NT8F3_MOUSE
ID NT8F3_MOUSE Reviewed; 226 AA.
AC Q9JIY8; Q8BQW2; Q91WM7;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=N-acetyltransferase family 8 member 3 {ECO:0000312|MGI:MGI:2136449};
DE EC=2.3.1.48 {ECO:0000269|PubMed:25123547};
DE AltName: Full=Camello-like protein 3 {ECO:0000303|PubMed:11397015};
DE AltName: Full=N-acetyltransferase CML3 {ECO:0000303|PubMed:11397015};
GN Name=Nat8f3 {ECO:0000312|MGI:MGI:2136449};
GN Synonyms=Cml3 {ECO:0000303|PubMed:11397015};
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] {ECO:0000312|EMBL:AAF80485.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
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:0000312|EMBL:BAC32679.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC32679.1};
RC TISSUE=Corpora quadrigemina {ECO:0000312|EMBL:BAC32679.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3] {ECO:0000312|EMBL:AAH14696.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH14696.1};
RC TISSUE=Kidney {ECO:0000312|EMBL:AAH14696.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=25123547; DOI=10.1038/srep06076;
RA Karmodiya K., Anamika K., Muley V., Pradhan S.J., Bhide Y., Galande S.;
RT "Camello, a novel family of Histone Acetyltransferases that acetylate
RT histone H4 and is essential for zebrafish development.";
RL Sci. Rep. 4:6076-6076(2014).
CC -!- FUNCTION: Has histone acetyltransferase activity in vitro, with
CC specificity for histone H4. {ECO:0000269|PubMed:25123547}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC Evidence={ECO:0000269|PubMed:25123547};
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000305|PubMed:25123547};
CC Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear
CC region {ECO:0000305|PubMed:25123547}. Cytoplasm
CC {ECO:0000305|PubMed:25123547}. Note=C-terminally tagged constructs
CC localize to the nuclear membrane and perinuclear region. N-terminally
CC tagged constructs show a punctate cytoplasmic distribution.
CC {ECO:0000269|PubMed:25123547}.
CC -!- SIMILARITY: Belongs to the camello family. {ECO:0000305}.
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DR EMBL; AF163316; AAF80485.1; -; mRNA.
DR EMBL; AK046314; BAC32679.1; -; mRNA.
DR EMBL; BC014696; AAH14696.1; -; mRNA.
DR EMBL; BC092089; AAH92089.1; -; mRNA.
DR RefSeq; NP_001032931.1; NM_001037842.3.
DR RefSeq; NP_001188318.1; NM_001201389.1.
DR RefSeq; XP_017177330.1; XM_017321841.1.
DR AlphaFoldDB; Q9JIY8; -.
DR SMR; Q9JIY8; -.
DR STRING; 10090.ENSMUSP00000084938; -.
DR iPTMnet; Q9JIY8; -.
DR PhosphoSitePlus; Q9JIY8; -.
DR jPOST; Q9JIY8; -.
DR MaxQB; Q9JIY8; -.
DR PaxDb; Q9JIY8; -.
DR PeptideAtlas; Q9JIY8; -.
DR PRIDE; Q9JIY8; -.
DR DNASU; 93674; -.
DR Ensembl; ENSMUST00000087656; ENSMUSP00000084938; ENSMUSG00000079495.
DR Ensembl; ENSMUST00000174143; ENSMUSP00000133846; ENSMUSG00000079495.
DR GeneID; 100504710; -.
DR GeneID; 93674; -.
DR KEGG; mmu:100504710; -.
DR KEGG; mmu:93674; -.
DR UCSC; uc009cqc.3; mouse.
DR CTD; 100504710; -.
DR CTD; 93674; -.
DR MGI; MGI:2136449; Nat8f3.
DR VEuPathDB; HostDB:ENSMUSG00000079495; -.
DR eggNOG; KOG3139; Eukaryota.
DR GeneTree; ENSGT00950000182932; -.
DR HOGENOM; CLU_013985_10_1_1; -.
DR InParanoid; Q9JIY8; -.
DR OMA; WILAGCC; -.
DR OrthoDB; 1341682at2759; -.
DR PhylomeDB; Q9JIY8; -.
DR TreeFam; TF324687; -.
DR BioGRID-ORCS; 100504710; 1 hit in 56 CRISPR screens.
DR BioGRID-ORCS; 93674; 3 hits in 33 CRISPR screens.
DR ChiTaRS; Nat8f3; mouse.
DR PRO; PR:Q9JIY8; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9JIY8; protein.
DR Bgee; ENSMUSG00000079495; Expressed in proximal tubule and 29 other tissues.
DR Genevisible; Q9JIY8; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISO:MGI.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISA:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0031965; C:nuclear membrane; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0047198; F:cysteine-S-conjugate N-acetyltransferase activity; ISO:MGI.
DR GO; GO:0010485; F:H4 histone acetyltransferase activity; IDA:MGI.
DR GO; GO:0004468; F:lysine N-acetyltransferase activity, acting on acetyl phosphate as donor; ISO:MGI.
DR GO; GO:0008080; F:N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0050435; P:amyloid-beta metabolic process; ISO:MGI.
DR GO; GO:0003401; P:axis elongation; ISO:MGI.
DR GO; GO:0001702; P:gastrulation with mouth forming second; NAS:UniProtKB.
DR GO; GO:0006749; P:glutathione metabolic process; ISO:MGI.
DR GO; GO:0016573; P:histone acetylation; IDA:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0007162; P:negative regulation of cell adhesion; ISA:MGI.
DR GO; GO:0018003; P:peptidyl-lysine N6-acetylation; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
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 1: Evidence at protein level;
KW Acyltransferase; Cytoplasm; Membrane; Nucleus; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..226
FT /note="N-acetyltransferase family 8 member 3"
FT /id="PRO_0000284690"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 61..220
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT CONFLICT 11
FT /note="D -> G (in Ref. 2; BAC32679)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="L -> I (in Ref. 3; AAH92089/AAH14696)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="S -> SP (in Ref. 3; AAH92089/AAH14696)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="R -> PW (in Ref. 2; BAC32679)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 226 AA; 25956 MW; D3CAD187E847B5FA CRC64;
MAPYHIRKYQ DSDHRSVVDL FRRGMEEHIP ATFRHMLLLP RTLLLLLGVP LTLFLASGSW
LLVLLSILTL FLSLWFLAKY TWEKHVMNCL HTDMADITRT YLSSHSSCFW VAESRGQTVG
MVAARPVKDP LLQKKQLQLL HLSVSLQHRR EGLGKAMVRT VLQFAQMQGF SEVVLSTSML
QYAALALYQG MGFQKTGETF YTYLSRLRKS PMINLKYSLT SREGDL
