PEA15_RAT
ID PEA15_RAT Reviewed; 130 AA.
AC Q5U318; Q78ZC9;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Astrocytic phosphoprotein PEA-15;
DE AltName: Full=15 kDa phosphoprotein enriched in astrocytes;
GN Name=Pea15;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Chneiweiss H.M., Fauquet M.;
RT "High conservation of PEA-15 mRNAs among mammals.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 55-83, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61; SER-90; SER-104 AND
RP SER-116, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Blocks Ras-mediated inhibition of integrin activation and
CC modulates the ERK MAP kinase cascade. Inhibits RPS6KA3 activities by
CC retaining it in the cytoplasm. Inhibits both TNFRSF6- and TNFRSF1A-
CC mediated CASP8 activity and apoptosis. Regulates glucose transport by
CC controlling both the content of SLC2A1 glucose transporters on the
CC plasma membrane and the insulin-dependent trafficking of SLC2A4 from
CC the cell interior to the surface (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds RPS6KA3, MAPK3 and MAPK1. Interacts with CASP8 and FADD.
CC Transient interaction with PLD1 and PLD2 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Associated with microtubules.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated by protein kinase C and calcium-calmodulin-
CC dependent protein kinase. These phosphorylation events are modulated by
CC neurotransmitters or hormones (By similarity). {ECO:0000250}.
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DR EMBL; AJ243949; CAB51573.1; -; mRNA.
DR EMBL; BC085766; AAH85766.1; -; mRNA.
DR RefSeq; NP_001013249.1; NM_001013231.1.
DR AlphaFoldDB; Q5U318; -.
DR BMRB; Q5U318; -.
DR SMR; Q5U318; -.
DR DIP; DIP-57338N; -.
DR IntAct; Q5U318; 2.
DR MINT; Q5U318; -.
DR STRING; 10116.ENSRNOP00000064962; -.
DR iPTMnet; Q5U318; -.
DR PhosphoSitePlus; Q5U318; -.
DR jPOST; Q5U318; -.
DR PaxDb; Q5U318; -.
DR PRIDE; Q5U318; -.
DR Ensembl; ENSRNOT00000111137; ENSRNOP00000091255; ENSRNOG00000046996.
DR GeneID; 364052; -.
DR KEGG; rno:364052; -.
DR CTD; 8682; -.
DR RGD; 1306055; Pea15.
DR eggNOG; KOG3573; Eukaryota.
DR GeneTree; ENSGT00390000000230; -.
DR HOGENOM; CLU_159419_0_0_1; -.
DR InParanoid; Q5U318; -.
DR OMA; VEYRTTV; -.
DR OrthoDB; 1425994at2759; -.
DR PhylomeDB; Q5U318; -.
DR TreeFam; TF332405; -.
DR Reactome; R-RNO-112409; RAF-independent MAPK1/3 activation.
DR Reactome; R-RNO-5673001; RAF/MAP kinase cascade.
DR PRO; PR:Q5U318; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000046996; Expressed in cerebellum and 20 other tissues.
DR Genevisible; Q5U318; RN.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR GO; GO:0000165; P:MAPK cascade; IEA:InterPro.
DR GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; ISO:RGD.
DR GO; GO:0046325; P:negative regulation of glucose import; ISO:RGD.
DR GO; GO:1902043; P:positive regulation of extrinsic apoptotic signaling pathway via death domain receptors; ISO:RGD.
DR GO; GO:0043278; P:response to morphine; IEP:RGD.
DR CDD; cd08338; DED_PEA15; 1.
DR Gene3D; 1.10.533.10; -; 1.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR001875; DED_dom.
DR InterPro; IPR029546; PEA15_DED.
DR Pfam; PF01335; DED; 1.
DR SMART; SM00031; DED; 1.
DR SUPFAM; SSF47986; SSF47986; 1.
DR PROSITE; PS50168; DED; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Cytoplasm; Direct protein sequencing; Phosphoprotein;
KW Reference proteome; Sugar transport; Transport.
FT CHAIN 1..130
FT /note="Astrocytic phosphoprotein PEA-15"
FT /id="PRO_0000252682"
FT DOMAIN 3..81
FT /note="DED"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00065"
FT REGION 98..107
FT /note="Microtubule-binding"
FT /evidence="ECO:0000255"
FT REGION 122..129
FT /note="Microtubule-binding"
FT /evidence="ECO:0000255"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100,
FT ECO:0007744|PubMed:22673903"
SQ SEQUENCE 130 AA; 15040 MW; 8D0F93A40B299FB2 CRC64;
MAEYGTLLQD LTNNITLEDL EQLKSACKED IPSEKSEEIT TGSAWFSFLE SHNKLDKDNL
SYIEHIFEIS RRPDLLTMVV DYRTRVLKIS EEDELDTKLT RIPSAKKYKD IIRQPSEEEI
IKLAPPPKKA
