PUM3_RAT
ID PUM3_RAT Reviewed; 647 AA.
AC Q562C7; Q4G054;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Pumilio homolog 3 {ECO:0000305};
GN Name=Pum3 {ECO:0000312|RGD:1564753};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver, and Thymus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Inhibits the poly(ADP-ribosyl)ation activity of PARP1 and the
CC degradation of PARP1 by CASP3 following genotoxic stress. Binds to
CC double-stranded RNA or DNA without sequence specificity. Involved in
CC development of the eye and of primordial germ cells.
CC {ECO:0000250|UniProtKB:Q15397, ECO:0000250|UniProtKB:X1WGX5}.
CC -!- SUBUNIT: Interacts with PARP1 (via catalytic domain).
CC {ECO:0000250|UniProtKB:Q15397}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q15397}. Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q15397}. Chromosome
CC {ECO:0000250|UniProtKB:Q15397}. Note=Localizes predominantly in the
CC nucleolus with minor punctate signals in the nucleoplasm.
CC {ECO:0000250|UniProtKB:Q15397}.
CC -!- DOMAIN: A 90 degree bend between Pumilio repeats 3 and 4 gives rise to
CC a L-shaped protein. {ECO:0000250|UniProtKB:Q15397}.
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DR EMBL; BC092579; AAH92579.1; -; mRNA.
DR EMBL; BC098744; AAH98744.2; -; mRNA.
DR RefSeq; NP_001020207.1; NM_001025036.1.
DR RefSeq; XP_006231308.1; XM_006231246.3.
DR AlphaFoldDB; Q562C7; -.
DR SMR; Q562C7; -.
DR STRING; 10116.ENSRNOP00000034834; -.
DR iPTMnet; Q562C7; -.
DR PhosphoSitePlus; Q562C7; -.
DR jPOST; Q562C7; -.
DR PaxDb; Q562C7; -.
DR PRIDE; Q562C7; -.
DR GeneID; 499339; -.
DR KEGG; rno:499339; -.
DR CTD; 9933; -.
DR RGD; 1564753; Pum3.
DR VEuPathDB; HostDB:ENSRNOG00000012574; -.
DR eggNOG; KOG2050; Eukaryota.
DR HOGENOM; CLU_013994_0_1_1; -.
DR InParanoid; Q562C7; -.
DR OMA; WILDDVY; -.
DR OrthoDB; 845051at2759; -.
DR PhylomeDB; Q562C7; -.
DR TreeFam; TF312954; -.
DR PRO; PR:Q562C7; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000012574; Expressed in spleen and 19 other tissues.
DR Genevisible; Q562C7; RN.
DR GO; GO:0005694; C:chromosome; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0010835; P:regulation of protein ADP-ribosylation; ISS:UniProtKB.
DR GO; GO:0006417; P:regulation of translation; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR012959; CPL_dom.
DR InterPro; IPR033133; PUM-HD.
DR InterPro; IPR040059; PUM3.
DR InterPro; IPR001313; Pumilio_RNA-bd_rpt.
DR PANTHER; PTHR13389; PTHR13389; 1.
DR Pfam; PF08144; CPL; 1.
DR SMART; SM00025; Pumilio; 6.
DR SUPFAM; SSF48371; SSF48371; 2.
DR PROSITE; PS50302; PUM; 5.
DR PROSITE; PS50303; PUM_HD; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Chromosome; DNA-binding; Nucleus; Reference proteome; Repeat;
KW RNA-binding.
FT CHAIN 1..647
FT /note="Pumilio homolog 3"
FT /id="PRO_0000075931"
FT DOMAIN 142..509
FT /note="PUM-HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00318"
FT REPEAT 176..211
FT /note="Pumilio 1"
FT /evidence="ECO:0000250|UniProtKB:Q15397"
FT REPEAT 212..247
FT /note="Pumilio 2"
FT /evidence="ECO:0000250|UniProtKB:Q15397"
FT REPEAT 248..276
FT /note="Pumilio 3"
FT /evidence="ECO:0000250|UniProtKB:Q15397"
FT REPEAT 288..324
FT /note="Pumilio 4"
FT /evidence="ECO:0000250|UniProtKB:Q15397"
FT REPEAT 325..360
FT /note="Pumilio 5"
FT /evidence="ECO:0000250|UniProtKB:Q15397"
FT REPEAT 361..396
FT /note="Pumilio 6"
FT /evidence="ECO:0000250|UniProtKB:Q15397"
FT REPEAT 397..434
FT /note="Pumilio 7"
FT /evidence="ECO:0000250|UniProtKB:Q15397"
FT REPEAT 435..503
FT /note="Pumilio 8"
FT /evidence="ECO:0000250|UniProtKB:Q15397"
FT REPEAT 504..550
FT /note="Pumilio 9"
FT /evidence="ECO:0000250|UniProtKB:Q15397"
FT REPEAT 551..595
FT /note="Pumilio 10"
FT /evidence="ECO:0000250|UniProtKB:Q15397"
FT REPEAT 596..635
FT /note="Pumilio 11"
FT /evidence="ECO:0000250|UniProtKB:Q15397"
FT REGION 1..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 105..117
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q15397"
FT COMPBIAS 10..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 33
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BKS9"
SQ SEQUENCE 647 AA; 72786 MW; 59AFDE6F6D502AC6 CRC64;
MEVKGKKKIT GKSPQTSQGK NKFHKNSESS SAKAFPRKAA KEGGPKVTSK NFEKGATKPG
KKRVKQFKNK PQGGKGPKDK FQKANKFNKK RKFQPDGKSD ESAAKKPKWD DFKKKKKELK
QNRQLSDKTN YDVVVRAKHI WESLRRKDCD KEKRVKLMSD LQKLIQGKIK TIAFAHDSTR
VIQCLIQYGS EEQRKWAFEE LQGDLVELSK AKYSRNIVKK FLMYGSKPQI AEIIRSFKGH
VRKMLRHSEA SAIVEYAYND KAILEQRNML TEELYGNTFQ LYKSADHPTL EKVLEVQPGK
LELILDEMKQ ILTPMAQKEA VIKHSLVHKV FLDFFTYAPP KLRSELIEAI REAVVYLAHT
HDGARVAMHC LWHGTPKDRK VIVKTMKTYV EKIANGQYSH LVLLAAFDCI DDTKLVKQII
ISEVISSLPS IVNDKYGRKV LLYLLSPRAP AHLVPEIIQL LQKGDGNAHS KKDTAIRRRE
LLESISPALL SYLQGHTREV VLDKSVCVLV SDILGSATGD AQPAMDAIAG LAAEELYPGG
KDGELHIAEH PAGHLVLKWL IEQDKKIKEN GKEGCFAKTL VECVGMKNLK SWASINRGAI
VLSSLLQSCD QDVVNKVKAG LKTLIPTLEK TKSTSKGIQT LLEKLTA
