位置:首页 > 蛋白库 > ANKL1_CAEEL
ANKL1_CAEEL
ID   ANKL1_CAEEL             Reviewed;         704 AA.
AC   G5EGA3;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 2.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Ankyrin repeat and LEM domain-containing protein 1 homolog {ECO:0000305};
DE            EC=3.1.-.- {ECO:0000269|PubMed:22383942};
DE   AltName: Full=LEM-domain containing protein 3 {ECO:0000250|UniProtKB:Q8NAG6};
GN   Name=lem-3 {ECO:0000312|WormBase:F42H11.2};
GN   Synonyms=rad-1 {ECO:0000312|WormBase:F42H11.2};
GN   ORFNames=F42H11.2 {ECO:0000312|WormBase:F42H11.2};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN   [1] {ECO:0000312|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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] {ECO:0000305}
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION,
RP   DEVELOPMENTAL STAGE, AND MUTAGENESIS OF LEU-659.
RX   PubMed=22383942; DOI=10.1371/journal.pone.0024555;
RA   Dittrich C.M., Kratz K., Sendoel A., Gruenbaum Y., Jiricny J.,
RA   Hengartner M.O.;
RT   "LEM-3 - a LEM domain containing nuclease involved in the DNA damage
RT   response in C. elegans.";
RL   PLoS ONE 7:E24555-E24555(2012).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND MUTAGENESIS OF
RP   141-PHE--VAL-250; 190-ARG--LYS-704; SER-192; SER-194; TYR-556 AND GLY-558.
RX   PubMed=29463814; DOI=10.1038/s41467-018-03135-w;
RA   Hong Y., Sonneville R., Wang B., Scheidt V., Meier B., Woglar A.,
RA   Demetriou S., Labib K., Jantsch V., Gartner A.;
RT   "LEM-3 is a midbody-tethered DNA nuclease that resolves chromatin bridges
RT   during late mitosis.";
RL   Nat. Commun. 9:728-728(2018).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 190-ARG--LYS-704.
RX   PubMed=29879106; DOI=10.1371/journal.pgen.1007453;
RA   Hong Y., Velkova M., Silva N., Jagut M., Scheidt V., Labib K., Jantsch V.,
RA   Gartner A.;
RT   "The conserved LEM-3/Ankle1 nuclease is involved in the combinatorial
RT   regulation of meiotic recombination repair and chromosome segregation in
RT   Caenorhabditis elegans.";
RL   PLoS Genet. 14:E1007453-E1007453(2018).
CC   -!- FUNCTION: Endonuclease which, in association with baf-1, plays an
CC       essential role during embryogenesis in the DNA repair response
CC       following DNA damage probably by ensuring proper chromosome segregation
CC       (PubMed:22383942). Also required during postembryonic cell divisions
CC       after DNA damage caused by ionizing radiation to ensure normal cell
CC       proliferation (PubMed:22383942). Resolves chromatin bridges in late
CC       mitosis that result from incomplete DNA replication, defective
CC       chromosome condensation or unresolved recombination intermediates
CC       (PubMed:29463814). Together with brc-1, contributes to genome integrity
CC       by resolving mitotic chromatin bridges that result from incomplete
CC       processing of DNA breaks (PubMed:29463814). In parallel to the slx-
CC       1/mus-81 pathway, acts in processing early recombination intermediates
CC       in meiotic prophase I to prevent illegitimate recombination
CC       (PubMed:29879106). Also involved in processing remaining, erroneous
CC       recombination intermediates that persist into the second meiotic
CC       division (PubMed:29879106). {ECO:0000269|PubMed:22383942,
CC       ECO:0000269|PubMed:29463814, ECO:0000269|PubMed:29879106}.
CC   -!- ACTIVITY REGULATION: Inhibited by EDTA. {ECO:0000269|PubMed:22383942}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22383942,
CC       ECO:0000269|PubMed:29463814, ECO:0000269|PubMed:29879106}. Nucleus
CC       {ECO:0000269|PubMed:29879106}. Chromosome
CC       {ECO:0000269|PubMed:29463814}. Midbody {ECO:0000269|PubMed:29463814}.
CC       Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:29463814}.
CC       Note=Localizes to foci-like structures outside the nucleus
CC       (PubMed:22383942, PubMed:29463814, PubMed:29879106). In pachytene,
CC       localizes to foci both in and outside of the nucleus (PubMed:29879106).
CC       Colocalizes with air-2 between dividing nuclei in meiosis II
CC       (PubMed:29879106). In mitosis, localizes to the center of chromatin
CC       bridges that are formed in response to DNA defects (PubMed:29463814).
