ANKL2_CAEEL
ID ANKL2_CAEEL Reviewed; 603 AA.
AC H2KZB2; Q5W7E5;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Ankyrin repeat and LEM domain-containing protein 2 homolog;
DE AltName: Full=LEM domain-containing protein 4-like;
GN Name=lem-4; Synonyms=lem-4l; ORFNames=Y55F3BR.8;
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, SUBCELLULAR LOCATION, INTERACTION WITH BAF-1 AND PROTEIN
RP PHOSPHATASE 2A, AND MUTAGENESIS OF ALA-229.
RX PubMed=22770216; DOI=10.1016/j.cell.2012.04.043;
RA Asencio C., Davidson I.F., Santarella-Mellwig R., Ly-Hartig T.B., Mall M.,
RA Wallenfang M.R., Mattaj I.W., Gorjanacz M.;
RT "Coordination of kinase and phosphatase activities by Lem4 enables nuclear
RT envelope reassembly during mitosis.";
RL Cell 150:122-135(2012).
CC -!- FUNCTION: Involved in mitotic nuclear envelope reassembly by promoting
CC dephosphorylation of baf-1 during mitotic exit. Coordinates the control
CC of baf-1 dephosphorylation by inhibiting VRK1 kinase and promoting
CC dephosphorylation of baf-1 by protein phosphatase 2A (PP2A), thereby
CC facilitating nuclear envelope assembly. It is unclear whether it acts
CC as a real PP2A regulatory subunit or whether it is involved in
CC recruitment of the PP2A complex. {ECO:0000269|PubMed:22770216}.
CC -!- SUBUNIT: Interacts with baf-1. Interacts with protein phosphatase 2A
CC (PP2A) components. {ECO:0000269|PubMed:22770216}.
CC -!- INTERACTION:
CC H2KZB2; Q19848: vrk-1; NbExp=2; IntAct=EBI-6258914, EBI-2414048;
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:22770216};
CC Single-pass membrane protein {ECO:0000269|PubMed:22770216}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=H2KZB2-1; Sequence=Displayed;
CC Name=b;
CC IsoId=H2KZB2-2; Sequence=VSP_044191;
CC -!- SIMILARITY: Belongs to the ANKLE2 family. {ECO:0000305}.
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DR EMBL; FO080861; CCD67295.1; -; Genomic_DNA.
DR EMBL; FO080861; CCD67296.1; -; Genomic_DNA.
DR RefSeq; NP_001023514.1; NM_001028343.2. [H2KZB2-1]
DR RefSeq; NP_001023515.1; NM_001028344.3. [H2KZB2-2]
DR AlphaFoldDB; H2KZB2; -.
DR SMR; H2KZB2; -.
DR BioGRID; 42071; 2.
DR IntAct; H2KZB2; 2.
DR STRING; 6239.Y55F3BR.8a; -.
DR EPD; H2KZB2; -.
DR PaxDb; H2KZB2; -.
DR PeptideAtlas; H2KZB2; -.
DR EnsemblMetazoa; Y55F3BR.8a.1; Y55F3BR.8a.1; WBGene00021945. [H2KZB2-1]
DR EnsemblMetazoa; Y55F3BR.8b.1; Y55F3BR.8b.1; WBGene00021945. [H2KZB2-2]
DR GeneID; 176911; -.
DR KEGG; cel:CELE_Y55F3BR.8; -.
DR UCSC; Y55F3BR.8a; c. elegans.
DR CTD; 176911; -.
DR WormBase; Y55F3BR.8a; CE31657; WBGene00021945; lem-4. [H2KZB2-1]
DR WormBase; Y55F3BR.8b; CE37730; WBGene00021945; lem-4. [H2KZB2-2]
DR eggNOG; ENOG502QQ4Z; Eukaryota.
DR GeneTree; ENSGT00390000016767; -.
DR HOGENOM; CLU_484166_0_0_1; -.
DR InParanoid; H2KZB2; -.
DR OMA; RFNALHI; -.
DR OrthoDB; 567264at2759; -.
DR PhylomeDB; H2KZB2; -.
DR Reactome; R-CEL-2995383; Initiation of Nuclear Envelope (NE) Reformation.
DR PRO; PR:H2KZB2; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00021945; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051721; F:protein phosphatase 2A binding; IDA:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007084; P:mitotic nuclear membrane reassembly; IMP:UniProtKB.
DR GO; GO:0042326; P:negative regulation of phosphorylation; IDA:UniProtKB.
DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; IDA:UniProtKB.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR035007; ANKLE2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR PANTHER; PTHR12349:SF4; PTHR12349:SF4; 2.
DR SMART; SM00248; ANK; 2.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ANK repeat; Cell cycle; Cell division; Membrane;
KW Mitosis; Nucleus; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..603
FT /note="Ankyrin repeat and LEM domain-containing protein 2
FT homolog"
FT /id="PRO_0000419469"
FT TRANSMEM 2..22
FT /note="Helical; Signal-anchor for type III membrane
FT protein"
FT /evidence="ECO:0000255"
FT REPEAT 161..190
FT /note="ANK 1"
FT REPEAT 221..250
FT /note="ANK 2"
FT REGION 446..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..23
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_044191"
FT MUTAGEN 229
FT /note="A->V: In ax475 mutant; temperature-sensitive mutant.
FT No visible phenotype at 16 degrees Celsius. At 25 degrees
FT Celsius embryos die early during development due to defects
FT in nuclear envelope reassembly."
FT /evidence="ECO:0000269|PubMed:22770216"
SQ SEQUENCE 603 AA; 67054 MW; 64AE263FC7673C92 CRC64;
MGRKSAILAV ILAIIYFRSN FSKMSNTPVQ ETEGPVYVAY SMEDMLKSPR DLYKSVKEVA
KFVNSAEGKS MSARFKKFGT PREAMDFLAY GDAPTTPKTV PPVAPTEPNS PFSGVNRIQM
NEFKKYVEKG DMENFLRLVD SNPRFLVNTG GDVASIVMEG FRYNALHIAA KAGQTEIIAK
ILELIQNIDF LIRLYGTGAD DVTLRKINIL DSYLNTPDKG NSDTPLHFAS KFGKIGVVRV
LTENSATDRT LLNKSGKSAL DCAGERYTGE DKDMVQRDIH LAIEGFYVFL HRNPTTGSTQ
LTVSQKPPAT YSTSPTTATV TVSAQAGPFF TEREARDFAK SWQTAGKELK RTDFDKGWER
VGRVLAEQSE AMWRETWHFL GSMELLDLGS EQGLGVLEAF LREKRRGNLR NSEISEISTK
KSIFRRGIHA RKLDFGILDG EKSAEISENL TPDGSDSADD EDDDDIFYDT FSEIPAAAEK
SINDPDDTLG SLTDRFAAIS IFSPLPPPPP PQWSNSPNFD YSEGEDSFAT PPTTPPPTFV
ADDEPCKIDN DLFEVLAQIS SELISKFPLT QDYVQKLGKL TAHDRSTWRP IDSPARCDSR
RKI
