PABPB_XENLA
ID PABPB_XENLA Reviewed; 633 AA.
AC Q6IP09;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Polyadenylate-binding protein 1-B;
DE Short=PABP-1-B;
DE Short=Poly(A)-binding protein 1-B;
DE Short=xPABP1-B;
DE AltName: Full=Cytoplasmic poly(A)-binding protein 1-B;
GN Name=pabpc1-b;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000312|EMBL:AAH72110.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH72110.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Binds the poly(A) tail of mRNA. Prevents mRNA deadenylation
CC and confers poly(A) stability. Stimulates the translation of mRNAs to
CC which it is bound, acting, at least in part, with dazl (By similarity).
CC {ECO:0000250|UniProtKB:P20965}.
CC -!- SUBUNIT: The C-terminus self-associates, interacts with dazl and
CC interacts with the C-terminus of epabp independently of RNA. RRM 1 and
CC RRM 2 interact with both eif4g1 and paip1, and the C-terminus also
CC interacts with paip1. Interaction with eif4g1 is necessary for
CC translation of mRNAs required for oocyte maturation. Interacts with the
CC translation termination factor sup35/erf3 (By similarity).
CC {ECO:0000250|UniProtKB:P20965}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Associated with polysomes.
CC {ECO:0000250}.
CC -!- DOMAIN: RRM4, together with the C- and N-terminal regions, is
CC sufficient for RNA-binding. RRM 1 has no RNA-binding activity itself,
CC but improves discrimination between poly(A) and poly(U) in combination
CC with the other repeats (By similarity). {ECO:0000250|UniProtKB:P20965}.
CC -!- SIMILARITY: Belongs to the polyadenylate-binding protein type-1 family.
CC {ECO:0000305}.
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DR EMBL; BC072110; AAH72110.1; -; mRNA.
DR EMBL; BC108462; AAI08463.1; -; mRNA.
DR RefSeq; NP_001085069.1; NM_001091600.1.
DR AlphaFoldDB; Q6IP09; -.
DR SMR; Q6IP09; -.
DR DNASU; 432140; -.
DR GeneID; 432140; -.
DR KEGG; xla:432140; -.
DR CTD; 432140; -.
DR Xenbase; XB-GENE-6255999; pabpc1.L.
DR OMA; SHAEQKD; -.
DR OrthoDB; 1027234at2759; -.
DR Proteomes; UP000186698; Chromosome 6L.
DR Bgee; 432140; Expressed in lung and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005844; C:polysome; ISS:UniProtKB.
DR GO; GO:0031370; F:eukaryotic initiation factor 4G binding; ISS:UniProtKB.
DR GO; GO:0008143; F:poly(A) binding; ISS:UniProtKB.
DR GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
DR GO; GO:0031047; P:gene silencing by RNA; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0048255; P:mRNA stabilization; ISS:UniProtKB.
DR GO; GO:0060212; P:negative regulation of nuclear-transcribed mRNA poly(A) tail shortening; ISS:UniProtKB.
DR GO; GO:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISS:UniProtKB.
DR GO; GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; ISS:UniProtKB.
DR GO; GO:0006412; P:translation; 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; 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; 3.
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 2: Evidence at transcript level;
KW Cytoplasm; mRNA processing; Protein biosynthesis; Reference proteome;
KW Repeat; RNA-binding; Translation regulation.
FT CHAIN 1..633
FT /note="Polyadenylate-binding protein 1-B"
FT /id="PRO_0000233953"
FT DOMAIN 11..89
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 99..175
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 191..268
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 294..370
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 540..617
FT /note="PABC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00641"
FT REGION 452..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 633 AA; 70421 MW; 204B6DE4E1CD26CB CRC64;
MNPSAPSYPM ASLYVGDLHP DVTEAMLYEK FSPAGPILSI RVCRDMITRR SLGYAYVNFQ
QPADAERALD TMNFDVIKGK PVRIMWSQRD PSLRKSGVGN IFIKNLDKSI DNKALYDTFS
AFGNILSCKV VCDENGSKGY GFVHFETQEA AERAIDKMNG MLLNDRKVFV GRFKSRKERE
AELGARAKEF TNVYIKNFGE DMDDERLKEW FGQYGAALSV KVMTDDHGKS RGFGFVSFER
HEDAQKAVDD MNGKDLNGKA IFVGRAQKKV ERQTELKRKF EQMKQDRITR YQGVNLYVKN
LDDGIDDERL RKEFTPFGSI TSAKVMMEGG RSKGFGFVCF SSPEEATKAV TEMNGRIVAT
KPLYVALAQR KEERQAHLTN QYMQRMASVR VPNPVINPYQ PPPSSYFMAA IPPAQNRAAY
YPPGQIAQLR PSPRWTAQGA RPHPFQNMAG AIRPSAPRPP TFSTMRPTSQ VPRVMSAQRV
ANTSTQTMGP RPTTAAAAAT SAVRTVPQYK YAAGVRNTQQ HLNTQPQVAM QQPAVHVQGQ
EPLTASMLAA APPQEQKQML GERLFPLIQA MHPTLAGKIT GMLLEIDNSE LLHMLESPES
LRSKVDEAVA VLQAHQAKEA AQKVVSATGV PTA
