UNC83_CAEEL
ID UNC83_CAEEL Reviewed; 1041 AA.
AC Q23064; Q95WB6;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Nuclear migration protein unc-83;
DE AltName: Full=Uncoordinated protein 83;
GN Name=unc-83 {ECO:0000303|PubMed:11748140, ECO:0000312|WormBase:W01A11.3a};
GN ORFNames=W01A11.3 {ECO:0000312|WormBase:W01A11.3a};
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 [MRNA] (ISOFORMS A; B AND C), FUNCTION,
RP CHARACTERIZATION, AND INTERACTION WITH UNC-84.
RC STRAIN=Bristol N2;
RX PubMed=11748140; DOI=10.1242/dev.128.24.5039;
RA Starr D.A., Hermann G.J., Malone C.J., Fixsen W., Priess J.R.,
RA Horvitz H.R., Han M.;
RT "unc-83 encodes a novel component of the nuclear envelope and is essential
RT for proper nuclear migration.";
RL Development 128:5039-5050(2001).
RN [2]
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 [3]
RP FUNCTION, INTERACTION WITH UNC-84, SUBCELLULAR LOCATION, DOMAIN, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF 1025-GLY--VAL-1041; TYR-1034;
RP 1038-PRO-PRO-1039; PRO-1038; PRO-1039 AND PRO-1040.
RX PubMed=16481402; DOI=10.1091/mbc.e05-09-0894;
RA McGee M.D., Rillo R., Anderson A.S., Starr D.A.;
RT "UNC-83 IS a KASH protein required for nuclear migration and is recruited
RT to the outer nuclear membrane by a physical interaction with the SUN
RT protein UNC-84.";
RL Mol. Biol. Cell 17:1790-1801(2006).
RN [4]
RP FUNCTION, INTERACTION WITH KLC-2, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=19605495; DOI=10.1242/dev.038596;
RA Meyerzon M., Fridolfsson H.N., Ly N., McNally F.J., Starr D.A.;
RT "UNC-83 is a nuclear-specific cargo adaptor for kinesin-1-mediated nuclear
RT migration.";
RL Development 136:2725-2733(2009).
RN [5]
RP FUNCTION, INTERACTION WITH BICD-1; DLC-1 AND NUD-2, SUBUNIT, SUBCELLULAR
RP LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=20005871; DOI=10.1016/j.ydbio.2009.12.004;
RA Fridolfsson H.N., Ly N., Meyerzon M., Starr D.A.;
RT "UNC-83 coordinates kinesin-1 and dynein activities at the nuclear envelope
RT during nuclear migration.";
RL Dev. Biol. 338:237-250(2010).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20921138; DOI=10.1083/jcb.201004118;
RA Fridolfsson H.N., Starr D.A.;
RT "Kinesin-1 and dynein at the nuclear envelope mediate the bidirectional
RT migrations of nuclei.";
RL J. Cell Biol. 191:115-128(2010).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=21411627; DOI=10.1091/mbc.e10-08-0733;
RA Tapley E.C., Ly N., Starr D.A.;
RT "Multiple mechanisms actively target the SUN protein UNC-84 to the inner
RT nuclear membrane.";
RL Mol. Biol. Cell 22:1739-1752(2011).
RN [8]
RP FUNCTION.
RX PubMed=25023515; DOI=10.1083/jcb.201405081;
RA Cain N.E., Tapley E.C., McDonald K.L., Cain B.M., Starr D.A.;
RT "The SUN protein UNC-84 is required only in force-bearing cells to maintain
RT nuclear envelope architecture.";
RL J. Cell Biol. 206:163-172(2014).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=27697906; DOI=10.1242/dev.141192;
RA Bone C.R., Chang Y.T., Cain N.E., Murphy S.P., Starr D.A.;
RT "Nuclei migrate through constricted spaces using microtubule motors and
RT actin networks in C. elegans hypodermal cells.";
RL Development 143:4193-4202(2016).
