PDCD4_PONAB
ID PDCD4_PONAB Reviewed; 469 AA.
AC Q5R8S3;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Programmed cell death protein 4;
GN Name=PDCD4;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Inhibits translation initiation and cap-dependent
CC translation. May excert its function by hindering the interaction
CC between EIF4A1 and EIF4G. Inhibits the helicase activity of EIF4A.
CC Modulates the activation of JUN kinase. Down-regulates the expression
CC of MAP4K1, thus inhibiting events important in driving invasion,
CC namely, MAPK85 activation and consequent JUN-dependent transcription.
CC May play a role in apoptosis. Tumor suppressor. Inhibits tumor
CC promoter-induced neoplastic transformation. Binds RNA (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts (via MI domains) with EIF4A2 (By similarity).
CC Interacts (via MI domains) with EIF4A1 (via N-terminal domain).
CC Heterotrimer with EIF4A1; one molecule of PDCD4 binds two molecules of
CC EIF4A1. Interacts with EIF4G1. May form a complex with EIF4A1 and
CC EIF4G1. The interaction between PDCD4 and EIF4A1 interferes with the
CC interaction between EIF4A1 and EIF4G. When phosphorylated, interacts
CC with BTRC and FBXW11 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Note=Shuttles between the nucleus and cytoplasm. Predominantly nuclear
CC under normal growth conditions, and when phosphorylated at Ser-457 (By
CC similarity). {ECO:0000250}.
CC -!- DOMAIN: Binds EIF4A1 via both MI domains. {ECO:0000250}.
CC -!- PTM: Polyubiquitinated, leading to its proteasomal degradation. Rapidly
CC degraded in response to mitogens. Phosphorylation of the phosphodegron
CC promotes interaction with BTRC and proteasomal degradation (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated at Ser-67 by RPS6KB1 in response to mitogens;
CC phosphorylation promotes proteasomal degradation of PDCD4.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PDCD4 family. {ECO:0000305}.
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DR EMBL; CR859676; CAH91837.1; -; mRNA.
DR RefSeq; NP_001126062.1; NM_001132590.1.
DR AlphaFoldDB; Q5R8S3; -.
DR BMRB; Q5R8S3; -.
DR SMR; Q5R8S3; -.
DR STRING; 9601.ENSPPYP00000003086; -.
DR PRIDE; Q5R8S3; -.
DR GeneID; 100173014; -.
DR KEGG; pon:100173014; -.
DR CTD; 27250; -.
DR eggNOG; KOG0403; Eukaryota.
DR InParanoid; Q5R8S3; -.
DR OrthoDB; 434771at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:InterPro.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR003891; Initiation_fac_eIF4g_MI.
DR InterPro; IPR039778; PDCD4.
DR PANTHER; PTHR12626; PTHR12626; 1.
DR Pfam; PF02847; MA3; 2.
DR SMART; SM00544; MA3; 2.
DR SUPFAM; SSF48371; SSF48371; 2.
DR PROSITE; PS51366; MI; 2.
PE 2: Evidence at transcript level;
KW Acetylation; Apoptosis; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; Tumor suppressor; Ubl conjugation.
FT CHAIN 1..469
FT /note="Programmed cell death protein 4"
FT /id="PRO_0000256521"
FT DOMAIN 163..284
FT /note="MI 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT DOMAIN 326..449
FT /note="MI 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 58..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 58..64
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 70..76
FT /note="Phosphodegron"
FT /evidence="ECO:0000250"
FT MOTIF 448..454
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 11..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q53EL6"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JID1"
FT MOD_RES 67
FT /note="Phosphoserine; by PKB and RPS6KB1"
FT /evidence="ECO:0000250|UniProtKB:Q53EL6"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53EL6"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53EL6"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53EL6"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53EL6"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53EL6"
FT MOD_RES 152
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q53EL6"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53EL6"
FT MOD_RES 317
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53EL6"
FT MOD_RES 457
FT /note="Phosphoserine; by PKB"
FT /evidence="ECO:0000250|UniProtKB:Q53EL6"
SQ SEQUENCE 469 AA; 51711 MW; F9FEC5D2554DD5BE CRC64;
MDVENEQILN VNPADPDNLS DSLFSGDEES AGTEEIKNEI NGNWISASSI NEARINAKAK
RRLRKNSSRD SGRGDSVSDN GSDTLRSGVT VPTSPKGRLL DRRSRSGKGR GLPKKGGAGG
KGVWGTPGQV YDVEEVDVKD PNYDDDQENC VYETVVLPLD ERAFEKTLTP IIQEYFEHGD
TNEVAEMLRD LNLGEMKSGV PVLAVSLALE GKASHREMTS KLLSDLCGTV MSTSDVEKSF
DKSLKDLPEL ALDTPRAPQL VGQFIARAVG DGILCNTYID SYKGTVDCVQ ARAALDKATV
LLSMSKGGKR KDSVWGSGGG QQSVNHLVKE IDMLLKEYLL SGDISEAEHC LKELEVPHFH
HELVYEAIIM VLESTGESTF KMILDLLKSL WKSSTITVDQ MKRGYERIYN EIPDINLDVP
HSYSVLERFV EECFQAGIIS KQLRDLCPSR GRKRFVSEGD GGRLKPESY
