Q9DBG5 (PLIN3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Perilipin-3

Alternative name(s):
Cargo selection protein TIP47
Mannose-6-phosphate receptor-binding protein 1

Gene names

Name:	Plin3
Synonyms:	M6prbp1, Tip47

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	437 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Transport
Cellular component	Cytoplasm Endosome Lipid droplet Membrane
Domain	Coiled coil
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell lipid particle Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 437

437

Perilipin-3

PRO_0000099891

Regions

Coiled coil

251 – 284

34

Potential

Coiled coil

357 – 410

54

Potential

Amino acid modifications

Modified residue

65

1

N6-acetyllysine By similarity

Modified residue

130

1

Phosphoserine By similarity

Modified residue

174

1

Phosphothreonine By similarity

Modified residue

179

1

Phosphoserine By similarity

Modified residue

183

1

Phosphoserine By similarity

Secondary structure

1

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437

Helix Strand Turn

Details...

Beta strand

207 – 210

4

Helix

212 – 216

5

Helix

227 – 235

9

Beta strand

239 – 242

4

Helix

243 – 245

3

Helix

248 – 287

40

Helix

324 – 350

27

Turn

351 – 354

4

Helix

357 – 376

20

Helix

377 – 379

3

Helix

383 – 385

3

Helix

388 – 413

26

Beta strand

421 – 427

7

Sequences

	Sequence		Length	Mass (Da)
	Q9DBG5 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: F7CDD3A754A5C04D	FASTA	437	47,262
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	"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.

IPI

IPI00319270.

RefSeq

NP_080112.1. NM_025836.3.

UniGene

Mm.311696.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1SZI	X-ray	2.80	A	191-437	[»]

ProteinModelPortal

Q9DBG5.

SMR

Q9DBG5. Positions 206-431.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9DBG5. 1 interaction.

STRING

10090.ENSMUSP00000019726.

PTM databases

PhosphoSite

Q9DBG5.

2D gel databases

REPRODUCTION-2DPAGE

IPI00319270.

Proteomic databases

PaxDb

Q9DBG5.

PRIDE

Q9DBG5.

Protocols and materials databases

DNASU

66905.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000019726; ENSMUSP00000019726; ENSMUSG00000024197.

GeneID

66905.

KEGG

mmu:66905.

UCSC

uc008dbn.1. mouse.

Organism-specific databases

CTD

10226.

MGI

MGI:1914155. Plin3.

Phylogenomic databases

eggNOG

NOG81115.

GeneTree

ENSGT00500000044795.

HOGENOM

HOG000033816.

HOVERGEN

HBG002935.

InParanoid

Q9DBG5.

OMA

FAPGITE.

OrthoDB

EOG41ZFB4.

Gene expression databases

ArrayExpress

Q9DBG5.

Bgee

Q9DBG5.

CleanEx

MM_M6PRBP1.

Genevestigator

Q9DBG5.

GermOnline

ENSMUSG00000024197. Mus musculus.

Family and domain databases

InterPro

IPR004279. Perilipin.
[Graphical view]

PANTHER

PTHR14024. PTHR14024. 1 hit.

Pfam

PF03036. Perilipin. 1 hit.
[Graphical view]

PIRSF

PIRSF036881. PAT. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q9DBG5.

NextBio

322981.

SOURCE

Search...

Entry information

Entry name

PLIN3_MOUSE

Accession

Primary (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:	April 3, 2013
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program