ACATN_MOUSE
ID ACATN_MOUSE Reviewed; 550 AA.
AC Q99J27; Q9WTN1;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Acetyl-coenzyme A transporter 1;
DE Short=AT-1;
DE Short=Acetyl-CoA transporter 1;
DE AltName: Full=Solute carrier family 33 member 1;
GN Name=Slc33a1; Synonyms=Acatn;
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], FUNCTION, DEVELOPMENTAL STAGE, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Melanoma;
RX PubMed=10570973; DOI=10.1016/s0378-1119(99)00361-3;
RA Bora R.S., Kanamori A., Hirabayashi Y.;
RT "Cloning and characterization of a putative mouse acetyl-CoA transporter
RT cDNA.";
RL Gene 238:455-462(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10812068; DOI=10.1016/s0014-5793(00)01524-6;
RA Bora R.S., Ichikawa S., Kanamori A., Hirabayashi Y.;
RT "Genomic structure and promoter analysis of putative mouse acetyl-CoA
RT transporter gene.";
RL FEBS Lett. 473:169-172(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=129, and FVB/N; TISSUE=Eye, Kidney, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17208939; DOI=10.1074/mcp.m600218-mcp200;
RA Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT MS/MS/MS.";
RL Mol. Cell. Proteomics 6:669-676(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Liver, Lung, Pancreas, and Spleen;
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: Probable acetyl-CoA transporter necessary for O-acetylation
CC of gangliosides (PubMed:10570973). Negatively regulates BMP signaling
CC (By similarity). {ECO:0000250|UniProtKB:O00400,
CC ECO:0000269|PubMed:10570973}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in all adult tissues examined including
CC brain, heart, kidney, liver and spleen, with maximum expression in
CC liver and kidney. {ECO:0000269|PubMed:10570973}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed at day 7 of embryonic
CC development. Detected at lower levels throughout the later stages of
CC embryonic development. {ECO:0000269|PubMed:10570973}.
CC -!- SIMILARITY: Belongs to the SLC33A transporter family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB016795; BAA76933.1; -; mRNA.
DR EMBL; AB037368; BAA93087.1; -; Genomic_DNA.
DR EMBL; BC005616; AAH05616.1; -; mRNA.
DR EMBL; BC054395; AAH54395.1; -; mRNA.
DR EMBL; BC063104; AAH63104.1; -; mRNA.
DR CCDS; CCDS17382.1; -.
DR RefSeq; NP_001258964.1; NM_001272035.1.
DR RefSeq; NP_056543.2; NM_015728.5.
DR AlphaFoldDB; Q99J27; -.
DR BioGRID; 197916; 3.
DR STRING; 10090.ENSMUSP00000029402; -.
DR GlyGen; Q99J27; 1 site.
DR iPTMnet; Q99J27; -.
DR PhosphoSitePlus; Q99J27; -.
DR SwissPalm; Q99J27; -.
DR EPD; Q99J27; -.
DR jPOST; Q99J27; -.
DR MaxQB; Q99J27; -.
DR PaxDb; Q99J27; -.
DR PeptideAtlas; Q99J27; -.
DR PRIDE; Q99J27; -.
DR ProteomicsDB; 285836; -.
DR DNASU; 11416; -.
DR Ensembl; ENSMUST00000029402; ENSMUSP00000029402; ENSMUSG00000027822.
DR Ensembl; ENSMUST00000160883; ENSMUSP00000125713; ENSMUSG00000027822.
DR Ensembl; ENSMUST00000161659; ENSMUSP00000123986; ENSMUSG00000027822.
DR GeneID; 11416; -.
DR KEGG; mmu:11416; -.
DR UCSC; uc008pkd.2; mouse.
DR CTD; 9197; -.
DR MGI; MGI:1332247; Slc33a1.
DR VEuPathDB; HostDB:ENSMUSG00000027822; -.
DR eggNOG; KOG3574; Eukaryota.
DR GeneTree; ENSGT00940000154019; -.
DR HOGENOM; CLU_020502_1_0_1; -.
DR InParanoid; Q99J27; -.
DR OMA; LWFWGIT; -.
DR OrthoDB; 1300300at2759; -.
DR PhylomeDB; Q99J27; -.
DR TreeFam; TF300008; -.
DR Reactome; R-MMU-425397; Transport of vitamins, nucleosides, and related molecules.
DR BioGRID-ORCS; 11416; 16 hits in 76 CRISPR screens.
DR ChiTaRS; Slc33a1; mouse.
DR PRO; PR:Q99J27; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q99J27; protein.
DR Bgee; ENSMUSG00000027822; Expressed in lacrimal gland and 252 other tissues.
DR Genevisible; Q99J27; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008521; F:acetyl-CoA transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015295; F:solute:proton symporter activity; IBA:GO_Central.
DR GO; GO:0030509; P:BMP signaling pathway; ISO:MGI.
DR GO; GO:0060395; P:SMAD protein signal transduction; ISO:MGI.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR024371; AcetylCoA_trans_1-like.
DR InterPro; IPR004752; AmpG_permease/AT-1.
DR InterPro; IPR036259; MFS_trans_sf.
DR PANTHER; PTHR12778; PTHR12778; 1.
DR Pfam; PF13000; Acatn; 2.
DR SUPFAM; SSF103473; SSF103473; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..550
FT /note="Acetyl-coenzyme A transporter 1"
FT /id="PRO_0000076166"
FT TOPO_DOM 1..74
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..113
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 135..141
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..175
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 197..217
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..256
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..277
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 278..300
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 322..344
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 345..365
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 366..375
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 397..405
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 427..509
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 510..530
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 531..550
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17208939,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 255..257
FT /note="VTL -> GNP (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 274..275
FT /note="LV -> SL (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="Q -> P (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 337
FT /note="V -> E (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 550 AA; 61075 MW; 5A55A7F40A2A9661 CRC64;
MSPTISHKDS SRQRRSGMFS HALDMKSGPL PPGGWDDSRR DSVGGEGDRE VLLGDAGPGD
LPKAPRSYRS ELSSILLLLF LYVLQGIPLG LAGSIPLILQ SKNVSYTDQA FFSFVFWPFS
LKLLWAPLVD AVYFKNFGRR KSWLVPTQYT LGIFMIYLST QVDRLLGNID GRTPDVVALT
VTFFLFEFLA ATQDIAVDGW ALTMLSRENV GYASTCNSVG QTAGYFLGNV LFLALESADF
CNKYLRFQPQ PRGIVTLSDF LFFWGTVFLI TTTLVALLKK ENREASIVKE ETQGITDTYK
LLFSIIKMPA VLAFCLLILT SKIGFSAADA VTGLKLVEEG VPKEHLALLA VPMVPLQIIL
PLLISKYTAG PQPLNIFYKA MPYRLLLGLE YALLVWWTPK VEHQGGFPLY YYIIVLLSYA
LHQVTLYSMY VSIMAFNAKV SDPLIGGTYM TLLNTVSNLG GNWPSTVALW LVDPLTVKEC
VGASNQNCRT PDAIELCKKL GGSCVTALDG YYVESIICVL IGFGWWFFLG PKFKKLQDEG
PSSWKCKRNN
