DAF31_CAEEL
ID DAF31_CAEEL Reviewed; 182 AA.
AC O61219;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=N-alpha-acetyltransferase daf-31 {ECO:0000305};
DE EC=2.3.1.255 {ECO:0000250|UniProtKB:P41227};
DE AltName: Full=Abnormal dauer formation protein 31 {ECO:0000312|WormBase:K07H8.3};
GN Name=daf-31 {ECO:0000312|WormBase:K07H8.3};
GN ORFNames=K07H8.3 {ECO:0000312|WormBase:K07H8.3};
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]
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]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=25330189; DOI=10.1371/journal.pgen.1004699;
RA Chen D., Zhang J., Minnerly J., Kaul T., Riddle D.L., Jia K.;
RT "daf-31 encodes the catalytic subunit of N alpha-acetyltransferase that
RT regulates Caenorhabditis elegans development, metabolism and adult
RT lifespan.";
RL PLoS Genet. 10:E1004699-E1004699(2014).
CC -!- FUNCTION: Catalytic subunit of the N-terminal acetyltransferase A
CC (NatA) complex which displays alpha (N-terminal) acetyltransferase
CC activity (By similarity). Plays a role in regulating larval
CC development, metabolism and longevity. Functions downstream or
CC alongside daf-3, daf-12 and daf-16 in the dauer formation pathway.
CC Functions upstream of daf-15 to enable animal development.
CC {ECO:0000250|UniProtKB:P41227, ECO:0000269|PubMed:25330189}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal glycyl-[protein] = CoA + H(+) + N-
CC terminal N(alpha)-acetylglycyl-[protein]; Xref=Rhea:RHEA:50496,
CC Rhea:RHEA-COMP:12666, Rhea:RHEA-COMP:12700, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64723,
CC ChEBI:CHEBI:133369; EC=2.3.1.255;
CC Evidence={ECO:0000250|UniProtKB:P41227};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-alanyl-[protein] = CoA + H(+) + N-
CC terminal N(alpha)-acetyl-L-alanyl-[protein]; Xref=Rhea:RHEA:50500,
CC Rhea:RHEA-COMP:12701, Rhea:RHEA-COMP:12702, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64718,
CC ChEBI:CHEBI:83683; EC=2.3.1.255;
CC Evidence={ECO:0000250|UniProtKB:P41227};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-seryl-[protein] = CoA + H(+) + N-
CC terminal N(alpha)-acetyl-L-seryl-[protein]; Xref=Rhea:RHEA:50504,
CC Rhea:RHEA-COMP:12703, Rhea:RHEA-COMP:12704, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64738,
CC ChEBI:CHEBI:83690; EC=2.3.1.255;
CC Evidence={ECO:0000250|UniProtKB:P41227};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-valyl-[protein] = CoA + H(+) + N-
CC terminal N(alpha)-acetyl-L-valyl-[protein]; Xref=Rhea:RHEA:50508,
CC Rhea:RHEA-COMP:12705, Rhea:RHEA-COMP:12706, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64741,
CC ChEBI:CHEBI:133371; EC=2.3.1.255;
CC Evidence={ECO:0000250|UniProtKB:P41227};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-cysteinyl-[protein] = CoA + H(+) +
CC N-terminal N(alpha)-acetyl-L-cysteinyl-[protein];
CC Xref=Rhea:RHEA:50512, Rhea:RHEA-COMP:12707, Rhea:RHEA-COMP:12708,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:65250, ChEBI:CHEBI:133372; EC=2.3.1.255;
CC Evidence={ECO:0000250|UniProtKB:P41227};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-threonyl-[protein] = CoA + H(+) + N-
CC terminal N(alpha)-acetyl-L-threonyl-[protein]; Xref=Rhea:RHEA:50516,
CC Rhea:RHEA-COMP:12709, Rhea:RHEA-COMP:12710, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64739,
CC ChEBI:CHEBI:133375; EC=2.3.1.255;
CC Evidence={ECO:0000250|UniProtKB:P41227};
CC -!- SUBUNIT: Component of the N-terminal acetyltransferase A (NatA)
CC complex. {ECO:0000250|UniProtKB:P41227}.
