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O60664 (PLIN3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Perilipin-3
Alternative name(s):
47 kDa mannose 6-phosphate receptor-binding protein
Short name=47 kDa MPR-binding protein
Cargo selection protein TIP47
Mannose-6-phosphate receptor-binding protein 1
Placental protein 17
Short name=PP17
Gene names
Name:PLIN3
Synonyms:M6PRBP1, TIP47
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length434 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. Ref.1

Subunit structure

Homooligomer. Interacts with M6PR (via the cytoplasmic domain). Interacts with IGF2R (via the cytoplasmic domain). Isoform 2 may exist as a homodimer (known as PP17C). Ref.1

Subcellular location

Cytoplasm. Endosome membrane; Peripheral membrane protein; Cytoplasmic side Potential. Lipid droplet Potential. Note: Membrane associated on endosomes. Detected in the envelope and the core of lipid bodies and in lipid sails. Ref.1 Ref.10

Sequence similarities

Belongs to the perilipin family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Q9WMX25EBI-725795,EBI-6863748From a different organism.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O60664-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: PP17b.
Isoform 2 (identifier: O60664-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-183: Missing.
Note: PP17a.
Isoform 3 (identifier: O60664-3)

The sequence of this isoform differs from the canonical sequence as follows:
     321-321: Missing.
Isoform 4 (identifier: O60664-4)

The sequence of this isoform differs from the canonical sequence as follows:
     116-127: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.12
Chain2 – 434433Perilipin-3
PRO_0000099890

Regions

Coiled coil252 – 27726 Potential
Coiled coil353 – 37725 Potential

Amino acid modifications

Modified residue21N-acetylserine Ref.12 Ref.16 Ref.17
Modified residue651N6-acetyllysine Ref.13
Modified residue1301Phosphoserine Ref.11 Ref.14
Modified residue1701Phosphothreonine Ref.11
Modified residue1751Phosphoserine Ref.11
Modified residue1791Phosphoserine Ref.11

Natural variations

Alternative sequence1 – 183183Missing in isoform 2.
VSP_004664
Alternative sequence116 – 12712Missing in isoform 4.
VSP_047038
Alternative sequence3211Missing in isoform 3.
VSP_040325
Natural variant561I → V. Ref.1 Ref.2 Ref.3 Ref.8
Corresponds to variant rs8289 [ dbSNP | Ensembl ].
VAR_022780
Natural variant2751V → A. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.8
Corresponds to variant rs9973235 [ dbSNP | Ensembl ].
VAR_024559

Experimental info

Sequence conflict771G → W in AAD11622. Ref.2
Sequence conflict109 – 1113ILQ → MLR in AAD11622. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 11, 2011. Version 3.
Checksum: 67B2B9CDBC523043

FASTA43447,075
        10         20         30         40         50         60 
MSADGAEADG STQVTVEEPV QQPSVVDRVA SMPLISSTCD MVSAAYASTK ESYPHIKTVC 

        70         80         90        100        110        120 
DAAEKGVRTL TAAAVSGAQP ILSKLEPQIA SASEYAHRGL DKLEENLPIL QQPTEKVLAD 

       130        140        150        160        170        180 
TKELVSSKVS GAQEMVSSAK DTVATQLSEA VDATRGAVQS GVDKTKSVVT GGVQSVMGSR 

       190        200        210        220        230        240 
LGQMVLSGVD TVLGKSEEWA DNHLPLTDAE LARIATSLDG FDVASVQQQR QEQSYFVRLG 

       250        260        270        280        290        300 
SLSERLRQHA YEHSLGKLRA TKQRAQEALL QLSQVLSLME TVKQGVDQKL VEGQEKLHQM 

       310        320        330        340        350        360 
WLSWNQKQLQ GPEKEPPKPE QVESRALTMF RDIAQQLQAT CTSLGSSIQG LPTNVKDQVQ 

       370        380        390        400        410        420 
QARRQVEDLQ ATFSSIHSFQ DLSSSILAQS RERVASAREA LDHMVEYVAQ NTPVTWLVGP 

       430 
FAPGITEKAP EEKK 

« Hide

Isoform 2 [UniParc].

Checksum: 3C7AEC3FBE9429DF
Show »

FASTA25128,158
Isoform 3 [UniParc].

Checksum: 8716B72B11C7FE65
Show »

FASTA43346,947
Isoform 4 [UniParc].

