PATL1_RAT
ID PATL1_RAT Reviewed; 770 AA.
AC B5DF93;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Protein PAT1 homolog 1;
DE AltName: Full=PAT1-like protein 1;
DE AltName: Full=Protein PAT1 homolog b;
DE Short=Pat1b;
GN Name=Patl1;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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).
CC -!- FUNCTION: RNA-binding protein involved in deadenylation-dependent
CC decapping of mRNAs, leading to the degradation of mRNAs. Acts as a
CC scaffold protein that connects deadenylation and decapping machinery.
CC Required for cytoplasmic mRNA processing body (P-body) assembly.
CC {ECO:0000250|UniProtKB:Q86TB9}.
CC -!- SUBUNIT: Interacts (via region A) with DDX6/RCK. Interacts (via region
CC H and region C) with LSM1 and LSM4. Interacts (via region N) with
CC DCP1A, DCP2, EDC3, EDC4 and XRN1. Interacts with the CCR4-NOT complex.
CC Interacts with the Lsm-containing SMN-Sm protein complex. Interacts
CC with EIF4ENIF1/4E-T. {ECO:0000250|UniProtKB:Q86TB9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000250|UniProtKB:Q86TB9}.
CC Nucleus {ECO:0000250|UniProtKB:Q86TB9}. Nucleus, PML body
CC {ECO:0000250|UniProtKB:Q86TB9}. Nucleus speckle
CC {ECO:0000250|UniProtKB:Q86TB9}. Note=Predominantly cytoplasmic.
CC Shuttles between the nucleus and the cytoplasm in a CRM1-dependent
CC manner. Enriched in splicing speckles. Localization to nuclear foci and
CC speckles requires active transcription. Excluded from the nucleolus.
CC {ECO:0000250|UniProtKB:Q86TB9}.
CC -!- DOMAIN: The region C, also named Pat-C, is required for RNA-binding and
CC mediates the binding with the Lsm-containing SMN-Sm protein complex and
CC the decapping machinery. It folds into an alpha-alpha superhelix,
CC exposing conserved and basic residues on one side of the domain.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PAT1 family. {ECO:0000305}.
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DR EMBL; CH473953; EDM12901.1; -; Genomic_DNA.
DR EMBL; BC168974; AAI68974.1; -; mRNA.
DR RefSeq; NP_001101990.1; NM_001108520.2.
DR AlphaFoldDB; B5DF93; -.
DR SMR; B5DF93; -.
DR STRING; 10116.ENSRNOP00000059542; -.
DR iPTMnet; B5DF93; -.
DR PhosphoSitePlus; B5DF93; -.
DR jPOST; B5DF93; -.
DR PaxDb; B5DF93; -.
DR PeptideAtlas; B5DF93; -.
DR PRIDE; B5DF93; -.
DR Ensembl; ENSRNOT00000066247; ENSRNOP00000059542; ENSRNOG00000021052.
DR GeneID; 361736; -.
DR KEGG; rno:361736; -.
DR UCSC; RGD:1305514; rat.
DR CTD; 219988; -.
DR RGD; 1305514; Patl1.
DR eggNOG; KOG4592; Eukaryota.
DR GeneTree; ENSGT00520000055649; -.
DR HOGENOM; CLU_009778_1_0_1; -.
DR InParanoid; B5DF93; -.
DR OMA; LPQHPLM; -.
DR OrthoDB; 950451at2759; -.
DR PhylomeDB; B5DF93; -.
DR Reactome; R-RNO-430039; mRNA decay by 5' to 3' exoribonuclease.
DR PRO; PR:B5DF93; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Proteomes; UP000234681; Chromosome 1.
DR Bgee; ENSRNOG00000021052; Expressed in skeletal muscle tissue and 19 other tissues.
DR Genevisible; B5DF93; RN.
DR GO; GO:0030014; C:CCR4-NOT complex; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0000932; C:P-body; ISS:UniProtKB.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0034046; F:poly(G) binding; ISO:RGD.
DR GO; GO:0008266; F:poly(U) RNA binding; ISO:RGD.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; ISS:UniProtKB.
DR GO; GO:0033962; P:P-body assembly; ISS:UniProtKB.
DR InterPro; IPR039900; Pat1-like.
DR InterPro; IPR019167; PAT1_dom.
DR PANTHER; PTHR21551; PTHR21551; 1.
DR Pfam; PF09770; PAT1; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding.
FT CHAIN 1..770
FT /note="Protein PAT1 homolog 1"
FT /id="PRO_0000404575"
FT REGION 1..397
FT /note="Involved in nuclear foci localization"
FT /evidence="ECO:0000250"
FT REGION 1..84
FT /note="Region A; interaction with DDX6/RCK"
FT /evidence="ECO:0000250"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..388
FT /note="Region N; interaction with decapping machinery"
FT /evidence="ECO:0000250"
FT REGION 223..397
FT /note="Involved in RNA-binding"
FT /evidence="ECO:0000250"
FT REGION 320..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..448
FT /note="Region H"
FT /evidence="ECO:0000250"
FT REGION 398..770
FT /note="Involved in nuclear speckle localization"
FT /evidence="ECO:0000250"
FT REGION 449..770
FT /note="Region C"
FT /evidence="ECO:0000250"
FT MOTIF 86..95
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 9..33
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86TB9"
FT MOD_RES 178
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q3TC46"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86TB9"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86TB9"
FT MOD_RES 194
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q86TB9"
FT MOD_RES 217
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q86TB9"
FT MOD_RES 223
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q86TB9"
FT MOD_RES 263
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q86TB9"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86TB9"
FT MOD_RES 284
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q3TC46"
FT MOD_RES 385
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q3TC46"
SQ SEQUENCE 770 AA; 86869 MW; 938B9109B061DB5E CRC64;
MFRYESLEDC PLDEDEDAFQ GLGEEDEEID QFNDDTFGSG AVDDDWQEAH ERLAELEEKL
PVAADEQTGN GERDEMDLLG DHEENLAERL SKMVIENELE DPAVMRAVQT RPVLQPQPGS
LNSSIWDGSE VLRRIRGPLL AQEMPTVSVL EYALPQRPPQ GPEDDRDLSE RALPRRSTSP
IIGSPPVRAV PIGTPPKQMA VPSFNQQILC PKPVHVRPPM PPRYPAPYGE RMSPNQLCSV
PNSSLLGHPF PPSVPPVLSP LQRAQLLGGA QLQPGRMSPS QFARVPGFVG SPLAAMNPKL
LQGRVGQMLP PAPGFRAFFS APPPATPPPQ QHPPGPGPHL QNLRPQAPMF RPDTTHLHPQ
HRRLLHQRQL QSRNQHRNLN GTGDRGGHRV SHQDHLRKDP YANLMLQREK DWVSKIQMMQ
LQSTDPYLDD FYYQNYFEKL EKSSAAEEMQ GDGPKKERTK LITPQVARLE HAYKPVQFEG
SLGKLTVSSV NNPRKMIDAV VTSRSEDDET KEKQVRDKRR KTLVIIEKTY SLLLDVEDYE
RRYLLSLEEE RPALTDERKH KIWSMYDNLR GKLPGQERPS DDHFVQIMCI RKGKRMVARI
LPFLSTEQAA DILMATARNL PFLIKKDAQD EVLPCLLSPF SLLLYHLPSV TVTSLLQQLM
NLPQSATAPA PSNSHLTAVL QNKFGLSLLL ILLSRGEDLH SSDPTVESTQ NNQWTEVMFM
ATQELLRIPQ AALAKPISIP TNLVSLFSRY VDRQKLNLLE TKLQLVQGMR
