NAT8B_HUMAN
ID NAT8B_HUMAN Reviewed; 227 AA.
AC Q9UHF3; Q0VAD9; Q6NT18;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Putative N-acetyltransferase 8B;
DE EC=2.3.1.-;
DE AltName: Full=Acetyltransferase 1;
DE Short=ATase1;
DE AltName: Full=Camello-like protein 2;
GN Name=NAT8B {ECO:0000312|HGNC:HGNC:30235};
GN Synonyms=CML2 {ECO:0000312|EMBL:AAF22299.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1] {ECO:0000312|EMBL:AAF22299.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Colon tumor {ECO:0000312|EMBL:AAF22299.1};
RX PubMed=11397015; DOI=10.1006/dbio.2001.0261;
RA Popsueva A.E., Luchinskaya N.N., Ludwig A.V., Zinovjeva O.Y.,
RA Poteryaev D.A., Feigelman M.M., Ponomarev M.B., Berekelya L.,
RA Belyavsky A.V.;
RT "Overexpression of camello, a member of a novel protein family, reduces
RT blastomere adhesion and inhibits gastrulation in Xenopus laevis.";
RL Dev. Biol. 234:483-496(2001).
RN [2] {ECO:0000305}
RP POLYMORPHISM.
RX PubMed=16395595; DOI=10.1007/s00439-005-0125-6;
RA Hahn Y., Lee B.;
RT "Human-specific nonsense mutations identified by genome sequence
RT comparisons.";
RL Hum. Genet. 119:169-178(2006).
RN [3]
RP FUNCTION, INTERACTION WITH BACE1, SUBCELLULAR LOCATION, AND INDUCTION BY
RP CERAMIDES.
RX PubMed=19011241; DOI=10.1074/jbc.m804901200;
RA Ko M.H., Puglielli L.;
RT "Two endoplasmic reticulum (ER)/ER Golgi intermediate compartment-based
RT lysine acetyltransferases post-translationally regulate BACE1 levels.";
RL J. Biol. Chem. 284:2482-2492(2009).
RN [4]
RP FUNCTION, INTERACTION WITH PROM1, AND SUBCELLULAR LOCATION.
RX PubMed=24556617; DOI=10.1016/j.jmb.2014.02.012;
RA Mak A.B., Pehar M., Nixon A.M., Williams R.A., Uetrecht A.C., Puglielli L.,
RA Moffat J.;
RT "Post-translational regulation of CD133 by ATase1/ATase2-mediated lysine
RT acetylation.";
RL J. Mol. Biol. 426:2175-2182(2014).
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 (PubMed:24556617). May also regulate amyloid beta-
CC peptide secretion through acetylation of BACE1 and the regulation of
CC its expression in neurons (PubMed:19011241).
CC {ECO:0000269|PubMed:19011241, ECO:0000269|PubMed:24556617}.
CC -!- SUBUNIT: Interacts with PROM1. Interacts with BACE1.
CC {ECO:0000269|PubMed:19011241, ECO:0000269|PubMed:24556617}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate
CC compartment membrane; Single-pass type II membrane protein. Endoplasmic
CC reticulum membrane; Single-pass type II membrane protein. Note=Enriched
CC in the Endoplasmic reticulum-Golgi intermediate compartment.
CC -!- INDUCTION: Up-regulated by ceramides. {ECO:0000269|PubMed:19011241}.
CC -!- SIMILARITY: Belongs to the camello family.
CC {ECO:0000269|PubMed:11397015}.
CC -!- CAUTION: Could be the product of a pseudogene. Two nonsense mutations
CC at positions 16 and 168 are found in the reference genome (GRCh38/hg38)
CC and all transcripts except AF185571. However, the existence of the
CC functional NAT8B protein shown here is supported by its detection in
CC human cell lines with a specific antibody and the inhibition of its
CC expression with specific siRNAs (PubMed:24556617).
CC {ECO:0000305|PubMed:24556617}.
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DR EMBL; AF185571; AAF22299.1; -; mRNA.
DR RefSeq; NP_057431.2; NM_016347.2.
DR AlphaFoldDB; Q9UHF3; -.
DR SMR; Q9UHF3; -.
DR BioGRID; 119557; 20.
DR IntAct; Q9UHF3; 1.
DR iPTMnet; Q9UHF3; -.
DR PhosphoSitePlus; Q9UHF3; -.
DR BioMuta; NAT8B; -.
DR MassIVE; Q9UHF3; -.
DR PeptideAtlas; Q9UHF3; -.
DR PRIDE; Q9UHF3; -.
DR ProteomicsDB; 84340; -.
DR DNASU; 51471; -.
DR GeneID; 51471; -.
DR KEGG; hsa:51471; -.
DR CTD; 51471; -.
DR DisGeNET; 51471; -.
DR GeneCards; NAT8B; -.
DR HGNC; HGNC:30235; NAT8B.
DR MIM; 608190; gene.
DR neXtProt; NX_Q9UHF3; -.
DR PharmGKB; PA162396978; -.
DR InParanoid; Q9UHF3; -.
DR PhylomeDB; Q9UHF3; -.
DR BRENDA; 2.3.1.32; 2681.
DR PathwayCommons; Q9UHF3; -.
DR Reactome; R-HSA-977225; Amyloid fiber formation.
DR SignaLink; Q9UHF3; -.
DR BioGRID-ORCS; 51471; 8 hits in 197 CRISPR screens.
DR GenomeRNAi; 51471; -.
DR Pharos; Q9UHF3; Tbio.
DR PRO; PR:Q9UHF3; -.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; Q9UHF3; protein.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0004468; F:lysine N-acetyltransferase activity, acting on acetyl phosphate as donor; IDA:UniProtKB.
DR GO; GO:0008080; F:N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:1990000; P:amyloid fibril formation; TAS:Reactome.
DR GO; GO:0050435; P:amyloid-beta metabolic process; IMP:UniProtKB.
DR GO; GO:0001702; P:gastrulation with mouth forming second; NAS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0018003; P:peptidyl-lysine N6-acetylation; IDA:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP: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..227
FT /note="Putative N-acetyltransferase 8B"
FT /id="PRO_0000284685"
FT TOPO_DOM 1..42
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..63
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..227
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 61..214
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ SEQUENCE 227 AA; 25366 MW; E45FBA89E1E03CB0 CRC64;
MAPYHIRKYQ ESDRKSVVGL LSGGMAEHAP ATFRRLLKLP RTLILLLGGA LALLLVSGSW
ILALVFSLSL LPALWFLAKK PWTRYVDIAL RTDMSDITKS YLSECGSCFW VAESEEKVVG
TVGALPVDDP TLREKRLQLF HLSVDNEHRG QGIAKALVRT VLQFARDQGY SEVVLDTSNI
QLSAMGLYQS LGFKKTGQSF FHVWARLVDL HTVHFIYHLP SAQAGRL
