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Q9DBG5 (PLIN3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Perilipin-3
Alternative name(s):
Cargo selection protein TIP47
Mannose-6-phosphate receptor-binding protein 1
Gene names
Name:Plin3
Synonyms:M6prbp1, Tip47
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length437 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for the transport of mannose 6-phosphate receptors (MPR) from endosomes to the trans-Golgi network By similarity.

Subunit structure

Homooligomer. Interacts with M6PR (via the cytoplasmic domain). Interacts with IGF2R (via the cytoplasmic domain) By similarity.

Subcellular location

Cytoplasm By similarity. Endosome membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Lipid droplet By similarity. Note: Membrane associated on endosomes. Detected in the envelope and the core of lipid bodies and in lipid sails By similarity.

Sequence similarities

Belongs to the perilipin family.

Sequence caution

The sequence BAC33798.1 differs from that shown. Reason: Frameshift at position 400.

Ontologies

Keywords
   Biological processTransport
   Cellular componentCytoplasm
Endosome
Lipid droplet
Membrane
   DomainCoiled coil
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processtransport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentendosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

lipid particle

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 437436Perilipin-3
PRO_0000099891

Regions

Coiled coil251 – 28434 Potential
Coiled coil357 – 41054 Potential

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue651N6-acetyllysine
Modified residue1301Phosphoserine By similarity
Modified residue1741Phosphothreonine By similarity
Modified residue1791Phosphoserine By similarity
Modified residue1831Phosphoserine By similarity

Secondary structure

........................ 437
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9DBG5 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: F7CDD3A754A5C04D

FASTA43747,262
        10         20         30         40         50         60 
MSSNGTDAPA EAQAAMEEPV VQPSVVDRVA GLPLISSTYG MVSAAYTSTK ENYPHVRTVC 

        70         80         90        100        110        120 
DVAEKGVKTL TTAAVSTAQP ILSKLEPQIA TASEYAHRGL DRLQESLPIL QQPTEKVLAD 

       130        140        150        160        170        180 
TKELVSSTVS GAQEMVSSSV SSAKETVATR VTGAVDVTLG AVQNSVDKTK SAMTSGVQSV 

       190        200        210        220        230        240 
MGSRVGQMVI SGVDRVLVKS EAWADNRLPL TEAELALIAT PPEDSDMASL QQQRQEQNYF 

       250        260        270        280        290        300 
VRLGSLSERL RNHAYEHSLG KLQNARQKAQ ETLQQLTSVL GLMESVKQGV DQRLGEGQEK 

       310        320        330        340        350        360 
LHQMWLSWNQ KTPQDAEKDP AKPEQVEARA LSMFRDITQQ LQSMCVALGA SIQGLPSHVR 

       370        380        390        400        410        420 
EQAQQARSQV NDLQATFSGI HSFQDLSAGV LAQTRERIAR AREALDNTVE YVAQNTPAMW 

       430 
LVGPFAPGIT EKTPEGK 

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryo, Head and 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].
Strain: FVB/N.
Tissue: Mammary tumor.
[3]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-65, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[4]"Structure of a lipid droplet protein; the PAT family member TIP47."
Hickenbottom S.J., Kimmel A.R., Londos C., Hurley J.H.
Structure 12:1199-1207(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 191-437.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK004970 mRNA. Translation: BAB23708.1.
AK012517 mRNA. Translation: BAB28291.1.
AK049537 mRNA. Translation: BAC33798.1. Frameshift.
AK050140 mRNA. Translation: BAC34089.1.
AK132313 mRNA. Translation: BAE21098.1.
AK167214 mRNA. Translation: BAE39340.1.
BC011116 mRNA. Translation: AAH11116.1.
RefSeqNP_080112.1. NM_025836.3.
UniGeneMm.311696.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1SZIX-ray2.80A191-437[»]
ProteinModelPortalQ9DBG5.
SMRQ9DBG5. Positions 206-431.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9DBG5. 2 interactions.
MINTMINT-1748486.
STRING10090.ENSMUSP00000019726.

PTM databases

PhosphoSiteQ9DBG5.

2D gel databases

REPRODUCTION-2DPAGEIPI00319270.

Proteomic databases

PaxDbQ9DBG5.
PRIDEQ9DBG5.

Protocols and materials databases

DNASU66905.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000019726; ENSMUSP00000019726; ENSMUSG00000024197.
GeneID66905.
KEGGmmu:66905.
UCSCuc008dbn.1. mouse.

Organism-specific databases

CTD10226.
MGIMGI:1914155. Plin3.

Phylogenomic databases

eggNOGNOG81115.
GeneTreeENSGT00500000044795.
HOGENOMHOG000033816.
HOVERGENHBG002935.
InParanoidQ9DBG5.
OMAQEQSYFV.
OrthoDBEOG7SN8CD.
TreeFamTF328397.

Gene expression databases

ArrayExpressQ9DBG5.
BgeeQ9DBG5.
CleanExMM_M6PRBP1.
GenevestigatorQ9DBG5.

Family and domain databases

InterProIPR004279. Perilipin.
[Graphical view]
PANTHERPTHR14024. PTHR14024. 1 hit.
PfamPF03036. Perilipin. 1 hit.
[Graphical view]
PIRSFPIRSF036881. PAT. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9DBG5.
NextBio322981.
PROQ9DBG5.
SOURCESearch...

Entry information

Entry namePLIN3_MOUSE
AccessionPrimary (citable) accession number: Q9DBG5
Secondary accession number(s): Q3TK05, Q8BKV9, Q9CZK1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: June 1, 2001
Last modified: March 19, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot