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Protein

Sterol O-acyltransferase 1

Gene

Soat1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-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
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Cholesterol 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621641. Soat1.

Subcellular locationi

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

GO - Cellular componenti

Complete GO annotation...

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

InterProiIPR004299. MBOAT_fam.
IPR014371. Oat_ACAT_DAG_ARE.
IPR030687. Sterol_acyltranf_meta.
[Graphical view]
PANTHERiPTHR10408. PTHR10408. 1 hit.
PfamiPF03062. MBOAT. 1 hit.
[Graphical view]
PIRSFiPIRSF000439. Oat_ACAT_DAG_ARE. 1 hit.
PIRSF500230. Sterol_acyltranf_ACAT. 1 hit.

Sequencei

Sequence statusi: Complete.

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

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.

Cross-referencesi

Sequence databases

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

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000005677.

Chemistry databases

BindingDBiO70536.
ChEMBLiCHEMBL285.

Proteomic databases

PaxDbiO70536.
PRIDEiO70536.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi81782.
KEGGirno:81782.
UCSCiRGD:621641. rat.

Organism-specific databases

CTDi6646.
RGDi621641. Soat1.

Phylogenomic databases

eggNOGiKOG0380. Eukaryota.
COG5056. LUCA.
HOGENOMiHOG000020782.
HOVERGENiHBG058198.
InParanoidiO70536.
KOiK00637.
PhylomeDBiO70536.

Miscellaneous databases

PROiO70536.

Family and domain databases

InterProiIPR004299. MBOAT_fam.
IPR014371. Oat_ACAT_DAG_ARE.
IPR030687. Sterol_acyltranf_meta.
[Graphical view]
PANTHERiPTHR10408. PTHR10408. 1 hit.
PfamiPF03062. MBOAT. 1 hit.
[Graphical view]
PIRSFiPIRSF000439. Oat_ACAT_DAG_ARE. 1 hit.
PIRSF500230. Sterol_acyltranf_ACAT. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiSOAT1_RAT
AccessioniPrimary (citable) accession number: O70536
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: August 1, 1998
Last modified: October 5, 2016
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.