NAT8B_MOUSE
ID NAT8B_MOUSE Reviewed; 232 AA.
AC E0CYC6;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=Putative N-acetyltransferase 8B {ECO:0000305};
DE EC=2.3.1.- {ECO:0000255|PROSITE-ProRule:PRU00532};
DE AltName: Full=Camello-like protein 2 {ECO:0000250|UniProtKB:Q9UHF3};
DE AltName: Full=Putative acetyltransferase 1 {ECO:0000305};
DE Short=ATase1 {ECO:0000303|PubMed:22267734};
GN Name=Nat8b-ps {ECO:0000312|MGI:MGI:3644831};
GN Synonyms=Cml2 {ECO:0000250|UniProtKB:Q9UHF3};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=22267734; DOI=10.1074/jbc.m111.310136;
RA Ding Y., Ko M.H., Pehar M., Kotch F., Peters N.R., Luo Y., Salamat S.M.,
RA Puglielli L.;
RT "Biochemical inhibition of the acetyltransferases ATase1 and ATase2 reduces
RT beta-secretase (BACE1) levels and Abeta generation.";
RL J. Biol. Chem. 287:8424-8433(2012).
CC -!- FUNCTION: May have a lysine N-acetyltransferase activity catalyzing
CC peptidyl-lysine N6-acetylation of various proteins. Thereby, may
CC regulate apoptosis through the acetylation and the regulation of the
CC expression of PROM1. May also regulate amyloid beta-peptide secretion
CC through acetylation of BACE1 and the regulation of its expression in
CC neurons. {ECO:0000250|UniProtKB:Q9UHF3}.
CC -!- SUBUNIT: Interacts with PROM1. Interacts with BACE1.
CC {ECO:0000250|UniProtKB:Q9UHF3}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate
CC compartment membrane {ECO:0000250|UniProtKB:Q9UHF3}; Single-pass type
CC II membrane protein {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9UHF3}; Single-pass type II membrane protein
CC {ECO:0000255}. Note=Enriched in the endoplasmic reticulum-Golgi
CC intermediate compartment. {ECO:0000250|UniProtKB:Q9UHF3}.
CC -!- TISSUE SPECIFICITY: Expressed in brain (at protein level).
CC {ECO:0000269|PubMed:22267734}.
CC -!- SIMILARITY: Belongs to the camello family. {ECO:0000305}.
CC -!- CAUTION: Could be the product of a pseudogene. However an antibody
CC which recognizes both Nat8 and Nat8B detects a product of approximately
CC 27 kDa in brain extracts, which provides some evidence for existence of
CC this protein (PubMed:22267734). {ECO:0000305|PubMed:22267734}.
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DR EMBL; AC158679; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; E0CYC6; -.
DR SMR; E0CYC6; -.
DR STRING; 10090.ENSMUSP00000124315; -.
DR jPOST; E0CYC6; -.
DR MaxQB; E0CYC6; -.
DR PaxDb; E0CYC6; -.
DR PeptideAtlas; E0CYC6; -.
DR PRIDE; E0CYC6; -.
DR ProteomicsDB; 287607; -.
DR MGI; MGI:3644831; Nat8b-ps.
DR eggNOG; KOG3139; Eukaryota.
DR InParanoid; E0CYC6; -.
DR PhylomeDB; E0CYC6; -.
DR TreeFam; TF324687; -.
DR ChiTaRS; Nat8f2; mouse.
DR PRO; PR:E0CYC6; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; E0CYC6; protein.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004468; F:lysine N-acetyltransferase activity, acting on acetyl phosphate as donor; ISS:UniProtKB.
DR GO; GO:0008080; F:N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0050435; P:amyloid-beta metabolic process; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0018003; P:peptidyl-lysine N6-acetylation; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 5: Uncertain;
KW Acyltransferase; Endoplasmic reticulum; Membrane; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..232
FT /note="Putative N-acetyltransferase 8B"
FT /id="PRO_0000416112"
FT TOPO_DOM 1..62
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 84..232
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 79..224
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ SEQUENCE 232 AA; 26389 MW; 1E2B50E66D7A3F59 CRC64;
MPRFEAQKSS MVPYHIRQYQ DSDHKRVVDV FTTGAEEYIP STFRHVLRLP RTFLLLLGVP
LALVLVSGSW ILAVICIFFL LLLLRLLARQ PWKEYVAKCL QTYMVDITKS YLNVHGACFW
VAESGGQVVG IVAAQPVKDP PLGRKQLQLF RLSVSSQHRG QGIAKALTRT VLQFARDQSY
SDVVLETSTL QQGAMTLYLG MGFKKTGQYF KSMFWRLVDI CFIQLNYSFP SA
