Full text data of PLIN3
PLIN3
(M6PRBP1, TIP47)
[Confidence: low (only semi-automatic identification from reviews)]
Perilipin-3 (47 kDa mannose 6-phosphate receptor-binding protein; 47 kDa MPR-binding protein; Cargo selection protein TIP47; Mannose-6-phosphate receptor-binding protein 1; Placental protein 17; PP17)
Perilipin-3 (47 kDa mannose 6-phosphate receptor-binding protein; 47 kDa MPR-binding protein; Cargo selection protein TIP47; Mannose-6-phosphate receptor-binding protein 1; Placental protein 17; PP17)
UniProt
O60664
ID PLIN3_HUMAN Reviewed; 434 AA.
AC O60664; A8K4Y9; K7EQF4; Q53G77; Q9BS03; Q9UBD7; Q9UP92;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 11-JAN-2011, sequence version 3.
DT 22-JAN-2014, entry version 131.
DE RecName: Full=Perilipin-3;
DE AltName: Full=47 kDa mannose 6-phosphate receptor-binding protein;
DE Short=47 kDa MPR-binding protein;
DE AltName: Full=Cargo selection protein TIP47;
DE AltName: Full=Mannose-6-phosphate receptor-binding protein 1;
DE AltName: Full=Placental protein 17;
DE Short=PP17;
GN Name=PLIN3; Synonyms=M6PRBP1, TIP47;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS VAL-56 AND ALA-275,
RP FUNCTION, INTERACTION WITH M6PR AND IGF2R, HOMOOLIGOMERIZATION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=9590177; DOI=10.1016/S0092-8674(00)81171-X;
RA Diaz E., Pfeffer S.R.;
RT "TIP47: a cargo selection device for mannose 6-phosphate receptor
RT trafficking.";
RL Cell 93:433-443(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANTS VAL-56 AND
RP ALA-275.
RC TISSUE=Placenta;
RX PubMed=9874244; DOI=10.1046/j.1432-1327.1998.2580752.x;
RA Than N.G., Sumegi B., Than G.N., Kispal G., Bohn H.;
RT "Cloning and sequence analysis of cDNAs encoding human placental
RT tissue protein 17 (PP17) variants.";
RL Eur. J. Biochem. 258:752-757(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANTS VAL-56 AND
RP ALA-275.
RC TISSUE=Placenta;
RX PubMed=10393528; DOI=10.1159/000030062;
RA Than N.G., Sumegi B., Than G.N., Kispal G., Bohn H.;
RT "Cloning and sequencing of human oncodevelopmental soluble placental
RT tissue protein 17 (PP17): homology with adipophilin and the mouse
RT adipose differentiation-related protein.";
RL Tumor Biol. 20:184-192(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP ALA-275.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP ALA-275.
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT
RP ALA-275.
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
RP VAL-56 AND ALA-275.
RC TISSUE=Colon, and Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP CHARACTERIZATION.
RC TISSUE=Placenta;
RX PubMed=6856484;
RA Bohn H., Kraus W., Winckler W.;
RT "Purification and characterization of two new soluble placental tissue
RT proteins (PP13 and PP17).";
RL Oncodev. Biol. Med. 4:343-350(1983).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=15545278; DOI=10.1074/jbc.M407194200;
RA Robenek H., Lorkowski S., Schnoor M., Troyer D.;
RT "Spatial integration of TIP47 and adipophilin in macrophage lipid
RT bodies.";
RL J. Biol. Chem. 280:5789-5794(2005).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130; THR-170; SER-175
RP AND SER-179, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-65, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Required for the transport of mannose 6-phosphate
CC receptors (MPR) from endosomes to the trans-Golgi network.
CC -!- SUBUNIT: Homooligomer. Interacts with M6PR (via the cytoplasmic
CC domain). Interacts with IGF2R (via the cytoplasmic domain).
CC Isoform 2 may exist as a homodimer (known as PP17C).