Checksum: DB98F133BF2A206E
Show »

FASTA42245,803

References

« Hide 'large scale' references
[1]"TIP47: a cargo selection device for mannose 6-phosphate receptor trafficking."
Diaz E., Pfeffer S.R.
Cell 93:433-443(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS VAL-56 AND ALA-275, FUNCTION, INTERACTION WITH M6PR AND IGF2R, HOMOOLIGOMERIZATION, SUBCELLULAR LOCATION.
[2]"Cloning and sequence analysis of cDNAs encoding human placental tissue protein 17 (PP17) variants."
Than N.G., Sumegi B., Than G.N., Kispal G., Bohn H.
Eur. J. Biochem. 258:752-757(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANTS VAL-56 AND ALA-275.
Tissue: Placenta.
[3]"Cloning and sequencing of human oncodevelopmental soluble placental tissue protein 17 (PP17): homology with adipophilin and the mouse adipose differentiation-related protein."
Than N.G., Sumegi B., Than G.N., Kispal G., Bohn H.
Tumor Biol. 20:184-192(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANTS VAL-56 AND ALA-275.
Tissue: Placenta.
[4]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ALA-275.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ALA-275.
[6]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), VARIANT ALA-275.
[7]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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] (ISOFORM 1), VARIANTS VAL-56 AND ALA-275.
Tissue: Colon and Muscle.
[9]"Purification and characterization of two new soluble placental tissue proteins (PP13 and PP17)."
Bohn H., Kraus W., Winckler W.
Oncodev. Biol. Med. 4:343-350(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
Tissue: Placenta.
[10]"Spatial integration of TIP47 and adipophilin in macrophage lipid bodies."
Robenek H., Lorkowski S., Schnoor M., Troyer D.
J. Biol. Chem. 280:5789-5794(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[11]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130; THR-170; SER-175 AND SER-179, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[13]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-65, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF057140 mRNA. Translation: AAC39751.1.
AF055574 mRNA. Translation: AAD11622.1.
AF051314 mRNA. Translation: AAD11619.1.
AF051315 mRNA. Translation: AAD11620.1.
BT007235 mRNA. Translation: AAP35899.1.
AK291104 mRNA. Translation: BAF83793.1.
AK223054 mRNA. Translation: BAD96774.1.
AK225045 mRNA. No translation available.
AC027319 Genomic DNA. No translation available.
BC001590 mRNA. Translation: AAH01590.1.
BC005818 mRNA. Translation: AAH05818.1.
BC007566 mRNA. Translation: AAH07566.1.
BC019278 mRNA. Translation: AAH19278.1.
CCDSCCDS12137.1. [O60664-1]
CCDS59337.1. [O60664-4]
CCDS59338.1. [O60664-3]
RefSeqNP_001157661.1. NM_001164189.1. [O60664-3]
NP_001157666.1. NM_001164194.1. [O60664-4]
NP_005808.3. NM_005817.4. [O60664-1]
UniGeneHs.140452.

3D structure databases

ProteinModelPortalO60664.
SMRO60664. Positions 202-427.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115520. 45 interactions.
IntActO60664. 10 interactions.
MINTMINT-5000803.
STRING9606.ENSP00000221957.

Chemistry

DrugBankDB01279. Galsulfase.
DB01271. Idursulfase.

PTM databases

PhosphoSiteO60664.

2D gel databases

REPRODUCTION-2DPAGEIPI00303882.

Proteomic databases

MaxQBO60664.
PaxDbO60664.
PRIDEO60664.

Protocols and materials databases

DNASU10226.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000221957; ENSP00000221957; ENSG00000105355. [O60664-1]
ENST00000585479; ENSP00000465596; ENSG00000105355. [O60664-3]
ENST00000592528; ENSP00000467803; ENSG00000105355. [O60664-4]
GeneID10226.
KEGGhsa:10226.
UCSCuc002mbj.2. human. [O60664-1]
uc002mbl.3. human. [O60664-3]

Organism-specific databases

CTD10226.
GeneCardsGC19M004839.
H-InvDBHIX0014673.
HGNCHGNC:16893. PLIN3.
HPAHPA006427.
MIM602702. gene.
neXtProtNX_O60664.
PharmGKBPA165394001.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG81115.
HOGENOMHOG000033816.
HOVERGENHBG002935.
InParanoidO60664.
OMAQEQSYFV.
OrthoDBEOG7SN8CD.
PhylomeDBO60664.
TreeFamTF328397.

Gene expression databases

ArrayExpressO60664.
BgeeO60664.
CleanExHS_M6PRBP1.
GenevestigatorO60664.

Family and domain databases

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

Other

ChiTaRSPLIN3. human.
GeneWikiM6PRBP1.
GenomeRNAi10226.
NextBio38722.
PMAP-CutDBO60664.
PROO60664.
SOURCESearch...

Entry information

Entry namePLIN3_HUMAN
AccessionPrimary (citable) accession number: O60664
Secondary accession number(s): A8K4Y9 expand/collapse secondary AC list , K7EQF4, Q53G77, Q9BS03, Q9UBD7, Q9UP92
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 11, 2011
Last modified: July 9, 2014
This is version 137 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM