ID   SERB1_RAT               Reviewed;         407 AA.
AC   Q6AXS5; Q8VHU3;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2004, sequence version 2.
DT   02-SEP-2026, entry version 146.
DE   RecName: Full=SERPINE1 mRNA-binding protein 1;
DE   AltName: Full=PAI1 RNA-binding protein 1;
DE            Short=PAI-RBP1;
DE   AltName: Full=Plasminogen activator inhibitor 1 RNA-binding protein;
DE   AltName: Full=RDA288 {ECO:0000303|PubMed:14988380};
GN   Name=Serbp1; Synonyms=Pairbp1, Rda288;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT VAL-55.
RC   STRAIN=Sprague-Dawley; TISSUE=Oligodendrocyte;
RX   PubMed=12112363; DOI=10.1002/glia.10092;
RA   Blasi F., Ciarrocchi A., Luddi A., Strazza M., Riccio M., Santi S.,
RA   Arcone R., Pietropaolo C., D'Angelo R., Costantino-Ceccarini E., Melli M.;
RT   "Stage-specific gene expression in early differentiating
RT   oligodendrocytes.";
RL   Glia 39:114-123(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-19.
RX   PubMed=11001948; DOI=10.1074/jbc.m006538200;
RA   Heaton J.H., Dlakic W.M., Dlakic M., Gelehrter T.D.;
RT   "Identification and cDNA cloning of a novel RNA-binding protein that
RT   interacts with the cyclic nucleotide-responsive sequence in the type-1
RT   plasminogen activator inhibitor mRNA.";
RL   J. Biol. Chem. 276:3341-3347(2001).
RN   [4]
RP   PROTEIN SEQUENCE OF 17-32; 40-67; 79-91; 93-102; 112-122; 137-145; 209-216;
RP   225-236; 286-293 AND 329-344, AND IDENTIFICATION OF ISOFORM 1.
RX   PubMed=14988380; DOI=10.1210/en.2004-0067;
RA   Peluso J.J., Pappalardo A., Fernandez G., Wu C.A.;
RT   "Involvement of an unnamed protein, RDA288, in the mechanism through which
RT   progesterone mediates its antiapoptotic action in spontaneously
RT   immortalized granulosa cells.";
RL   Endocrinology 145:3014-3022(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-197; SER-203; SER-234
RP   AND SER-329, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237 (ISOFORM 2),
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Ribosome-binding protein that promotes ribosome hibernation,
CC       a process during which ribosomes are stabilized in an inactive state
CC       and preserved from proteasomal degradation (By similarity). Acts via
CC       its association with EEF2/eEF2 factor, sequestering EEF2/eEF2 at the A-
CC       site of the ribosome and promoting ribosome stabilization and storage
CC       in an inactive state (By similarity). May also play a role in the
CC       regulation of mRNA stability: binds to the 3'-most 134 nt of the
CC       SERPINE1/PAI1 mRNA, a region which confers cyclic nucleotide regulation
CC       of message decay. Seems to play a role in PML-nuclear bodies formation
CC       (By similarity). {ECO:0000250|UniProtKB:Q8NC51,
CC       ECO:0000250|UniProtKB:Q9CY58}.
CC   -!- SUBUNIT: Associates with mature 80S ribosomes (By similarity).
CC       Interacts with EEF2/eEF2; interaction sequesters EEF2/eEF2 at the A-
CC       site of the ribosome, thereby blocking the interaction sites of the
CC       mRNA-tRNA complex, promoting ribosome stabilization and hibernation.
CC       Interacts with SPIN1 (By similarity). Interacts with CHD3 and TDRD3 (By
CC       similarity). Interacts with ZDHHC17 (via ANK repeats) (By similarity).
CC       {ECO:0000250|UniProtKB:Q8NC51, ECO:0000250|UniProtKB:Q9CY58}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8NC51}. Nucleus
CC       {ECO:0000250|UniProtKB:Q8NC51}. Cytoplasm, perinuclear region
CC       {ECO:0000250|UniProtKB:Q8NC51}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6AXS5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6AXS5-2; Sequence=VSP_011636;
CC   -!- PTM: Phosphorylation by MTOR inhibits SERBP1 and relieves ribosome
CC       hibernation. {ECO:0000250|UniProtKB:Q8NC51}.
CC   -!- SIMILARITY: Belongs to the SERBP1-HABP4 family. {ECO:0000305}.
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DR   EMBL; AF388527; AAL57768.1; -; mRNA.
DR   EMBL; BC079337; AAH79337.1; -; mRNA.
DR   RefSeq; NP_659554.1; NM_145086.1. [Q6AXS5-2]
DR   RefSeq; XP_006236678.1; XM_006236616.4. [Q6AXS5-1]
DR   AlphaFoldDB; Q6AXS5; -.
DR   SMR; Q6AXS5; -.
DR   BioGRID; 251582; 2.
DR   FunCoup; Q6AXS5; 3991.
DR   IntAct; Q6AXS5; 10.
DR   STRING; 10116.ENSRNOP00000009503; -.
DR   iPTMnet; Q6AXS5; -.
DR   PhosphoSitePlus; Q6AXS5; -.
DR   jPOST; Q6AXS5; -.
DR   PaxDb; 10116-ENSRNOP00000009503; -.
