658). Component of the unc-83-unc-84 LINC (LInker of Nucleoskeleton and Cytoskeleton) complex where it recruits and interacts with unc-83 to form a bridge connecting the nuclear envelope to the cytoskeleton which allows for nuclear transport along microtubules (PubMed:11748140, PubMed:16481402). Its role in nuclear migration may be in association with lamin, lmn-1 (PubMed:25057012). Regulates nuclear migrations in one-cell embryos, controlling the posterior migration of the male pronucleus following fertilization (PubMed:21798253). Not required for centrosome attachment to the nucleus (PubMed:10375507, PubMed:11907270). Plays a role in the maintenance of the nuclear envelope architecture in body wall muscle cells (PubMed:25023515). May be involved in DNA damage repair through an association with zyg-12 (PubMed:27956467). Potentially has roles in homologous recombination, double strand break repair and meiotic recombination (PubMed:27956467). Specifically, may in part inhibit non-homologous end joining repair, most likely through recruiting fan-1 to the nucleoplasm, to facilitate the repair of DNA cross-links (PubMed:27956467). {ECO:0000269|PubMed:10375507, ECO:0000269|PubMed:11748140, ECO:0000269|PubMed:11907270, ECO:0000269|PubMed:12169658, ECO:0000269|PubMed:16481402, ECO:0000269|PubMed:20921138, ECO:0000269|PubMed:21411627, ECO:0000269|PubMed:21798253, ECO:0000269|PubMed:23150597, ECO:0000269|PubMed:25023515, ECO:0000269|PubMed:25057012, ECO:0000269|PubMed:27956467}.
DE  Reference Proteome: Yes;
DE  Interaction: P90740; IntAct: EBI-333119; Score: 0.00
DE  Interaction: G5EFL5; IntAct: EBI-341426; Score: 0.00
DE  Interaction: O45904; IntAct: EBI-343574; Score: 0.00
DE  Interaction: Q23064; IntAct: EBI-3884847; Score: 0.37
DE  Interaction: P34258; IntAct: EBI-6532488; Score: 0.37
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0016021;
GO  GO:0005639;
GO  GO:0034993;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0005521;
GO  GO:0043495;
GO  GO:0040011;
GO  GO:0007399;
GO  GO:0006998;
GO  GO:0007097;
GO  GO:0030473;
GO  GO:0018991;
GO  GO:0009791;
GO  GO:0030334;
GO  GO:0040025;
TP  Membrane Topology: Transmembrane; Source: UniProt - Curator Inference {ECO:0000305|PubMed:21411627};
SQ  MAPATEADNNFDTHEWKSEFASTRSGRNSPNIFAKVRRKLLLTPPVRNARSPRLTEEELDALTGDLPYATNYTYAYSKIY
SQ  DPSLPDHWEVPNLGGTTSGSLSEQEHWSAASLSRQLLYILRFPVYLVLHVITYILEAFYHVIKITSFTIWDYLLYLVKLA
SQ  KTRYYAYQDHRRRTALIRNRQEPFSTKAARSIRRFFEILVYVVLTPYRMLTRSNNGVEQYQYRSIKDQLENERASRMTTR
SQ  SQTLERSRKFDGLSKSPARRAAPAFVKTSTITRITAKVFSSSPFGEGTSENITPTVVTTRTVKQRSVTPRFRQTRATREA
SQ  ITRALDTPELEIDTPLSTYGLRSRGLSHLNTPEPTFDIGHAAATSTPLFPQETYNYQYEEATGNKIKTAFTWLGYLILFP
SQ  FFAARHVWYTFYDYGKSAYMKLTNYQQAPMETIHVRDINEPAPSSSDVHDAVGVSWRIRIADFLSSFVATIVEAHQVVFA
SQ  MFKGGIVETVSYFGGLFAGLTDKKSSKFSWCQILGLLLALLFAIFLLGFLTSDNTAIRVKEITKDKNASKKSEGSLPAVP
SQ  IWISAANHVKHYTWMVKEFVVDIAFDTYNYGKSTIGRLGTTPRYAWDLIASGCGAVGNGLKSVLSSSFRFIDFCAGKLFY
SQ  YGSDGFLSANKSIGTFFNGCYETLYNGCTAIVGHTKSFIYNASNAVYNFFSTIFAGLLNFSTSSQNSILSLLKSFGTGIT
SQ  NIFYNFIYAPIAGVFNFAGDNYMYFFNEVAAVFGKVYNSVVSVLKTVINWILFLIAYPFSLCTRAWIRISQYAPEDVVQV
SQ  IPIPQAITPTPDVERIVEEPLRKVTDVEDEELVIIPAPAPKPIPVPAPTPAPVIIHQTNVVETVDKDAIIKEVTEKLRAE
SQ  LSAQFQQELSAKFEQNYNTIIEQLKMENTNIQYDKNHLEAIIRQMIYEYDTDKTGKVDYALESSGGAVVSTRCSETYKSY
SQ  TRLEKFWDIPIYYFHYSPRVVIQRNSKSLFPGECWCFKESRGYIAVELSHFIDVSSISYEHIGSEVAPEGNRSSAPKGVL
SQ  VWAYKQIDDLNSRVLIGDYTYDLDGPPLQFFLAKHKPDFPVKFVELEVTSNYGAPFTCLYRLRVHGKVVQV
//