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Protein

Perilipin-3

Gene

Plin3

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

Functioni

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

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Perilipin-3
Alternative name(s):
Cargo selection protein TIP47
Mannose-6-phosphate receptor-binding protein 1
Gene namesi
Name:Plin3
Synonyms:M6prbp1, Tip47
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1914155. Plin3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Lipid droplet, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 437436Perilipin-3PRO_0000099891Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei65 – 651N6-acetyllysine1 Publication
Modified residuei130 – 1301PhosphoserineBy similarity
Modified residuei174 – 1741PhosphothreonineBy similarity
Modified residuei179 – 1791PhosphoserineBy similarity
Modified residuei183 – 1831PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9DBG5.
PaxDbiQ9DBG5.
PRIDEiQ9DBG5.

2D gel databases

REPRODUCTION-2DPAGEIPI00319270.

PTM databases

PhosphoSiteiQ9DBG5.

Expressioni

Gene expression databases

BgeeiQ9DBG5.
CleanExiMM_M6PRBP1.
ExpressionAtlasiQ9DBG5. baseline and differential.
GenevisibleiQ9DBG5. MM.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi211801. 1 interaction.
IntActiQ9DBG5. 2 interactions.
MINTiMINT-1748486.
STRINGi10090.ENSMUSP00000019726.

Structurei

Secondary structure

1
437
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi207 – 2104Combined sources
Helixi212 – 2165Combined sources
Helixi227 – 2359Combined sources
Beta strandi239 – 2424Combined sources
Helixi243 – 2453Combined sources
Helixi248 – 28740Combined sources
Helixi324 – 35027Combined sources
Turni351 – 3544Combined sources
Helixi357 – 37620Combined sources
Helixi377 – 3793Combined sources
Helixi383 – 3853Combined sources
Helixi388 – 41326Combined sources
Beta strandi421 – 4277Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SZIX-ray2.80A191-437[»]
ProteinModelPortaliQ9DBG5.
SMRiQ9DBG5. Positions 206-431.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9DBG5.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili251 – 28434Sequence AnalysisAdd
BLAST
Coiled coili357 – 41054Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the perilipin family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG81115.
GeneTreeiENSGT00500000044795.
HOGENOMiHOG000033816.
HOVERGENiHBG002935.
InParanoidiQ9DBG5.
OMAiQEQSYFV.
OrthoDBiEOG7SN8CD.
PhylomeDBiQ9DBG5.
TreeFamiTF328397.

Family and domain databases

InterProiIPR004279. Perilipin.
[Graphical view]
PANTHERiPTHR14024. PTHR14024. 1 hit.
PfamiPF03036. Perilipin. 1 hit.
[Graphical view]
PIRSFiPIRSF036881. PAT. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9DBG5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSNGTDAPA EAQAAMEEPV VQPSVVDRVA GLPLISSTYG MVSAAYTSTK
60 70 80 90 100
ENYPHVRTVC DVAEKGVKTL TTAAVSTAQP ILSKLEPQIA TASEYAHRGL
110 120 130 140 150
DRLQESLPIL QQPTEKVLAD TKELVSSTVS GAQEMVSSSV SSAKETVATR
160 170 180 190 200
VTGAVDVTLG AVQNSVDKTK SAMTSGVQSV MGSRVGQMVI SGVDRVLVKS
210 220 230 240 250
EAWADNRLPL TEAELALIAT PPEDSDMASL QQQRQEQNYF VRLGSLSERL
260 270 280 290 300
RNHAYEHSLG KLQNARQKAQ ETLQQLTSVL GLMESVKQGV DQRLGEGQEK
310 320 330 340 350
LHQMWLSWNQ KTPQDAEKDP AKPEQVEARA LSMFRDITQQ LQSMCVALGA
360 370 380 390 400
SIQGLPSHVR EQAQQARSQV NDLQATFSGI HSFQDLSAGV LAQTRERIAR
410 420 430
AREALDNTVE YVAQNTPAMW LVGPFAPGIT EKTPEGK
Length:437
Mass (Da):47,262
Last modified:June 1, 2001 - v1
Checksum:iF7CDD3A754A5C04D
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS28901.1.
RefSeqiNP_080112.1. NM_025836.3.
UniGeneiMm.311696.

Genome annotation databases

EnsembliENSMUST00000019726; ENSMUSP00000019726; ENSMUSG00000024197.
GeneIDi66905.
KEGGimmu:66905.
UCSCiuc008dbn.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS28901.1.
RefSeqiNP_080112.1. NM_025836.3.
UniGeneiMm.311696.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SZIX-ray2.80A191-437[»]
ProteinModelPortaliQ9DBG5.
SMRiQ9DBG5. Positions 206-431.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211801. 1 interaction.
IntActiQ9DBG5. 2 interactions.
MINTiMINT-1748486.
STRINGi10090.ENSMUSP00000019726.

PTM databases

PhosphoSiteiQ9DBG5.

2D gel databases

REPRODUCTION-2DPAGEIPI00319270.

Proteomic databases

MaxQBiQ9DBG5.
PaxDbiQ9DBG5.
PRIDEiQ9DBG5.

Protocols and materials databases

DNASUi66905.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000019726; ENSMUSP00000019726; ENSMUSG00000024197.
GeneIDi66905.
KEGGimmu:66905.
UCSCiuc008dbn.1. mouse.

Organism-specific databases

CTDi10226.
MGIiMGI:1914155. Plin3.

Phylogenomic databases

eggNOGiNOG81115.
GeneTreeiENSGT00500000044795.
HOGENOMiHOG000033816.
HOVERGENiHBG002935.
InParanoidiQ9DBG5.
OMAiQEQSYFV.
OrthoDBiEOG7SN8CD.
PhylomeDBiQ9DBG5.
TreeFamiTF328397.

Miscellaneous databases

EvolutionaryTraceiQ9DBG5.
NextBioi322981.
PROiQ9DBG5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DBG5.
CleanExiMM_M6PRBP1.
ExpressionAtlasiQ9DBG5. baseline and differential.
GenevisibleiQ9DBG5. MM.

Family and domain databases

InterProiIPR004279. Perilipin.
[Graphical view]
PANTHERiPTHR14024. PTHR14024. 1 hit.
PfamiPF03036. Perilipin. 1 hit.
[Graphical view]
PIRSFiPIRSF036881. PAT. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiPLIN3_MOUSE
AccessioniPrimary (citable) accession number: Q9DBG5
Secondary accession number(s): Q3TK05, Q8BKV9, Q9CZK1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: June 1, 2001
Last modified: June 24, 2015
This is version 101 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

External Data

Dasty 3

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 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.