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Protein

Sterol O-acyltransferase 1

Gene

Soat1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

Functioni

Catalyzes the formation of fatty acid-cholesterol esters. Plays a role in lipoprotein assembly and dietary cholesterol absorption.

Catalytic activityi

Acyl-CoA + cholesterol = CoA + cholesterol ester.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei455By similarity1

GO - Molecular functioni

  • cholesterol O-acyltransferase activity Source: GO_Central
  • sterol O-acyltransferase activity Source: RGD

GO - Biological processi

  • cholesterol esterification Source: InterPro
  • cholesterol homeostasis Source: InterPro
  • cholesterol metabolic process Source: RGD

Keywordsi

Molecular functionAcyltransferase, Transferase
Biological processCholesterol metabolism, Lipid metabolism, Steroid metabolism, Sterol metabolism

Names & Taxonomyi

Protein namesi
Recommended name:
Sterol O-acyltransferase 1 (EC:2.3.1.26By similarity)
Alternative name(s):
Acyl-coenzyme A:cholesterol acyltransferase 1
Short name:
ACAT-1
Cholesterol acyltransferase 1
Gene namesi
Name:Soat1
Synonyms:Acact, Acat
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621641 Soat1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 135CytoplasmicSequence analysisAdd BLAST135
Transmembranei136 – 154HelicalSequence analysisAdd BLAST19
Topological domaini155 – 176LumenalSequence analysisAdd BLAST22
Transmembranei177 – 196HelicalSequence analysisAdd BLAST20
Topological domaini197 – 219CytoplasmicSequence analysisAdd BLAST23
Transmembranei220 – 238HelicalSequence analysisAdd BLAST19
Topological domaini239 – 241LumenalSequence analysis3
Transmembranei242 – 259HelicalSequence analysisAdd BLAST18
Topological domaini260 – 496CytoplasmicSequence analysisAdd BLAST237
Transmembranei497 – 512HelicalSequence analysisAdd BLAST16
Topological domaini513 – 535LumenalSequence analysisAdd BLAST23

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL285

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002076431 – 545Sterol O-acyltransferase 1Add BLAST545

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei7PhosphoserineBy similarity1
Disulfide bondi523 ↔ 541By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiO70536
PRIDEiO70536

Interactioni

Subunit structurei

May form homo- or heterodimers. Interacts with UBIAD1.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000005677

Chemistry databases

BindingDBiO70536

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0380 Eukaryota
COG5056 LUCA
HOGENOMiHOG000020782
HOVERGENiHBG058198
InParanoidiO70536
KOiK00637
PhylomeDBiO70536

Family and domain databases

InterProiView protein in InterPro
IPR004299 MBOAT_fam
IPR014371 Oat_ACAT_DAG_ARE
IPR030687 Sterol_acyltranf_meta
PANTHERiPTHR10408 PTHR10408, 1 hit
PfamiView protein in Pfam
PF03062 MBOAT, 1 hit
PIRSFiPIRSF000439 Oat_ACAT_DAG_ARE, 1 hit
PIRSF500230 Sterol_acyltranf_ACAT, 1 hit

Sequence (1+)i

Sequence statusi: Complete.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.iShow all

O70536-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVGEETSLRN RLSRSAENPE QDEAQKNLLD THRNGHITMK QLIAKKRQLA
60 70 80 90 100
AEAEELKPLF LKEVGCHFDD FVTNLIDKSA SLDNGGCALT TFSILEEMKN
110 120 130 140 150
NHRAKDLRAP PEQGKIFISR RSLLDELFEV DHIRTIYHMF IALLIIFILS
160 170 180 190 200
TLVVDYIDEG RLVLEFSLLA YAFGQFPIVI WTWWAMFLST LAIPYFLFQR
210 220 230 240 250
WAHGYSKSSH PLIYSLIHGA FFLVFQLGIL GFIPTYVVLA YTLPPASRFI
260 270 280 290 300
LILEQIRLVM KAHSYVRENV PRVLSAAKEK SSTVPVPTVN QYLYFLFAPT
310 320 330 340 350
LIYRDSYPRT PTVRWGYVAM QFLQVFGCLF YVYYIFERLC APLFRNIKQE
360 370 380 390 400
PFSARVLVLC VFNSILPGVL MLFLSFFAFL HCWLNAFAEM LRFGDRMFYK
410 420 430 440 450
DWWNSTSYSN YYRTWNVVVH DWLYYYVYKD LLWFFSKRFR PAAMLAVFAL
460 470 480 490 500
SAVVHEYALA VCLSYFYPVL FVLFMFFGMA FNFIVNDSRK RPVWNIMVRA
510 520 530 540
SLFLGHGVIL CFYSQEWYAR QRCPLKNPTF LDYVRPRTWT CRYVF
Length:545
Mass (Da):64,146
Last modified:August 1, 1998 - v1
Checksum:i40129EF21257BEBF
GO

Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
G3V6J2G3V6J2_RAT
O-acyltransferase
Soat1 rCG_46333
545Annotation score:

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D86373 mRNA Translation: BAA25372.1
RefSeqiNP_112380.1, NM_031118.1
UniGeneiRn.59

Genome annotation databases

GeneIDi81782
KEGGirno:81782
UCSCiRGD:621641 rat

Similar proteinsi

Entry informationi

Entry nameiSOAT1_RAT
AccessioniPrimary (citable) accession number: O70536
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: August 1, 1998
Last modified: May 23, 2018
This is version 113 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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