PATL1_XENLA
ID PATL1_XENLA Reviewed; 718 AA.
AC Q32N92; Q4KLU5; Q6GPP2;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 2.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Protein PAT1 homolog 1;
DE AltName: Full=PAT1-like protein 1;
DE AltName: Full=Protein PAT1 homolog b;
DE Short=Pat1b;
DE Short=xPat1b;
GN Name=patl1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Embryo, and Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION, INTERACTION WITH
RP RIBONUCLEOPROTEIN COMPLEX, TISSUE SPECIFICITY, AND PHOSPHORYLATION AT
RP SER-62.
RX PubMed=20826699; DOI=10.1261/rna.2295410;
RA Marnef A., Maldonado M., Bugaut A., Balasubramanian S., Kress M., Weil D.,
RA Standart N.;
RT "Distinct functions of maternal and somatic Pat1 protein paralogs.";
RL RNA 16:2094-2107(2010).
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 (By
CC similarity). When tethered to a reporter mRNA, able to repress
CC translation (PubMed:20826699). {ECO:0000250|UniProtKB:Q86TB9,
CC ECO:0000269|PubMed:20826699}.
CC -!- SUBUNIT: Interacts with ribonucleoprotein complex components.
CC {ECO:0000269|PubMed:20826699}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:20826699}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q32N92-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q32N92-2; Sequence=VSP_040579;
CC -!- DEVELOPMENTAL STAGE: Only starts to be expressed in late oogenesis
CC (stage IV) and is relatively abundant in eggs and embryos, peaking at
CC embryonic stages 12-20, corresponding to gastrula and neural fold
CC stages. At stage 42, which corresponds to the tadpole-like stage,
CC present in neuron-rich tissues such as eye and brain (at protein
CC level).
CC -!- SIMILARITY: Belongs to the PAT1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH73071.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH73071.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH98995.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI08770.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC098995; AAH98995.1; ALT_INIT; mRNA.
DR EMBL; BC108769; AAI08770.1; ALT_INIT; mRNA.
DR EMBL; BC073071; AAH73071.1; ALT_SEQ; mRNA.
DR RefSeq; XP_018081080.1; XM_018225591.1. [Q32N92-2]
DR AlphaFoldDB; Q32N92; -.
DR SMR; Q32N92; -.
DR iPTMnet; Q32N92; -.
DR GeneID; 443620; -.
DR KEGG; xla:443620; -.
DR CTD; 443620; -.
DR Xenbase; XB-GENE-5808835; patl1.L.
DR OrthoDB; 950451at2759; -.
DR Proteomes; UP000186698; Chromosome 7L.
DR Bgee; 443620; Expressed in egg cell and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0000932; C:P-body; IDA:UniProtKB.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0002151; F:G-quadruplex RNA binding; IDA:MGI.
DR GO; GO:0034046; F:poly(G) binding; IDA:MGI.
DR GO; GO:0008266; F:poly(U) RNA binding; IDA:MGI.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0030371; F:translation repressor activity; IDA:MGI.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; ISS:UniProtKB.
DR GO; GO:0010607; P:negative regulation of cytoplasmic mRNA processing body assembly; IDA:MGI.
DR GO; GO:0017148; P:negative regulation of translation; IDA: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 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding.
FT CHAIN 1..718
FT /note="Protein PAT1 homolog 1"
FT /id="PRO_0000404576"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20826699"
FT VAR_SEQ 238
FT /note="A -> AQ (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_040579"
SQ SEQUENCE 718 AA; 80077 MW; C475BDB026E47832 CRC64;
MESLVDGDGF PDLEEDEDID QFNDDTFGAG AVDDDWREEH ERLAEMEEKL PATHILARVT
SSPINDLLGD QQEELEQSLN QLVRENEEPA LPQGSLTQFS AGMNSSIWDT SRTIRPIRGP
LLMEDMTPLS ILHEYGLATV APPGRDDTER DASERALPRR STSPVIGSPP VRAVPIGTPP
KHGASPNFSH TQVLCPNPIH IRASSAFSGP HNNPASILRH PFPSALSPLQ RAQLLGGAQT
VAAQMSPSQF SRPGLHGPTL ASVAPKLLQG HVGQMVAPVG GGFRPFFGVP SAPGAHIKNM
SLRSQQQFRP DTTHLHPQHR RMLYQRQQNR NQHRGVNGSG GERTCRPAQM ELNRRDPYAG
LMLQREKEWV CRIQLLQLQS TDPYHDDYYY QNYFEKLDKL SVSQDRSREG PKKERTKLIT
PQVAKLEHTY KPVQFEGSLG KLTVSSVNNP RKMIDAVATS RSEEDETREK QVRDKKRQTL
VIIEKMFSLL LDLEDFERRF SLCCEEAEHE VLTEEQKQKL QQLCDTLRGK EVGERVAEEQ
FVQIMCIRKG KRMISRILPL LPLQLAAAVL SIMAHNLLFL IKKDIQDQAL PCLAATCSLV
LCQLSLPALT SLLQNLCGAT SQQQLSSILQ NKFGLTLLYQ ILERGEDLLS SGDPMSQSQP
TWTSLVVQAA HCLLQVSELS LPRPLCSPLT ALAHFSRYLD TQNSSLLQSK LGSTNGTL