CC       Forms initially a ring like structure encircling chromatin bridges
CC       between two separated daughter cells until in late telophase, localizes
CC       to the center of chromatin bridges (PubMed:29463814). Colocalizes with
CC       air-2 at the midbody (PubMed:29463814). Midbody localization depends on
CC       the formation of the central spindle and the midbody and on air-2
CC       (PubMed:29463814). Colocalizes with the central spindle component zen-4
CC       at the central spindle (PubMed:29463814). {ECO:0000269|PubMed:22383942,
CC       ECO:0000269|PubMed:29463814, ECO:0000269|PubMed:29879106}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in embryos.
CC       {ECO:0000269|PubMed:22383942, ECO:0000269|PubMed:29463814}.
CC   -!- PTM: Phosphorylated. Phosphorylated during telophase when localized at
CC       the midbody. {ECO:0000269|PubMed:29463814}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BX284601; CAB05722.2; -; Genomic_DNA.
DR   RefSeq; NP_492539.2; NM_060138.3.
DR   AlphaFoldDB; G5EGA3; -.
DR   SMR; G5EGA3; -.
DR   STRING; 6239.F42H11.2; -.
DR   EPD; G5EGA3; -.
DR   PaxDb; G5EGA3; -.
DR   PeptideAtlas; G5EGA3; -.
DR   PRIDE; G5EGA3; -.
DR   EnsemblMetazoa; F42H11.2.1; F42H11.2.1; WBGene00002276.
DR   GeneID; 172792; -.
DR   KEGG; cel:CELE_F42H11.2; -.
DR   CTD; 172792; -.
DR   WormBase; F42H11.2; CE47022; WBGene00002276; lem-3.
DR   eggNOG; KOG0504; Eukaryota.
DR   GeneTree; ENSGT00940000168304; -.
DR   HOGENOM; CLU_391936_0_0_1; -.
DR   InParanoid; G5EGA3; -.
DR   OMA; CYILIDP; -.
DR   OrthoDB; 487558at2759; -.
DR   PRO; PR:G5EGA3; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00002276; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0000793; C:condensed chromosome; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR   GO; GO:1990023; C:mitotic spindle midzone; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR   GO; GO:0051233; C:spindle midzone; IDA:UniProtKB.
DR   GO; GO:0004520; F:endodeoxyribonuclease activity; IDA:WormBase.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR   GO; GO:0072711; P:cellular response to hydroxyurea; IDA:UniProtKB.
DR   GO; GO:0071479; P:cellular response to ionizing radiation; IGI:UniProtKB.
DR   GO; GO:0000737; P:DNA catabolic process, endonucleolytic; IDA:WormBase.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IGI:UniProtKB.
DR   GO; GO:0009792; P:embryo development ending in birth or egg hatching; IGI:UniProtKB.
DR   GO; GO:0000070; P:mitotic sister chromatid segregation; IGI:UniProtKB.
DR   GO; GO:0000003; P:reproduction; IMP:WormBase.
DR   GO; GO:0000712; P:resolution of meiotic recombination intermediates; IGI:UniProtKB.
DR   GO; GO:0009411; P:response to UV; IMP:WormBase.
DR   GO; GO:0010225; P:response to UV-C; IMP:WormBase.
DR   GO; GO:0010165; P:response to X-ray; IMP:WormBase.
DR   Gene3D; 1.10.720.40; -; 1.
DR   Gene3D; 1.25.40.20; -; 1.
DR   InterPro; IPR034998; ANKLE1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR000305; GIY-YIG_endonuc.
DR   InterPro; IPR011015; LEM/LEM-like_dom_sf.
DR   InterPro; IPR003887; LEM_dom.
DR   PANTHER; PTHR46427; PTHR46427; 1.
DR   Pfam; PF13637; Ank_4; 1.
DR   Pfam; PF03020; LEM; 1.
DR   SMART; SM00248; ANK; 2.
DR   SMART; SM00540; LEM; 1.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   SUPFAM; SSF63451; SSF63451; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
DR   PROSITE; PS50164; GIY_YIG; 1.
DR   PROSITE; PS50954; LEM; 1.
PE   1: Evidence at protein level;
KW   ANK repeat; Cell cycle; Cell division; Chromosome; Cytoplasm; Cytoskeleton;
KW   DNA damage; DNA repair; Endonuclease; Hydrolase; Meiosis; Mitosis;
KW   Nuclease; Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..704
FT                   /note="Ankyrin repeat and LEM domain-containing protein 1
FT                   homolog"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000438147"
FT   REPEAT          28..59
FT                   /note="ANK 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          63..93
FT                   /note="ANK 2"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          425..470
FT                   /note="LEM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00313"
FT   DOMAIN          525..635
FT                   /note="GIY-YIG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00977"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          247..293
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          314..358
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          381..421
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        339..358
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        381..405
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        406..421
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         141..250
FT                   /note="Missing: In tm3468; lack of phosphorylation."
