ID H9G6I5_ANOCA Unreviewed; 584 AA.
AC H9G6I5;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 3.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Polyadenylate-binding protein {ECO:0000256|RuleBase:RU362004};
DE Short=PABP {ECO:0000256|RuleBase:RU362004};
GN Name=PABPC4 {ECO:0000313|Ensembl:ENSACAP00000002571.4};
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000002571.4, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000002571.4}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000002571.4};
RG The Genome Sequencing Platform;
RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACAP00000002571.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Binds the poly(A) tail of mRNA.
CC {ECO:0000256|RuleBase:RU362004}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|RuleBase:RU362004}.
CC -!- SIMILARITY: Belongs to the polyadenylate-binding protein type-1 family.
CC {ECO:0000256|ARBA:ARBA00008557, ECO:0000256|RuleBase:RU362004}.
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DR AlphaFoldDB; H9G6I5; -.
DR STRING; 28377.ENSACAP00000002571; -.
DR Ensembl; ENSACAT00000002636.4; ENSACAP00000002571.4; ENSACAG00000002544.4.
DR eggNOG; KOG0123; Eukaryota.
DR GeneTree; ENSGT00940000154788; -.
DR HOGENOM; CLU_012062_22_2_1; -.
DR InParanoid; H9G6I5; -.
DR TreeFam; TF300458; -.
DR Proteomes; UP000001646; Unplaced.
DR Bgee; ENSACAG00000002544; Expressed in skeletal muscle tissue and 12 other cell types or tissues.
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: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:0061515; P:myeloid cell development; IEA:Ensembl.
DR GO; GO:0043488; P:regulation of mRNA stability; IEA:Ensembl.
DR CDD; cd12379; RRM2_I_PABPs; 1.
DR CDD; cd12380; RRM3_I_PABPs; 1.
DR CDD; cd12381; RRM4_I_PABPs; 1.
DR Gene3D; 3.30.70.330; -; 4.
DR Gene3D; 1.10.1900.10; c-terminal domain of poly(a) binding protein; 1.
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 NCBIfam; TIGR01628; PABP-1234; 1.
DR PANTHER; PTHR24012:SF491; POLYADENYLATE-BINDING PROTEIN; 1.
DR PANTHER; PTHR24012; RNA BINDING PROTEIN; 1.
DR Pfam; PF00658; PABP; 1.
DR Pfam; PF00076; RRM_1; 4.
DR SMART; SM00517; PolyA; 1.
DR SMART; SM00360; RRM; 3.
DR SMART; SM00361; RRM_1; 3.
DR SUPFAM; SSF63570; PABC (PABP) domain; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 2.
DR PROSITE; PS51309; PABC; 1.
DR PROSITE; PS50102; RRM; 3.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|RuleBase:RU362004};
KW Reference proteome {ECO:0000313|Proteomes:UP000001646};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176,
KW ECO:0000256|RuleBase:RU362004}.
FT DOMAIN 54..130
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 146..223
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 249..325
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 492..569
FT /note="PABC"
FT /evidence="ECO:0000259|PROSITE:PS51309"
FT REGION 388..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..456
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 584 AA; 64903 MW; FE8287F8BE3BE2B9 CRC64;
MITRRSLFYA YVNFQQPADA ERALDTMNFD VIKGKPIRIM WSQRDPSLRK SGVGNVFIKN
LDKSIDNKAL YDTFSAFGNI LSCKVVCDEN GSKGYAFVHF ETQDAADRAI EKMNGMLLND
RKVFVGRFKS RKEREAELGA KAKEFTNVYI KNFGDDMDDE RLKELFGKYG KTLSVKVMTD
PTGKSKGFGF VSFEKHEEAN KAVEEMNGKD INGKMVFVGR AQKKVERQAE LKRRFEQLKQ
ERISRYQGVN LYIKNLDDTI DDEKLRKEFS PFGSITSAKV MLEEGRSKGF GFVCFSSPEE
ATKAVTEMNG RIVGSKPLYV ALAQRKEERK AHLTNQYMQR IAGMRALPAN AILNQFQPAA
GGYFMPAVPQ AQSRPPYYAP NQMTQIRPNP RWQQGGRPQG FQGMPNMRQS GPRPNLRHLA
PAGNAQASRG LPGAPQRVGI PPTGPNLAPR PPAAAQVPRA VPPYKYASSV RSPHPAVQPL
QAPQPAVHVQ GQEPLTASML AAAPPQEQKQ MLGERLFPLI QAMHLSLAGK ITGMLLEIDN
SELLHMLESP ESLRSKVEEA VAVLQAHQAK KEAAQKVGIV AATS
//
