NAA15_PONAB
ID NAA15_PONAB Reviewed; 866 AA.
AC Q5R4J9;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=N-alpha-acetyltransferase 15, NatA auxiliary subunit;
DE AltName: Full=NMDA receptor-regulated protein 1;
GN Name=NAA15; Synonyms=NARG1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Auxillary subunit of the N-terminal acetyltransferase A
CC (NatA) complex which displays alpha (N-terminal) acetyltransferase
CC activity. The NAT activity may be important for vascular, hematopoietic
CC and neuronal growth and development. Required to control retinal
CC neovascularization in adult ocular endothelial cells. In complex with
CC XRCC6 and XRCC5 (Ku80), up-regulates transcription from the osteocalcin
CC promoter (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the N-terminal acetyltransferase A (NatA) complex
CC composed of NAA10 or probably NAA11 and NAA15 (By similarity).
CC Interacts with XRCC6, NAA50 and XRCC5 (By similarity). Associates with
CC HYPK when in a complex with NAA10 (By similarity). Interaction with
CC HYPK reduces the capacity to interact with NAA50 (By similarity).
CC {ECO:0000250|UniProtKB:Q9BXJ9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Mainly cytoplasmic, nuclear in some cases. {ECO:0000250}.
CC -!- PTM: Cleaved by caspases during apoptosis. {ECO:0000250}.
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DR EMBL; CR861248; CAH93317.1; -; mRNA.
DR RefSeq; NP_001126952.1; NM_001133480.1.
DR AlphaFoldDB; Q5R4J9; -.
DR SMR; Q5R4J9; -.
DR STRING; 9601.ENSPPYP00000016837; -.
DR GeneID; 100173970; -.
DR KEGG; pon:100173970; -.
DR CTD; 80155; -.
DR eggNOG; KOG1156; Eukaryota.
DR InParanoid; Q5R4J9; -.
DR OrthoDB; 792708at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR InterPro; IPR021183; NatA_aux_su.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF12569; NARP1; 1.
DR Pfam; PF13181; TPR_8; 1.
DR PIRSF; PIRSF000422; N-terminal-AcTrfase-A_aux_su; 1.
DR SMART; SM00028; TPR; 5.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 5.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; TPR repeat.
FT CHAIN 1..866
FT /note="N-alpha-acetyltransferase 15, NatA auxiliary
FT subunit"
FT /id="PRO_0000106296"
FT REPEAT 46..79
FT /note="TPR 1"
FT REPEAT 80..113
FT /note="TPR 2"
FT REPEAT 148..184
FT /note="TPR 3"
FT REPEAT 224..257
FT /note="TPR 4"
FT REPEAT 374..407
FT /note="TPR 5"
FT REPEAT 409..441
FT /note="TPR 6"
FT REPEAT 485..522
FT /note="TPR 7"
FT REPEAT 672..705
FT /note="TPR 8"
FT REGION 500..866
FT /note="Interaction with HYPK"
FT /evidence="ECO:0000250"
FT REGION 575..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 262
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXJ9"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXJ9"
FT MOD_RES 537
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXJ9"
FT MOD_RES 588
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXJ9"
FT MOD_RES 735
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXJ9"
FT MOD_RES 756
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXJ9"
FT MOD_RES 855
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXJ9"
FT MOD_RES 856
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXJ9"
SQ SEQUENCE 866 AA; 101352 MW; FB32A1F942A774D8 CRC64;
MPAVSLPPKE NALFKRILRC YEHKQYRNGL KFCKQILSNP KFAEHGETLA MKGLTLNCLG
KKEEAYELVR RGLRNDLKSH VCWHVYGLLQ RSDKKYDEAI KCYRNALKWD KDNLQILRDL
SLLQIQMRDL EGYRETRYQL LQLRPAQRAS WIGYAIAYHL LEDYEMAAKI LEEFRKTQQT
SPDKVDYEYS ELLLYQNQVL REAGLYREAL EHLCTYEKQI CDKLAVEETK GELLLQLCRL
EDAADVYRGL QERNPENWAY YKGLEKALKP ANMLERLKIY EEAWTKYPRG LVPRRLPLNF
LSGEKFKECL DKFLRMNFSK GCPPVFNTLR SLYKDKEKVA IIEELVVGYE TSLKSCRLFN
PNDDGKEEPP TTLLWVQYYL AQHYDKIGQP SIALEYINTA IESTPTLIEL FLVKAKIYKH
AGNIKEAARW MDEAQALDTA DRFINSKCAK YMLKANLIKE AEEMCSKFTR EGTSAVENLN
EMQCMWFQTE CAQAYKAMNK FGEALKKCYE IERHFIEITD DQFDFHTYCM RKITLRSYVD
LLKLEDVLRQ HPFYFKAARI AIEIYLKLHD NPLTDENKEH EADTANMSDK ELKKLRNKQR
RAQKKAQIEE EKKNAEKEKQ QRNQKKKKDD DDEEIGGPKE ELIPEKLAKV ETPLEEAIKF
LTPLKNLVKN KIETHLFAFE IYFRKEKFLL MLQSVKRAFA IDSSHPWLHE CMIRLFNTAV
CESKDLSDTV RTVLKQEMHR LFGATNPKNF NETFLKRNSD SLPHRLSAAK MVYYLDPSSQ
KRAIELATTL DESLTNRNLQ TCMEVLETLY DGSLGDCKEA AEIYRANCHK LFPYALAFMP
PGYEEDMKIT VNGDSSAEAE ELANEI
