NAA25_CAEEL
ID NAA25_CAEEL Reviewed; 958 AA.
AC Q21986;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-2002, sequence version 3.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=N-terminal acetyltransferase B complex subunit NAA25 homolog {ECO:0000250|UniProtKB:Q14CX7};
DE AltName: Full=Central region assembly in meiosis abnormal protein 1 {ECO:0000312|WormBase:R13F6.10};
DE AltName: Full=N-terminal acetyltransferase B complex subunit MDM20 homolog {ECO:0000250|UniProtKB:Q14CX7};
GN Name=cra-1 {ECO:0000312|WormBase:R13F6.10};
GN ORFNames=R13F6.10 {ECO:0000312|WormBase:R13F6.10};
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 DISRUPTION PHENOTYPE.
RX PubMed=18535664; DOI=10.1371/journal.pgen.1000088;
RA Smolikov S., Schild-Prufert K., Colaiacovo M.P.;
RT "CRA-1 uncovers a double-strand break-dependent pathway promoting the
RT assembly of central region proteins on chromosome axes during C. elegans
RT meiosis.";
RL PLoS Genet. 4:E1000088-E1000088(2008).
RN [3]
RP FUNCTION, INTERACTION WITH ACER-1, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=25768301; DOI=10.1371/journal.pgen.1005029;
RA Gao J., Kim H.M., Elia A.E., Elledge S.J., Colaiacovo M.P.;
RT "NatB domain-containing cra-1 antagonizes hydrolase acer-1 linking acetyl-
RT CoA metabolism to the initiation of recombination during C. elegans
RT meiosis.";
RL PLoS Genet. 11:E1005029-E1005029(2015).
CC -!- FUNCTION: Non-catalytic subunit of the NatB complex which catalyzes
CC acetylation of the N-terminal methionine residues of proteins beginning
CC with Met-Asp or Met-Glu (By similarity). Required for chromosome
CC organization and arrangement; specifically for assembly of the central
CC region components of the synaptonemal complex onto chromosomes during
CC meiosis and for DNA double stranded break formation and repair
CC (PubMed:18535664, PubMed:25768301). Acts downstream of xnd-1 to
CC regulate levels of histone acetylation in germ and somatic cell nuclei
CC by controlling acetyl-CoA production through antagonizing the acetyl-
CC CoA hydrolase activity of acer-1 (PubMed:25768301).
CC {ECO:0000250|UniProtKB:Q14CX7, ECO:0000269|PubMed:18535664,
CC ECO:0000269|PubMed:25768301}.
CC -!- SUBUNIT: Component of the N-terminal acetyltransferase B (NatB) complex
CC (By similarity). Interacts with acer-1 (PubMed:25768301).
CC {ECO:0000250|UniProtKB:Q14CX7, ECO:0000269|PubMed:25768301}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14CX7}. Nucleus
CC {ECO:0000269|PubMed:25768301}. Chromosome
CC {ECO:0000269|PubMed:25768301}. Note=Localizes to meiotic germline
CC nuclei where it is first expressed in early prophase nuclei with
CC expression increasing as nuclei progress into the pachytene stage.
CC Expressed from interphase to prophase and at low levels from
CC prometaphase to anaphase in mitotic nuclei. Highly expressed on
CC autosomes during early to mid prophase. {ECO:0000269|PubMed:25768301}.
CC -!- TISSUE SPECIFICITY: Expressed in germline and somatic cells.
CC {ECO:0000269|PubMed:25768301}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryo and adult.
CC {ECO:0000269|PubMed:25768301}.
CC -!- DISRUPTION PHENOTYPE: High embryonic and larval lethality with viable
CC progeny displaying a high incidence of males phenotype
CC (PubMed:18535664, PubMed:25768301). Defective chromosomal
CC morphogenesis, segregation and alignment due to the failure of central
CC region components of the synaptonemal complex to assemble onto
CC chromosomes during meiosis (PubMed:18535664). Severe chromosomal and
CC meiotic defects include a delay in chromosome dispersal upon entry into
CC the pachytene stage; impaired stability of homologous pairing
CC interactions resulting in a failure to form chiasmata for crossover
CC recombination, and increased DNA double strand break repair upon entry
CC into and throughout the pachytene stage of meiosis possibly resulting
CC in impaired meiotic recombination (PubMed:18535664). Germ cell defects
CC resulting in increased germ cell apoptosis (PubMed:18535664). Decreased
CC histone acetylation in meiotic germ cell nuclei from the premeiotic tip
CC to the late pachytene stage with the most prominent decrease upon
CC meiotic entry and during the pachytene stages (PubMed:25768301).
CC Decreased acetyl-CoA production (PubMed:25768301). RNAi-mediated
CC knockdown results in reduced histone H2AK5 acetylation
CC (PubMed:25768301). {ECO:0000269|PubMed:18535664,
CC ECO:0000269|PubMed:25768301}.