CC -!- INTERACTION:
CC Q9WMX2:- (xeno); NbExp=5; IntAct=EBI-725795, EBI-6863748;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Endosome membrane; Peripheral
CC membrane protein; Cytoplasmic side (Potential). Lipid droplet
CC (Potential). Note=Membrane associated on endosomes. Detected in
CC the envelope and the core of lipid bodies and in lipid sails.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O60664-1; Sequence=Displayed;
CC Note=PP17b;
CC Name=2;
CC IsoId=O60664-2; Sequence=VSP_004664;
CC Note=PP17a;
CC Name=3;
CC IsoId=O60664-3; Sequence=VSP_040325;
CC Name=4;
CC IsoId=O60664-4; Sequence=VSP_047038;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the perilipin family.
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DR EMBL; AF057140; AAC39751.1; -; mRNA.
DR EMBL; AF055574; AAD11622.1; -; mRNA.
DR EMBL; AF051314; AAD11619.1; -; mRNA.
DR EMBL; AF051315; AAD11620.1; -; mRNA.
DR EMBL; BT007235; AAP35899.1; -; mRNA.
DR EMBL; AK291104; BAF83793.1; -; mRNA.
DR EMBL; AK223054; BAD96774.1; -; mRNA.
DR EMBL; AK225045; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC027319; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001590; AAH01590.1; -; mRNA.
DR EMBL; BC005818; AAH05818.1; -; mRNA.
DR EMBL; BC007566; AAH07566.1; -; mRNA.
DR EMBL; BC019278; AAH19278.1; -; mRNA.
DR RefSeq; NP_001157661.1; NM_001164189.1.
DR RefSeq; NP_001157666.1; NM_001164194.1.
DR RefSeq; NP_005808.3; NM_005817.4.
DR UniGene; Hs.140452; -.
DR ProteinModelPortal; O60664; -.
DR SMR; O60664; 202-427.
DR IntAct; O60664; 10.
DR MINT; MINT-5000803; -.
DR STRING; 9606.ENSP00000221957; -.
DR DrugBank; DB01279; Galsulfase.
DR DrugBank; DB01271; Idursulfase.
DR PhosphoSite; O60664; -.
DR REPRODUCTION-2DPAGE; IPI00303882; -.
DR PaxDb; O60664; -.
DR PRIDE; O60664; -.
DR DNASU; 10226; -.
DR Ensembl; ENST00000221957; ENSP00000221957; ENSG00000105355.
DR Ensembl; ENST00000585479; ENSP00000465596; ENSG00000105355.
DR Ensembl; ENST00000592528; ENSP00000467803; ENSG00000105355.
DR GeneID; 10226; -.
DR KEGG; hsa:10226; -.
DR UCSC; uc002mbj.2; human.
DR CTD; 10226; -.
DR GeneCards; GC19M004839; -.
DR H-InvDB; HIX0014673; -.
DR HGNC; HGNC:16893; PLIN3.
DR HPA; HPA006427; -.
DR MIM; 602702; gene.
DR neXtProt; NX_O60664; -.
DR PharmGKB; PA165394001; -.
DR eggNOG; NOG81115; -.
DR HOGENOM; HOG000033816; -.
DR HOVERGEN; HBG002935; -.
DR InParanoid; O60664; -.
DR OMA; QEQSYFV; -.
DR OrthoDB; EOG7SN8CD; -.
DR PhylomeDB; O60664; -.
DR ChiTaRS; PLIN3; human.
DR GeneWiki; M6PRBP1; -.
DR GenomeRNAi; 10226; -.
DR NextBio; 38722; -.
DR PMAP-CutDB; O60664; -.
DR PRO; PR:O60664; -.
DR ArrayExpress; O60664; -.
DR Bgee; O60664; -.
DR CleanEx; HS_M6PRBP1; -.
DR Genevestigator; O60664; -.
DR GO; GO:0005768; C:endosome; TAS:ProtInc.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; TAS:ProtInc.
DR GO; GO:0005811; C:lipid particle; IDA:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; TAS:ProtInc.
DR InterPro; IPR004279; Perilipin.
DR PANTHER; PTHR14024; PTHR14024; 1.
DR Pfam; PF03036; Perilipin; 1.
DR PIRSF; PIRSF036881; PAT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Complete proteome;
KW Cytoplasm; Endosome; Lipid droplet; Membrane; Phosphoprotein;
KW Polymorphism; Reference proteome; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 434 Perilipin-3.
FT /FTId=PRO_0000099890.
FT COILED 252 277 Potential.
FT COILED 353 377 Potential.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 65 65 N6-acetyllysine.
FT MOD_RES 130 130 Phosphoserine.
