PATL2_XENLA
ID PATL2_XENLA Reviewed; 733 AA.
AC Q4V7K4; Q789A7; Q91817; Q91818;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Protein PAT1 homolog 2;
DE AltName: Full=PAT1-like protein 2;
DE AltName: Full=Protein P100;
DE AltName: Full=Protein PAT1 homolog a;
DE Short=Pat1a;
DE Short=XPat1a;
GN Name=patl2;
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 [MRNA], PROTEIN SEQUENCE OF 381-406; 410-419 AND
RP 505-519, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Ovary;
RX PubMed=1606954; DOI=10.1111/j.1432-1033.1992.tb16973.x;
RA Rother R.P., Frank M.B., Thomas P.S.;
RT "Purification, primary structure, bacterial expression and subcellular
RT distribution of an oocyte-specific protein in Xenopus.";
RL Eur. J. Biochem. 206:673-683(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INTERACTION WITH CPEB.
RX PubMed=17942399; DOI=10.1074/jbc.m704629200;
RA Minshall N., Reiter M.H., Weil D., Standart N.;
RT "CPEB interacts with an ovary-specific eIF4E and 4E-T in early Xenopus
RT oocytes.";
RL J. Biol. Chem. 282:37389-37401(2007).
RN [4]
RP FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=20471969; DOI=10.1016/j.ydbio.2010.05.006;
RA Nakamura Y., Tanaka K.J., Miyauchi M., Huang L., Tsujimoto M.,
RA Matsumoto K.;
RT "Translational repression by the oocyte-specific protein P100 in Xenopus.";
RL Dev. Biol. 344:272-283(2010).
RN [5]
RP FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION, INTERACTION WITH
RP RIBONUCLEOPROTEIN COMPLEX, AND TISSUE SPECIFICITY.
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 that acts as a translational repressor.
CC When overexpressed, able to disperse P-bodies.
CC {ECO:0000269|PubMed:20471969, ECO:0000269|PubMed:20826699}.
CC -!- SUBUNIT: Interacts with ribonucleoprotein complex components. Interacts
CC with cpeb. {ECO:0000269|PubMed:17942399, ECO:0000269|PubMed:20826699}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1606954}. Nucleus
CC {ECO:0000269|PubMed:20826699}.
CC -!- TISSUE SPECIFICITY: Oocyte-specific protein. Expressed throughout
CC oogenesis but is not detectable in eggs, embryos, nor in adult tissues
CC (at protein level). {ECO:0000269|PubMed:1606954,
CC ECO:0000269|PubMed:20826699}.
CC -!- DEVELOPMENTAL STAGE: Already expressed in the smallest stage I oocytes.
CC Then it decreases during oocyte growth until stage VI (at protein
CC level). {ECO:0000269|PubMed:20471969}.
CC -!- SIMILARITY: Belongs to the PAT1 family. {ECO:0000305}.
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DR EMBL; M76720; AAA49921.1; -; mRNA.
DR EMBL; M76721; AAA49922.1; -; mRNA.
DR EMBL; BC097860; AAH97860.1; -; mRNA.
DR PIR; S23468; S23468.
DR RefSeq; NP_001085311.1; NM_001091842.1.
DR AlphaFoldDB; Q4V7K4; -.
DR SMR; Q4V7K4; -.
DR BioGRID; 101894; 9.
DR IntAct; Q4V7K4; 1.
DR PRIDE; Q4V7K4; -.
DR DNASU; 443730; -.
DR GeneID; 443730; -.
DR KEGG; xla:443730; -.
DR CTD; 443730; -.
DR Xenbase; XB-GENE-5892260; patl2.L.
DR OrthoDB; 950451at2759; -.
DR Proteomes; UP000186698; Chromosome 2L.
DR Bgee; 443730; Expressed in ovary and 7 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000932; C:P-body; IDA:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; IPI:UniProtKB.
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; IEA:InterPro.
DR GO; GO:0010607; P:negative regulation of cytoplasmic mRNA processing body assembly; TAS:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; IDA: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; Direct protein sequencing; Nucleus; Reference proteome;
KW RNA-binding.
FT CHAIN 1..733
FT /note="Protein PAT1 homolog 2"
FT /id="PRO_0000404579"
FT REGION 42..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 38
FT /note="V -> W (in Ref. 1; AAA49921/AAA49922)"
FT /evidence="ECO:0000305"
FT CONFLICT 602
FT /note="T -> P (in Ref. 1; AAA49922)"
FT /evidence="ECO:0000305"
FT CONFLICT 604
FT /note="I -> F (in Ref. 1; AAA49921)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 733 AA; 83391 MW; E4BDA0991895FDD1 CRC64;
MNLGSEQILP EDFYLAEEGA LLEEMAEEDE EIDLYNEVTF GLDQESDEEP VKLEDDHTKP
IQMPEAPKEE EPEALQPVKE AKGSEKAPLH EVKIVVEPHE DHVDLSIDSG GHTMNSTMDD
SELGDPAVMK AFHGKPTLES LDSAVVDSGI GSTWSELDTD YDQSGMDSGL WEASPKVSTY
ATGQILEDKA ILRIMERAPY LPPTNLEFLG SPLQRGFMPS QRLQGPEMGA MSPKPYRPRF
MRQQSPLVPR SMRPSYPFTP PRRGPSVFAP NQSPGFVSQT PFRPMSPNVS TPTRPMTPKM
VRMHFGPMSP SPSFSPFFSP MGNALQRFKV PGHVTQLHPQ HRRILSQRQR PQSSSRRQWE
SRPDPYASLM SQKEKEWVIK LQMIQLQSEN PHLDDYYYQA YYENLERKLS EEEFLGERKK
REPTKLVTPY IQKAETYESV VHIEGSLGQV AVSTCYSPRR AIDAVSYAMP DEAIKALGYQ
RLRVLKHAEK VFLMFLEVEE LARKMSHIPE EEHVHFQHKQ NYKVQRIYDV LKIAPCHNEE
ESEFLQLLQV GKGKKLVARL LPFLRSEQAR EILLLVVQHL TFLIKNDSAE ESLSVLYGPL
KTIINGLSFT ELIGVTQELT RPLPESNDLP LTLAFQNQFG ISLLYCLLSH GERLLSSDLP
MEPCIGDFEK WTDTVFLVAK ELSHVSKSSM VEPLFLPSNL LSLFCRYLDK QTIHKLEDKM
ECPVIPPYTA VPS
