PTMS_RAT
ID PTMS_RAT Reviewed; 102 AA.
AC P04550;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Parathymosin;
DE AltName: Full=Zinc-binding 11.5 kDa protein;
GN Name=Ptms; Synonyms=Znbp;
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.
RX PubMed=2759245; DOI=10.1016/0014-5793(89)80930-5;
RA Trompeter H.-I., Brand I.A., Soeling H.-D.;
RT "The primary sequence of the PFK-1 inactivating zinc-binding protein as
RT deduced from cDNA sequencing. Identity of the zinc-binding protein with rat
RT parathymosin.";
RL FEBS Lett. 253:63-66(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Fischer; TISSUE=Liver;
RX PubMed=1544455; DOI=10.1016/0014-5793(92)80068-r;
RA Trompeter H.-I., Soeling H.-D.;
RT "Cloning and characterisation of a gene encoding the 11.5 kDa zinc-binding
RT protein (parathymosin-alpha).";
RL FEBS Lett. 298:245-248(1992).
RN [3]
RP PROTEIN SEQUENCE OF 5-15, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP NUCLEOTIDE SEQUENCE OF 23-102.
RC TISSUE=Spleen;
RX PubMed=3377505; DOI=10.1016/0003-9861(88)90640-6;
RA Frangou-Lazaridis M., Clinton M., Goodall G.J., Horecker B.L.;
RT "Prothymosin alpha and parathymosin: amino acid sequences deduced from the
RT cloned rat spleen cDNAs.";
RL Arch. Biochem. Biophys. 263:305-310(1988).
RN [5]
RP PRELIMINARY PROTEIN SEQUENCE OF 2-102, CLEAVAGE OF INITIATOR METHIONINE,
RP AND ACETYLATION AT SER-2.
RX PubMed=3456585; DOI=10.1073/pnas.83.5.1242;
RA Komiyama T., Pan L.-X., Haritos A.A., Wideman J.W., Pan Y.-C.E., Chang M.,
RA Rogers I., Horecker B.L.;
RT "The primary structure of rat parathymosin.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:1242-1245(1986).
RN [6]
RP PRELIMINARY PROTEIN SEQUENCE OF 2-31.
RX PubMed=3856246; DOI=10.1073/pnas.82.4.1050;
RA Haritos A.A., Salvin S.B., Blacher R., Stein S., Horecker B.L.;
RT "Parathymosin alpha: a peptide from rat tissues with structural homology to
RT prothymosin alpha.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:1050-1053(1985).
RN [7]
RP SEQUENCE REVISION TO 1-5.
RX PubMed=3421960; DOI=10.1016/s0006-291x(88)80528-x;
RA Panneerselvam C., Clinton M., Wellner D., Horecker B.L.;
RT "Bovine parathymosin: amino acid sequence and comparison with rat
RT parathymosin.";
RL Biochem. Biophys. Res. Commun. 155:539-545(1988).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-5 AND THR-52, AND
RP 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: Parathymosin may mediate immune function by blocking the
CC effect of prothymosin alpha which confers resistance to certain
CC opportunistic infections.
CC -!- SIMILARITY: Belongs to the pro/parathymosin family. {ECO:0000305}.
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DR EMBL; M20616; AAA42249.1; -; mRNA.
DR EMBL; M33025; AAA41810.1; -; mRNA.
DR EMBL; X64053; CAA45411.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X16481; CAA34501.1; -; mRNA.
DR PIR; S02031; S02031.
DR PIR; S05212; B31512.
DR PIR; S20422; S20422.
DR RefSeq; NP_114181.1; NM_031975.2.
DR AlphaFoldDB; P04550; -.
DR SMR; P04550; -.
DR BioGRID; 249838; 1.
DR IntAct; P04550; 1.
DR STRING; 10116.ENSRNOP00000022209; -.
DR iPTMnet; P04550; -.
DR PhosphoSitePlus; P04550; -.
DR jPOST; P04550; -.
DR PaxDb; P04550; -.
DR PRIDE; P04550; -.
DR GeneID; 83801; -.
DR KEGG; rno:83801; -.
DR UCSC; RGD:621529; rat.
DR CTD; 5763; -.
DR RGD; 621529; Ptms.
DR VEuPathDB; HostDB:ENSRNOG00000060098; -.
DR eggNOG; ENOG502SSXW; Eukaryota.
DR HOGENOM; CLU_087174_1_0_1; -.
DR InParanoid; P04550; -.
DR OMA; ACDDCEG; -.
DR PRO; PR:P04550; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000060098; Expressed in frontal cortex and 19 other tissues.
DR ExpressionAtlas; P04550; baseline and differential.
DR Genevisible; P04550; RN.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004857; F:enzyme inhibitor activity; TAS:RGD.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IDA:RGD.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR004931; Pro/parathymosin.
DR PANTHER; PTHR22745; PTHR22745; 1.
DR Pfam; PF03247; Prothymosin; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Immunity; Phosphoprotein;
KW Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3456585"
FT CHAIN 2..102
FT /note="Parathymosin"
FT /id="PRO_0000191634"
FT REGION 1..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..74
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:3456585"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 4
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P20962"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D0J8"
FT MOD_RES 15
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P20962"
FT MOD_RES 52
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 92
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P20962"
SQ SEQUENCE 102 AA; 11559 MW; 1C1713A59BDD7C44 CRC64;
MSEKSVEAAA ELSAKDLKEK KDKVEEKAGR KERKKEVVEE EENGAEEEEE ETAEDGEDDD
EGDEEDEEEE EEEDEGPVRK RTAEEEDEAD PKRQKTENGA SA
