PUM1_CHICK
ID PUM1_CHICK Reviewed; 1189 AA.
AC Q2VB19; Q5F4A7;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Pumilio homolog 1 {ECO:0000305};
GN Name=PUM1; ORFNames=RCJMB04_1f11 {ECO:0000303|PubMed:15642098};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=White leghorn; TISSUE=Testis;
RX PubMed=17474090; DOI=10.1002/mrd.20765;
RA Lee J.Y., Lim J.M., Kim D.K., Zheng Y.H., Moon S., Han B.K., Song K.D.,
RA Kim H., Han J.Y.;
RT "Identification and gene expression profiling of the Pum1 and Pum2 members
RT of the Pumilio family in the chicken.";
RL Mol. Reprod. Dev. 75:184-190(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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 the CCR4-POP2-NOT
CC deadenylase leading to translational inhibition and mRNA degradation.
CC Also mediates deadenylation-independent repression by promoting
CC accessibility of miRNAs. {ECO:0000250|UniProtKB:Q14671,
CC ECO:0000250|UniProtKB:Q80U78}.
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=Q2VB19-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2VB19-2; Sequence=VSP_029839;
CC -!- TISSUE SPECIFICITY: Detected in embryonic male and female gonads,
CC heart, liver and muscle. Detected in adult brain, testis, ovary, heart,
CC lung, spleen, kidney and muscle. {ECO:0000269|PubMed:17474090}.
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}.
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DR EMBL; DQ275191; ABB83588.1; -; mRNA.
DR EMBL; AJ851393; CAH65027.1; -; mRNA.
DR RefSeq; NP_001012858.1; NM_001012840.2.
DR RefSeq; XP_015153021.1; XM_015297535.1. [Q2VB19-1]
DR AlphaFoldDB; Q2VB19; -.
DR SMR; Q2VB19; -.
DR STRING; 9031.ENSGALP00000000832; -.
DR PaxDb; Q2VB19; -.
DR Ensembl; ENSGALT00000048377; ENSGALP00000046081; ENSGALG00000042598. [Q2VB19-2]
DR Ensembl; ENSGALT00000050930; ENSGALP00000055364; ENSGALG00000042598. [Q2VB19-1]
DR GeneID; 419554; -.
DR KEGG; gga:419554; -.
DR CTD; 9698; -.
DR VEuPathDB; HostDB:geneid_419554; -.
DR eggNOG; KOG1488; Eukaryota.
DR GeneTree; ENSGT00940000158079; -.
DR HOGENOM; CLU_004017_0_0_1; -.
DR InParanoid; Q2VB19; -.
DR OMA; YRNAASS; -.
DR OrthoDB; 207351at2759; -.
DR PhylomeDB; Q2VB19; -.
DR TreeFam; TF318160; -.
DR Reactome; R-GGA-432722; Golgi Associated Vesicle Biogenesis.
DR PRO; PR:Q2VB19; -.
DR Proteomes; UP000000539; Chromosome 23.
DR Bgee; ENSGALG00000042598; Expressed in colon and 13 other tissues.
DR ExpressionAtlas; Q2VB19; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0000932; C:P-body; ISS:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0008344; P:adult locomotory behavior; ISS:UniProtKB.
DR GO; GO:0035196; P:miRNA processing; IBA:GO_Central.
DR GO; GO:0061157; P:mRNA destabilization; ISS:UniProtKB.
DR GO; GO:2000637; P:positive regulation of miRNA-mediated gene silencing; ISS:UniProtKB.
DR GO; GO:0016441; P:post-transcriptional gene silencing; ISS:UniProtKB.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; IBA:GO_Central.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0043488; P:regulation of mRNA stability; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR GO; GO:0048863; P:stem cell differentiation; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; Reference proteome; Repeat; RNA-binding;
KW Translation regulation.
