TPD54_PONAB
ID TPD54_PONAB Reviewed; 206 AA.
AC Q5RCT1;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=Tumor protein D54;
DE AltName: Full=Tumor protein D52-like 2;
GN Name=TPD52L2;
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 -!- SUBUNIT: Forms a homodimer or heterodimer with other members of the
CC family. Interacts with MAL2 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TPD52 family. {ECO:0000305}.
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DR EMBL; CR858187; CAH90426.1; -; mRNA.
DR RefSeq; NP_001125212.1; NM_001131740.1.
DR AlphaFoldDB; Q5RCT1; -.
DR SMR; Q5RCT1; -.
DR STRING; 9601.ENSPPYP00000012569; -.
DR GeneID; 100172104; -.
DR KEGG; pon:100172104; -.
DR CTD; 7165; -.
DR HOGENOM; CLU_080743_1_0_1; -.
DR InParanoid; Q5RCT1; -.
DR OrthoDB; 1225782at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR InterPro; IPR007327; TPD52.
DR PANTHER; PTHR19307; PTHR19307; 1.
DR Pfam; PF04201; TPD52; 2.
PE 2: Evidence at transcript level;
KW Acetylation; Coiled coil; Phosphoprotein; Reference proteome.
FT CHAIN 1..206
FT /note="Tumor protein D54"
FT /id="PRO_0000185746"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 38..82
FT /evidence="ECO:0000255"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O43399"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43399"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43399"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43399"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43399"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43399"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43399"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43399"
FT MOD_RES 163
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O43399"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43399"
FT MOD_RES 173
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O43399"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CYZ2"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43399"
SQ SEQUENCE 206 AA; 22198 MW; F87A26A5C3A73782 CRC64;
MDSAGQDINL NSPNKGLLSD SMTDVPVDTG VAARTPAVEG LTEAEEEELR AELTKVEEEI
VTLRQVLAAK ERHCGELKRR LGLSTLGGLK QNLSRSWHDV QVSNAYVKTS EKLGEWNEKV
TQSDLYKKTQ ETLSQAGQKT SAALSTMGSA ISRKLGDMRN SATFKSFEDR VGTIKSKVVG
DRENGSDSLP SSAGSGDKPL SDPAPF