FT MOD_RES 170 170 Phosphothreonine.
FT MOD_RES 175 175 Phosphoserine.
FT MOD_RES 179 179 Phosphoserine.
FT VAR_SEQ 1 183 Missing (in isoform 2).
FT /FTId=VSP_004664.
FT VAR_SEQ 116 127 Missing (in isoform 4).
FT /FTId=VSP_047038.
FT VAR_SEQ 321 321 Missing (in isoform 3).
FT /FTId=VSP_040325.
FT VARIANT 56 56 I -> V (in dbSNP:rs8289).
FT /FTId=VAR_022780.
FT VARIANT 275 275 V -> A (in dbSNP:rs9973235).
FT /FTId=VAR_024559.
FT CONFLICT 77 77 G -> W (in Ref. 2; AAD11622).
FT CONFLICT 109 111 ILQ -> MLR (in Ref. 2; AAD11622).
SQ SEQUENCE 434 AA; 47075 MW; 67B2B9CDBC523043 CRC64;
MSADGAEADG STQVTVEEPV QQPSVVDRVA SMPLISSTCD MVSAAYASTK ESYPHIKTVC
DAAEKGVRTL TAAAVSGAQP ILSKLEPQIA SASEYAHRGL DKLEENLPIL QQPTEKVLAD
TKELVSSKVS GAQEMVSSAK DTVATQLSEA VDATRGAVQS GVDKTKSVVT GGVQSVMGSR
LGQMVLSGVD TVLGKSEEWA DNHLPLTDAE LARIATSLDG FDVASVQQQR QEQSYFVRLG
SLSERLRQHA YEHSLGKLRA TKQRAQEALL QLSQVLSLME TVKQGVDQKL VEGQEKLHQM
WLSWNQKQLQ GPEKEPPKPE QVESRALTMF RDIAQQLQAT CTSLGSSIQG LPTNVKDQVQ
QARRQVEDLQ ATFSSIHSFQ DLSSSILAQS RERVASAREA LDHMVEYVAQ NTPVTWLVGP
FAPGITEKAP EEKK
//
ID PLIN3_HUMAN Reviewed; 434 AA.
AC O60664; A8K4Y9; K7EQF4; Q53G77; Q9BS03; Q9UBD7; Q9UP92;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 11-JAN-2011, sequence version 3.
DT 22-JAN-2014, entry version 131.
DE RecName: Full=Perilipin-3;
DE AltName: Full=47 kDa mannose 6-phosphate receptor-binding protein;
DE Short=47 kDa MPR-binding protein;
DE AltName: Full=Cargo selection protein TIP47;
DE AltName: Full=Mannose-6-phosphate receptor-binding protein 1;
DE AltName: Full=Placental protein 17;
DE Short=PP17;
GN Name=PLIN3; Synonyms=M6PRBP1, TIP47;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS VAL-56 AND ALA-275,
RP FUNCTION, INTERACTION WITH M6PR AND IGF2R, HOMOOLIGOMERIZATION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=9590177; DOI=10.1016/S0092-8674(00)81171-X;
RA Diaz E., Pfeffer S.R.;
RT "TIP47: a cargo selection device for mannose 6-phosphate receptor
RT trafficking.";
RL Cell 93:433-443(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANTS VAL-56 AND
RP ALA-275.
RC TISSUE=Placenta;
RX PubMed=9874244; DOI=10.1046/j.1432-1327.1998.2580752.x;
RA Than N.G., Sumegi B., Than G.N., Kispal G., Bohn H.;
RT "Cloning and sequence analysis of cDNAs encoding human placental
RT tissue protein 17 (PP17) variants.";
RL Eur. J. Biochem. 258:752-757(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANTS VAL-56 AND
RP ALA-275.
RC TISSUE=Placenta;
RX PubMed=10393528; DOI=10.1159/000030062;
RA Than N.G., Sumegi B., Than G.N., Kispal G., Bohn H.;
RT "Cloning and sequencing of human oncodevelopmental soluble placental
RT tissue protein 17 (PP17): homology with adipophilin and the mouse
RT adipose differentiation-related protein.";
RL Tumor Biol. 20:184-192(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP ALA-275.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP ALA-275.
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT
RP ALA-275.
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
RP VAL-56 AND ALA-275.