FT                   /evidence="ECO:0000269|PubMed:29463814"
FT   MUTAGEN         190..704
FT                   /note="Missing: In mn155; increase of rad-51 foci in
FT                   meiotic prophase and increase in rmh-1 foci in mid
FT                   pachytene. In a RNAi-mediated mcm-7 or capg-1 knockdown,
FT                   unresolved chromatin bridges at the end of cell division
FT                   and reduced embryonic viability."
FT                   /evidence="ECO:0000269|PubMed:29463814,
FT                   ECO:0000269|PubMed:29879106"
FT   MUTAGEN         192
FT                   /note="S->A: Increased sensitivity to ionizing radiation,
FT                   decreased localization to the midbody and lack of
FT                   phosphorylation; when associated with Ala-194. In a RNAi-
FT                   mediated capg-1 knockdown, delayed midbody localization and
FT                   persistent chromatin bridge formation; when associated with
FT                   Ala-194."
FT                   /evidence="ECO:0000269|PubMed:29463814"
FT   MUTAGEN         194
FT                   /note="S->A: Increased sensitivity to ionizing radiation,
FT                   decreased localization to the midbody and lack of
FT                   phosphorylation; when associated with Ala-192. In a RNAi-
FT                   mediated capg-1 knockdown, delayed midbody localization and
FT                   persistent chromatin bridge formation; when associated with
FT                   Ala-192."
FT                   /evidence="ECO:0000269|PubMed:29463814"
FT   MUTAGEN         556
FT                   /note="Y->A: Failure to localize to midbodies and
FT                   hypersensitivity to ionizing radiation; when associated
FT                   with Ala-558. In a RNAi-mediated capg-1 knockdown,
FT                   excessive and persistent chromatin-bridge formation; when
FT                   associated with Ala-558."
FT                   /evidence="ECO:0000269|PubMed:29463814"
FT   MUTAGEN         558
FT                   /note="G->A: Failure to localize to midbodies and
FT                   hypersensitivity to ionizing radiation; when associated
FT                   with Ala-556. In a RNAi-mediated capg-1 knockdown,
FT                   excessive and persistent chromatin-bridge formation; when
FT                   associated with Ala-556."
FT                   /evidence="ECO:0000269|PubMed:29463814"
FT   MUTAGEN         659
FT                   /note="L->F: In op444; severe reduction in endonucleolytic
FT                   activity. Severe embryonic lethality of progeny of adults
FT                   treated with X-ray, UV-C light or cisplatin characterized
FT                   by chromosome mis-segregation and formation of anaphase
FT                   bridges. Irradiated L1 larvae are uncoordinated and have a
FT                   protruding vulva. In germline cells, cell cycle arrest and
FT                   apoptosis following DNA damage are not affected. In
FT                   addition, progeny of non-irradiated adults die at the
FT                   embryonic stage in a baf-1 and unc-32 mutant background."
FT                   /evidence="ECO:0000269|PubMed:22383942"
SQ   SEQUENCE   704 AA;  78240 MW;  1B108403842BA56D CRC64;
     MPPNGAITTT PRSRMPPTTP SSGKSRPKKE TLHYLAASSS TTSVDAARTL LERGANVNAI
     DRDGATPLHY ACTHDNVAMA QLLLTFGADP MSADKLGRTA YSIAKGNTLR FLRRYKKSSN
     RQRLGFFRRF FACHSRNETF FIVRNNQEVA PLRPTALAEA ASISFNRGNV LTNSYRCAKK
     KIRATFHAIR RSRSNSTATL QDVVLTSEGI RTVTTPSRRA PKATVYAKRS MSVSDLLLIP
     DRRDIKNEDV KTRGSPVKKT RGTGRSRTPE AILNPRKQRT PVNHHKRSKS QETKLVAMPS
     PNSMAYYNTS RARNAGLRPA PSAPPLSPEP AIAAVKTPKT PTTPKTSKGR SKSPANTTAY
     FTADESLELL GNNMEKLNIE SKSAKSSKLK TPSKPTTSSS TSFSSAEDDK EAEVSTPTTV
     DDGEIRKIRR LREGELKSEL KKFGISPAGP LDARTRRLYE KKLLIERRKI TNRGYSPDAD
     VVSCRNSPQL ELVLRNGFLP ADFASRARKC DENVRSEFSG NGFGYNAFCY LIMDPRILGS
     NVENLTLETF VRSIFYVGKG SKNRPLAHFI DARNERRDKL DKLKTCEKLK TIDELWTLGF
     GIPRHEISHG VSDEEAFVRE ASIIEAVKLK NLRNKKAGEF HGTTKSWDNI TKSEYGTFLL
     DRALSTLKLE GIRLITEDNL PDSLYPYVNN RRGAGGGRTP KTPK
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024