NT8F3_RAT
ID NT8F3_RAT Reviewed; 228 AA.
AC Q9QXS4;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=N-acetyltransferase family 8 member 3 {ECO:0000312|RGD:621607};
DE EC=2.3.1.48 {ECO:0000250|UniProtKB:Q9JIY8};
DE AltName: Full=Camello-like protein 3 {ECO:0000312|RGD:621607};
DE AltName: Full=N-acetyltransferase CML3 {ECO:0000312|RGD:621607};
GN Name=Nat8f3 {ECO:0000312|RGD:621607};
GN Synonyms=Cml3 {ECO:0000312|RGD:621607};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000269|PubMed:15057822};
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAF22304.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 12-228.
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).
CC -!- FUNCTION: Has histone acetyltransferase activity in vitro, with
CC specificity for histone H4. {ECO:0000250|UniProtKB:Q9JIY8}.
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:0000250|UniProtKB:Q9JIY8};
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250|UniProtKB:Q9JIY8};
CC Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear
CC region {ECO:0000250|UniProtKB:Q9JIY8}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9JIY8}. 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:0000250|UniProtKB:Q9JIY8}.
CC -!- SIMILARITY: Belongs to the camello family.
CC {ECO:0000269|PubMed:11397015}.
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DR EMBL; AABR03032859; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF187814; AAF22304.1; -; mRNA.
DR RefSeq; XP_006225036.1; XM_006224974.3.
DR RefSeq; XP_006236860.1; XM_006236798.3.
DR AlphaFoldDB; Q9QXS4; -.
DR SMR; Q9QXS4; -.
DR STRING; 10116.ENSRNOP00000021103; -.
DR PaxDb; Q9QXS4; -.
DR PRIDE; Q9QXS4; -.
DR Ensembl; ENSRNOT00000099291; ENSRNOP00000092145; ENSRNOG00000067962.
DR Ensembl; ENSRNOT00000114629; ENSRNOP00000093260; ENSRNOG00000067962.
DR GeneID; 113892; -.
DR UCSC; RGD:621607; rat.
DR CTD; 93674; -.
DR RGD; 621607; Nat8f3.
DR eggNOG; KOG3139; Eukaryota.
DR GeneTree; ENSGT00950000182932; -.
DR HOGENOM; CLU_013985_10_1_1; -.
DR InParanoid; Q9QXS4; -.
DR OMA; NKCHRAD; -.
DR OrthoDB; 1341682at2759; -.
DR PhylomeDB; Q9QXS4; -.
DR TreeFam; TF324687; -.
DR PRO; PR:Q9QXS4; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000015763; Expressed in adult mammalian kidney and 19 other tissues.
DR Genevisible; Q9QXS4; RN.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0010485; F:H4 histone acetyltransferase activity; ISO:RGD.
DR GO; GO:0008080; F:N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0001702; P:gastrulation with mouth forming second; NAS:UniProtKB.
DR GO; GO:0016573; P:histone acetylation; ISO:RGD.
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 2: Evidence at transcript level;
KW Acyltransferase; Cytoplasm; Membrane; Nucleus; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..228
FT /note="N-acetyltransferase family 8 member 3"
FT /id="PRO_0000284691"
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..217
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ SEQUENCE 228 AA; 26038 MW; C8E896A0434688F9 CRC64;
MAPYHIRKYQ DSDHRSVVNL FCRGTEEHIS ASFRYMLLLP GTLLILLGVP LTLFLASGSW
LLVLLSTLTL LVSLWLLAKY PWEKYTAMCL HSDMADIPRT YLSSHYSCFW VAESRGQMVG
IIAVLPVKDP LLQRKQLQLR HLSVSLEHRR EGIGRAMVRT ALQFAEMQGF SEVVLVTSML
QYAALALYQS MGFQKTGEFF YTFVSRLRNS PMICLKYCLT SALNDLKT