RC TISSUE=Colon, and Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP CHARACTERIZATION.
RC TISSUE=Placenta;
RX PubMed=6856484;
RA Bohn H., Kraus W., Winckler W.;
RT "Purification and characterization of two new soluble placental tissue
RT proteins (PP13 and PP17).";
RL Oncodev. Biol. Med. 4:343-350(1983).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=15545278; DOI=10.1074/jbc.M407194200;
RA Robenek H., Lorkowski S., Schnoor M., Troyer D.;
RT "Spatial integration of TIP47 and adipophilin in macrophage lipid
RT bodies.";
RL J. Biol. Chem. 280:5789-5794(2005).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130; THR-170; SER-175
RP AND SER-179, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-65, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Required for the transport of mannose 6-phosphate
CC receptors (MPR) from endosomes to the trans-Golgi network.
CC -!- SUBUNIT: Homooligomer. Interacts with M6PR (via the cytoplasmic
CC domain). Interacts with IGF2R (via the cytoplasmic domain).
CC Isoform 2 may exist as a homodimer (known as PP17C).
CC -!- INTERACTION:
CC Q9WMX2:- (xeno); NbExp=5; IntAct=EBI-725795, EBI-6863748;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Endosome membrane; Peripheral
CC membrane protein; Cytoplasmic side (Potential). Lipid droplet
CC (Potential). Note=Membrane associated on endosomes. Detected in
CC the envelope and the core of lipid bodies and in lipid sails.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O60664-1; Sequence=Displayed;
CC Note=PP17b;
CC Name=2;
CC IsoId=O60664-2; Sequence=VSP_004664;
CC Note=PP17a;
CC Name=3;
CC IsoId=O60664-3; Sequence=VSP_040325;
CC Name=4;
CC IsoId=O60664-4; Sequence=VSP_047038;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the perilipin family.
CC -----------------------------------------------------------------------
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DR EMBL; AF057140; AAC39751.1; -; mRNA.
DR EMBL; AF055574; AAD11622.1; -; mRNA.
DR EMBL; AF051314; AAD11619.1; -; mRNA.
DR EMBL; AF051315; AAD11620.1; -; mRNA.
DR EMBL; BT007235; AAP35899.1; -; mRNA.
DR EMBL; AK291104; BAF83793.1; -; mRNA.
DR EMBL; AK223054; BAD96774.1; -; mRNA.
DR EMBL; AK225045; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC027319; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001590; AAH01590.1; -; mRNA.
DR EMBL; BC005818; AAH05818.1; -; mRNA.
DR EMBL; BC007566; AAH07566.1; -; mRNA.
DR EMBL; BC019278; AAH19278.1; -; mRNA.
DR RefSeq; NP_001157661.1; NM_001164189.1.
DR RefSeq; NP_001157666.1; NM_001164194.1.
DR RefSeq; NP_005808.3; NM_005817.4.
DR UniGene; Hs.140452; -.
DR ProteinModelPortal; O60664; -.
DR SMR; O60664; 202-427.
DR IntAct; O60664; 10.
DR MINT; MINT-5000803; -.
DR STRING; 9606.ENSP00000221957; -.
DR DrugBank; DB01279; Galsulfase.
DR DrugBank; DB01271; Idursulfase.
DR PhosphoSite; O60664; -.
DR REPRODUCTION-2DPAGE; IPI00303882; -.
DR PaxDb; O60664; -.
DR PRIDE; O60664; -.
DR DNASU; 10226; -.
DR Ensembl; ENST00000221957; ENSP00000221957; ENSG00000105355.
DR Ensembl; ENST00000585479; ENSP00000465596; ENSG00000105355.
DR Ensembl; ENST00000592528; ENSP00000467803; ENSG00000105355.
DR GeneID; 10226; -.
DR KEGG; hsa:10226; -.
DR UCSC; uc002mbj.2; human.
DR CTD; 10226; -.
DR GeneCards; GC19M004839; -.
DR H-InvDB; HIX0014673; -.
DR HGNC; HGNC:16893; PLIN3.
DR HPA; HPA006427; -.
DR MIM; 602702; gene.
DR neXtProt; NX_O60664; -.
DR PharmGKB; PA165394001; -.
DR eggNOG; NOG81115; -.
DR HOGENOM; HOG000033816; -.
