PAXT1_CAEEL
ID PAXT1_CAEEL Reviewed; 335 AA.
AC Q21738;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Partner of xrn-2 protein 1 {ECO:0000312|WormBase:R05D11.6};
GN Name=paxt-1 {ECO:0000312|WormBase:R05D11.6};
GN ORFNames=R05D11.6 {ECO:0000312|WormBase:R05D11.6};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, INTERACTION WITH XRN-2, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, DOMAIN, AND DISRUPTION PHENOTYPE.
RX PubMed=24462208; DOI=10.1016/j.molcel.2014.01.001;
RA Miki T.S., Richter H., Rueegger S., Grosshans H.;
RT "PAXT-1 promotes XRN2 activity by stabilizing it through a conserved
RT domain.";
RL Mol. Cell 53:351-360(2014).
RN [3] {ECO:0000305, ECO:0007744|PDB:5FIR}
RP X-RAY CRYSTALLOGRAPHY (2.84 ANGSTROMS) OF 2-75 IN COMPLEX WITH XRN-2,
RP FUNCTION, DOMAIN, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF CYS-54 AND
RP TYR-56.
RX PubMed=26779609; DOI=10.1038/nsmb.3155;
RA Richter H., Katic I., Gut H., Grosshans H.;
RT "Structural basis and function of XRN2 binding by XTB domains.";
RL Nat. Struct. Mol. Biol. 23:164-171(2016).
CC -!- FUNCTION: Plays a role in maintenance of steady-state concentration and
CC turnover of microRNAs (miRNA) by degradation of mature miRNA in complex
CC with the exoribonuclease xrn-2 (PubMed:26779609). Stabilizes and
CC enhances the accumulation and activity of the exoribonuclease xrn-2,
CC and thus contributes to miRNA turnover (PubMed:24462208,
CC PubMed:26779609). {ECO:0000269|PubMed:24462208,
CC ECO:0000269|PubMed:26779609}.
CC -!- SUBUNIT: Interacts (via N-terminus) with xrn-2; the interaction is
CC direct. {ECO:0000269|PubMed:24462208, ECO:0000269|PubMed:26779609}.
CC -!- INTERACTION:
CC Q21738; Q9U299: xrn-2; NbExp=5; IntAct=EBI-11705385, EBI-320499;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:24462208}.
CC Nucleus, nucleoplasm {ECO:0000269|PubMed:24462208}.
CC -!- DEVELOPMENTAL STAGE: Ubiquitously expressed throughout development.
CC {ECO:0000269|PubMed:24462208}.
CC -!- DOMAIN: XTBD domain is necessary for interaction with xrn-2.
CC {ECO:0000269|PubMed:24462208, ECO:0000269|PubMed:26779609}.
CC -!- DISRUPTION PHENOTYPE: At 26 degrees Celsius 80% of progeny arrest at
CC the L1 stage of larval development (PubMed:24462208). Reduced xrn-2
CC levels (PubMed:24462208, PubMed:26779609).
CC {ECO:0000269|PubMed:24462208, ECO:0000269|PubMed:26779609}.
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DR EMBL; BX284601; CAA99893.2; -; Genomic_DNA.
DR PIR; T23924; T23924.
DR RefSeq; NP_492325.2; NM_059924.6.
DR PDB; 5FIR; X-ray; 2.84 A; B/D/F/H/J/L=2-75.
DR PDBsum; 5FIR; -.
DR AlphaFoldDB; Q21738; -.
DR SMR; Q21738; -.
DR ComplexPortal; CPX-420; xtbd-paxt-1 complex.
DR DIP; DIP-61981N; -.
DR IntAct; Q21738; 1.
DR STRING; 6239.R05D11.6.1; -.
DR EPD; Q21738; -.
DR PaxDb; Q21738; -.
DR PeptideAtlas; Q21738; -.
DR EnsemblMetazoa; R05D11.6.1; R05D11.6.1; WBGene00011034.
DR UCSC; R05D11.6; c. elegans.
DR WormBase; R05D11.6; CE32473; WBGene00011034; paxt-1.
DR eggNOG; ENOG502S4FT; Eukaryota.
DR GeneTree; ENSGT00940000175672; -.
DR HOGENOM; CLU_051406_0_0_1; -.
DR InParanoid; Q21738; -.
DR OMA; WESDDAW; -.
DR OrthoDB; 1585243at2759; -.
DR SABIO-RK; Q21738; -.
DR PRO; PR:Q21738; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00011034; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005730; C:nucleolus; IDA:WormBase.
DR GO; GO:0005654; C:nucleoplasm; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0010587; P:miRNA catabolic process; EXP:ComplexPortal.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0060965; P:negative regulation of miRNA-mediated gene silencing; EXP:ComplexPortal.
DR InterPro; IPR021859; XTBD.
DR Pfam; PF11952; XTBD; 1.
DR PROSITE; PS51827; XTBD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; mRNA processing; Nucleus; Reference proteome.
FT CHAIN 1..335
FT /note="Partner of xrn-2 protein 1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000437440"
FT DOMAIN 7..91
FT /note="XRN2-binding (XTBD)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01171"
FT REGION 95..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 54
FT /note="C->G: Reduced xrn-2 binding."
FT /evidence="ECO:0000269|PubMed:26779609"
FT MUTAGEN 56
FT /note="Y->A: In xe29; lethal at 26 degrees Celsius at the
FT L1 stage of larval development and abolishes xrn-2
FT binding."
FT /evidence="ECO:0000269|PubMed:26779609"
FT HELIX 3..8
FT /evidence="ECO:0007829|PDB:5FIR"
FT HELIX 17..30
FT /evidence="ECO:0007829|PDB:5FIR"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:5FIR"
FT HELIX 36..50
FT /evidence="ECO:0007829|PDB:5FIR"
FT HELIX 58..68
FT /evidence="ECO:0007829|PDB:5FIR"
FT TURN 69..72
FT /evidence="ECO:0007829|PDB:5FIR"
SQ SEQUENCE 335 AA; 37494 MW; 96C7EDA67AA4CA02 CRC64;
MGKLEDVEAE KKLWESDDAW ELRKAFMLAH YDDYPKIQLQ CLSQLFINVT LLGCEYSQTL
MQKIRTMGAG IAANKDRTKT GSYVKASAAK KRQAVKTSDL EGASDESKKV KMEKSPSPVA
RESFDERLGK LKASLAMTPH HLTGEQMMKT ATNSCLMKWH VNKINQKIEI TIDRYVAFRH
TFSQYCVDPR DCAINTLIES ILSCDAAVHE ESYEIRFDGV PVDECYAKSV TRRLAKIKSA
VSNGAHTVKG LTTYLDAVNM SMIQNTQKLE GWSQQLDLVT ADLLLSSRVL SSTECTKPAM
ATIANQMSED VCQLILNDKI NVINSMKSHS SLAFQ