FT CHAIN 1..1189
FT /note="Pumilio homolog 1"
FT /id="PRO_0000312356"
FT DOMAIN 829..1171
FT /note="PUM-HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00318"
FT REPEAT 849..884
FT /note="Pumilio 1"
FT REPEAT 885..920
FT /note="Pumilio 2"
FT REPEAT 921..958
FT /note="Pumilio 3"
FT REPEAT 959..994
FT /note="Pumilio 4"
FT REPEAT 995..1030
FT /note="Pumilio 5"
FT REPEAT 1031..1066
FT /note="Pumilio 6"
FT REPEAT 1067..1102
FT /note="Pumilio 7"
FT REPEAT 1106..1145
FT /note="Pumilio 8"
FT REGION 24..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 743..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 864..868
FT /note="Adenine-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 900..904
FT /note="Uracil-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 936..940
FT /note="Adenine-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 974..978
FT /note="Non-specific-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 1010..1014
FT /note="Adenine-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 1046..1050
FT /note="Uracil-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 1082..1086
FT /note="Guanine-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 1083..1086
FT /note="Guanine-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 1125..1129
FT /note="Uracil-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT COMPBIAS 24..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..774
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 145..240
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15642098"
FT /id="VSP_029839"
FT CONFLICT 719
FT /note="K -> E (in Ref. 2; CAH65027)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1189 AA; 126677 MW; 8DEF142368A9783A CRC64;
MSVACVLKRK AVLWQDSFSP HLKQHAQDTA NPNMPVVLTS GTGSQAQPQP AANQALAAGT
HSSPVPGSIG VAGRSQDDAM VDYFFQRQHG EQLGGGGSGG GGYNNSKHRW PTGDNIHAEH
QVRSMDELNH DFQALALEGR AMGEQLLPGK KFWESDDSSK DGPKGIFLGD QWRDSAWGTS
DHSVSQPIMV QRRPGQGFHV NSEVNSVLSP RSESGGLGVS MVEYVLSSSP GDSCLRKGGF
GPRDAENDEN DKGDKKNKGT FDGDKLGDLK EEGDVMDKTN GLPVQNGIDT DVKDFSRTPG
NCQNSASEVD LLGPNQNGSE GLAQLASTNG AKPVEDFSNI ESQSVPLDPM EHVGMEPLQF
DYSGTQVPVD SAAATVGLFD YNSQQQLFQR PNALAVQQLT AAQQQQYALA AAHQPHIAGL
APAAFVPNPY IISAAPPGTD PYAAGLAAAA TLGPAVVPHQ YYGVTPWGVY PASLFQQQAA
AAAAATNSAN QQTTQQTQQG QQQVLRGGAS QRPLTPNQNQ QGQQTDPLVA AAAVNSALAF
GQGLAAGMPG YPVLAPAAYY DQTGALVVNA GARNGLGAPV RLVAPAPVII SSSAAQAAVA
AAAASANGAA GGLAGTTNGP FRPLGTQQPQ PQPQQQPTNN LASSSFYGNN SLSSNSQSSS
LFSQGSAQPA NTSLGFGSSS SLGATLGSAL GGFGTAVANS NTGSGSRRDS LTGSSDLYKR
TSSSLTPIGH SFYNGLGFSS SPGPVGMPLP SQGPGHSQTP PPSLSSHGSS SSLNLGGLTN
GSGRYISAAP GAEAKYRSAS SASSLFSPSS TLFPSSRLRY GMSDVMPSGR SRLLEDFRNN
RYPNLQLREI AGHIMEFSQD QHGSRFIQLK LERATPAERQ LVFNEILQAA YQLMVDVFGN
YVIQKFFEFG SLEQKLALAE RIRGHVLSLA LQMYGCRVIQ KALEFIPPDQ QVINEMVREL
DGHVLKCVKD QNGNHVVQKC IECVQPQSLQ FIIDAFKGQV FALSTHPYGC RVIQRILEHC
LPEQTLPILE ELHQHTEQLV QDQYGNYVIQ HVLEHGRPED KSKIVAEIRG NVLVLSQHKF
ASNVVEKCVT HASRTERAML IDEVCTMNDG PHSALYTMMK DQYANYVVQK MIDVAEPAQR
KIVMHKIRPH IATLRKYTYG KHILAKLEKY YMKNGVDLGP ICGPPNGII
