PAP1B_DICDI
ID PAP1B_DICDI Reviewed; 814 AA.
AC Q1ZXC2;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Polyadenylate-binding protein 1-B;
DE Short=PABP-1-B;
DE Short=Poly(A)-binding protein, cytoplasmic 1-B;
GN Name=pabpc1B; ORFNames=DDB_G0290745;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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 (By similarity). {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; AAFI02000169; EAS66827.1; -; Genomic_DNA.
DR RefSeq; XP_001134510.1; XM_001134510.1.
DR AlphaFoldDB; Q1ZXC2; -.
DR SMR; Q1ZXC2; -.
DR STRING; 44689.DDB0233386; -.
DR PaxDb; Q1ZXC2; -.
DR EnsemblProtists; EAS66827; EAS66827; DDB_G0290745.
DR GeneID; 8627795; -.
DR KEGG; ddi:DDB_G0290745; -.
DR dictyBase; DDB_G0290745; pabpc1B.
DR eggNOG; KOG0123; Eukaryota.
DR HOGENOM; CLU_012062_22_4_1; -.
DR InParanoid; Q1ZXC2; -.
DR OMA; AGPWREY; -.
DR PhylomeDB; Q1ZXC2; -.
DR Reactome; R-DDI-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-DDI-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-DDI-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR PRO; PR:Q1ZXC2; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; ISS:dictyBase.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
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; 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; SM00360; RRM; 4.
DR SMART; SM00361; RRM_1; 3.
DR SUPFAM; SSF54928; SSF54928; 3.
DR SUPFAM; SSF63570; SSF63570; 1.
DR PROSITE; PS51309; PABC; 1.
DR PROSITE; PS50102; RRM; 4.
PE 3: Inferred from homology;
KW Cytoplasm; mRNA processing; Nucleus; Reference proteome; Repeat;
KW RNA-binding.
FT CHAIN 1..814
FT /note="Polyadenylate-binding protein 1-B"
FT /id="PRO_0000328599"
FT DOMAIN 184..264
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 274..350
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 359..455
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 470..547
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 732..813
FT /note="PABC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00641"
FT REGION 1..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..98
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..153
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 814 AA; 91242 MW; 663BDDE5296AEF25 CRC64;
MVPTTESHEN NMPDNAAITQ QQQDATTSSS SSVATQPPQS QIPPQPQYQY QMAPPPQTHH
VHPHHVHPHH QQHPGYVPSH HHHHQQHHHH HPHHVGVPNL HHSIHQQQHP GYVPSHHHHQ
QQHHHHQHQH QHHQHQHHQH QHHQHHQHHQ HHHTSPMGAG AGAAGMPILS MSPIGAYQPP
HQLTSLYVGD LAADVNEIIL NELFSKVGRN AIASIHVCRD SNTLRSLGYA YVNFFNNHDA
ERALDTLNYT LVHGKPCRIM WSYRDPTKRK TNVGNIFVKN LEKGVDNAML YDTFSSFGNI
LSCKVEFEKG ISKGYGYVHF ETNDSAEKAI EKVNGTLILG KPINVERFVS KVERYKVENK
VFFRNADESI TIEILQQELS NRFGEIESCI LKNDANGKSK GLGLVEFKNQ EDAQKILTES
GALIISTIDG TTTVSSNGGT IEINGKPITI DRIKSKVERF TEYRKKTTDL SLFINNIDES
IDRDLIKEEF AKHGTIIGIK IVQDENARNK GFGFISFSEI QEAQKALDSL NGFTFGSKQI
QVSFSNKDNN QINNKLNGNS TKITKNIIQG GASASQYTGY LPINRYQQHL PHQHINPMYT
QQPYFPQQQQ SSSSSQPSSS QPQPSSPSHL NGNTTTTSPN TRYSKTLNGT TPFKKSNLPQ
NANGTNNNNN NNNTNINKSN NTTQSNGFRN KRVPNGKPRY NNNNNSSNNN NNNNTTTNVT
TTPSSTETTT PKTTITLEFI TNATAEEATE TLGSEVYNLV LAKYNNNIEL AAKIAGMIVD
AVPEHKELFE IISNGQIQSK IEEAKSLLDQ PDQE