ID   NAA35_MOUSE             Reviewed;         725 AA.
AC   Q6PHQ8; Q05CD3; Q8BYJ9; Q8K3H2;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=N-alpha-acetyltransferase 35, NatC auxiliary subunit;
DE   AltName: Full=Embryonic growth-associated protein;
DE   AltName: Full=Protein MAK10 homolog;
GN   Name=Naa35; Synonyms=Egap, Mak10;
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 [MRNA], SUBCELLULAR LOCATION, INTERACTION WITH NAA38,
RP   AND FUNCTION IN CELL PROLIFERATION.
RX   PubMed=16484612; DOI=10.1161/01.res.0000214539.86593.7a;
RA   Wenzlau J.M., Garl P.J., Simpson P., Stenmark K.R., West J., Artinger K.B.,
RA   Nemenoff R.A., Weiser-Evans M.C.M.;
RT   "Embryonic growth-associated protein is one subunit of a novel N-terminal
RT   acetyltransferase complex essential for embryonic vascular development.";
RL   Circ. Res. 98:846-855(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary tumor;
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=Heart, Liver, Lung, Spleen, and Testis;
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).
CC   -!- FUNCTION: Auxillary component of the N-terminal acetyltransferase C
CC       (NatC) complex which catalyzes acetylation of N-terminal methionine
CC       residues. Involved in regulation of apoptosis and proliferation of
CC       smooth muscle cells. {ECO:0000269|PubMed:16484612}.
CC   -!- SUBUNIT: Component of the N-terminal acetyltransferase C (NatC)
CC       complex, which is composed of NAA35, NAA38 and NAA30.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16484612}.
CC   -!- SIMILARITY: Belongs to the MAK10 family. {ECO:0000305}.
CC   -!- CAUTION: PubMed:16484612 decribes a Naa35/Egap-containing complex as
CC       evolutionary conserved NatC complex; however, the mMak3 protein
CC       investigated in this context corresponds to mammalian NAA50 and not
CC       NAA30 and its interaction with NAA35 is ambiguous. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH27201.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR   EMBL; AY102701; AAM52342.1; -; mRNA.
DR   EMBL; AK039316; BAC30316.1; -; mRNA.
DR   EMBL; BC027201; AAH27201.1; ALT_SEQ; mRNA.
DR   EMBL; BC056435; AAH56435.1; -; mRNA.
DR   CCDS; CCDS26575.1; -.
DR   RefSeq; NP_084429.2; NM_030153.2.
DR   RefSeq; XP_006517522.1; XM_006517459.3.
DR   AlphaFoldDB; Q6PHQ8; -.
DR   SMR; Q6PHQ8; -.
DR   BioGRID; 219570; 5.
DR   IntAct; Q6PHQ8; 1.
DR   MINT; Q6PHQ8; -.
DR   STRING; 10090.ENSMUSP00000022038; -.
DR   iPTMnet; Q6PHQ8; -.
DR   PhosphoSitePlus; Q6PHQ8; -.
DR   EPD; Q6PHQ8; -.
DR   MaxQB; Q6PHQ8; -.
DR   PaxDb; Q6PHQ8; -.
DR   PeptideAtlas; Q6PHQ8; -.
DR   PRIDE; Q6PHQ8; -.
DR   ProteomicsDB; 287554; -.
DR   Antibodypedia; 13206; 102 antibodies from 21 providers.
DR   DNASU; 78689; -.
DR   Ensembl; ENSMUST00000022038; ENSMUSP00000022038; ENSMUSG00000021555.
DR   GeneID; 78689; -.
DR   KEGG; mmu:78689; -.
DR   UCSC; uc007quu.2; mouse.
DR   CTD; 60560; -.
DR   MGI; MGI:1925939; Naa35.
DR   VEuPathDB; HostDB:ENSMUSG00000021555; -.
DR   eggNOG; KOG2343; Eukaryota.
DR   GeneTree; ENSGT00390000002445; -.
