ID   PATL1_DANRE             Reviewed;         765 AA.
AC   A2RRV3;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 61.
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; ORFNames=zgc:158239;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235 AND SER-236, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18307296; DOI=10.1021/pr700667w;
RA   Lemeer S., Pinkse M.W.H., Mohammed S., van Breukelen B., den Hertog J.,
RA   Slijper M., Heck A.J.R.;
RT   "Online automated in vivo zebrafish phosphoproteomics: from large-scale
RT   analysis down to a single embryo.";
RL   J. Proteome Res. 7:1555-1564(2008).
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 with ribonucleoprotein complex components.
CC       {ECO:0000250|UniProtKB:Q32N92}.
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   -!- SIMILARITY: Belongs to the PAT1 family. {ECO:0000305}.
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DR   EMBL; BC131868; AAI31869.1; -; mRNA.
DR   RefSeq; NP_001076497.1; NM_001083028.1.
DR   AlphaFoldDB; A2RRV3; -.
DR   SMR; A2RRV3; -.
DR   STRING; 7955.ENSDARP00000091710; -.
DR   iPTMnet; A2RRV3; -.
DR   PaxDb; A2RRV3; -.
DR   PeptideAtlas; A2RRV3; -.
DR   PRIDE; A2RRV3; -.
DR   GeneID; 100009659; -.
DR   KEGG; dre:100009659; -.
DR   CTD; 219988; -.
DR   ZFIN; ZDB-GENE-070209-83; patl1.
DR   eggNOG; KOG4592; Eukaryota.
DR   InParanoid; A2RRV3; -.
DR   OrthoDB; 950451at2759; -.
DR   PhylomeDB; A2RRV3; -.
DR   Reactome; R-DRE-430039; mRNA decay by 5' to 3' exoribonuclease.
DR   PRO; PR:A2RRV3; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
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: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   1: Evidence at protein level;
KW   Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; RNA-binding.
FT   CHAIN           1..765
FT                   /note="Protein PAT1 homolog 1"
FT                   /id="PRO_0000320966"
FT   REGION          1..98
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          119..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          210..244
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..30
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..62
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        68..86
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         235
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18307296"
FT   MOD_RES         236
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18307296"
SQ   SEQUENCE   765 AA;  85940 MW;  19D9BD35016AC7CC CRC64;
     MFRFQSLDDD CTLEEEEGLV EEEDEIDQFN DDTFGAGAID DDWQEEHTRL AELDERVRDV
     LPGAGDSDTS HGGSNAHSSV LPPPSSSSRL YPDIDERGGG DLAESLTRLI LGSDPAIAGV
     GSTSSDRSHL PPMLSAHPPH PSALAGPSSL LRSYQQHQQF LHRGPAPLSQ INSHSIWENS
     MGFSPVSVNS GLIGQKEDKT LLSIIKEVGL PNRPPSLSRD EGRDLSERVP PPRSSSPVIG
     SPPVRAVPIG TPPKQPMSQI LNQQNNHPSA IHVRASVPMR FPPPFPERLS PNNLLSIAKS
     PLSHSPFPAG VNPVLSQIQR AQLLNSQVGQ FQRGPAPPLL QGGVGGFRPF FGQSGPRIGP
     HGPPLGHAPI RHNTTHLHPQ HRRMLSQRMQ NRGDHVGGRG VGERKNRDPY SNLMTQREKE
     WVAKIQMMQL QSTDPYLDDY YYQNYYEKME KRQERDRDNR KEHTTKLITP QVAKLEHTYR
     PVQFAGSLGK LTVSSVNNPR KMIDAVVTSR SDDEEKREKQ VWNKRRQILY TVEKMYSLLL
     EVQDFEKKFL QTPEHQRDVL LEQHKTHTLQ LYNSLREKEW DDRVSDEQCL MIMSVRKGKR
     LISRLLPFLP QPQAAAVVMG IARNLPALAK KDKQDQVLCW LVEPVSVVIQ SMSSTSLTDL
     LQELQGSEGQ LPLVLQNKFG VTLLYLILSE GERMQSSDPN CQLMDDNRWT ELVFSVTREL
     LKVPSSALSS PLFTPPNLVS LFSRYVDRQR LELLQEKLQI TALSR