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PAN3_SCHPO
ID   PAN3_SCHPO              Reviewed;         589 AA.
AC   Q9UST1;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 136.
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=ppk26; Synonyms=pan3 {ECO:0000255|HAMAP-Rule:MF_03181};
GN   ORFNames=SPBC336.14c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
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.
CC       ppk26/pan3 acts as a positive regulator for PAN activity, recruiting
CC       the catalytic subunit pan2 to mRNA via its interaction with RNA and
CC       with pab1. {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       ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
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}.
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DR   EMBL; CU329671; CAB58166.1; -; Genomic_DNA.
DR   PIR; T40252; T40252.
DR   RefSeq; NP_596134.1; NM_001022052.2.
DR   AlphaFoldDB; Q9UST1; -.
DR   SMR; Q9UST1; -.
DR   BioGRID; 276763; 47.
DR   STRING; 4896.SPBC336.14c.1; -.
DR   iPTMnet; Q9UST1; -.
DR   MaxQB; Q9UST1; -.
DR   PaxDb; Q9UST1; -.
DR   PRIDE; Q9UST1; -.
DR   EnsemblFungi; SPBC336.14c.1; SPBC336.14c.1:pep; SPBC336.14c.
DR   GeneID; 2540231; -.
DR   KEGG; spo:SPBC336.14c; -.
DR   PomBase; SPBC336.14c; ppk26.
DR   VEuPathDB; FungiDB:SPBC336.14c; -.
DR   eggNOG; KOG3741; Eukaryota.
DR   HOGENOM; CLU_016423_1_0_1; -.
DR   InParanoid; Q9UST1; -.
DR   OMA; IGPHSQN; -.
DR   PhylomeDB; Q9UST1; -.
DR   PRO; PR:Q9UST1; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0000932; C:P-body; IBA:GO_Central.
DR   GO; GO:0031251; C:PAN complex; ISO:PomBase.
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; IBA:GO_Central.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; ISO:PomBase.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   HAMAP; MF_03181; PAN3; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR030844; PAN3.
DR   InterPro; IPR041332; Pan3_PK.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR000571; Znf_CCCH.
DR   PANTHER; PTHR12272; PTHR12272; 2.
DR   Pfam; PF18101; Pan3_PK; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS50103; ZF_C3H1; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Coiled coil; Cytoplasm; Metal-binding; mRNA processing;
KW   Nucleotide-binding; Nucleus; Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..589
FT                   /note="PAN2-PAN3 deadenylation complex subunit pan3"
FT                   /id="PRO_0000256831"
FT   ZN_FING         34..63
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          201..457
FT                   /note="Pseudokinase domain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT   REGION          497..589
FT                   /note="Knob domain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT   COILED          458..496
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT   MOTIF           74..94
FT                   /note="PABPC-interacting motif-2 (PAM-2)"
FT                   /evidence="ECO:0000305"
FT   COMPBIAS        1..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         255
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT   BINDING         302..309
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
SQ   SEQUENCE   589 AA;  67267 MW;  A9835E7FA027DB18 CRC64;
     MSVRKNSPAS PKPTSRSRES SRSPSVTDLK DHSKAKRTLC RNILLYGSCK HSENGCAFRH
     DGPFIPSSEN LEQYSVKKKL NAASASFQPV RALPVKAAGA AVFVPKSQEK SLFLSRERTP
     VALSPGSHAI NPYNNASMLV NEPFHDDSGV YYTRQNQFKP TLYNLYNPQP SPMPTLLPYE
     RTVNGLFIDD TTRERIERKS EASRQTISAL PSIISSYTSL APLNTKLYRY KEQIGFSSWT
     YKCTSSIDGN AYVLKRLQDC SINIDTSTVD KLKNVFHPNI VPFHSAFHTD TFHDSSLLLI
     YDFYPCTTTL GELYLNNSKN SVKLEENRKI PERELWNYFF QLTIALSYLH KSGFACNKLT
     PSRILVDQTE RIRISGCADY ELVVSNKPPL EERKKQDFVD LGVVIANLAT GRTDMDMSSA
     ARAIYSTYSR EFYKAVLYFV SEVPEDKNLE LFLQNHIESF FPIMSSPYVE CEKMERKISD
     AFQHGRFFNI LCKIMFIIDN NRASREYPIA REKEISLIYL LRDYLFHQID EDECPVIDLY
     QVLNRLGKLD AGINQAIALI SRDELDCVSV SYGELKAWLD NVYEMEINS
 
 
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