DR   HOGENOM; CLU_011757_1_1_1; -.
DR   InParanoid; Q6PHQ8; -.
DR   OMA; ACLNRCR; -.
DR   OrthoDB; 1370304at2759; -.
DR   PhylomeDB; Q6PHQ8; -.
DR   TreeFam; TF320627; -.
DR   BioGRID-ORCS; 78689; 23 hits in 76 CRISPR screens.
DR   ChiTaRS; Naa35; mouse.
DR   PRO; PR:Q6PHQ8; -.
DR   Proteomes; UP000000589; Chromosome 13.
DR   RNAct; Q6PHQ8; protein.
DR   Bgee; ENSMUSG00000021555; Expressed in spermatocyte and 273 other tissues.
DR   ExpressionAtlas; Q6PHQ8; baseline and differential.
DR   Genevisible; Q6PHQ8; MM.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0031417; C:NatC complex; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0005844; C:polysome; ISO:MGI.
DR   GO; GO:0017196; P:N-terminal peptidyl-methionine acetylation; IEA:InterPro.
DR   GO; GO:0006474; P:N-terminal protein amino acid acetylation; IBA:GO_Central.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR   GO; GO:0048659; P:smooth muscle cell proliferation; IMP:UniProtKB.
DR   InterPro; IPR007244; Naa35/Mak10.
DR   PANTHER; PTHR21373; PTHR21373; 1.
DR   Pfam; PF04112; Mak10; 2.
PE   1: Evidence at protein level;
KW   Cytoplasm; Phosphoprotein; Reference proteome.
FT   CHAIN           1..725
FT                   /note="N-alpha-acetyltransferase 35, NatC auxiliary
FT                   subunit"
FT                   /id="PRO_0000308616"
FT   REGION          548..573
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         187
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VZE5"
FT   CONFLICT        246
FT                   /note="V -> L (in Ref. 1; AAM52342)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        608
FT                   /note="E -> G (in Ref. 2; BAC30316)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        666
FT                   /note="A -> T (in Ref. 1; AAM52342)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   725 AA;  83306 MW;  5362E77747B5F248 CRC64;
     MVMKATVDDD ASGWELGVPE KMEKSSTSWV DITQDFEDAC RELKLGELLH DKLFGLFEAM
     SAIEMMDPKM DAGMIGNQVN RKVLNFEQAI KDGTIKIKDL SLPELIGIMD TCFCCLITWL
     EGHSLAQTVF TCLYIHNPDF IEDPAMKAFA LGILKICDIA REKVNKAAVF EEEDFQSMTY
     GFKMANSVTD LRVTGMLKDV EDDLQRRVKS TRSRQGEERD PEVELEHQQC LAAFSRVKFT
     RVLLTVLIAF TKKETSAVAE AQKLMVQAAD LLSAIHTSLH HGIQAQNGTT KGDHPIMMGF
     EPLVNQRLLP PTFPRYAKII KREEMVNYFS RLIDRIKTVC EVVNLPNLHC ILDFFCEFSE
     QSPCVLSRSL LQTTFLVDNK KVFGTHLMQD MVKDALRSFV SPPVLSPKCC LYNNHQAKDC
     IDSFVTHCVR PFCSLVQIHG HNRARQRDKL GHILEEFATL QDEAEKVDAA LHTMLLKQEP
     QRQHLACLGT WVLYHNLRIM IQYLLSGFEL ELYSMHEYYY IYWYLSEFLY AWLMSTLSRA
     DGSQMAEERI MEEQQKGRSS KKTKKKKKVR PLSREITMSQ AYQNMCAGMF KTMVAFDMDG
     KVRKPKFELD SEQVRYEHRF APFNSVMTPP PVHYLQFKEM SDLNKYSPPP QSPELYVAAS
     KHFQQAKMIL ENIPNPDREV SRILKVAKPN FVVMKLLAGG HKKESKVPPE FDFSVHKYFP
     VVKLV