(data stored in ACNUC7421 zone)

SWISSPROT: PAN3_ASHGO

ID   PAN3_ASHGO              Reviewed;         612 AA.
AC   Q75BU9;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 103.
DE   RecName: Full=PAN2-PAN3 deadenylation complex subunit PAN3 {ECO:0000255|HAMAP-Rule:MF_03181};
DE   AltName: Full=PAB1P-dependent poly(A)-specific ribonuclease {ECO:0000255|HAMAP-Rule:MF_03181};
DE   AltName: Full=Poly(A)-nuclease deadenylation complex subunit 3 {ECO:0000255|HAMAP-Rule:MF_03181};
DE            Short=PAN deadenylation complex subunit 3 {ECO:0000255|HAMAP-Rule:MF_03181};
GN   Name=PAN3 {ECO:0000255|HAMAP-Rule:MF_03181}; OrderedLocusNames=ACR172W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Regulatory subunit of the poly(A)-nuclease (PAN)
CC       deadenylation complex, one of two cytoplasmic mRNA deadenylases
CC       involved in mRNA turnover. PAN specifically shortens poly(A) tails of
CC       RNA and the activity is stimulated by poly(A)-binding protein PAB1. PAN
CC       deadenylation is followed by rapid degradation of the shortened mRNA
CC       tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by
CC       two alternative mechanisms, namely exosome-mediated 3'-5'
CC       exonucleolytic degradation, or deadenlyation-dependent mRNA decaping
CC       and subsequent 5'-3' exonucleolytic degradation by XRN1. May also be
CC       involved in post-transcriptional maturation of mRNA poly(A) tails. PAN3
CC       acts as a positive regulator for PAN activity, recruiting the catalytic
CC       subunit PAN2 to mRNA via its interaction with RNA and with PAB1.
CC       {ECO:0000255|HAMAP-Rule:MF_03181}.
CC   -!- SUBUNIT: Homodimer. Forms a heterotrimer with a catalytic subunit PAN2
CC       to form the poly(A)-nuclease (PAN) deadenylation complex. Interacts
CC       (via PAM-2 motif) with poly(A)-binding protein PAB1 (via PABC domain),
CC       conferring substrate specificity of the enzyme complex.
CC       {ECO:0000255|HAMAP-Rule:MF_03181}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03181}.
CC   -!- DOMAIN: The N-terminal zinc finger binds to poly(A) RNA.
CC       {ECO:0000255|HAMAP-Rule:MF_03181}.
CC   -!- DOMAIN: Contains a pseudokinase domain. The protein kinase domain is
CC       predicted to be catalytically inactive because some of the residues
CC       important for catalytic activity are substituted and it lacks the
CC       equivalent of the binding site for a peptide substrate. However, it has
CC       retained an ATP-binding site and ATP-binding is required for mRNA
CC       degradation, stimulating the activity of the PAN2 nuclease in vitro.
CC       The nucleotide-binding site is juxtaposed to the RNase active site of
CC       PAN2 in the complex and may actually bind nucleosides of a poly(A) RNA
CC       rather than ATP, feeding the poly(A)-tail to the active site of the
CC       deadenylase and thus increasing the efficiency with which this
CC       distributive enzyme degrades oligo(A) RNAs. {ECO:0000255|HAMAP-
CC       Rule:MF_03181}.
CC   -!- DOMAIN: The pseudokinase domain, the coiled-coil (CC), and C-terminal
CC       knob domain (CK) form a structural unit (PKC) that forms an extensive
CC       high-affinity interaction surface for PAN2. {ECO:0000255|HAMAP-
CC       Rule:MF_03181}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. PAN3 family.
CC       {ECO:0000255|HAMAP-Rule:MF_03181}.
