PTMA_BOVIN
ID PTMA_BOVIN Reviewed; 110 AA.
AC P01252;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Prothymosin alpha;
DE Contains:
DE RecName: Full=Prothymosin alpha, N-terminally processed;
DE Contains:
DE RecName: Full=Thymosin alpha-1;
GN Name=PTMA;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP PROTEIN SEQUENCE OF 2-110.
RX PubMed=2901823; DOI=10.1016/0003-9861(88)90149-x;
RA Panneerselvam C., Wellner D., Horecker B.L.;
RT "The amino acid sequence of bovine thymus prothymosin alpha.";
RL Arch. Biochem. Biophys. 265:454-457(1988).
RN [2]
RP PROTEIN SEQUENCE OF 2-29, AND ACETYLATION AT SER-2.
RX PubMed=762108; DOI=10.1016/s0021-9258(17)37901-2;
RA Low T.L.K., Goldstein A.L.;
RT "The chemistry and biology of thymosin. II. Amino acid sequence analysis of
RT thymosin alpha1 and polypeptide beta1.";
RL J. Biol. Chem. 254:987-995(1979).
RN [3]
RP PHOSPHORYLATION AT THR-8; THR-13 AND THR-14 BY CK2.
RX PubMed=1426245; DOI=10.1016/0014-5793(92)80924-6;
RA Barcia M.G., Castro J.M., Jullien C.D., Gonzalez C.G., Freire M.;
RT "Prothymosin alpha is phosphorylated by casein kinase-2.";
RL FEBS Lett. 312:152-156(1992).
RN [4]
RP PHOSPHORYLATION AT SER-2, AND ACETYLATION AT SER-2.
RX PubMed=8485135; DOI=10.1021/bi00068a015;
RA Sburlati A.R., De La Rosa A., Batey D.W., Kurys G.L., Manrow R.E.,
RA Pannell L.K., Martin B.M., Sheeley D.M., Berger S.L.;
RT "Phosphorylation of human and bovine prothymosin alpha in vivo.";
RL Biochemistry 32:4587-4596(1993).
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 PIR; A01520; TNBOA1.
DR RefSeq; XP_003581926.1; XM_003581878.2.
DR RefSeq; XP_003585828.1; XM_003585780.2.
DR AlphaFoldDB; P01252; -.
DR BMRB; P01252; -.
DR SMR; P01252; -.
DR STRING; 9913.ENSBTAP00000003305; -.
DR iPTMnet; P01252; -.
DR PaxDb; P01252; -.
DR PeptideAtlas; P01252; -.
DR PRIDE; P01252; -.
DR Ensembl; ENSBTAT00000003305; ENSBTAP00000003305; ENSBTAG00000002549.
DR GeneID; 786336; -.
DR KEGG; bta:786336; -.
DR VEuPathDB; HostDB:ENSBTAG00000002549; -.
DR eggNOG; ENOG502S55T; Eukaryota.
DR GeneTree; ENSGT00940000155762; -.
DR HOGENOM; CLU_136539_0_1_1; -.
DR InParanoid; P01252; -.
DR OMA; RTPPMND; -.
DR TreeFam; TF350357; -.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000002549; Expressed in thymus and 104 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IDA:CAFA.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR DisProt; DP00814; -.
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..110
FT /note="Prothymosin alpha"
FT /id="PRO_0000423254"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000269|PubMed:2901823,
FT ECO:0000269|PubMed:762108, ECO:0000269|PubMed:8485135"
FT CHAIN 2..110
FT /note="Prothymosin alpha, N-terminally processed"
FT /id="PRO_0000299249"
FT PEPTIDE 2..29
FT /note="Thymosin alpha-1"
FT /id="PRO_0000029864"
FT REGION 1..110
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 44..81
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..110
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:762108,
FT ECO:0000269|PubMed:8485135"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8485135"
FT MOD_RES 8
FT /note="Phosphothreonine; by CK2"
FT /evidence="ECO:0000269|PubMed:1426245"
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; by CK2"
FT /evidence="ECO:0000269|PubMed:1426245"
FT MOD_RES 14
FT /note="Phosphothreonine; by CK2"
FT /evidence="ECO:0000269|PubMed:1426245"
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 101
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P06454"
FT MOD_RES 102
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P26350"
FT MOD_RES 106
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P06454"
FT CROSSLNK 102
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P06454"
SQ SEQUENCE 110 AA; 12072 MW; 51078AE43B9308D7 CRC64;
MSDAAVDTSS EITTKDLKEK KEVVEEAENG REAPANGNAN EENGEQEADN EVDEEEEEGG
EEEEEEEEGD GEEEDGDEDE EAEAATGKRA AEDDEDDDVD TKKQKTDEDD
