PUM1_XENLA
ID PUM1_XENLA Reviewed; 1190 AA.
AC Q66KI6; Q800L7;
DT 27-MAY-2015, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Pumilio homolog 1 {ECO:0000305};
DE Short=Pumilio-1;
DE Short=XPum {ECO:0000303|PubMed:12963108};
GN Name=pum1 {ECO:0000312|Xenbase:XB-GENE-957405};
GN Synonyms=pum1-A {ECO:0000312|EMBL:AAH80379.1};
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] (ISOFORM 2), FUNCTION, RNA-BINDING, TISSUE
RP SPECIFICITY, AND INTERACTION WITH CPEB1-A.
RC TISSUE=Ovary {ECO:0000312|EMBL:BAC57980.1};
RX PubMed=12963108; DOI=10.1016/s0925-4773(03)00160-6;
RA Nakahata S., Kotani T., Mita K., Kawasaki T., Katsu Y., Nagahama Y.,
RA Yamashita M.;
RT "Involvement of Xenopus Pumilio in the translational regulation that is
RT specific to cyclin B1 mRNA during oocyte maturation.";
RL Mech. Dev. 120:865-880(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH80379.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION, SUBUNIT, AND FUNCTION.
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:12963108, PubMed:21098481). Also mediates deadenylation-
CC independent repression by promoting accessibility of miRNAs (By
CC similarity). Acts as a post-transcriptional repressor of ccnb1 mRNA
CC during oocyte maturation (PubMed:12963108).
CC {ECO:0000250|UniProtKB:Q14671, ECO:0000250|UniProtKB:Q80U78,
CC ECO:0000269|PubMed:12963108, ECO:0000269|PubMed:21098481}.
CC -!- SUBUNIT: Interacts with cpeb1-a; interacts with unphosphorylated cpeb1-
CC a but not phosphorylated (PubMed:12963108). Component of a complex with
CC papd4, sympk, tacc3, parn, dazl and cpeb1 (PubMed:21098481).
CC {ECO:0000269|PubMed:12963108, 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q66KI6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q66KI6-2; Sequence=VSP_057677;
CC -!- TISSUE SPECIFICITY: Present in oocytes (at protein level).
CC {ECO:0000269|PubMed:12963108}.
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. Pum1 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. Phosphorylation takes place at the time of
CC dissociation of cpeb1-a from pum1 and the translational activation of
CC ccnb1 mRNA. {ECO:0000269|PubMed:21098481}.
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DR EMBL; AB091091; BAC57980.1; -; mRNA.
DR EMBL; BC080379; AAH80379.1; -; mRNA.
DR RefSeq; NP_001081119.1; NM_001087650.1. [Q66KI6-1]
DR AlphaFoldDB; Q66KI6; -.
DR SMR; Q66KI6; -.
DR IntAct; Q66KI6; 1.
DR DNASU; 394392; -.
DR GeneID; 394392; -.
DR KEGG; xla:394392; -.
DR CTD; 394392; -.
DR Xenbase; XB-GENE-957405; pum1.S.
DR OMA; CANHANA; -.
DR OrthoDB; 207351at2759; -.
DR Proteomes; UP000186698; Chromosome 2S.
DR Bgee; 394392; Expressed in brain 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; 8.
DR PROSITE; PS50303; PUM_HD; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Phosphoprotein; Reference proteome;
KW Repeat; RNA-binding; Translation regulation.
