NT8F2_MOUSE
ID NT8F2_MOUSE Reviewed; 238 AA.
AC Q8CHQ9; Q8C7E5; Q9JIY9;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=N-acetyltransferase family 8 member 2 {ECO:0000312|MGI:MGI:2136446};
DE EC=2.3.1.- {ECO:0000305};
DE AltName: Full=Camello-like protein 2 {ECO:0000303|PubMed:11397015};
DE AltName: Full=N-acetyltransferase-like protein CML2 {ECO:0000303|PubMed:11397015};
GN Name=Nat8f2 {ECO:0000312|MGI:MGI:2136446};
GN Synonyms=Cml2 {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:AAF80484.1}
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:BAC34261.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC34261.1};
RC TISSUE=Liver {ECO:0000312|EMBL:BAC34261.1};
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:AAH39773.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH39773.1};
RC TISSUE=Salivary gland {ECO:0000312|EMBL:AAH39773.1};
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=Liver;
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 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-204, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
RN [6]
RP FUNCTION.
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: Probable acetyltransferase (Probable). Has no detectable
CC histone acetyltransferase activity towards histone H3 or H4.
CC {ECO:0000269|PubMed:25123547, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the camello family.
CC {ECO:0000269|PubMed:11397015}.
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DR EMBL; AF163315; AAF80484.1; -; mRNA.
DR EMBL; AK050449; BAC34261.1; -; mRNA.
DR EMBL; BC039773; AAH39773.1; -; mRNA.
DR CCDS; CCDS20302.1; -.
DR RefSeq; NP_444326.2; NM_053096.3.
DR AlphaFoldDB; Q8CHQ9; -.
DR SMR; Q8CHQ9; -.
DR STRING; 10090.ENSMUSP00000044587; -.
DR iPTMnet; Q8CHQ9; -.
DR PhosphoSitePlus; Q8CHQ9; -.
DR jPOST; Q8CHQ9; -.
DR MaxQB; Q8CHQ9; -.
DR PaxDb; Q8CHQ9; -.
DR PeptideAtlas; Q8CHQ9; -.
DR PRIDE; Q8CHQ9; -.
DR ProteomicsDB; 283534; -.
DR DNASU; 93673; -.
DR Ensembl; ENSMUST00000045008; ENSMUSP00000044587; ENSMUSG00000033634.
DR GeneID; 93673; -.
DR KEGG; mmu:93673; -.
DR UCSC; uc009cqi.1; mouse.
DR CTD; 93673; -.
DR MGI; MGI:2136446; Nat8f2.
DR VEuPathDB; HostDB:ENSMUSG00000033634; -.
DR eggNOG; KOG3139; Eukaryota.
DR GeneTree; ENSGT00950000182932; -.
DR HOGENOM; CLU_013985_10_1_1; -.
DR InParanoid; Q8CHQ9; -.
DR OMA; FSIFTYR; -.
DR OrthoDB; 1341682at2759; -.
DR PhylomeDB; Q8CHQ9; -.
DR TreeFam; TF324687; -.
DR BioGRID-ORCS; 93673; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Nat8f2; mouse.
DR PRO; PR:Q8CHQ9; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8CHQ9; protein.
DR Bgee; ENSMUSG00000033634; Expressed in left lobe of liver and 43 other tissues.
DR Genevisible; Q8CHQ9; 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:0047198; F:cysteine-S-conjugate N-acetyltransferase activity; ISO: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:0001702; P:gastrulation with mouth forming second; NAS:UniProtKB.
DR GO; GO:0006749; P:glutathione metabolic process; ISO: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 Acetylation; Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..238
FT /note="N-acetyltransferase family 8 member 2"
FT /id="PRO_0000284688"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 69..212
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT MOD_RES 204
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT CONFLICT 160
FT /note="V -> L (in Ref. 1; AAF80484)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="V -> A (in Ref. 2; BAC34261)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 238 AA; 26424 MW; 40C2D89B2CF507B7 CRC64;
MAAYHIRQYQ EKDHKRVLEL FSSGMKELIP AAIRQMLTLP HSLLLLPGVP VTIVLMSASW
LLATLYSFLF LLCLWLIFWI SCRNYVAKSL QADLADITKS YLNAHGSFWV AESGDQVVGM
VGAQPVKDPP LGKKQMQLFR LSVSSQHRGQ GIAKALVRTV LQFARDQGYS DVVLETGSVQ
HSAQALYQAM GFQKTGQYFV SISKKLMGLS ILQFSYSLPF ASGPGYSGKY LKKGPIPC
