PBP1_CRYNH
ID PBP1_CRYNH Reviewed; 785 AA.
AC J9VND4;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2013, sequence version 2.
DT 25-MAY-2022, entry version 37.
DE RecName: Full=PAB1-binding protein 1 {ECO:0000303|PubMed:31681631};
DE AltName: Full=Poly(A)-binding protein-binding protein {ECO:0000305};
GN Name=PBP1 {ECO:0000303|PubMed:31681631};
GN ORFNames=CNAG_02046 {ECO:0000312|EMBL:AFR95773.2};
OS Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 /
OS CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=235443 {ECO:0000312|Proteomes:UP000010091};
RN [1] {ECO:0000312|Proteomes:UP000010091}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487;
RX PubMed=24743168; DOI=10.1371/journal.pgen.1004261;
RA Janbon G., Ormerod K.L., Paulet D., Byrnes E.J. III, Yadav V.,
RA Chatterjee G., Mullapudi N., Hon C.-C., Billmyre R.B., Brunel F.,
RA Bahn Y.-S., Chen W., Chen Y., Chow E.W.L., Coppee J.-Y., Floyd-Averette A.,
RA Gaillardin C., Gerik K.J., Goldberg J., Gonzalez-Hilarion S., Gujja S.,
RA Hamlin J.L., Hsueh Y.-P., Ianiri G., Jones S., Kodira C.D., Kozubowski L.,
RA Lam W., Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K.,
RA Proux C., Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A.,
RA Zeng Q., Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A.,
RA Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A.,
RA Cuomo C.A., Dietrich F.S.;
RT "Analysis of the genome and transcriptome of Cryptococcus neoformans var.
RT grubii reveals complex RNA expression and microevolution leading to
RT virulence attenuation.";
RL PLoS Genet. 10:E1004261-E1004261(2014).
RN [2] {ECO:0000305}
RP SUBCELLULAR LOCATION, PHOSPHORYLATION, IDENTIFICATION BY MASS SPECTROMETRY,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=27611567; DOI=10.1371/journal.ppat.1005873;
RA Park H.S., Chow E.W., Fu C., Soderblom E.J., Moseley M.A., Heitman J.,
RA Cardenas M.E.;
RT "Calcineurin Targets Involved in Stress Survival and Fungal Virulence.";
RL PLoS Pathog. 12:e1005873-e1005873(2016).
RN [3] {ECO:0000305}
RP INTERACTION WITH MKT1, AND DISRUPTION PHENOTYPE.
RX PubMed=31681631; DOI=10.3389/fcimb.2019.00355;
RA Son Y.E., Fu C., Jung W.H., Oh S.H., Kwak J.H., Cardenas M.E., Heitman J.,
RA Park H.S.;
RT "Pbp1-Interacting Protein Mkt1 Regulates Virulence and Sexual Reproduction
RT in Cryptococcus neoformans.";
RL Front. Cell. Infect. Microbiol. 9:355-355(2019).
CC -!- FUNCTION: Involved in post-transcriptional regulation of gene
CC expression by interactions with poly(A)-binding protein.
CC {ECO:0000250|UniProtKB:Q9USW1}.
CC -!- SUBUNIT: Interacts with MKT1. {ECO:0000269|PubMed:31681631}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000305|PubMed:27611567}.
CC Cytoplasm, Stress granule {ECO:0000305|PubMed:27611567}. Note=Localizes
CC to cytosolic puncta at 24 degrees Celsius (Probable). Localizes to
CC stress granules and P-bodies at 37 degrees Celsius (Probable).
CC {ECO:0000305|PubMed:27611567}.
CC -!- PTM: Phosphorylated (PubMed:27611567). Probably dephosphorylated by
CC calcineurin (PubMed:27611567). {ECO:0000269|PubMed:27611567}.