CC -!- FUNCTION: Cargo-specific adapter that is involved in nuclear migration
CC during development and thereafter (PubMed:11748140, PubMed:19605495,
CC PubMed:20005871, PubMed:20921138, PubMed:27697906). Component of the
CC unc-83-unc-84 LINC (LInker of Nucleoskeleton and Cytoskeleton) complex
CC where it interacts with unc-84 to form a bridge connecting the nuclear
CC envelope to the cytoskeleton which allows for nuclear transport along
CC microtubules (PubMed:11748140, PubMed:16481402, PubMed:25023515).
CC Within the complex, connects the nuclear envelope to the microtubule
CC cytoskeleton through the kinesin-1 light chain protein klc-2 (most
CC likely within the Kinesin 1 motor complex) to regulate nuclear
CC migrations (PubMed:19605495, PubMed:20921138). Moreover, within the
CC complex, also recruits the large microtubule-associated bicd-1-dlc-1-
CC egal-1 and lis-1-nud-2 complexes to the nuclear envelope to regulate
CC both the bidirectional migration of nuclei and the extent of nuclear
CC migrations (PubMed:20005871). Not required for centrosome attachment to
CC the nucleus (PubMed:11748140). {ECO:0000269|PubMed:11748140,
CC ECO:0000269|PubMed:16481402, ECO:0000269|PubMed:19605495,
CC ECO:0000269|PubMed:20005871, ECO:0000269|PubMed:20921138,
CC ECO:0000269|PubMed:25023515, ECO:0000269|PubMed:27697906}.
CC -!- SUBUNIT: Component of the unc-83-unc-84 LINC complex which contains at
CC least unc-83 and unc-84 (PubMed:11748140, PubMed:16481402). Within the
CC unc-83-unc-84 LINC complex interacts with unc-84 (via C-terminus); the
CC interaction is probably required to recruit unc-83 to the nuclear
CC envelope where it then recruits dynein and kinesin-1 complexes to
CC regulate nuclear migration (PubMed:11748140, PubMed:16481402).
CC Interacts with bicd-1 and dlc-1 (PubMed:20005871). Interacts with nud-2
CC (via C-terminus); the interaction is direct, and is required for
CC recruitment of nud-2 to the nuclear envelope (PubMed:20005871).
CC Interacts with klc-2; the interaction is direct (PubMed:19605495).
CC {ECO:0000269|PubMed:11748140, ECO:0000269|PubMed:16481402,
CC ECO:0000269|PubMed:19605495, ECO:0000269|PubMed:20005871}.
CC -!- INTERACTION:
CC Q23064-3; V6CJ04: bicd-1; NbExp=2; IntAct=EBI-2902257, EBI-2006416;
CC Q23064-3; Q22799: dlc-1; NbExp=2; IntAct=EBI-2902257, EBI-328324;
CC Q23064-3; O45717: nud-2; NbExp=5; IntAct=EBI-2902257, EBI-326083;
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:11748140,
CC ECO:0000269|PubMed:19605495, ECO:0000269|PubMed:20005871,
CC ECO:0000269|PubMed:27697906, ECO:0000305|PubMed:21411627}; Single-pass
CC type IV membrane protein {ECO:0000305}. Nucleus outer membrane
CC {ECO:0000269|PubMed:16481402}; Single-pass type IV membrane protein
CC {ECO:0000305}. Note=The transmembrane domain associates with the
CC nuclear envelope (PubMed:11748140). Co-localizes with unc-84 and lmn-1
CC at the nuclear envelope (PubMed:11748140).
CC {ECO:0000269|PubMed:11748140}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=a {ECO:0000312|WormBase:W01A11.3a};
CC IsoId=Q23064-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:W01A11.3b};
CC IsoId=Q23064-2; Sequence=VSP_007083;
CC Name=c {ECO:0000312|WormBase:W01A11.3c};
CC IsoId=Q23064-3; Sequence=VSP_007084;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in migratory nuclei
CC (PubMed:11748140). Expressed in a variety of cell-types, including
CC cells around the pharynx and in the uterus (PubMed:11748140).
CC {ECO:0000269|PubMed:11748140}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos and adults (PubMed:11748140).
CC First expressed at the nuclear envelope of migrating hyp7 nuclei, then,
CC at the bean embryonic stage, it is expressed in hyp7 cells, P cells and
CC intestinal cells (PubMed:11748140). {ECO:0000269|PubMed:11748140}.