DR   Ensembl; ENSRNOT00000106917.2; ENSRNOP00000086511.1; ENSRNOG00000005890.9. [Q6AXS5-1]
DR   Ensembl; ENSRNOT00055024001; ENSRNOP00055019588; ENSRNOG00055013935. [Q6AXS5-1]
DR   Ensembl; ENSRNOT00060041461; ENSRNOP00060034355; ENSRNOG00060023807. [Q6AXS5-1]
DR   Ensembl; ENSRNOT00065050684; ENSRNOP00065041657; ENSRNOG00065029303. [Q6AXS5-1]
DR   GeneID; 246303; -.
DR   KEGG; rno:246303; -.
DR   UCSC; RGD:619907; rat. [Q6AXS5-1]
DR   AGR; RGD:619907; -.
DR   CTD; 26135; -.
DR   RGD; 619907; Serbp1.
DR   eggNOG; KOG2945; Eukaryota.
DR   GeneTree; ENSGT00520000055591; -.
DR   HOGENOM; CLU_037366_2_1_1; -.
DR   InParanoid; Q6AXS5; -.
DR   OrthoDB; 87504at9989; -.
DR   PhylomeDB; Q6AXS5; -.
DR   PRO; PR:Q6AXS5; -.
DR   Proteomes; UP000002494; Chromosome 4.
DR   Bgee; ENSRNOG00000005890; Expressed in thymus and 20 other cell types or tissues.
DR   ExpressionAtlas; Q6AXS5; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:HGNC-UCL.
DR   GO; GO:0043022; F:ribosome binding; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; ISO:RGD.
DR   GO; GO:0032183; F:SUMO binding; ISS:UniProtKB.
DR   GO; GO:0061770; F:translation elongation factor binding; ISO:RGD.
DR   GO; GO:0030371; F:translation repressor activity; ISS:UniProtKB.
DR   GO; GO:0017148; P:negative regulation of translation; ISS:UniProtKB.
DR   GO; GO:0030578; P:PML body organization; ISS:UniProtKB.
DR   GO; GO:0042981; P:regulation of apoptotic process; IDA:RGD.
DR   GO; GO:0141014; P:ribosome hibernation; ISS:UniProtKB.
DR   InterPro; IPR039764; HABP4/SERBP1-like.
DR   InterPro; IPR006861; HABP4_PAIRBP1-bd.
DR   InterPro; IPR032381; IHABP4_N.
DR   PANTHER; PTHR12299; HYALURONIC ACID-BINDING PROTEIN 4; 1.
DR   PANTHER; PTHR12299:SF29; SERPINE1 MRNA-BINDING PROTEIN 1; 1.
DR   Pfam; PF04774; HABP4_PAI-RBP1; 1.
DR   Pfam; PF16174; IHABP4_N; 1.
DR   SMART; SM01233; HABP4_PAI-RBP1; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW   Isopeptide bond; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW   RNA-binding; Translation regulation; Ubl conjugation.
FT   CHAIN           1..407
FT                   /note="SERPINE1 mRNA-binding protein 1"
FT                   /id="PRO_0000058184"
FT   REGION          34..227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          242..289
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          327..407
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..68
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..80
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        89..114
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        122..162
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        164..182
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        183..199
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        242..256
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        261..274
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        327..341
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        362..371
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         25
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         52
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CY58"
FT   MOD_RES         68
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NC51"
FT   MOD_RES         122
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NC51"
FT   MOD_RES         140
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NC51"
FT   MOD_RES         165
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CY58"
FT   MOD_RES         188
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CY58"
FT   MOD_RES         197
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         199
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NC51"
FT   MOD_RES         203
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         205
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NC51"
FT   MOD_RES         208
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NC51"
FT   MOD_RES         211
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NC51"
FT   MOD_RES         216
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NC51"
FT   MOD_RES         221
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NC51"
FT   MOD_RES         226
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NC51"
FT   MOD_RES         234
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         328
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CY58"
FT   MOD_RES         329
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         363
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NC51"
FT   MOD_RES         366
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NC51"
FT   MOD_RES         369
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NC51"
FT   MOD_RES         391
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NC51"
FT   MOD_RES         393
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NC51"
FT   CROSSLNK        52
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NC51"
FT   CROSSLNK        102
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NC51"
FT   CROSSLNK        211
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NC51"
FT   CROSSLNK        228
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NC51"
FT   CROSSLNK        228
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NC51"
FT   CROSSLNK        280
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NC51"
FT   VAR_SEQ         233..247
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12112363,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_011636"
FT   VARIANT         55
FT                   /note="A -> V"
FT                   /evidence="ECO:0000269|PubMed:12112363"
FT   MOD_RES         Q6AXS5-2:237
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   407 AA;  44754 MW;  0553B5D4DED617A9 CRC64;
     MPGHLQEGFG CVVTNRFDQL FDDESDPFEV LKAAENKKKE AGGGGVGGPG AKSAAQAAAQ
     TNSNAAGKQL RKESQKDRKN PLPPSVGVAD KKEETQPPVA LKKEGIRRVG RRPDQQLQGD
     GKIIDRRPER RPPRERRFEK PLEEKGEGGE FSVDRPIIER PIRGRGGLGR GRGGRGRGMG
     RGDGFDSRGK REFDRHSGSD RSSFSHYSGL KHEDKRGGSG SHNWGTVKDE LTESPKYIQK
     QISYNCSDLE QSNVTEETPE GEEHPVADTE NKENEVEEVK EEGPKEMTLD EWKAIQNKDR
     AKVEFNIRKP NEGADGQWKK GFVLHKSKSE EAHAEDSVMD HHFRKPANDI TSQLEINFGD
     LGRPGRGGRG GRGGRGRGGR PNRGSRTDKS SASAPDVDDP EAFPALA
//