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Acetyl-coenzyme A transporter 1 (AT-1) (Acetyl-CoA transporter 1) (Solute carrier family 33 member 1)

 ACATN_HUMAN             Reviewed;         549 AA.
O00400; B2R5Q2; D3DNK4;
20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
01-JUL-1997, sequence version 1.
28-MAR-2018, entry version 138.
RecName: Full=Acetyl-coenzyme A transporter 1;
Short=AT-1;
Short=Acetyl-CoA transporter 1;
AltName: Full=Solute carrier family 33 member 1;
Name=SLC33A1; Synonyms=ACATN, AT1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
SUBCELLULAR LOCATION.
TISSUE=Melanoma;
PubMed=9096318; DOI=10.1073/pnas.94.7.2897;
Kanamori A., Nakayama J., Fukuda M.N., Stallcup W.B., Sasaki K.,
Fukuda M., Hirabayashi Y.;
"Expression cloning and characterization of a cDNA encoding a novel
membrane protein required for the formation of O-acetylated
gangliosides: a putative acetyl CoA transporter.";
Proc. Natl. Acad. Sci. U.S.A. 94:2897-2902(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[6]
FUNCTION, VARIANT SPG42 ARG-113, AND CHARACTERIZATION OF VARIANT SPG42
ARG-113.
PubMed=25402622; DOI=10.1002/humu.22732;
Mao F., Li Z., Zhao B., Lin P., Liu P., Zhai M., Liu Q., Shao C.,
Sun W., Gong Y.;
"Identification and Functional Analysis of a SLC33A1: c.339T>G
(p.Ser113Arg) Variant in the Original SPG42 Family.";
Hum. Mutat. 36:240-249(2015).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[8]
VARIANT [LARGE SCALE ANALYSIS] ALA-400.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[9]
VARIANT SPG42 ARG-113.
PubMed=19061983; DOI=10.1016/j.ajhg.2008.11.003;
Lin P., Li J., Liu Q., Mao F., Li J., Qiu R., Hu H., Song Y., Yang Y.,
Gao G., Yan C., Yang W., Shao C., Gong Y.;
"A missense mutation in SLC33A1, which encodes the acetyl-CoA
transporter, causes autosomal-dominant spastic paraplegia (SPG42).";
Am. J. Hum. Genet. 83:752-759(2008).
[10]
VARIANT CCHLND PRO-110, AND CHARACTERIZATION OF VARIANT CCHLND
PRO-110.
PubMed=22243965; DOI=10.1016/j.ajhg.2011.11.030;
Huppke P., Brendel C., Kalscheuer V., Korenke G.C., Marquardt I.,
Freisinger P., Christodoulou J., Hillebrand M., Pitelet G., Wilson C.,
Gruber-Sedlmayr U., Ullmann R., Haas S., Elpeleg O., Nurnberg G.,
Nurnberg P., Dad S., Moller L.B., Kaler S.G., Gartner J.;
"Mutations in SLC33A1 cause a lethal autosomal-recessive disorder with
congenital cataracts, hearing loss, and low serum copper and
ceruloplasmin.";
Am. J. Hum. Genet. 90:61-68(2012).
[11]
ERRATUM.
Huppke P., Brendel C., Kalscheuer V., Korenke G.C., Marquardt I.,
Freisinger P., Christodoulou J., Hillebrand M., Pitelet G., Wilson C.,
Gruber-Sedlmayr U., Ullmann R., Haas S., Elpeleg O., Nurnberg G.,
Nurnberg P., Dad S., Moller L.B., Kaler S.G., Gartner J.;
Am. J. Hum. Genet. 90:378-378(2012).
-!- FUNCTION: Probable acetyl-CoA transporter necessary for O-
acetylation of gangliosides (PubMed:9096318). Negatively regulates
BMP signaling (PubMed:25402622). {ECO:0000269|PubMed:25402622,
ECO:0000269|PubMed:9096318}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000305|PubMed:9096318}; Multi-pass membrane protein
{ECO:0000305|PubMed:9096318}.
-!- TISSUE SPECIFICITY: Ubiquitous. Detected in heart, brain,
placenta, lung, liver, skeletal muscle, kidney and pancreas. With
strongest signals in pancreas. {ECO:0000269|PubMed:9096318}.