DR HOVERGEN; HBG002935; -.
DR InParanoid; O60664; -.
DR OMA; QEQSYFV; -.
DR OrthoDB; EOG7SN8CD; -.
DR PhylomeDB; O60664; -.
DR ChiTaRS; PLIN3; human.
DR GeneWiki; M6PRBP1; -.
DR GenomeRNAi; 10226; -.
DR NextBio; 38722; -.
DR PMAP-CutDB; O60664; -.
DR PRO; PR:O60664; -.
DR ArrayExpress; O60664; -.
DR Bgee; O60664; -.
DR CleanEx; HS_M6PRBP1; -.
DR Genevestigator; O60664; -.
DR GO; GO:0005768; C:endosome; TAS:ProtInc.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; TAS:ProtInc.
DR GO; GO:0005811; C:lipid particle; IDA:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; TAS:ProtInc.
DR InterPro; IPR004279; Perilipin.
DR PANTHER; PTHR14024; PTHR14024; 1.
DR Pfam; PF03036; Perilipin; 1.
DR PIRSF; PIRSF036881; PAT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Complete proteome;
KW Cytoplasm; Endosome; Lipid droplet; Membrane; Phosphoprotein;
KW Polymorphism; Reference proteome; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 434 Perilipin-3.
FT /FTId=PRO_0000099890.
FT COILED 252 277 Potential.
FT COILED 353 377 Potential.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 65 65 N6-acetyllysine.
FT MOD_RES 130 130 Phosphoserine.
FT MOD_RES 170 170 Phosphothreonine.
FT MOD_RES 175 175 Phosphoserine.
FT MOD_RES 179 179 Phosphoserine.
FT VAR_SEQ 1 183 Missing (in isoform 2).
FT /FTId=VSP_004664.
FT VAR_SEQ 116 127 Missing (in isoform 4).
FT /FTId=VSP_047038.
FT VAR_SEQ 321 321 Missing (in isoform 3).
FT /FTId=VSP_040325.
FT VARIANT 56 56 I -> V (in dbSNP:rs8289).
FT /FTId=VAR_022780.
FT VARIANT 275 275 V -> A (in dbSNP:rs9973235).
FT /FTId=VAR_024559.
FT CONFLICT 77 77 G -> W (in Ref. 2; AAD11622).
FT CONFLICT 109 111 ILQ -> MLR (in Ref. 2; AAD11622).
SQ SEQUENCE 434 AA; 47075 MW; 67B2B9CDBC523043 CRC64;
MSADGAEADG STQVTVEEPV QQPSVVDRVA SMPLISSTCD MVSAAYASTK ESYPHIKTVC
DAAEKGVRTL TAAAVSGAQP ILSKLEPQIA SASEYAHRGL DKLEENLPIL QQPTEKVLAD
TKELVSSKVS GAQEMVSSAK DTVATQLSEA VDATRGAVQS GVDKTKSVVT GGVQSVMGSR
LGQMVLSGVD TVLGKSEEWA DNHLPLTDAE LARIATSLDG FDVASVQQQR QEQSYFVRLG
SLSERLRQHA YEHSLGKLRA TKQRAQEALL QLSQVLSLME TVKQGVDQKL VEGQEKLHQM
WLSWNQKQLQ GPEKEPPKPE QVESRALTMF RDIAQQLQAT CTSLGSSIQG LPTNVKDQVQ
QARRQVEDLQ ATFSSIHSFQ DLSSSILAQS RERVASAREA LDHMVEYVAQ NTPVTWLVGP
FAPGITEKAP EEKK
//
MIM
602702
*RECORD*
*FIELD* NO
602702
*FIELD* TI
*602702 PERILIPIN 3; PLIN3
;;MANNOSE 6-PHOSPHATE RECEPTOR-BINDING PROTEIN 1; M6PRBP1;;
read moreMPR-BINDING PROTEIN, 47-KD;;
MPR TAIL-INTERACTING PROTEIN, 47-KD; TIP47
*FIELD* TX
CLONING
Mannose 6-phosphate receptors (MPRs) transport newly synthesized
lysosomal hydrolases from the Golgi to prelysosomes and then return to
the Golgi for another round of transport. Using yeast 2-hybrid analysis
to identify proteins that interact with the cytoplasmic domains of
cation-independent MPR (IGF2R; 147280) and cation-dependent MPR (M6PR;
154540), Diaz and Pfeffer (1998) cloned TIP47. The deduced protein
contains 434 amino acids. Immunoblot analysis showed that it had an
apparent molecular mass of 47 kD.
