PR15A_BOVIN
ID PR15A_BOVIN Reviewed; 670 AA.
AC Q2KI51;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Protein phosphatase 1 regulatory subunit 15A;
DE AltName: Full=Growth arrest and DNA damage-inducible protein GADD34;
GN Name=PPP1R15A; Synonyms=GADD34;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Recruits the serine/threonine-protein phosphatase PPP1CA to
CC prevents excessive phosphorylation of the translation initiation factor
CC eIF-2A/EIF2S1, thereby reversing the shut-off of protein synthesis
CC initiated by stress-inducible kinases and facilitating recovery of
CC cells from stress. Down-regulates the TGF-beta signaling pathway by
CC promoting dephosphorylation of TGFB1 by PP1. May promote apoptosis by
CC inducing TP53 phosphorylation on 'Ser-15'. Plays an essential role in
CC autophagy by tuning translation during starvation, thus enabling
CC lysosomal biogenesis and a sustained autophagic flux.
CC {ECO:0000250|UniProtKB:O75807}.
CC -!- SUBUNIT: Interacts with PPP1CA. Interacts with EIF2S1 (By similarity).
CC Interacts with PCNA (By similarity). Interacts with LYN and KMT2A/MLL1.
CC Interacts with PPP1R1A and SMARCB1. Interacts with SMAD7. Interacts
CC with BAG1. Interacts with NOX4 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:O75807}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC membrane protein; Cytoplasmic side {ECO:0000250|UniProtKB:O75807}.
CC Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic
CC side {ECO:0000250|UniProtKB:O75807}. Note=Associates with membranes via
CC an N-terminal amphipathic intramembrane region.
CC {ECO:0000250|UniProtKB:O75807}.
CC -!- PTM: Phosphorylated on tyrosine by LYN; which impairs its
CC antiproliferative activity. {ECO:0000250|UniProtKB:O75807}.
CC -!- PTM: Polyubiquitinated. Exhibits a rapid proteasomal degradation with a
CC half-life under 1 hour, ubiquitination depends on endoplasmic reticulum
CC association. {ECO:0000250|UniProtKB:O75807}.
CC -!- SIMILARITY: Belongs to the PPP1R15 family. {ECO:0000305}.
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DR EMBL; BC112768; AAI12769.2; -; mRNA.
DR RefSeq; NP_001039643.1; NM_001046178.2.
DR AlphaFoldDB; Q2KI51; -.
DR STRING; 9913.ENSBTAP00000001702; -.
DR PaxDb; Q2KI51; -.
DR GeneID; 514688; -.
DR KEGG; bta:514688; -.
DR CTD; 23645; -.
DR eggNOG; ENOG502S745; Eukaryota.
DR InParanoid; Q2KI51; -.
DR OrthoDB; 391948at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0045936; P:negative regulation of phosphate metabolic process; IEA:UniProt.
DR GO; GO:0031400; P:negative regulation of protein modification process; IEA:UniProt.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR InterPro; IPR019523; Prot_Pase1_reg-su15A/B_C.
DR Pfam; PF10488; PP1c_bdg; 1.
PE 2: Evidence at transcript level;
KW Apoptosis; Endoplasmic reticulum; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Phosphoprotein; Reference proteome; Repeat;
KW Stress response; Translation regulation; Ubl conjugation.
FT CHAIN 1..670
FT /note="Protein phosphatase 1 regulatory subunit 15A"
FT /id="PRO_0000320516"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O75807"
FT INTRAMEM 22..39
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O75807"
FT TOPO_DOM 40..670
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O75807"
FT REPEAT 355..381
FT /note="1"
FT REPEAT 396..426
FT /note="2"
FT REPEAT 436..462
FT /note="3"
FT REPEAT 478..511
FT /note="4"
FT REGION 1..60
FT /note="Required for localization in the endoplasmic
FT reticulum"
FT /evidence="ECO:0000250|UniProtKB:O75807"
FT REGION 76..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..511
FT /note="4 X 34 AA approximate repeats"
FT REGION 355..511
FT /note="Interaction with SMAD7"
FT /evidence="ECO:0000250"
FT REGION 484..556
FT /note="Interaction with KMT2A/MLL1"
FT /evidence="ECO:0000250"
FT REGION 537..584
FT /note="Interaction with SMARCB1"
FT /evidence="ECO:0000250"
FT REGION 622..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..343
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..384
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..424
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..463
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..650
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 403
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O75807"
FT MOD_RES 443
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O75807"
FT MOD_RES 513
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O75807"
SQ SEQUENCE 670 AA; 73053 MW; A466F309C301F642 CRC64;
MAPGQMPHQP APWRGTHPLF LLSPLMGLLS RAWSLLRAPG PPEPWLVEAV TEADQGGAGL
EDEAKASLAT YHALWGRHPQ EETKDSGAAE EDREASPGAC PNLEAKHSLP EAWGLSDDDD
EKYGGEEATG VPREQKEFMD GQPAPLPLSL LIRSLPDLPG EEESKEEAVT GGGGNEVTAF
SFPLSHWECC PGEEEEEEEE NGEAVRVCRP VNGATEERTQ TEAATKTSMS PSSVGSHLRA
WECCSGKESE EEEKDKQAEK GDADPGPHFT SLAQRPSLRT WQHPSSAITE EEEDRDSEEM
GASSSVPLTS AFLSDWVYQP EDTEEEDEEE EDCDSEATED EGEAEVSSAT PPPSAFLSAW
VYRPGEDTEE EEDCDSEATE DEGEAEVSSA TPPTSAFLSA WVYQPGDTEE EEDCDSEATE
DEGEAEVSSA TPPPSAFLSA WVYRPGEDTE EEDEYEDEDN ESGAADLGPS PSLQTQSALL
RDQIYQPGEK TDGGEAAEKW GEAESCPFRV AIYLPGEKPP PPWDPPRLPL RLQRRLKSAQ
TPTRHQDLER LLKTRKVRFS EKVSIHPLVV WAGPAQAARR GPWEQFARDR SRFARRIAQV
QEELGPYLTP AARARAWARL GNPPTSLATV PAPTQTSPMT PIQATPLSHA LASPSPPCVS
PSLDLSGRRG
