CC134_MOUSE
ID CC134_MOUSE Reviewed; 229 AA.
AC Q8C7V8; Q3U3V9;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Coiled-coil domain-containing protein 134;
DE Flags: Precursor;
GN Name=Ccdc134;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Blastocyst, Dendritic cell, and Embryonic stem cell;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 thus promotes PCAF-
CC mediated H3K14 and H4K8 HAT activity. May inhibit TADA2A-mediated
CC TP53/p53 'Lys-321' acetylation, leading to reduced TP53 stability and
CC transcriptional activity. May also promote TADA2A-mediated XRCC6
CC acetylation thus 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8C7V8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C7V8-2; Sequence=VSP_021181;
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; AK049165; BAC33581.1; -; mRNA.
DR EMBL; AK145747; BAE26624.1; -; mRNA.
DR EMBL; AK154557; BAE32676.1; -; mRNA.
DR EMBL; BC072586; AAH72586.1; -; mRNA.
DR CCDS; CCDS37155.1; -. [Q8C7V8-1]
DR RefSeq; NP_001313517.1; NM_001326588.1. [Q8C7V8-2]
DR RefSeq; NP_766016.2; NM_172428.2. [Q8C7V8-1]
DR AlphaFoldDB; Q8C7V8; -.
DR IntAct; Q8C7V8; 1.
DR STRING; 10090.ENSMUSP00000086578; -.
DR PhosphoSitePlus; Q8C7V8; -.
DR EPD; Q8C7V8; -.
DR MaxQB; Q8C7V8; -.
DR PaxDb; Q8C7V8; -.
DR PeptideAtlas; Q8C7V8; -.
DR PRIDE; Q8C7V8; -.
DR ProteomicsDB; 265690; -. [Q8C7V8-1]
DR ProteomicsDB; 265691; -. [Q8C7V8-2]
DR Antibodypedia; 289; 229 antibodies from 29 providers.
DR DNASU; 76457; -.
DR Ensembl; ENSMUST00000089174; ENSMUSP00000086578; ENSMUSG00000068114. [Q8C7V8-1]
DR GeneID; 76457; -.
DR KEGG; mmu:76457; -.
DR UCSC; uc007wye.1; mouse. [Q8C7V8-1]
DR CTD; 79879; -.
DR MGI; MGI:1923707; Ccdc134.
DR VEuPathDB; HostDB:ENSMUSG00000068114; -.
DR eggNOG; ENOG502QVE7; Eukaryota.
DR GeneTree; ENSGT00390000020164; -.
DR HOGENOM; CLU_099195_0_0_1; -.
DR InParanoid; Q8C7V8; -.
DR OMA; NPFKADH; -.
DR OrthoDB; 1509108at2759; -.
DR PhylomeDB; Q8C7V8; -.
DR TreeFam; TF323839; -.
DR BioGRID-ORCS; 76457; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Ccdc134; mouse.
DR PRO; PR:Q8C7V8; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8C7V8; protein.
DR Bgee; ENSMUSG00000068114; Expressed in spermatocyte and 203 other tissues.
DR ExpressionAtlas; Q8C7V8; baseline and differential.
DR Genevisible; Q8C7V8; MM.
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; IMP:MGI.
DR GO; GO:0035162; P:embryonic hemopoiesis; IMP:MGI.
DR GO; GO:1990402; P:embryonic liver development; IMP:MGI.
DR GO; GO:0001890; P:placenta development; IMP:MGI.
DR GO; GO:0021591; P:ventricular system development; IMP:MGI.
DR InterPro; IPR026321; Coiled-coil_dom_con_pro_134.
DR PANTHER; PTHR14735; PTHR14735; 1.
DR Pfam; PF15002; ERK-JNK_inhib; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Endoplasmic reticulum;
KW Nucleus; Reference proteome; 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_0000254110"
FT REGION 182..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"
FT VAR_SEQ 1..37
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021181"
FT CONFLICT 75
FT /note="K -> R (in Ref. 1; BAE32676)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 229 AA; 26495 MW; A67A9628EECE1766 CRC64;
MDLLQFLAAF SVLLWPGTEV TGALKSTLDP SLKIYKKMFE VKRREQLLAL KNLAQLNDIH
QQYKILDVML KGLFKVLEDS RTVLIAADVL PDGPVPQDEK LKDAFSHVVE NTAFFGDVVL
RFPKIVHHYF DHNSNWNLLI RWGISFCNQT GVFDQGPHSP ILSLMAQELG ITEKDSDFRN
PFKTDQTEFI PSTDPFQKAL REEEKRRKKE ERRKEIRKGP RISRSQSEL