GENE FUNCTION
Diaz and Pfeffer (1998) showed that TIP47 bound selectively to the
cytoplasmic domains of both cation-independent and cation-dependent
MPRs. TIP47 was present in cytosol and on endosomes and was required for
MPR transport from endosomes to the trans-Golgi network in vitro and in
vivo. TIP47 recognized a phenylalanine/tryptophan signal in the tail of
cation-dependent MPR essential for its proper sorting within the
endosomal pathway. These data suggested that TIP47 binds MPR cytoplasmic
domains and facilitates their collection into transport vesicles
destined for the Golgi.
TIP47 recognizes the cytoplasmic domains of MPRs and is required for
endosome-to-Golgi transport. Carroll et al. (2001) demonstrated that
TIP47 binds directly to the RAB9 GTPase (300284) in its active,
GTP-bound conformation. Moreover, RAB9 increases the affinity of TIP47
for its cargo. A functional RAB9 binding site was required for TIP47
stimulation of MPR transport in vivo. Thus, Carroll et al. (2001)
concluded that a cytosolic cargo selection device may be selectively
recruited onto a specific organelle, and vesicle budding might be
coupled to the presence of an active RAB GTPase.
Aivazian et al. (2006) generated a RAB5 (179512)/RAB9 chimera, which
could bind both RAB5 and RAB9 effectors, and a RAB1 (179508)/RAB9
chimera, which could bind both RAB1 and RAB9 effectors, and examined the
role of effector binding on RAB localization. In both cases, changing
the cellular concentration of the RAB9 effector TIP47 moved a fraction
of the proteins from their parental RAB localization to that of RAB9.
They concluded that effector proteins and RABs rely on one another to
achieve correct steady state localizations.
By mutation and immunoblot analysis, Lopez-Verges et al. (2006) found
that TIP47 acted as a link between the human immunodeficiency virus
(HIV)-1 Gag and Env proteins by binding to the matrix domain of Gag and
to the cytoplasmic tail of the transmembrane gp41 subunit of Env.
Silencing of TIP47 impaired incorporation of Env into Gag particles as
well as HIV-1 infectivity, and it abolished coimmunoprecipitation of Gag
and Env. In contrast, overexpression of TIP47 enhanced incorporation of
Env into virions.
*FIELD* RF
1. Aivazian, D.; Serrano, R. L.; Pfeffer, S.: TIP47 is a key effector
for Rab9 localization. J. Cell Biol. 173: 917-926, 2006.
2. Carroll, K. S.; Hanna, J.; Simon, I.; Krise, J.; Barbero, P.; Pfeffer,
S. R.: Role of Rab9 GTPase in facilitating receptor recruitment by
TIP47. Science 292: 1373-1376, 2001.
3. Diaz, E.; Pfeffer, S. R.: TIP47: a cargo selection device for
mannose 6-phosphate receptor trafficking. Cell 93: 433-443, 1998.
4. Lopez-Verges, S.; Camus, G.; Blot, G.; Beauvoir, R.; Benarous,
R.; Berlioz-Torrent, C.: Tail-interacting protein TIP47 is a connector
between Gag and Env and is required for Env incorporation into HIV-1
virions. Proc. Nat. Acad. Sci. 103: 14947-14952, 2006.
*FIELD* CN
Paul J. Converse - updated: 1/26/2007
Matthew B. Gross - updated: 1/26/2007
Ada Hamosh - updated: 6/7/2001
*FIELD* CD
Stylianos E. Antonarakis: 6/9/1998
*FIELD* ED
mgross: 02/04/2010
mgross: 1/26/2007
alopez: 6/7/2001
terry: 6/7/2001
carol: 6/9/1998
*RECORD*
*FIELD* NO
602702
*FIELD* TI
*602702 PERILIPIN 3; PLIN3
;;MANNOSE 6-PHOSPHATE RECEPTOR-BINDING PROTEIN 1; M6PRBP1;;
read moreMPR-BINDING PROTEIN, 47-KD;;
MPR TAIL-INTERACTING PROTEIN, 47-KD; TIP47
*FIELD* TX
CLONING
Mannose 6-phosphate receptors (MPRs) transport newly synthesized
lysosomal hydrolases from the Golgi to prelysosomes and then return to
the Golgi for another round of transport. Using yeast 2-hybrid analysis
to identify proteins that interact with the cytoplasmic domains of
cation-independent MPR (IGF2R; 147280) and cation-dependent MPR (M6PR;
154540), Diaz and Pfeffer (1998) cloned TIP47. The deduced protein
contains 434 amino acids. Immunoblot analysis showed that it had an
apparent molecular mass of 47 kD.
