PAIRB_RAT
ID PAIRB_RAT Reviewed; 407 AA.
AC Q6AXS5; Q8VHU3;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Plasminogen activator inhibitor 1 RNA-binding protein;
DE AltName: Full=PAI1 RNA-binding protein 1;
DE Short=PAI-RBP1;
DE AltName: Full=RDA288 {ECO:0000303|PubMed:14988380};
DE AltName: Full=SERPINE1 mRNA-binding protein 1;
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: May play a role in the regulation of mRNA stability. Binds to
CC the 3'-most 134 nt of the SERPINE1/PAI1 mRNA, a region which confers
CC cyclic nucleotide regulation of message decay. Seems to play a role in
CC PML-nuclear bodies formation. {ECO:0000250|UniProtKB:Q8NC51}.
CC -!- SUBUNIT: Interacts with SPIN1 (By similarity). Interacts with CHD3 and
CC TDRD3. 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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_006236616.2. [Q6AXS5-1]
DR AlphaFoldDB; Q6AXS5; -.
DR BioGRID; 251582; 1.
DR IntAct; Q6AXS5; 9.
DR STRING; 10116.ENSRNOP00000009503; -.
DR iPTMnet; Q6AXS5; -.
DR PhosphoSitePlus; Q6AXS5; -.
DR jPOST; Q6AXS5; -.
DR PaxDb; Q6AXS5; -.
DR PRIDE; Q6AXS5; -.
DR Ensembl; ENSRNOT00000106917; ENSRNOP00000086511; ENSRNOG00000005890. [Q6AXS5-1]
DR GeneID; 246303; -.
DR KEGG; rno:246303; -.
DR UCSC; RGD:619907; rat. [Q6AXS5-1]
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 OMA; EEMNGFQ; -.
DR OrthoDB; 1183388at2759; -.
DR PhylomeDB; Q6AXS5; -.
DR TreeFam; TF318374; -.
DR PRO; PR:Q6AXS5; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000005890; Expressed in thymus and 20 other tissues.
DR Genevisible; Q6AXS5; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:HGNC-UCL.
DR GO; GO:0043022; F:ribosome binding; ISO:RGD.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0032183; F:SUMO binding; ISS:UniProtKB.
DR GO; GO:0030578; P:PML body organization; ISS:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; IDA:RGD.
DR InterPro; IPR039764; HABP4/SERBP1.
DR InterPro; IPR006861; HABP4_PAIRBP1-bd.
DR InterPro; IPR032381; IHABP4_N.
DR InterPro; IPR027205; SERBP1.
DR PANTHER; PTHR12299; PTHR12299; 1.
DR PANTHER; PTHR12299:SF29; PTHR12299:SF29; 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; Ubl conjugation.
FT CHAIN 1..407
FT /note="Plasminogen activator inhibitor 1 RNA-binding
FT protein"
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 55..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..289
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..348
FT /note="Basic and acidic 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 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 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
