PATL1_MOUSE
ID PATL1_MOUSE Reviewed; 770 AA.
AC Q3TC46; Q3TD30; Q3U4Q3; Q3UD09; Q6PD49; Q8BN50; Q8C3S7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 102.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, Eye, and Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-178; SER-179 AND SER-184, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177; SER-179 AND SER-184, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-217; ARG-223; ARG-263; ARG-284
RP AND ARG-385, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
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; AK085013; BAC39337.1; -; mRNA.
DR EMBL; AK087559; BAC39927.1; -; mRNA.
DR EMBL; AK150301; BAE29453.1; -; mRNA.
DR EMBL; AK154102; BAE32378.1; -; mRNA.
DR EMBL; AK170408; BAE41774.1; -; mRNA.
DR EMBL; AK170745; BAE41998.1; -; mRNA.
DR EMBL; AK170918; BAE42111.1; -; mRNA.
DR EMBL; BC058941; AAH58941.1; -; mRNA.
DR CCDS; CCDS37924.1; -.
DR RefSeq; NP_766223.2; NM_172635.3.
DR AlphaFoldDB; Q3TC46; -.
DR SMR; Q3TC46; -.
DR BioGRID; 230453; 1.
DR STRING; 10090.ENSMUSP00000060398; -.
DR iPTMnet; Q3TC46; -.
DR PhosphoSitePlus; Q3TC46; -.
DR EPD; Q3TC46; -.
DR jPOST; Q3TC46; -.
DR MaxQB; Q3TC46; -.
DR PaxDb; Q3TC46; -.
DR PeptideAtlas; Q3TC46; -.
DR PRIDE; Q3TC46; -.
DR ProteomicsDB; 287888; -.
DR Antibodypedia; 49853; 90 antibodies from 20 providers.
DR DNASU; 225929; -.
DR Ensembl; ENSMUST00000061618; ENSMUSP00000060398; ENSMUSG00000046139.
DR GeneID; 225929; -.
DR KEGG; mmu:225929; -.
DR UCSC; uc008gth.2; mouse.
DR CTD; 219988; -.
DR MGI; MGI:2147679; Patl1.
DR VEuPathDB; HostDB:ENSMUSG00000046139; -.
DR eggNOG; KOG4592; Eukaryota.
DR GeneTree; ENSGT00520000055649; -.
DR HOGENOM; CLU_009778_1_0_1; -.
DR InParanoid; Q3TC46; -.
DR OMA; LPQHPLM; -.
DR OrthoDB; 950451at2759; -.
DR PhylomeDB; Q3TC46; -.
DR TreeFam; TF323322; -.
DR Reactome; R-MMU-430039; mRNA decay by 5' to 3' exoribonuclease.
DR BioGRID-ORCS; 225929; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Patl1; mouse.
DR PRO; PR:Q3TC46; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q3TC46; protein.
DR Bgee; ENSMUSG00000046139; Expressed in embryonic post-anal tail and 225 other tissues.
DR ExpressionAtlas; Q3TC46; baseline and differential.
DR Genevisible; Q3TC46; MM.
DR GO; GO:0030014; C:CCR4-NOT complex; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
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:0002151; F:G-quadruplex RNA binding; ISO:MGI.
DR GO; GO:0034046; F:poly(G) binding; ISO:MGI.
DR GO; GO:0008266; F:poly(U) RNA binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0030371; F:translation repressor activity; ISO:MGI.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; ISS:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; ISO:MGI.
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 1: Evidence at protein level;
KW Cytoplasm; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding.
FT CHAIN 1..770
FT /note="Protein PAT1 homolog 1"
FT /id="PRO_0000320964"
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 155..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..397
FT /note="Involved in RNA-binding"
FT /evidence="ECO:0000250"
FT REGION 319..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..396
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:0007744|PubMed:21183079"
FT MOD_RES 178
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 194
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q86TB9"
FT MOD_RES 217
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 223
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 263
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86TB9"
FT MOD_RES 284
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 385
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CONFLICT 10
FT /note="C -> W (in Ref. 1; BAC39337)"
FT /evidence="ECO:0000305"
FT CONFLICT 13
FT /note="D -> H (in Ref. 1; BAC39337)"
FT /evidence="ECO:0000305"
FT CONFLICT 17
FT /note="D -> H (in Ref. 1; BAC39337)"
FT /evidence="ECO:0000305"
FT CONFLICT 20
FT /note="Q -> Y (in Ref. 1; BAC39337)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="N -> S (in Ref. 1; BAE41774)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="Q -> H (in Ref. 1; BAE32378)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="R -> G (in Ref. 1; BAC39927)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="P -> T (in Ref. 1; BAE32378)"
FT /evidence="ECO:0000305"
FT CONFLICT 389
FT /note="Q -> R (in Ref. 1; BAE42111/BAE32378)"
FT /evidence="ECO:0000305"
FT CONFLICT 698
FT /note="D -> G (in Ref. 1; BAE29453)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 770 AA; 86770 MW; 3F3E0A2E3DB54566 CRC64;
MFRYESLEDC PLDEDEDAFQ GLGEEDEEID QFNDDTFGSG AVDDDWQEAH ERLAELEEKL
PVAADEQTGN GERDEMDLLG DHEENLAERL SKMVIENELE DPAIMRAVQT RPVLQPQPGS
LNSSIWDGSE VLRRIRGPLL AQEMPTVSVL EYALPQRPLQ GPEDDRDLSE RALPRRSTSP
IIGSPPVRAV PIGTPPKQMA VPSFNQQILC PKPVHVRPPM PPRYPAPYGE RISPNQLCSV
PNSSLLGHPF PPNVPPVLSP LQRAQLLGGA QLQPGRMSPS QFARVPGFVG SPLAAMNPKL
LQGRVGQMLP PAPSFRAFFS APPPATPPPQ QHPPGPGPHL QNLRPQAPMF RADTTHLHPQ
HRRLLHQRQL QSRNQHRNLN GTGDRGGHQS SHQDHLRKDP YANLMLQREK DWVSKIQMMQ
LQSTDPYLDD FYYQNYFEKL EKLSAAEEIQ GDGPKKERTK LITPQVAKLE HAYQPVQFEG
SLGKLTVSSV NNPRKMIDAV VTSRSEDDET KEKQVRDKRR KTLVIIEKTY SLLLDVEDYE
RRYLLSLEEE RPALMDERKH KICSMYDNLR GKLPGQERPS DDHFVQIMCI RKGKRMVARI
LPFLSTEQAA DILMATARNL PFLIKKDAQD EVLPCLLSPF SLLLYHLPSV TVTSLLQQLM
NLPQSASAPA PSNSHLTAVL QNKFGLSLLL ILLSRGEDLQ SSDPAIESTQ NNQWTEVMFM
ATRELLRIPQ AALAKPISIP TNLVSLFSRY VDRQKLNLLE TKLQLVQGIR
