PTMA_RAT
ID PTMA_RAT Reviewed; 112 AA.
AC P06302; Q569C8;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Prothymosin alpha;
DE Contains:
DE RecName: Full=Prothymosin alpha, N-terminally processed;
DE Contains:
DE RecName: Full=Thymosin alpha;
GN Name=Ptma;
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 PRELIMINARY PROTEIN SEQUENCE OF 2-112, CLEAVAGE OF INITIATOR METHIONINE,
RP AND ACETYLATION AT SER-2.
RX PubMed=3855555; DOI=10.1073/pnas.82.2.343;
RA Haritos A.A., Blacher R., Stein S., Caldarella J., Horecker B.L.;
RT "Primary structure of rat thymus prothymosin alpha.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:343-346(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1989881; DOI=10.1002/j.1460-2075.1991.tb07929.x;
RA Eilers M., Schirm S., Bishop J.M.;
RT "The MYC protein activates transcription of the alpha-prothymosin gene.";
RL EMBO J. 10:133-141(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary, and Prostate;
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 [5]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=2269362; DOI=10.1016/0014-5793(90)80860-l;
RA Palvimo J., Linnala-Kankkunen A.;
RT "Identification of a low-Mr acidic nuclear protein as prothymosin alpha.";
RL FEBS Lett. 277:257-260(1990).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY MASS
RP 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: Prothymosin alpha may mediate immune function by conferring
CC resistance to certain opportunistic infections.
CC -!- SUBUNIT: Interacts with NUPR1; regulates apoptotic process.
CC {ECO:0000250|UniProtKB:P06454}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- PTM: Covalently linked to a small RNA of about 20 nucleotides.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the pro/parathymosin family. {ECO:0000305}.
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DR EMBL; M20035; AAA42241.1; -; mRNA.
DR EMBL; M86564; AAA40758.1; -; mRNA.
DR EMBL; M33024; AAA41931.1; -; mRNA.
DR EMBL; X55326; CAA39028.1; -; mRNA.
DR EMBL; BC061972; AAH61972.1; -; mRNA.
DR EMBL; BC092569; AAH92569.1; -; mRNA.
DR PIR; A32265; TNRTA.
DR RefSeq; NP_068508.1; NM_021740.1.
DR RefSeq; XP_003751326.1; XM_003751278.4.
DR RefSeq; XP_003752724.1; XM_003752676.4.
DR AlphaFoldDB; P06302; -.
DR BMRB; P06302; -.
DR SMR; P06302; -.
DR BioGRID; 1198718; 1.
DR BioGRID; 247900; 1.
DR IntAct; P06302; 1.
DR STRING; 10116.ENSRNOP00000025093; -.
DR iPTMnet; P06302; -.
DR PhosphoSitePlus; P06302; -.
DR jPOST; P06302; -.
DR PaxDb; P06302; -.
DR PRIDE; P06302; -.
DR GeneID; 100359583; -.
DR GeneID; 29222; -.
DR KEGG; rno:100359583; -.
DR KEGG; rno:29222; -.
DR UCSC; RGD:61829; rat.
DR CTD; 5757; -.
DR RGD; 61829; Ptma.
DR VEuPathDB; HostDB:ENSRNOG00000018584; -.
DR VEuPathDB; HostDB:ENSRNOG00000025731; -.
DR eggNOG; ENOG502S55T; Eukaryota.
DR HOGENOM; CLU_136539_0_1_1; -.
DR InParanoid; P06302; -.
DR OMA; RTPPMND; -.
DR TreeFam; TF350357; -.
DR PRO; PR:P06302; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000018584; Expressed in thymus and 19 other tissues.
DR Genevisible; P06302; RN.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0042393; F:histone binding; ISO:RGD.
DR GO; GO:0030154; P:cell differentiation; TAS:RGD.
DR GO; GO:0008283; P:cell population proliferation; TAS:RGD.
DR GO; GO:0043486; P:histone exchange; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:RGD.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:RGD.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IGI:CAFA.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:RGD.
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; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..112
FT /note="Prothymosin alpha"
FT /id="PRO_0000423258"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000269|PubMed:3855555"
FT CHAIN 2..112
FT /note="Prothymosin alpha, N-terminally processed"
FT /id="PRO_0000299253"
FT PEPTIDE 2..29
FT /note="Thymosin alpha"
FT /id="PRO_0000029867"
FT REGION 1..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..82
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P06454"
FT MOD_RES 2
FT /note="N-acetylserine; in Prothymosin alpha, N-terminally
FT processed"
FT /evidence="ECO:0000269|PubMed:3855555"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 8
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P01252"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06454"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06454"
FT MOD_RES 13
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P01252"
FT MOD_RES 14
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P01252"
FT MOD_RES 15
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P06454"
FT MOD_RES 15
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P26350"
FT MOD_RES 102
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P06454"
FT MOD_RES 103
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P26350"
FT MOD_RES 108
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P06454"
FT CROSSLNK 103
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P06454"
SQ SEQUENCE 112 AA; 12382 MW; FD145E1C06F133E8 CRC64;
MSDAAVDTSS EITTKDLKEK KEVVEEAENG RDAPANGNAQ NEENGEQEAD NEVDEEEEEG
GEEEEEEEEG DGEEEDGDED EEAEAPTGKR VAEDDEDDDV ETKKQKKTDE DD
