ID   CC134_RAT               Reviewed;         229 AA.
AC   Q5M862;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Coiled-coil domain-containing protein 134;
DE   Flags: Precursor;
GN   Name=Ccdc134;
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=Thymus;
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).
CC   -!- FUNCTION: In extracellular secreted form, promotes proliferation and
CC       activation of CD8(+) T cells, suggesting a cytokine-like function.
CC       Enhances cytotoxic anti-tumor activity of CD8(+) T cells. May inhibit
CC       ERK and JNK signaling activity. May suppress cell migration and
CC       invasion activity, via its effects on ERK and JNK signaling.
CC       {ECO:0000250|UniProtKB:Q9H6E4}.
CC   -!- FUNCTION: In the nucleus, enhances stability of the PCAF histone
CC       acetyltransferase (HAT) complex member TADA2A and promotes H3K14 and
CC       H4K8 HAT activity. May inhibit TADA2A-mediated TP53/p53 'Lys-321'
CC       acetylation, leading to reduced TP53 stability and transcriptional
CC       activity. May also promote TADA2A-mediated XRCC6 acetylation thus
CC       facilitating cell apoptosis in response to DNA damage.
CC       {ECO:0000250|UniProtKB:Q9H6E4}.
CC   -!- SUBUNIT: Interacts with TADA2A. Associates with the PCAF complex via
CC       TADA2A binding. {ECO:0000250|UniProtKB:Q9H6E4}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H6E4}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q9H6E4}. Secreted
CC       {ECO:0000250|UniProtKB:Q9H6E4}. Endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:Q9H6E4}. Note=Accumulates in the nucleus in
CC       response to UV irradiation. {ECO:0000250|UniProtKB:Q9H6E4}.
CC   -!- PTM: O-glycosylated, with additional sialic acid modifications.
CC       {ECO:0000250|UniProtKB:Q9H6E4}.
CC   -!- SIMILARITY: Belongs to the CCDC134 family. {ECO:0000305}.
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DR   EMBL; BC088206; AAH88206.1; -; mRNA.
DR   RefSeq; NP_001019526.1; NM_001024355.1.
DR   RefSeq; XP_006242175.1; XM_006242113.3.
DR   AlphaFoldDB; Q5M862; -.
DR   STRING; 10116.ENSRNOP00000052900; -.
DR   PaxDb; Q5M862; -.
DR   Ensembl; ENSRNOT00000056048; ENSRNOP00000052900; ENSRNOG00000007262.
DR   GeneID; 500909; -.
DR   KEGG; rno:500909; -.
DR   UCSC; RGD:1559657; rat.
DR   CTD; 79879; -.
DR   RGD; 1559657; Ccdc134.
DR   eggNOG; ENOG502QVE7; Eukaryota.
DR   GeneTree; ENSGT00390000020164; -.
DR   HOGENOM; CLU_099195_0_0_1; -.
DR   InParanoid; Q5M862; -.
DR   OMA; NPFKADH; -.
DR   OrthoDB; 1509108at2759; -.
DR   PhylomeDB; Q5M862; -.
DR   TreeFam; TF323839; -.
DR   PRO; PR:Q5M862; -.
DR   Proteomes; UP000002494; Chromosome 7.
DR   Bgee; ENSRNOG00000007262; Expressed in pancreas and 20 other tissues.
DR   Genevisible; Q5M862; RN.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0001525; P:angiogenesis; ISO:RGD.
DR   GO; GO:0035162; P:embryonic hemopoiesis; ISO:RGD.
DR   GO; GO:1990402; P:embryonic liver development; ISO:RGD.
DR   GO; GO:0001890; P:placenta development; ISO:RGD.
DR   GO; GO:0021591; P:ventricular system development; ISO:RGD.
DR   InterPro; IPR026321; Coiled-coil_dom_con_pro_134.
DR   PANTHER; PTHR14735; PTHR14735; 1.
DR   Pfam; PF15002; ERK-JNK_inhib; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Endoplasmic reticulum; Nucleus; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000250|UniProtKB:Q9H6E4"
FT   CHAIN           23..229
FT                   /note="Coiled-coil domain-containing protein 134"
FT                   /id="PRO_0000254111"
FT   REGION          191..229
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          196..218
FT                   /evidence="ECO:0000255"
FT   MOTIF           206..213
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H6E4"
FT   COMPBIAS        197..229
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   229 AA;  26437 MW;  E63DD474154E64A3 CRC64;
     MDLLQSLAVF FVLLLPGTEV TGTLKSTLDP SLKIYKKMFE VKRREQLLAL KNLAQLNDIH
     QQYKILDVML KGLFKVLEDS RTVLIAADVL PDGPLPQDEK LKDAFSHVVE NTAFFGDVVL
     RFPKIVHHYF DHNSNWNLLI RWGISFCNQT GVFDQGPHSP VLSLMAQELG ITEKDSDFQN
     PFTIDRTEFI PSTDPFQKAL REEEKRRKKE EKRKEIRKGP RISRSQSEL