GENE FUNCTION
Diaz and Pfeffer (1998) showed that TIP47 bound selectively to the
cytoplasmic domains of both cation-independent and cation-dependent
MPRs. TIP47 was present in cytosol and on endosomes and was required for
MPR transport from endosomes to the trans-Golgi network in vitro and in
vivo. TIP47 recognized a phenylalanine/tryptophan signal in the tail of
cation-dependent MPR essential for its proper sorting within the
endosomal pathway. These data suggested that TIP47 binds MPR cytoplasmic
domains and facilitates their collection into transport vesicles
destined for the Golgi.
TIP47 recognizes the cytoplasmic domains of MPRs and is required for
endosome-to-Golgi transport. Carroll et al. (2001) demonstrated that
TIP47 binds directly to the RAB9 GTPase (300284) in its active,
GTP-bound conformation. Moreover, RAB9 increases the affinity of TIP47
for its cargo. A functional RAB9 binding site was required for TIP47
stimulation of MPR transport in vivo. Thus, Carroll et al. (2001)
concluded that a cytosolic cargo selection device may be selectively
recruited onto a specific organelle, and vesicle budding might be
coupled to the presence of an active RAB GTPase.
Aivazian et al. (2006) generated a RAB5 (179512)/RAB9 chimera, which
could bind both RAB5 and RAB9 effectors, and a RAB1 (179508)/RAB9
chimera, which could bind both RAB1 and RAB9 effectors, and examined the
role of effector binding on RAB localization. In both cases, changing
the cellular concentration of the RAB9 effector TIP47 moved a fraction
of the proteins from their parental RAB localization to that of RAB9.
They concluded that effector proteins and RABs rely on one another to
achieve correct steady state localizations.
By mutation and immunoblot analysis, Lopez-Verges et al. (2006) found
that TIP47 acted as a link between the human immunodeficiency virus
(HIV)-1 Gag and Env proteins by binding to the matrix domain of Gag and
to the cytoplasmic tail of the transmembrane gp41 subunit of Env.
Silencing of TIP47 impaired incorporation of Env into Gag particles as
well as HIV-1 infectivity, and it abolished coimmunoprecipitation of Gag
and Env. In contrast, overexpression of TIP47 enhanced incorporation of
Env into virions.
*FIELD* RF
1. Aivazian, D.; Serrano, R. L.; Pfeffer, S.: TIP47 is a key effector
for Rab9 localization. J. Cell Biol. 173: 917-926, 2006.
2. Carroll, K. S.; Hanna, J.; Simon, I.; Krise, J.; Barbero, P.; Pfeffer,
S. R.: Role of Rab9 GTPase in facilitating receptor recruitment by
TIP47. Science 292: 1373-1376, 2001.
3. Diaz, E.; Pfeffer, S. R.: TIP47: a cargo selection device for
mannose 6-phosphate receptor trafficking. Cell 93: 433-443, 1998.
4. Lopez-Verges, S.; Camus, G.; Blot, G.; Beauvoir, R.; Benarous,
R.; Berlioz-Torrent, C.: Tail-interacting protein TIP47 is a connector
between Gag and Env and is required for Env incorporation into HIV-1
virions. Proc. Nat. Acad. Sci. 103: 14947-14952, 2006.
*FIELD* CN
Paul J. Converse - updated: 1/26/2007
Matthew B. Gross - updated: 1/26/2007
Ada Hamosh - updated: 6/7/2001
*FIELD* CD
Stylianos E. Antonarakis: 6/9/1998
*FIELD* ED
mgross: 02/04/2010
mgross: 1/26/2007
alopez: 6/7/2001
terry: 6/7/2001
carol: 6/9/1998