ID   TPD54_RAT               Reviewed;         220 AA.
AC   Q6PCT3;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Tumor protein D54;
DE   AltName: Full=Tumor protein D52-like 2;
GN   Name=Tpd52l2;
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 [LARGE SCALE MRNA].
RC   TISSUE=Pituitary;
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   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-180 AND SER-209, 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   -!- 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC059167; AAH59167.1; -; mRNA.
DR   RefSeq; NP_942039.1; NM_198744.2.
DR   AlphaFoldDB; Q6PCT3; -.
DR   SMR; Q6PCT3; -.
DR   BioGRID; 255374; 1.
DR   STRING; 10116.ENSRNOP00000020374; -.
DR   iPTMnet; Q6PCT3; -.
DR   PhosphoSitePlus; Q6PCT3; -.
DR   jPOST; Q6PCT3; -.
DR   PaxDb; Q6PCT3; -.
DR   PRIDE; Q6PCT3; -.
DR   GeneID; 296480; -.
DR   KEGG; rno:296480; -.
DR   UCSC; RGD:735167; rat.
DR   CTD; 7165; -.
DR   RGD; 735167; Tpd52l2.
DR   eggNOG; KOG4010; Eukaryota.
DR   HOGENOM; CLU_080743_1_0_1; -.
DR   InParanoid; Q6PCT3; -.
DR   OMA; KLGQWNE; -.
DR   OrthoDB; 1225782at2759; -.
DR   PhylomeDB; Q6PCT3; -.
DR   PRO; PR:Q6PCT3; -.
DR   Proteomes; UP000002494; Chromosome 3.
DR   Bgee; ENSRNOG00000015122; Expressed in cerebellum and 19 other tissues.
DR   Genevisible; Q6PCT3; RN.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR   InterPro; IPR007327; TPD52.
DR   PANTHER; PTHR19307; PTHR19307; 1.
DR   Pfam; PF04201; TPD52; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Coiled coil; Phosphoprotein; Reference proteome.
FT   CHAIN           1..220
FT                   /note="Tumor protein D54"
FT                   /id="PRO_0000185747"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          189..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          40..82
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..18
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:0007744|PubMed:22673903"
FT   MOD_RES         19
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         168
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CYZ2"
FT   MOD_RES         175
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O43399"
FT   MOD_RES         177
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O43399"
FT   MOD_RES         180
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         187
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O43399"
FT   MOD_RES         206
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CYZ2"
FT   MOD_RES         209
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   220 AA;  23992 MW;  505408FBFFABAFD8 CRC64;
     MDSASQDINL NSPNKGVLSD FMTDVPVDPG VVHRTPAVEG LTEVEEEELR AELAKVEEEI
     VTLRQVLAAK ERHCGELKRR LGLSTLGELK QNLSRSWHDV QGSTAYVKTS EKLGEWNEKV
     TQSDLYKKTQ ETLSQAGQKT SAALSTMGSA ISRKLGDMSS YSIRHSISMP VMRNSATFKS
     FEDRVGTIKS KVVGGRENGS DTLPSSPGSG DQTLPDHAPF