CC -!- DOMAIN: The KASH domain, which contains a transmembrane domain,
CC mediates nuclear envelope targeting. {ECO:0000269|PubMed:16481402}.
CC -!- DISRUPTION PHENOTYPE: Viable, but with failed nuclear migrations in
CC hyp7 hypodermal precursor cells (PubMed:11748140, PubMed:16481402,
CC PubMed:19605495, PubMed:20005871, PubMed:20921138). Hyp7 nuclei are
CC mislocalized to the dorsal cord of L1 stage larvae (PubMed:19605495).
CC {ECO:0000269|PubMed:11748140, ECO:0000269|PubMed:16481402,
CC ECO:0000269|PubMed:19605495, ECO:0000269|PubMed:20005871,
CC ECO:0000269|PubMed:20921138}.
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DR EMBL; AF338767; AAL15621.1; -; mRNA.
DR EMBL; BX284605; CCD74262.1; -; Genomic_DNA.
DR PIR; T29644; T29644.
DR RefSeq; NP_001076749.1; NM_001083280.2. [Q23064-1]
DR AlphaFoldDB; Q23064; -.
DR SMR; Q23064; -.
DR BioGRID; 44079; 35.
DR ComplexPortal; CPX-1385; unc-83-unc-84 LINC complex.
DR IntAct; Q23064; 15.
DR STRING; 6239.W01A11.3a; -.
DR EPD; Q23064; -.
DR PaxDb; Q23064; -.
DR EnsemblMetazoa; W01A11.3a.1; W01A11.3a.1; WBGene00006815. [Q23064-1]
DR GeneID; 179033; -.
DR KEGG; cel:CELE_W01A11.3; -.
DR UCSC; W01A11.3a; c. elegans. [Q23064-1]
DR CTD; 179033; -.
DR WormBase; W01A11.3a; CE31077; WBGene00006815; unc-83. [Q23064-1]
DR WormBase; W01A11.3b; CE40370; WBGene00006815; unc-83. [Q23064-2]
DR WormBase; W01A11.3c; CE40371; WBGene00006815; unc-83. [Q23064-3]
DR eggNOG; ENOG502SGIJ; Eukaryota.
DR InParanoid; Q23064; -.
DR OMA; MVRIESH; -.
DR OrthoDB; 166865at2759; -.
DR PRO; PR:Q23064; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00006815; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR ExpressionAtlas; Q23064; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0005640; C:nuclear outer membrane; IDA:UniProtKB.
DR GO; GO:0045503; F:dynein light chain binding; IPI:WormBase.
DR GO; GO:0040011; P:locomotion; IMP:WormBase.
DR GO; GO:0007399; P:nervous system development; IMP:WormBase.
DR GO; GO:0007097; P:nuclear migration; IMP:WormBase.
DR GO; GO:0030473; P:nuclear migration along microtubule; IMP:UniProtKB.
DR GO; GO:0018991; P:oviposition; IMP:WormBase.
DR GO; GO:0009791; P:post-embryonic development; IMP:WormBase.
DR GO; GO:0090435; P:protein localization to nuclear envelope; IMP:UniProtKB.
DR GO; GO:0030334; P:regulation of cell migration; TAS:WormBase.
DR GO; GO:0040025; P:vulval development; IMP:WormBase.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Developmental protein; Membrane;
KW Nucleus; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..1041
FT /note="Nuclear migration protein unc-83"
FT /id="PRO_0000065721"
FT TRANSMEM 1005..1024
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT DOMAIN 986..1041
FT /note="KASH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00385"
FT REGION 258..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 785..816
FT /evidence="ECO:0000255"
FT COILED 931..951
FT /evidence="ECO:0000255"
FT COMPBIAS 470..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..301
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_007084"
FT VAR_SEQ 1..66
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_007083"
FT MUTAGEN 1025..1041
FT /note="Missing: Does not localize to the nuclear envelope
FT of hyp7 hypodermal precursor cells."
FT /evidence="ECO:0000269|PubMed:16481402"
FT MUTAGEN 1034
FT /note="Y->A: Localizes normally to the nuclear envelope of
FT hyp7 hypodermal precursor cells and interacts with unc-84,
FT however hyp7 hypodermal precursor cells exhibit failed
FT nuclear migration."