-!- DISEASE: Spastic paraplegia 42, autosomal dominant (SPG42)
[MIM:612539]: A form of spastic paraplegia, a neurodegenerative
disorder characterized by a slow, gradual, progressive weakness
and spasticity of the lower limbs. Rate of progression and the
severity of symptoms are quite variable. Initial symptoms may
include difficulty with balance, weakness and stiffness in the
legs, muscle spasms, and dragging the toes when walking. In some
forms of the disorder, bladder symptoms (such as incontinence) may
appear, or the weakness and stiffness may spread to other parts of
the body. {ECO:0000269|PubMed:19061983,
ECO:0000269|PubMed:25402622}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Congenital cataracts, hearing loss, and neurodegeneration
(CCHLND) [MIM:614482]: An autosomal recessive disorder
characterized by congenital cataracts, severe psychomotor
retardation, and hearing loss associated with decreased serum
ceruloplasmin and copper. Brain MRI shows cerebral and cerebellar
atrophy and hypomyelination. {ECO:0000269|PubMed:22243965}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the SLC33A transporter family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Mendelian genes solute carrier family 33
(acetyl-CoA transporter), member 1 (SLC33A1); Note=Leiden Open
Variation Database (LOVD);
URL="http://www.lovd.nl/SLC33A1";
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EMBL; D88152; BAA20072.1; -; mRNA.
EMBL; AK312268; BAG35199.1; -; mRNA.
EMBL; CH471052; EAW78743.1; -; Genomic_DNA.
EMBL; CH471052; EAW78744.1; -; Genomic_DNA.
EMBL; BC014416; AAH14416.1; -; mRNA.
CCDS; CCDS3173.1; -.
RefSeq; NP_001177921.1; NM_001190992.1.
RefSeq; NP_004724.1; NM_004733.3.
UniGene; Hs.478031; -.
ProteinModelPortal; O00400; -.
BioGrid; 114632; 59.
IntAct; O00400; 58.
MINT; O00400; -.
STRING; 9606.ENSP00000352456; -.
BindingDB; O00400; -.
ChEMBL; CHEMBL3638338; -.
TCDB; 2.A.1.25.1; the major facilitator superfamily (mfs).
iPTMnet; O00400; -.
PhosphoSitePlus; O00400; -.
BioMuta; SLC33A1; -.
EPD; O00400; -.
MaxQB; O00400; -.
PaxDb; O00400; -.
PeptideAtlas; O00400; -.
PRIDE; O00400; -.
DNASU; 9197; -.
Ensembl; ENST00000359479; ENSP00000352456; ENSG00000169359.
Ensembl; ENST00000392845; ENSP00000376587; ENSG00000169359.
GeneID; 9197; -.
KEGG; hsa:9197; -.
UCSC; uc003fan.6; human.
CTD; 9197; -.
DisGeNET; 9197; -.
EuPathDB; HostDB:ENSG00000169359.13; -.
GeneCards; SLC33A1; -.
HGNC; HGNC:95; SLC33A1.
HPA; HPA042430; -.
MalaCards; SLC33A1; -.
MIM; 603690; gene.
MIM; 612539; phenotype.
MIM; 614482; phenotype.
neXtProt; NX_O00400; -.
OpenTargets; ENSG00000169359; -.
Orphanet; 171863; Autosomal dominant spastic paraplegia type 42.
Orphanet; 300313; Congenital cataract-hearing loss-severe developmental delay syndrome.
PharmGKB; PA24432; -.
eggNOG; KOG3574; Eukaryota.
eggNOG; COG0477; LUCA.
GeneTree; ENSGT00730000111115; -.
HOGENOM; HOG000194770; -.
HOVERGEN; HBG052723; -.
InParanoid; O00400; -.
KO; K03372; -.
OMA; LWFWGIT; -.
OrthoDB; EOG091G06Y7; -.
PhylomeDB; O00400; -.
TreeFam; TF300008; -.
Reactome; R-HSA-425397; Transport of vitamins, nucleosides, and related molecules.
Reactome; R-HSA-5619061; Defective SLC33A1 causes spastic paraplegia 42 (SPG42).
ChiTaRS; SLC33A1; human.
GenomeRNAi; 9197; -.
PRO; PR:O00400; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000169359; -.
CleanEx; HS_SLC33A1; -.
ExpressionAtlas; O00400; baseline and differential.
Genevisible; O00400; HS.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:ProtInc.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0008521; F:acetyl-CoA transmembrane transporter activity; TAS:Reactome.
GO; GO:0015295; F:solute:proton symporter activity; IBA:GO_Central.
GO; GO:0030509; P:BMP signaling pathway; IDA:UniProtKB.
GO; GO:0060395; P:SMAD protein signal transduction; IDA:UniProtKB.
GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
InterPro; IPR024371; Acetyl-CoA_trnpstr_1.
InterPro; IPR004752; AmpG_permease/AT-1.
InterPro; IPR036259; MFS_trans_sf.
Pfam; PF13000; Acatn; 2.
SUPFAM; SSF103473; SSF103473; 2.
TIGRFAMs; TIGR00901; 2A0125; 1.
