PUM2_XENLA
ID PUM2_XENLA Reviewed; 1173 AA.
AC E3WDQ9;
DT 27-MAY-2015, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Pumilio homolog 2 {ECO:0000305};
DE Short=Pumilio-2;
GN Name=pum2;
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], FUNCTION, SUBUNIT, AND PHOSPHORYLATION.
RX PubMed=21098481; DOI=10.1074/jbc.m110.155523;
RA Ota R., Kotani T., Yamashita M.;
RT "Biochemical characterization of Pumilio1 and Pumilio2 in Xenopus
RT oocytes.";
RL J. Biol. Chem. 286:2853-2863(2011).
CC -!- FUNCTION: Sequence-specific RNA-binding protein that acts as a post-
CC transcriptional repressor by binding the 3'-UTR of mRNA targets. Binds
CC to an RNA consensus sequence, the Pumilio Response Element (PRE), 5'-
CC UGUANAUA-3', that is related to the Nanos Response Element (NRE).
CC Mediates post-transcriptional repression of transcripts via different
CC mechanisms: acts via direct recruitment of deadenylase complexes
CC leading to translational inhibition and mRNA degradation
CC (PubMed:21098481). Also mediates deadenylation-independent repression
CC by promoting accessibility of miRNAs. {ECO:0000250|UniProtKB:Q14671,
CC ECO:0000250|UniProtKB:Q80U78, ECO:0000269|PubMed:21098481}.
CC -!- SUBUNIT: Component of a complex with papd4, sympk, tacc3, parn, dazl
CC and cpeb1 (PubMed:21098481). {ECO:0000269|PubMed:21098481}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14671}.
CC Cytoplasm, P-body {ECO:0000250|UniProtKB:Q14671}. Cytoplasmic granule
CC {ECO:0000250|UniProtKB:Q14671}.
CC -!- DOMAIN: The pumilio repeats mediate the association with RNA by packing
CC together to form a right-handed superhelix that approximates a half
CC donut. RNA-binding occurs on the concave side of the surface. Pum2 is
CC composed of 8 pumilio repeats of 36 residues; each repeat binds a
CC single nucleotide in its RNA target. Residues at positions 12 and 16 of
CC the pumilio repeat bind each RNA base via hydrogen bonding or van der
CC Waals contacts with the Watson-Crick edge, while the amino acid at
CC position 13 makes a stacking interaction. The recognition of RNA by
CC pumilio repeats is base specific: cysteine and glutamine at position 12
CC and 16, respectively, bind adenine; asparagine and glutamine bind
CC uracil; and serine and glutamate bind guanine.
CC {ECO:0000250|UniProtKB:Q14671}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:21098481}.
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DR EMBL; AB565475; BAJ41096.1; -; mRNA.
DR RefSeq; NP_001233239.1; NM_001246310.1.
DR AlphaFoldDB; E3WDQ9; -.
DR SMR; E3WDQ9; -.
DR IntAct; E3WDQ9; 1.
DR MaxQB; E3WDQ9; -.
DR GeneID; 100653503; -.
DR KEGG; xla:100653503; -.
DR CTD; 100653503; -.
DR Xenbase; XB-GENE-6486498; pum2.L.
DR OrthoDB; 207351at2759; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Bgee; 100653503; Expressed in blastula and 19 other tissues.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR CDD; cd07920; Pumilio; 1.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR033133; PUM-HD.
DR InterPro; IPR033712; Pumilio_RNA-bd.
DR InterPro; IPR001313; Pumilio_RNA-bd_rpt.
DR Pfam; PF00806; PUF; 8.
DR SMART; SM00025; Pumilio; 8.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50302; PUM; 9.
DR PROSITE; PS50303; PUM_HD; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Reference proteome; Repeat; RNA-binding;
KW Translation regulation.
