PABP_CANAL
ID PABP_CANAL Reviewed; 629 AA.
AC Q5AI15; A0A1D8PD14;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Polyadenylate-binding protein, cytoplasmic and nuclear;
DE Short=PABP;
DE Short=Poly(A)-binding protein;
DE AltName: Full=Polyadenylate tail-binding protein;
GN Name=PAB1; OrderedLocusNames=CAALFM_C103370WA;
GN ORFNames=CaO19.10555, CaO19.3037;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
CC -!- FUNCTION: Binds the poly(A) tail of mRNA. Appears to be an important
CC mediator of the multiple roles of the poly(A) tail in mRNA biogenesis,
CC stability and translation. In the nucleus, involved in both mRNA
CC cleavage and polyadenylation. Is also required for efficient mRNA
CC export to the cytoplasm. Acts in concert with a poly(A)-specific
CC nuclease (PAN) to affect poly(A) tail shortening, which may occur
CC concomitantly with either nucleocytoplasmic mRNA transport or
CC translational initiation. In the cytoplasm, stimulates translation
CC initiation and regulates mRNA decay through translation termination-
CC coupled poly(A) shortening, probably mediated by PAN (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the polyadenylate-binding protein type-1 family.
CC {ECO:0000305}.
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DR EMBL; CP017623; AOW26018.1; -; Genomic_DNA.
DR RefSeq; XP_721535.1; XM_716442.2.
DR AlphaFoldDB; Q5AI15; -.
DR SMR; Q5AI15; -.
DR BioGRID; 1219985; 2.
DR STRING; 237561.Q5AI15; -.
DR PRIDE; Q5AI15; -.
DR GeneID; 3636891; -.
DR KEGG; cal:CAALFM_C103370WA; -.
DR CGD; CAL0000195952; orf19.10555.
DR VEuPathDB; FungiDB:C1_03370W_A; -.
DR eggNOG; KOG0123; Eukaryota.
DR HOGENOM; CLU_012062_22_4_1; -.
DR InParanoid; Q5AI15; -.
DR OrthoDB; 1027234at2759; -.
DR PRO; PR:Q5AI15; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0010494; C:cytoplasmic stress granule; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0005840; C:ribosome; IEA:EnsemblFungi.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:0008143; F:poly(A) binding; IBA:GO_Central.
DR GO; GO:0008266; F:poly(U) RNA binding; IBA:GO_Central.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IEA:EnsemblFungi.
DR GO; GO:0034236; F:protein kinase A catalytic subunit binding; IEA:EnsemblFungi.
DR GO; GO:0008428; F:ribonuclease inhibitor activity; IEA:EnsemblFungi.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0060211; P:regulation of nuclear-transcribed mRNA poly(A) tail shortening; IEA:EnsemblFungi.
DR GO; GO:0006446; P:regulation of translational initiation; IEA:EnsemblFungi.
DR CDD; cd12379; RRM2_I_PABPs; 1.
DR Gene3D; 3.30.70.330; -; 4.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR036053; PABP-dom.
DR InterPro; IPR006515; PABP_1234.
DR InterPro; IPR002004; PABP_HYD.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR045305; RRM2_I_PABPs.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003954; RRM_dom_euk.
DR Pfam; PF00658; PABP; 1.
DR Pfam; PF00076; RRM_1; 4.
DR SMART; SM00517; PolyA; 1.
DR SMART; SM00360; RRM; 4.
DR SMART; SM00361; RRM_1; 4.
DR SUPFAM; SSF54928; SSF54928; 2.
DR SUPFAM; SSF63570; SSF63570; 1.
DR TIGRFAMs; TIGR01628; PABP-1234; 1.
DR PROSITE; PS51309; PABC; 1.
DR PROSITE; PS50102; RRM; 4.
PE 3: Inferred from homology;
KW Cytoplasm; mRNA processing; mRNA transport; Nucleus; Reference proteome;
KW Repeat; RNA-binding; Translation regulation; Transport.
FT CHAIN 1..629
FT /note="Polyadenylate-binding protein, cytoplasmic and
FT nuclear"
FT /id="PRO_0000295384"
FT DOMAIN 52..130
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 140..217
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 233..310
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 336..413
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 537..618
FT /note="PABC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00641"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 629 AA; 70418 MW; 0B375DF3980C10D9 CRC64;
MSAAETNQLQ ESMEKLNIGS TTEEQSAAAA TTTADQSAEE QGESSGVAEN SASLYVGELN
PSVNEATLFE IFSPIGQVSS IRVCRDAVSK KSLGYAYVNY HKYEDGEKAI EELNYNPIEG
RPCRIMWSQR DPSARRSGDG NIFIKNLHPA IDNKALHDTF SAFGKILSCK VATDEFGQSK
CFGFVHYETA EAAEAAIENV NGMLLNDREV FVGKHISKKD RESKFEEMKA NFTNIYVKNI
DLNYSEESFE KLFSPFGKIT SIYLEKDQDG KSKGFGFVNF EDHESAVKAV EELNDKEING
QKIYVGRAQK KRERLEELKK QYEAVRLEKL AKYQGVNLFV KNLDDTIDSE KLEEEFKPFG
TITSAKVMVD EAGKSKGFGF VCFTTPEEAT KAITEMNTRM INGKPLYVAL AQRKDVRRSQ
LEQQIQARNQ MRMQNAAAGG LPGQFIPPMF YGQQGFFPPN GRGNAPYPGP NPQMMMRGRG
QPFPEQWPRP GPNGQPVPVY GIPPQFQQDF NGQNMRPQQQ QQQQPRGGYY PNRNQTSKRD
LAAIISSVPQ DQQKRILGEE LYPKIVATGK AQEPEAAGKI TGMMLGLENQ EILDLLDDDE
LFNNHFEDAL TAFEEYKKSE AAGNAEEQA
