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Protein

Sterol O-acyltransferase 2

Gene

Soat2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Plays a role in lipoprotein assembly and dietary cholesterol absorption. In addition to its acyltransferase activity, it may act as a ligase. May provide cholesteryl esters for lipoprotein secretion from hepatocytes and intestinal mucosa (By similarity).By similarity

Catalytic activityi

Acyl-CoA + cholesterol = CoA + cholesterol ester.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei436 – 4361Sequence analysis

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
  • response to nutrient 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 2 (EC:2.3.1.26)
Alternative name(s):
Acyl-coenzyme A:cholesterol acyltransferase 2
Short name:
ACAT-2
Cholesterol acyltransferase 2
Gene namesi
Name:Soat2
Synonyms:Acat2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi628865. Soat2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 121121CytoplasmicSequence analysisAdd
BLAST
Transmembranei122 – 14019HelicalSequence analysisAdd
BLAST
Topological domaini141 – 15919LumenalSequence analysisAdd
BLAST
Transmembranei160 – 17819HelicalSequence analysisAdd
BLAST
Topological domaini179 – 20224CytoplasmicSequence analysisAdd
BLAST
Transmembranei203 – 22119HelicalSequence analysisAdd
BLAST
Topological domaini222 – 342121LumenalSequence analysisAdd
BLAST
Transmembranei343 – 36523HelicalSequence analysisAdd
BLAST
Topological domaini366 – 477112CytoplasmicSequence analysisAdd
BLAST
Transmembranei478 – 49619HelicalSequence analysisAdd
BLAST
Topological domaini497 – 52428LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2096983.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 524524Sterol O-acyltransferase 2PRO_0000255713Add
BLAST

Proteomic databases

PaxDbiQ7TQM4.
PRIDEiQ7TQM4.

Interactioni

Subunit structurei

May form homo- or heterodimers.By similarity

Protein-protein interaction databases

MINTiMINT-4570296.
STRINGi10116.ENSRNOP00000015367.

Chemistry

BindingDBiQ7TQM4.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0380. Eukaryota.
COG5056. LUCA.
HOGENOMiHOG000020782.
HOVERGENiHBG058198.
InParanoidiQ7TQM4.
KOiK00637.
PhylomeDBiQ7TQM4.

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.

Q7TQM4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEPKAPQLRR RERQGEEQEN GACGEGNTRT HRAPDLVQWT RHMEAVKTQC
60 70 80 90 100
LEQAQRELAE LMDRAIWEAV QAYPKQDRPL PSTASDSTRK TQELHPGKRK
110 120 130 140 150
VFITRKSLLD ELMGVQHFRT IYHMFIAGLC VLIISTLAID FIDEGRLMLE
160 170 180 190 200
FDLLLFSFGQ LPLALMMWVP MFLSTLLLPY QTLRLWARPR SGGAWTLGAS
210 220 230 240 250
LGCVLLAAHA AVLCVLPVHV SVKHELPPAS RCVLVFEQVR FLMKSYSFLR
260 270 280 290 300
ETVPGIFCVR GGKGICTPSF SSYLYFLFCP TLIYRETYPR TPSIRWNYVA
310 320 330 340 350
KNFAQALGCL LYACFILGRL CVPVFANMSR EPFSTRALLL SILHATGPGI
360 370 380 390 400
FMLLLIFFAF LHCWLNAFAE MLRFGDRMFY RDWWNSTSFS NYYRTWNVVV
410 420 430 440 450
HDWLYSYVYQ DGLWLLGRQG RGAAMLGVFL VSALVHEYIF CFVLGFFYPV
460 470 480 490 500
MLILFLVVGG LLNFTMNDRH TGPAWNILMW TFLFLGQGIQ VSLYCQEWYA
510 520
RRHCPLPQPT FWELVTPRSW SCHP
Length:524
Mass (Da):60,498
Last modified:October 1, 2003 - v1
Checksum:i75CE7DE53F03C88A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB101480 mRNA. Translation: BAC78210.1.
RefSeqiNP_714950.2. NM_153728.2.
UniGeneiRn.83628.

Genome annotation databases

GeneIDi266770.
KEGGirno:266770.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB101480 mRNA. Translation: BAC78210.1.
RefSeqiNP_714950.2. NM_153728.2.
UniGeneiRn.83628.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4570296.
STRINGi10116.ENSRNOP00000015367.

Chemistry

BindingDBiQ7TQM4.
ChEMBLiCHEMBL2096983.

Proteomic databases

PaxDbiQ7TQM4.
PRIDEiQ7TQM4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi266770.
KEGGirno:266770.

Organism-specific databases

CTDi8435.
RGDi628865. Soat2.

Phylogenomic databases

eggNOGiKOG0380. Eukaryota.
COG5056. LUCA.
HOGENOMiHOG000020782.
HOVERGENiHBG058198.
InParanoidiQ7TQM4.
KOiK00637.
PhylomeDBiQ7TQM4.

Miscellaneous databases

PROiQ7TQM4.

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 nameiSOAT2_RAT
AccessioniPrimary (citable) accession number: Q7TQM4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: October 1, 2003
Last modified: July 6, 2016
This is version 80 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.