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TPD52_RABIT
ID   TPD52_RABIT             Reviewed;         184 AA.
AC   Q95212;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Tumor protein D52;
DE   AltName: Full=28 kDa calcium-dependent phosphoprotein;
DE   AltName: Full=pp28;
GN   Name=TPD52; Synonyms=CSPP28;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Gastric fundus;
RX   PubMed=8702730; DOI=10.1074/jbc.271.33.20096;
RA   Parente J.A., Goldenring J.R., Petropoulos A.C., Hellman U., Chew C.S.;
RT   "Purification, cloning, and expression of a novel, endogenous, calcium-
RT   sensitive, 28-kDa phosphoprotein.";
RL   J. Biol. Chem. 271:20096-20101(1996).
CC   -!- SUBUNIT: Forms a homodimer or heterodimer with other members of the
CC       family. {ECO:0000250}.
CC   -!- PTM: Phosphorylated in a calcium/calmodulin-dependent manner.
CC   -!- SIMILARITY: Belongs to the TPD52 family. {ECO:0000305}.
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DR   EMBL; U35428; AAC48616.1; -; mRNA.
DR   RefSeq; NP_001075829.1; NM_001082360.1.
DR   AlphaFoldDB; Q95212; -.
DR   SMR; Q95212; -.
DR   GeneID; 100009212; -.
DR   KEGG; ocu:100009212; -.
DR   CTD; 7163; -.
DR   InParanoid; Q95212; -.
DR   OrthoDB; 1225782at2759; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0030183; P:B cell differentiation; ISS:UniProtKB.
DR   InterPro; IPR007327; TPD52.
DR   PANTHER; PTHR19307; PTHR19307; 1.
DR   Pfam; PF04201; TPD52; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Phosphoprotein; Reference proteome.
FT   CHAIN           1..184
FT                   /note="Tumor protein D52"
FT                   /id="PRO_0000185740"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          147..184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          22..74
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        162..184
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         136
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62393"
SQ   SEQUENCE   184 AA;  19809 MW;  8CEA3C2CD6AC3DC4 CRC64;
     MDRGEQGLLR TDTVPEEAED AAATISATET LSEEEQEELR RELAKVEEEI QTLSQVLAAR
     EKHLAEIKRK LGINSLQELK QNIAKGWQDV TATSAYKKTS ETLSQAGQKA SAAFSSVGSV
     ITKKLEDVKN SPTFKSFEEK VENLKSKVGG TKPAGGDFGE VLNSTANASA TSGEPVPEQT
     QEGL
 
 
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