FT CHAIN 1..1173
FT /note="Pumilio homolog 2"
FT /id="PRO_0000433159"
FT DOMAIN 815..1155
FT /note="PUM-HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00318"
FT REPEAT 835..870
FT /note="Pumilio 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00317"
FT REPEAT 871..906
FT /note="Pumilio 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00317"
FT REPEAT 907..942
FT /note="Pumilio 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00317"
FT REPEAT 943..978
FT /note="Pumilio 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00317"
FT REPEAT 979..1014
FT /note="Pumilio 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00317"
FT REPEAT 1015..1050
FT /note="Pumilio 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00317"
FT REPEAT 1051..1086
FT /note="Pumilio 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00317"
FT REPEAT 1087..1129
FT /note="Pumilio 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00317"
FT REPEAT 1130..1167
FT /note="Pumilio 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00317"
FT REGION 41..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 730..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 850..854
FT /note="Adenine-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 886..890
FT /note="Uracil-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 922..926
FT /note="Adenine-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 958..962
FT /note="Non-specific-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 994..998
FT /note="Adenine-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 1030..1034
FT /note="Uracil-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 1066..1070
FT /note="Guanine-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 1109..1113
FT /note="Uracil-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
SQ SEQUENCE 1173 AA; 127103 MW; 79C67A01718ABD0F CRC64;
MNVPCVVGMN EVAWQESRGI MHASSGQEAL GVGVGMVPSG VSSAGQAHGN NPHAMPPGAP
SAQVPLSGRS QDDATVGYFF QRQAGEQLNG YSNKHRWPTG DSIDAAVRSV DEMNHDFQAL
ALESRGMGEL LPAKKFWEHE DPAKDGQKGM FLADEWRENT WGASHHSMSQ PIMVQRRPGQ
GFHGNHDVAS VLSPRSESGG LGVSMVEYVL SSSPADKLDP RFRKGVFSVR DCELDGPEKG
EQKCKASPFE EEKKRDLISA DTDNVSKLNG RGLPNGIESD CKDFNRTPGS RQASPTEITE
RIGPNSISAE VLGQHQNPMS NKPLSDEFPS TESQNLDGME QVGLHSLQFD YPGNQIQMDS
AGAGVGLFDY NTQQQMFQRQ NALTVQQLTA AQQQQQQFTL AAAQQPHLAG MFSTGLAPAA
FVPNPYIISA GHPGADPYTT LAGPAVVSPQ YYGIPWGVYP AGLFQQQAAA AAQAANSNNQ
QAATQASQGQ QQVMRATSNQ RPLTPNQAQQ GQQPESLAAA NQAQIFGQGL ATSMPGYQLL
TPTAYYDQTG ALVVGPGARA GLAAQVRLVA SAPVLLSPAA AQAATATGAN SLTGATNGMF
RQMGPQQQQQ QQQQQHQQQQ QQPNANLHSN SFYGNSTMSN NSQSSSLFSP GPGQPGSTSL
GFGSSNSLGA AIGSAFGGFG SSVGNSAGSS GSRRDSLSAS CDLYKRSSSS LAAIGQPYYN
SLGFSSSPSP ISMPLPSQTS GHSLTPPPSL SSHGSSSSLH LGGLTNGSGR YFSAAPGAEA
KYRSAANTSS FFSSNSQLFP PSRLRYNRAD IMPSGRSRLL EDFRNNRFPN LQLRDLMGHI
VEFSQDQHGS RFIQQKLERA SPAERQLVFS EILQAAYQLM TDVFGNYVIQ KFFEFGSMDQ
KLALATRIRG HVLPLALQMY GCRVIQKALE SISTDQQSEM VRELDGHVLK CVKDQNGNHV
VQKCIECVTP QSLHFIIEAF KGQVYVLSTH PYGCRVIQRI LEHCTPEQTL PILEELHQST
EQLVQDQYGN YVIQHVLEHG RSDDKSKIVC EVRGQVLVLS QHKFASNVVE KCVTHSSRTE
RAFLIDEICC QNDGPHSALY TMMKDQYANY VVQKMIDMAE PAQRKIIMHK IRPHITTLRK
YTYGKHILAK LEKYYMKNSP DLGLLVGPSN GML