CC -!- SIMILARITY: Belongs to the MDM20/NAA25 family. {ECO:0000305}.
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DR EMBL; FO081247; CCD70181.1; -; Genomic_DNA.
DR PIR; T16751; T16751.
DR RefSeq; NP_498494.2; NM_066093.4.
DR AlphaFoldDB; Q21986; -.
DR SMR; Q21986; -.
DR BioGRID; 41171; 34.
DR IntAct; Q21986; 1.
DR MINT; Q21986; -.
DR STRING; 6239.R13F6.10; -.
DR EPD; Q21986; -.
DR PaxDb; Q21986; -.
DR PeptideAtlas; Q21986; -.
DR EnsemblMetazoa; R13F6.10.1; R13F6.10.1; WBGene00020068.
DR GeneID; 175956; -.
DR KEGG; cel:CELE_R13F6.10; -.
DR UCSC; R13F6.10; c. elegans.
DR CTD; 175956; -.
DR WormBase; R13F6.10; CE31579; WBGene00020068; cra-1.
DR eggNOG; KOG2053; Eukaryota.
DR GeneTree; ENSGT00950000183174; -.
DR HOGENOM; CLU_008075_0_0_1; -.
DR InParanoid; Q21986; -.
DR OMA; CMASSIL; -.
DR OrthoDB; 1022953at2759; -.
DR PhylomeDB; Q21986; -.
DR PRO; PR:Q21986; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00020068; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031416; C:NatB complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0017196; P:N-terminal peptidyl-methionine acetylation; IBA:GO_Central.
DR InterPro; IPR019183; N-acetylTrfase_B_cplx_non-cat.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR22767:SF3; PTHR22767:SF3; 1.
DR Pfam; PF09797; NatB_MDM20; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
PE 1: Evidence at protein level;
KW Chromosome; Chromosome partition; Cytoplasm; DNA damage; DNA recombination;
KW DNA repair; Meiosis; Nucleus; Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..958
FT /note="N-terminal acetyltransferase B complex subunit NAA25
FT homolog"
FT /evidence="ECO:0000305"
FT /id="PRO_0000106422"
FT REPEAT 7..42
FT /note="TPR 1"
FT /evidence="ECO:0000255"
FT REPEAT 78..111
FT /note="TPR 2"
FT /evidence="ECO:0000255"
FT REPEAT 320..353
FT /note="TPR 3"
FT /evidence="ECO:0000255"
SQ SEQUENCE 958 AA; 109226 MW; F850BD980A384D11 CRC64;
MSKAELAVLE RRLRPIYDSL DSQQFKKALS DCDKVLKKHP NTSAAKVLKA LTLIRLEKLA
DATEILEALD VPGAHHDELT LQAFVHCYRD SNQHMKVVTL YERIIQVDPS EHNLTQLFMA
YSREKMYKEQ QKIGMRLYKD FGNAPYYFWS VMSLIMQAQE NPELGKKMLL PLADKMCQTQ
VEKSGYTEGS SAELDLQLLI LEGQEKWKEC AAFLDRPQAS VLPMAPYNLV EKGMDFLMKD
KQYKRVDQLA MEAVTKMPDN WNLWKIITES TICQIEQCLE SDNKENIELA HNFVKRLGLL
IEKVQKQVGY KSRAPFIATF FAYKQIGKLT KQIPDMDDMT SIFGEQVDKM LEYAKNFYKK
PVCFADLQMF FCDLTSEQKS NFLKGIDLWI GEVSAKDDVE GDESKVWAII LTERCRRALG
EYEKMDAAGH RSLFQQCIAQ IAAPERTEHA QGVLCNLTVS HLWDAYRKEN DLTKFYEMIL
LLEFVAASNK TDPMCKLALI RAYSALCATG RISALVKTLD IKVIQMDTLG HLTFPVYETS
GRFNLAIIQN TQLSLMYEQA EKEIQDCIAQ AYRNGKFSAI PRMTAASKHM KLSAQKTACD
VMNRYLSSLF VLDDVDQITV TLWGDEDPIG EKRIDWKQLI DTRDFNAIPY TETEEYEALL
DDMKKRTFKE LIDISELRST LCRALGAVGR VTHENMEPRL ARLQLKMTVM EFKQHLEYCC
REYPSFLIPS KLAQSPAPHH LSQWVHSGGL QMVLEYLEAA VKLVDILDSG EHPEKSLVGT
RTEMATKLIK LIEIPPKRKE GEKLPPFWIV DPIIKSSRAL QTIAAIQVVL RLIEKVVLKL
VKNVPTAVPE PVGKGKGKKD KKAAEEAMTK ALDECKAVVF LEHIRAMHVE LRSAGNFLHT
YLGQMLALED EYIPSNIGED LGGAKAALEG MHNPVASRLQ RSFLNTCEDM HTTIKLRF