FT CHAIN 1..1190
FT /note="Pumilio homolog 1"
FT /id="PRO_0000433158"
FT DOMAIN 830..1172
FT /note="PUM-HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00318"
FT REPEAT 850..885
FT /note="Pumilio 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00317"
FT REPEAT 886..921
FT /note="Pumilio 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00317"
FT REPEAT 922..959
FT /note="Pumilio 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00317"
FT REPEAT 960..995
FT /note="Pumilio 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00317"
FT REPEAT 996..1031
FT /note="Pumilio 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00317"
FT REPEAT 1032..1067
FT /note="Pumilio 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00317"
FT REPEAT 1068..1103
FT /note="Pumilio 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00317"
FT REPEAT 1107..1146
FT /note="Pumilio 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00317"
FT REGION 38..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 744..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 865..869
FT /note="Adenine-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 901..905
FT /note="Uracil-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 937..941
FT /note="Adenine-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 975..979
FT /note="Non-specific-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 1011..1015
FT /note="Adenine-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 1047..1051
FT /note="Uracil-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 1083..1087
FT /note="Guanine-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 1126..1130
FT /note="Uracil-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT COMPBIAS 617..675
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..777
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 419..423
FT /note="Missing (in isoform 2)"
FT /id="VSP_057677"
FT CONFLICT 641
FT /note="N -> I (in Ref. 1; BAC57980)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1190 AA; 127485 MW; 897F4045D629DAAB CRC64;
MSVACVLKRK TVLWQDSFSP HLKQYPEGTL NHNMPVVLTS GPVGQQQPPQ PPTHSALATG
PHASPVGGSM GVAGRSQDDA MVDYFFQRQH GEQLGGGGSG GGGYNNSKHR WPTGDNIHAE
HQVRSMDELN HDFQALALEG RAMGEQLLTG KKFWETDDSN KDGPKGIFLG DQWRESTWGA
SDHSVSQPIM VQRRPGQGFH VSSEVNSVLS PRSESGGLGV SMVEYVLSSS PGDSCLRKGA
FGPRDTEGDE NEKVDKKNKG VYEGDKLGDL KEEADSMDKC NGLPVQNGID GDVKDFSRTP
GNCQASASEV DLLGSIQNGS EGLVQLTNNN GAKPVEDFGG IESQSVQLDP MEHVGMEPLQ
FDYQGNQVPV DSGAAAVGLF DYNSQQQLFQ RPNALTVQQL TAAQQQQYAL AAAHQQHIGM
FSAGLAPAAF VPNPYIISAA PPGTDPYAAG LAAAATLGPA VVPHQYYGVT PWGVYPANLF
QQQAAAAAAA SNSASQQNNP QSQQGQQQVL RAGGNQRPLT PNQNQQGQQT DQLVAAAAVN
SALAFGQGLA AGMPGYPMLA PAAYYDQTGA LVVNTGARNG LGGPVRLVAP ASVIISQSAA
QAAVAAAAAS ANGPAGTANG PFRQLNSQQP QGQPQPQGNQ NLASSSFYGN SSMNSNSQSS
SLFSQSSGQP GNSSLGFGSS GSLGATLSSA LGGFGTAVAN SNTNSGSRRD SLTGSSDIYK
RTSSSLTPIG HSFYNGLGFS SSPGPVGMPL PSQGPSHSQT PPPSLSSHGS STSLNLGGLT
NGSGRYISAA PGAEAKYRSA SSASSLFSPS STLFPSSRLR YGMSDVMPSG RSRLLEDFRN
NRYPNLQLRE IAGHIMEFSQ DQHGSRFIQL KLERATPAER QLVFNEILQA AYQLMVDVFG
NYVIQKFFEF GSLEQKLALA ERIRGHVLSL ALQMYGCRVI QKALEFIPPD QQVINEMVRE
LDGHVLKCVK DQNGNHVVQK CIECVQPQSL QFIIDAFKSQ VFALSTHPYG CRVIQRILEH
CLPEQTLPIL EELHQHTEQL VQDQYGNYVI QHVLEHGRPE DKSKIVAEIR GNVLVLSQHK
FASNVVEKCV THASRTERAM LIDEVCTMND GPHSALYTMM KDQYANYVVQ KMIDVAEPAQ
RKIVMHKIRP HIATLRKYTY GKHILAKLEK YYMKNGMDLG PMCGPSNGII
