ID   PTMA_PONAB              Reviewed;         110 AA.
AC   Q5R790;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 71.
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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Prothymosin alpha may mediate immune function by conferring
CC       resistance to certain opportunistic infections. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with NUPR1; regulates apoptotic process.
CC       {ECO:0000250|UniProtKB:P06454}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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; CR860228; CAH92370.1; -; mRNA.
DR   RefSeq; NP_001126395.1; NM_001132923.1.
DR   AlphaFoldDB; Q5R790; -.
DR   BMRB; Q5R790; -.
DR   SMR; Q5R790; -.
DR   STRING; 9601.ENSPPYP00000004369; -.
DR   GeneID; 100173377; -.
DR   KEGG; pon:100173377; -.
DR   CTD; 5757; -.
DR   eggNOG; ENOG502S55T; Eukaryota.
DR   InParanoid; Q5R790; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   InterPro; IPR004931; Pro/parathymosin.
DR   PANTHER; PTHR22745; PTHR22745; 1.
DR   Pfam; PF03247; Prothymosin; 1.
PE   3: Inferred from homology;
KW   Acetylation; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW   Ubl conjugation.
FT   CHAIN           1..110
FT                   /note="Prothymosin alpha"
FT                   /id="PRO_0000423257"
FT   INIT_MET        1
FT                   /note="Removed; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P01252"
FT   CHAIN           2..110
FT                   /note="Prothymosin alpha, N-terminally processed"
FT                   /id="PRO_0000299252"
FT   PEPTIDE         2..29
FT                   /note="Thymosin alpha"
FT                   /id="PRO_0000424825"
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:0000250|UniProtKB:P01252"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P01252"
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         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;  12102 MW;  22D9A43E79819018 CRC64;
     MSDAAVDTSS EITTKDLKEK KEVVEEAENG RDVPANGNAN EENGEQEADN EVDEEEEEGG
     EEEEEEEEGD GEEEDGDEDE EAESATGKRA AEDDEDDDVD TKKQKTDEDD