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PAN3_CRYNB
ID   PAN3_CRYNB              Reviewed;         684 AA.
AC   P0CP51; Q55L85; Q5KA98;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 50.
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=CNBJ0990;
OS   Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS   (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=283643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-3501A;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
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}.
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DR   EMBL; AAEY01000049; EAL18457.1; -; Genomic_DNA.
DR   RefSeq; XP_773104.1; XM_768011.1.
DR   AlphaFoldDB; P0CP51; -.
DR   SMR; P0CP51; -.
DR   EnsemblFungi; AAW46022; AAW46022; CNJ02470.
DR   EnsemblFungi; EAL18457; EAL18457; CNBJ0990.
DR   GeneID; 4938439; -.
DR   KEGG; cnb:CNBJ0990; -.
DR   VEuPathDB; FungiDB:CNBJ0990; -.
DR   HOGENOM; CLU_016423_2_0_1; -.
DR   Proteomes; UP000001435; Chromosome 10.
DR   GO; GO:0031251; C:PAN complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IEA:UniProtKB-UniRule.
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; 1.
DR   Pfam; PF18101; Pan3_PK; 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; Zinc; Zinc-finger.
FT   CHAIN           1..684
FT                   /note="PAN2-PAN3 deadenylation complex subunit PAN3"
FT                   /id="PRO_0000410183"
FT   ZN_FING         36..65
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          68..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          112..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          263..544
FT                   /note="Pseudokinase domain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT   REGION          387..412
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          584..684
FT                   /note="Knob domain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT   COILED          545..583
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT   COMPBIAS        19..38
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..142
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         326
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT   BINDING         375..382
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT   BINDING         444..445
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
SQ   SEQUENCE   684 AA;  75082 MW;  C278F58E2770A483 CRC64;
     MLPPPKSAAV QIVRPPSPSS EKAKEKEKKH SPEKRETAQR ICRNVMIYGY CKYQDQGCIY
     YHPPAGADPS TPQNSSPVAH APTPSAPTPL AGTPAREKPT LSIEHLAAPV FVPKGLDSSP
     RASTPSVPTP SAPTPPVWPS LPSTGLLPRQ DVQVSAQPSH AQLSATASPM AYDDPSHIAL
     SAAHAHAQAQ ALTHGILDPH AHAPPVDQSM YLPPRQPLDY NLYAAPLPSI GGNPLYPTHP
     HAFFVSDDLR RAIQAKQEAV YAGANGASAP GLPQELGVYH SLIPLPLPAP TAQCPPTQSQ
     PSKVYGLPSP VYRATSEVDG NTYCLRRVEG FKLVNQLAFA SMDTWRRMRH PNIVGLKEAF
     TTKTFGDNSL IMVYDYHPLS TTLYDEYLSP NPPEPSPASA LANQPPKRRS SPPERILWSY
     VTQIANALKA IHSSGLAVRN LDASKILLTG KNRIRLNGCG VWDVLAFDNK TPVQAFQQED
     LLSFGKLIIS LTCDFFQPTL PFSLPLEHIS RHYSSDLSNL ILYLISKPAQ GQIKSIDEVV
     KMMGPRILNE LDAVQSYADV LENELGAEVE NGRIVRLLTK LGFINERAEF ELDPRWSDTG
     DRYILKLFRD YVFHSVGVDG KPILDLSHVL VCLNKLDAGL DERVMLVSRD DQSCLVVSYR
     EIKHCIEAAF NELKNAGNNH RVHR
 
 
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