CC -!- TISSUE SPECIFICITY: Expressed in head and tail hypodermal cells,
CC hypodermal seam cells, pharynx, intestine and head and tail neurons.
CC {ECO:0000269|PubMed:25330189}.
CC -!- DEVELOPMENTAL STAGE: Expressed from larval stage L1 to adulthood.
CC {ECO:0000269|PubMed:25330189}.
CC -!- DISRUPTION PHENOTYPE: The majority of animals die within five days
CC following dauer-like arrest, but surviving animals grow to the L4
CC larval developmental stage or adulthood. Animals display a dauer-like
CC phenotype in response to pheromone and starvation, form dauer alae and
CC have a constricted pharynx. Unlike dauer defective animals, these
CC animals are not temperature sensitive and do not complete dauer
CC morphogenesis. Animals have an increased propensity to accumulate fat.
CC RNAi-mediated knock-down also induces a dauer-like phenotype and fat
CC accumulation. However, knock-down does not influence the lifespan of
CC animals. {ECO:0000269|PubMed:25330189}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. ARD1 subfamily.
CC {ECO:0000305}.
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DR EMBL; FO081300; CCD70602.1; -; Genomic_DNA.
DR PIR; T33023; T33023.
DR RefSeq; NP_501392.1; NM_068991.4.
DR AlphaFoldDB; O61219; -.
DR SMR; O61219; -.
DR STRING; 6239.K07H8.3; -.
DR EPD; O61219; -.
DR PaxDb; O61219; -.
DR PeptideAtlas; O61219; -.
DR EnsemblMetazoa; K07H8.3.1; K07H8.3.1; WBGene00000923.
DR GeneID; 177622; -.
DR KEGG; cel:CELE_K07H8.3; -.
DR UCSC; K07H8.3; c. elegans.
DR CTD; 177622; -.
DR WormBase; K07H8.3; CE18023; WBGene00000923; daf-31.
DR eggNOG; KOG3235; Eukaryota.
DR GeneTree; ENSGT00940000174781; -.
DR HOGENOM; CLU_013985_7_2_1; -.
DR InParanoid; O61219; -.
DR OMA; MSMQNAN; -.
DR OrthoDB; 1489230at2759; -.
DR PhylomeDB; O61219; -.
DR BRENDA; 2.3.1.255; 1045.
DR PRO; PR:O61219; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00000923; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0031415; C:NatA complex; ISS:WormBase.
DR GO; GO:0004596; F:peptide alpha-N-acetyltransferase activity; ISS:WormBase.
DR GO; GO:1990190; F:peptide-glutamate-N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:1990189; F:peptide-serine-N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0043054; P:dauer exit; IMP:WormBase.
DR GO; GO:0040024; P:dauer larval development; IMP:WormBase.
DR GO; GO:0008340; P:determination of adult lifespan; IGI:WormBase.
DR GO; GO:0032504; P:multicellular organism reproduction; IMP:WormBase.
DR GO; GO:0006474; P:N-terminal protein amino acid acetylation; ISS:WormBase.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IMP:WormBase.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR045047; Ard1-like.
DR InterPro; IPR000182; GNAT_dom.
DR PANTHER; PTHR23091; PTHR23091; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Reference proteome; Transferase.
FT CHAIN 1..182
FT /note="N-alpha-acetyltransferase daf-31"
FT /id="PRO_0000432622"
FT DOMAIN 1..152
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT REGION 162..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 182 AA; 21163 MW; A431ED91129B44A8 CRC64;
MNIRCARVDD LMSMQNANLM CLPENYQMKY YFYHALSWPQ LSYIAEDHKG NVVGYVLAKM
EEDPGEEPHG HITSLAVKRS YRRLGLANKM MDQTARAMVE TYNAKYVSLH VRVSNRAALN
LYKNTLKFEI VDTEPKYYAD GEDAYAMRRD LAKWAEERNI EPADREAYTT AKTTDDKKKN
RS