CC -!- DISRUPTION PHENOTYPE: Abnormal sexual reproduction; decreases MFalpha1
CC expression and abolishes basidiospore chain formation (PubMed:27611567,
CC PubMed:31681631). Decreases virulence in a mouse intranasal inhalation
CC model for pulmonary infection; virulence is completely lost in a double
CC knockout with CRZ1 (PubMed:27611567). Resistance to high temperature;
CC resistance is suppressed in a double knockout with CRZ1
CC (PubMed:27611567, PubMed:31681631). Resistance to tacrolimus
CC (calcineurin inhibitor) (PubMed:27611567). Resistance to dithiothreitol
CC (ER stress inducer) (PubMed:27611567). Resistance to tunicamycin (ER
CC stress inducer) (PubMed:27611567). {ECO:0000269|PubMed:27611567,
CC ECO:0000269|PubMed:31681631}.
CC -!- SIMILARITY: Belongs to the ataxin-2 family. {ECO:0000305}.
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DR EMBL; CP003825; AFR95773.2; -; Genomic_DNA.
DR RefSeq; XP_012049868.1; XM_012194478.1.
DR AlphaFoldDB; J9VND4; -.
DR EnsemblFungi; AFR95773; AFR95773; CNAG_02046.
DR GeneID; 23885704; -.
DR VEuPathDB; FungiDB:CNAG_02046; -.
DR HOGENOM; CLU_426506_0_0_1; -.
DR Proteomes; UP000010091; Chromosome 6.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:UniProtKB-SubCell.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR InterPro; IPR045117; ATXN2-like.
DR InterPro; IPR009604; LsmAD_domain.
DR PANTHER; PTHR12854; PTHR12854; 1.
DR Pfam; PF06741; LsmAD; 1.
DR SMART; SM01272; LsmAD; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Translation regulation.
FT CHAIN 1..785
FT /note="PAB1-binding protein 1"
FT /id="PRO_0000450881"
FT REGION 1..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 669..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..685
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..730
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..762
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..785
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 785 AA; 84453 MW; 7FC66CCE9FEB40DF CRC64;
MSNERGRGRG GNRGGRGGME GGSARRGAWR NGPPPAGSFP HSRGGSPALG QSPTPRMSIN
DHMHDLKIVQ GERKGFQTDT DISRAAGPVE RELQPWVPDG PSPPPQSNGG SGNADFETFG
TTNNITWDQF ETNERLFGAK TDFKEELYTT KLNKSGPDFH KREKEAERLA KQIMGQTSKN
AHIAEERGQA TDIRDEEEKY SGVSRAPNAY VPPSARRAMG QSSAALRPNP TFESNTNGST
PIPAKPASPA AHETAPPAPE RRISDDPVGS KPEAPAMKVT GTTIRPITEN AEVTVNGTNV
TAETKPELSG VVNEWRQFVG TEREKVEAKK QSVLKSEKEK QLADFKKFQA NFKVPLPLPK
DILPILSKDE AKQKDIEAKA TNALQAAKER KLSIAKDSPA KSPVILNSVK SDAPKPAPPK
KIVMKIPEIP PFNPAKRKAP AVPVPESATQ DIKLITSPAP SNGSLASQAT KLNPTASTFV
FKPRADAAPF KPGQPSVSPS IAPHQPSAGP SNTSASTAVP KGNAFFRDKL PEKTHINARE
DFNPWKHGPV PRPNTVGTGW PYPGRKVGVP PPFMSPAAPP QMQMQFEDDP TSPSPHPAQP
AMMPGMPPNY PPYGRFQPGM PPPYGVPGGM QNPMFSPGPH FSPHPGQPMG QPQHMMPGGP
QPNMPMYFQN GMPQNPAFLP PQMQQFPHNP QRPGPGPGPG GPQMFYPNQM PPMPHQTPLQ
QHPVPFSGPS PAQPQFQHQH QHQHQHPHQQ APPPPPVQMS PAHSTPSGPG GVVQGGPQQN
GQTQG
