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Protein

StAR-related lipid transfer protein 4

Gene

Stard4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

May be involved in the intracellular transport of sterols or other lipids. May bind cholesterol or other sterols.

GO - Molecular functioni

GO - Biological processi

  • cholesterol esterification Source: CACAO
  • lipid transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Lipid transport, Transport

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
StAR-related lipid transfer protein 4
Alternative name(s):
START domain-containing protein 4
Short name:
StARD4
Gene namesi
Name:Stard4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:2156764. Stard4.

Subcellular locationi

GO - Cellular componenti

  • cytoplasmic, membrane-bounded vesicle Source: MGI
  • cytosol Source: CACAO
  • endoplasmic reticulum Source: CACAO
  • mitochondrion Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 224224StAR-related lipid transfer protein 4PRO_0000220668Add
BLAST

Proteomic databases

EPDiQ99JV5.
MaxQBiQ99JV5.
PaxDbiQ99JV5.
PRIDEiQ99JV5.

PTM databases

iPTMnetiQ99JV5.
PhosphoSiteiQ99JV5.

Expressioni

Tissue specificityi

Expressed in most tissues, with highest levels in liver and in kidney.

Inductioni

Down-regulated by dietary cholesterol.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000025236.

Structurei

Secondary structure

1
224
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi20 – 3819Combined sources
Helixi42 – 443Combined sources
Beta strandi46 – 505Combined sources
Beta strandi55 – 606Combined sources
Beta strandi62 – 7716Combined sources
Helixi79 – 868Combined sources
Beta strandi87 – 893Combined sources
Helixi90 – 956Combined sources
Beta strandi99 – 10911Combined sources
Beta strandi112 – 1198Combined sources
Turni123 – 1264Combined sources
Beta strandi131 – 14111Combined sources
Beta strandi144 – 1518Combined sources
Beta strandi161 – 1633Combined sources
Beta strandi168 – 1769Combined sources
Beta strandi179 – 18911Combined sources
Helixi199 – 22123Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JSSX-ray2.20A/B1-224[»]
5BRLX-ray2.00A/B13-222[»]
ProteinModelPortaliQ99JV5.
SMRiQ99JV5. Positions 13-222.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99JV5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 224209STARTPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 START domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410IPNZ. Eukaryota.
ENOG4111F97. LUCA.
HOGENOMiHOG000137345.
HOVERGENiHBG106946.
InParanoidiQ99JV5.
PhylomeDBiQ99JV5.

Family and domain databases

Gene3Di3.30.530.20. 1 hit.
InterProiIPR023393. START-like_dom.
IPR002913. START_lipid-bd_dom.
[Graphical view]
PfamiPF01852. START. 1 hit.
[Graphical view]
SMARTiSM00234. START. 1 hit.
[Graphical view]
PROSITEiPS50848. START. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q99JV5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADPESPWSQ IGRKIKLEGL SDVASISTKL QNTLIQYHSI KEDEWRVAKK
60 70 80 90 100
VKDVTVWRKP SEEFNGYLYK AQGVMDDVVN NVIDHIRPGP WRLDWDRLMT
110 120 130 140 150
SLDVLEHFEE NCCVMRYTTA GQLLNIISPR EFVDFSYTVG YEEGLLSCGV
160 170 180 190 200
SVEWSETRPE FVRGYNHPCG WFCVPLKDSP SQSLLTGYIQ TDLRGMIPQS
210 220
AVDTAMASTL ANFYSDLRKG LRKA
Length:224
Mass (Da):25,579
Last modified:June 1, 2001 - v1
Checksum:i104B7D3052EEF064
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti41 – 411K → E in strain: C57BL/6.
Natural varianti51 – 511V → A in strain: C57BL/6.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF480298 mRNA. Translation: AAL87128.1.
AF480297 mRNA. Translation: AAL87127.1.
BC005642 mRNA. Translation: AAH05642.1.
CCDSiCCDS29123.1.
RefSeqiNP_598535.1. NM_133774.4.
UniGeneiMm.127058.
Mm.393277.

Genome annotation databases

GeneIDi170459.
KEGGimmu:170459.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF480298 mRNA. Translation: AAL87128.1.
AF480297 mRNA. Translation: AAL87127.1.
BC005642 mRNA. Translation: AAH05642.1.
CCDSiCCDS29123.1.
RefSeqiNP_598535.1. NM_133774.4.
UniGeneiMm.127058.
Mm.393277.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JSSX-ray2.20A/B1-224[»]
5BRLX-ray2.00A/B13-222[»]
ProteinModelPortaliQ99JV5.
SMRiQ99JV5. Positions 13-222.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000025236.

PTM databases

iPTMnetiQ99JV5.
PhosphoSiteiQ99JV5.

Proteomic databases

EPDiQ99JV5.
MaxQBiQ99JV5.
PaxDbiQ99JV5.
PRIDEiQ99JV5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi170459.
KEGGimmu:170459.

Organism-specific databases

CTDi134429.
MGIiMGI:2156764. Stard4.

Phylogenomic databases

eggNOGiENOG410IPNZ. Eukaryota.
ENOG4111F97. LUCA.
HOGENOMiHOG000137345.
HOVERGENiHBG106946.
InParanoidiQ99JV5.
PhylomeDBiQ99JV5.

Miscellaneous databases

EvolutionaryTraceiQ99JV5.
PROiQ99JV5.
SOURCEiSearch...

Family and domain databases

Gene3Di3.30.530.20. 1 hit.
InterProiIPR023393. START-like_dom.
IPR002913. START_lipid-bd_dom.
[Graphical view]
PfamiPF01852. START. 1 hit.
[Graphical view]
SMARTiSM00234. START. 1 hit.
[Graphical view]
PROSITEiPS50848. START. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The cholesterol-regulated StarD4 gene encodes a StAR-related lipid transfer protein with two closely related homologues, StarD5 and StarD6."
    Soccio R.E., Adams R.M., Romanowski M.J., Sehayek E., Burley S.K., Breslow J.L.
    Proc. Natl. Acad. Sci. U.S.A. 99:6943-6948(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6J and FVB.
    Tissue: Liver.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Mammary tumor.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  4. "Crystal structure of the Mus musculus cholesterol-regulated START protein 4 (StarD4) containing a StAR-related lipid transfer domain."
    Romanowski M.J., Soccio R.E., Breslow J.L., Burley S.K.
    Proc. Natl. Acad. Sci. U.S.A. 99:6949-6954(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).

Entry informationi

Entry nameiSTAR4_MOUSE
AccessioniPrimary (citable) accession number: Q99JV5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 106 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.