FT /evidence="ECO:0000269|PubMed:16481402"
FT MUTAGEN 1038..1039
FT /note="PP->AA: Localizes normally to the nuclear envelope
FT of hyp7 hypodermal precursor cells, however hyp7 hypodermal
FT precursor cells exhibit failed nuclear migration."
FT /evidence="ECO:0000269|PubMed:16481402"
FT MUTAGEN 1038
FT /note="P->A: Localizes normally to the nuclear envelope of
FT hyp7 hypodermal precursor cells, however hyp7 hypodermal
FT precursor cells exhibit failed nuclear migration. Rescues
FT the nuclear migration defect in hyp7 hypodermal precursor
FT cells in the null mutant."
FT /evidence="ECO:0000269|PubMed:16481402"
FT MUTAGEN 1039
FT /note="P->A: Localizes normally to the nuclear envelope of
FT hyp7 hypodermal precursor cells, however hyp7 hypodermal
FT precursor cells exhibit failed nuclear migration. Rescues
FT the nuclear migration defect in hyp7 hypodermal precursor
FT cells in the null mutant."
FT /evidence="ECO:0000269|PubMed:16481402"
FT MUTAGEN 1040
FT /note="P->A: Localizes normally to the nuclear envelope of
FT hyp7 hypodermal precursor cells and interacts with unc-84,
FT however hyp7 hypodermal precursor cells exhibit failed
FT nuclear migration. Rescues the nuclear migration defect in
FT hyp7 hypodermal precursor cells in the null mutant."
FT /evidence="ECO:0000269|PubMed:16481402"
SQ SEQUENCE 1041 AA; 117821 MW; BB403A9A7C41A01F CRC64;
MDVMDSFSEV EMPNDISSED HLLKVIESSA EEVDIFLENC SSLYNLILDS LHNLTSKTIS
CECLDEMTST LEKSAKKILA ERPEAENSVL LRLNTICCAM DQLRVQHNSR MMSGADSDTA
SSARSSTSSS TGEMRLWLHE VERRLEINEK RIRVEPNLQL LLSDQQALQL EIQHEGQLLV
NRLNKQIKDD HDSDSSEEEK RKTCVDAIRK RWHTIYLNSL SLVCRIEELI NHQQASEDSE
SDPDLVGPPI KRARIRTVGH LTASDTEESE ADEEDRHSQT ETVVTEDDNV LPFAENEYES
IMDGRVTVDS CTSSSEDQMV EQSTNKKWES VLQDVGYSSG ENSIHEALNT CADHLVPETS
DMRRKRIECS PVKAFYRTVQ LEDMSDLEVT KAINHDVEEE PNLSDSMYVN HDSTFLATQN
LPEYDEVMAL MDDDDLPMDM SMTESFNTKW REIHGQKKPL RRASRPSREQ MNLIAKSSCD
ASSEDSSEGE NQTNLEDDPE MMSVSFNSAQ FDTSSPLKRQ RSARGLKNAS FLYDSLEMDG
SFCSTRSEML PPCKTRSLAR RKLRVRRMPR SMSDGEQLGV VSSKPEGMMT PMIRVSPPST
PVRRLLRKLD EQIRNRDSDT APEHSDAAQA YEWDEYNPPQ KDDSISDRHI QTMTDISDQL
MNIDDDFAEH FGTSSAIRLI EESKSHLRVV LKALEESDSN IPQLSNFELI ARSNLRQVDE
ALKIQSGNQP SFLETSTLQD LRSEWANLYE SIRSPFARIM HQVKKFAATL QEVSSMASLG
DVDIRSKEDV AKTLDAVTAI ERRLSSERQE LRDLLASSSF RDVAKDLSCE FESVSEGYDD
AVDKIGKMAH SLSQVKGEWD AWNSRQNDIR NAMVRIESHL KEGQMDNKMI ADEMELCQER
MNSLETMCNY LTASLGSIQN ESNSKNLPDF KAELSIYSNA LARLKDRFND MIRVPTPPTV
QFHPPEPLPS LARSMTTQTA EMESETENEP LTIAEAISSS RLIKFTFALS LLAALAAIFY
YHVFGKPFGP HVTYVNGPPP V