1: Evidence at protein level;
Cataract; Complete proteome; Deafness; Disease mutation;
Endoplasmic reticulum; Glycoprotein; Hereditary spastic paraplegia;
Membrane; Neurodegeneration; Phosphoprotein; Polymorphism;
Reference proteome; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 549 Acetyl-coenzyme A transporter 1.
/FTId=PRO_0000076165.
TOPO_DOM 1 74 Cytoplasmic. {ECO:0000255}.
TRANSMEM 75 95 Helical. {ECO:0000255}.
TOPO_DOM 96 113 Extracellular. {ECO:0000255}.
TRANSMEM 114 134 Helical. {ECO:0000255}.
TOPO_DOM 135 141 Cytoplasmic. {ECO:0000255}.
TRANSMEM 142 162 Helical. {ECO:0000255}.
TOPO_DOM 163 175 Extracellular. {ECO:0000255}.
TRANSMEM 176 196 Helical. {ECO:0000255}.
TOPO_DOM 197 217 Cytoplasmic. {ECO:0000255}.
TRANSMEM 218 238 Helical. {ECO:0000255}.
TOPO_DOM 239 256 Extracellular. {ECO:0000255}.
TRANSMEM 257 277 Helical. {ECO:0000255}.
TOPO_DOM 278 299 Cytoplasmic. {ECO:0000255}.
TRANSMEM 300 320 Helical. {ECO:0000255}.
TOPO_DOM 321 343 Extracellular. {ECO:0000255}.
TRANSMEM 344 364 Helical. {ECO:0000255}.
TOPO_DOM 365 378 Cytoplasmic. {ECO:0000255}.
TRANSMEM 379 398 Helical. {ECO:0000255}.
TOPO_DOM 399 404 Extracellular. {ECO:0000255}.
TRANSMEM 405 425 Helical. {ECO:0000255}.
TOPO_DOM 426 508 Cytoplasmic. {ECO:0000255}.
TRANSMEM 509 529 Helical. {ECO:0000255}.
TOPO_DOM 530 549 Extracellular. {ECO:0000255}.
MOD_RES 22 22 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 42 42 Phosphoserine.
{ECO:0000250|UniProtKB:Q99J27}.
CARBOHYD 103 103 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VARIANT 110 110 A -> P (in CCHLND; the mutant protein is
present at normal levels in patient
fibroblasts; the mutant protein fails to
localize normally to the Golgi apparatus
and instead shows punctate staining in
the cytoplasm; dbSNP:rs281875283).
{ECO:0000269|PubMed:22243965}.
/FTId=VAR_067915.
VARIANT 113 113 S -> R (in SPG42; significant increase in
the amount of nuclear phosphorylated
SMAD1-SMAD5-SMAD8 protein complex; marked
increase of the BMPR1A protein level; no
change for BMPR2 protein level; decrease
of BMPR1A degradation;
dbSNP:rs121909484).
{ECO:0000269|PubMed:19061983,
ECO:0000269|PubMed:25402622}.
/FTId=VAR_054850.
VARIANT 171 171 D -> G (in dbSNP:rs3804769).
/FTId=VAR_050631.
VARIANT 400 400 V -> A (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035776.
SEQUENCE 549 AA; 60909 MW; ABDE59DEDEBAA9A5 CRC64;
MSPTISHKDS SRQRRPGNFS HSLDMKSGPL PPGGWDDSHL DSAGREGDRE ALLGDTGTGD
FLKAPQSFRA ELSSILLLLF LYVLQGIPLG LAGSIPLILQ SKNVSYTDQA FFSFVFWPFS
LKLLWAPLVD AVYVKNFGRR KSWLVPTQYI LGLFMIYLST QVDRLLGNTD DRTPDVIALT
VAFFLFEFLA ATQDIAVDGW ALTMLSRENV GYASTCNSVG QTAGYFLGNV LFLALESADF
CNKYLRFQPQ PRGIVTLSDF LFFWGTVFLI TTTLVALLKK ENEVSVVKEE TQGITDTYKL
LFAIIKMPAV LTFCLLILTA KIGFSAADAV TGLKLVEEGV PKEHLALLAV PMVPLQIILP
LIISKYTAGP QPLNTFYKAM PYRLLLGLEY ALLVWWTPKV EHQGGFPIYY YIVVLLSYAL
HQVTVYSMYV SIMAFNAKVS DPLIGGTYMT LLNTVSNLGG NWPSTVALWL VDPLTVKECV
GASNQNCRTP DAVELCKKLG GSCVTALDGY YVESIICVFI GFGWWFFLGP KFKKLQDEGS
SSWKCKRNN


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Genprice Inc, Invoices and accounting
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