DR   EMBL; AE016816; AAS51398.1; -; Genomic_DNA.
DR   RefSeq; NP_983574.1; NM_208927.1.
DR   SMR; Q75BU9; -.
DR   STRING; 33169.AAS51398; -.
DR   EnsemblFungi; AAS51398; AAS51398; AGOS_ACR172W.
DR   GeneID; 4619706; -.
DR   KEGG; ago:AGOS_ACR172W; -.
DR   HOGENOM; HOG000007619; -.
DR   InParanoid; Q75BU9; -.
DR   KO; K12572; -.
DR   OMA; HEYTSEN; -.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:0000932; C:P-body; IBA:GO_Central.
DR   GO; GO:0031251; C:PAN complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008143; F:poly(A) binding; IEA:EnsemblFungi.
DR   GO; GO:0004535; F:poly(A)-specific ribonuclease activity; IEA:EnsemblFungi.
DR   GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IBA:GO_Central.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IBA:GO_Central.
DR   GO; GO:0010606; P:positive regulation of cytoplasmic mRNA processing body assembly; IBA:GO_Central.
DR   GO; GO:0006301; P:postreplication repair; IEA:EnsemblFungi.
DR   HAMAP; MF_03181; PAN3; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR030844; PAN3.
DR   InterPro; IPR041332; Pan3_PK.
DR   InterPro; IPR000571; Znf_CCCH.
DR   PANTHER; PTHR12272; PTHR12272; 1.
DR   Pfam; PF18101; Pan3_PK; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50103; ZF_C3H1; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q75BU9.
DR   SWISS-2DPAGE; Q75BU9.
KW   ATP-binding; Coiled coil; Cytoplasm; Metal-binding; mRNA processing;
KW   Nucleotide-binding; Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..612
FT                   /note="PAN2-PAN3 deadenylation complex subunit PAN3"
FT                   /id="PRO_0000295356"
FT   ZN_FING         10..39
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT   NP_BIND         336..343
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT   NP_BIND         389..390
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT   REGION          231..481
FT                   /note="Pseudokinase domain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT   REGION          521..612
FT                   /note="Knob domain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT   COILED          482..520
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT   MOTIF           84..104
FT                   /note="PABPC-interacting motif-2 (PAM-2)"
FT                   /evidence="ECO:0000305"
FT   MOTIF           111..131
FT                   /note="PABPC-interacting motif-2 (PAM-2)"
FT                   /evidence="ECO:0000305"
FT   BINDING         286
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
SQ   SEQUENCE   612 AA;  67391 MW;  CD7EFA9F06029B00 CRC64;
     MMMNKSKTDW AKDTPCKNIT IYGYCKYEND GCIFNHGKPL STSSNTGGAA AGSAEDSAAS
     GGVTVGNTGK STFNAKTATS FTPSVAIPDF NNIPSFTPER IVSSPAGDGA TAFTPSFNPY
     GSDSFNPSAN VSGPGSAVFA AASGNAGASA TAAPRSQSVH VGTGGYLPLA GTAFPTVYPP
     SHSILQYHLY APDPPPHLQV PLKANERTPE TLFIPNNLRE HLLKRNLSAL QVFPSDGNLP
     DIVGDYFGLV PLEFHNRQTG KGRYLGHQNS LYKVFSNFDG KVYIIRRIHD VKTTDVGQIS
     LPFRKWQKVS CPNVVKVKDA FTTLAFGDSS LCVVHDYYPQ SNSLYETHVA NYTVVPVTQK
     YLWSYLVQLS NALNEVHRHG LSMNNISLDK VIVTGDPGRI KVGDSAVHDI LAFDEGRDIA
     KEQQADYSAV GALLMDLAQR MLGTRDQPLD SMDIDPLFKR VLAYLLSDEK KTIAEFTALF
     SHKMLDIISS SQTYSEYIEQ HLSRELENGR LFRLMCKLNF IFGRMESSMD IHWSEAGDKF
     PIILFYDYVF HQVDENGKSV MDLTHVLRCL NKLDTGVSEK IILVTPDEMN CIIISYKELK
     DSIDSTFRSM TQ
//

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