CC115_MOUSE
ID CC115_MOUSE Reviewed; 180 AA.
AC Q8VE99; Q3TS67;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Coiled-coil domain-containing protein 115;
DE AltName: Full=Coiled-coil protein 1;
DE Short=Ccp1;
GN Name=Ccdc115;
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].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 19-180.
RC STRAIN=C57BL/6J; TISSUE=Tongue;
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 [3]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP INDUCTION.
RX PubMed=16378758; DOI=10.1016/j.modgep.2005.07.004;
RA Pellicano F., Inglis-Broadgate S.L., Pante G., Ansorge W., Iwata T.;
RT "Expression of coiled-coil protein 1, a novel gene downstream of FGF2, in
RT the developing brain.";
RL Gene Expr. Patterns 6:285-293(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC 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: Accessory component of the proton-transporting vacuolar (V)-
CC ATPase protein pump involved in intracellular iron homeostasis. In
CC aerobic conditions, required for intracellular iron homeostasis, thus
CC triggering the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and
CC leading to HIF1A hydroxylation and subsequent proteasomal degradation.
CC Necessary for endolysosomal acidification and lysosomal degradation (By
CC similarity). May be involved in Golgi homeostasis (By similarity).
CC {ECO:0000250|UniProtKB:Q96NT0}.
CC -!- SUBUNIT: Accessory component of the multisubunit proton-transporting
CC vacuolar (V)-ATPase protein pump. {ECO:0000250|UniProtKB:Q96NT0}.
CC -!- SUBCELLULAR LOCATION: Endosome {ECO:0000269|PubMed:16378758}. Lysosome
CC {ECO:0000269|PubMed:16378758}. Endoplasmic reticulum-Golgi intermediate
CC compartment {ECO:0000250|UniProtKB:Q96NT0}. Cytoplasmic vesicle, COPI-
CC coated vesicle {ECO:0000250|UniProtKB:Q96NT0}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q96NT0}. Note=Seems not to be associated with
CC recycling endosomes. {ECO:0000269|PubMed:16378758}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the heart, liver, kidney
CC and testis and at lower levels in the brain and lung. Undetectable in
CC the spleen and muscles. {ECO:0000269|PubMed:16378758}.
CC -!- DEVELOPMENTAL STAGE: Strongly expressed at 13.5 dpc in a ventro-lateral
CC area of striatum and piriform cortex. At 14.5 dpc, some of the positive
CC cells shift toward the cortical plate. At this stage, strongly observed
CC at the superficial layer of dorsal cortex, whereas that of ventral
CC cortex decreases in its intensity. Expression extended further dorsally
CC at 16.5 dpc. In the dorsal cortex, expressed in the ventricular zone at
CC 13.5 dpc. At later stages, expression shifts to the cortical plate. At
CC 15.5 dpc, localizes to both ventricular zone and cortical plate. At
CC 16.5 dpc, almost all expression is in the deeper cortical plate,
CC although some expressing cells are still detectable in the ventricular
CC zone. In the lateral cortex, weak expression in the lateral ganglionic
CC eminence at 13.5 dpc. At 15.5 dpc, strongly detected in the progenitor
CC zones of the lateral ganglionic eminence and medial ganglionic
CC eminence, as well as in tangentially migrating cells in the superficial
CC area of lateral cortex. In the striatum and ventro-lateral cortex,
CC expressed at both 13.5 dpc and 15.5 dpc. {ECO:0000269|PubMed:16378758}.
CC -!- INDUCTION: Modestly up-regulated by FGF2.
CC {ECO:0000269|PubMed:16378758}.
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DR EMBL; BC019430; AAH19430.1; -; mRNA.
DR EMBL; AK162237; BAE36808.1; -; mRNA.
DR CCDS; CCDS14866.1; -.
DR RefSeq; NP_081435.1; NM_027159.2.
DR AlphaFoldDB; Q8VE99; -.
DR SMR; Q8VE99; -.
DR STRING; 10090.ENSMUSP00000042918; -.
DR iPTMnet; Q8VE99; -.
DR PhosphoSitePlus; Q8VE99; -.
DR EPD; Q8VE99; -.
DR MaxQB; Q8VE99; -.
DR PaxDb; Q8VE99; -.
DR PeptideAtlas; Q8VE99; -.
DR PRIDE; Q8VE99; -.
DR ProteomicsDB; 265577; -.
DR Antibodypedia; 33494; 67 antibodies from 20 providers.
DR DNASU; 69668; -.
DR Ensembl; ENSMUST00000042493; ENSMUSP00000042918; ENSMUSG00000042111.
DR GeneID; 69668; -.
DR KEGG; mmu:69668; -.
DR UCSC; uc011wja.1; mouse.
DR CTD; 84317; -.
DR MGI; MGI:1916918; Ccdc115.
DR VEuPathDB; HostDB:ENSMUSG00000042111; -.
DR eggNOG; ENOG502S392; Eukaryota.
DR GeneTree; ENSGT00390000012929; -.
DR HOGENOM; CLU_107415_0_0_1; -.
DR InParanoid; Q8VE99; -.
DR OMA; RMEPRVC; -.
DR OrthoDB; 1605528at2759; -.
DR PhylomeDB; Q8VE99; -.
DR TreeFam; TF324647; -.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR BioGRID-ORCS; 69668; 27 hits in 71 CRISPR screens.
DR ChiTaRS; Ccdc115; mouse.
DR PRO; PR:Q8VE99; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8VE99; protein.
DR Bgee; ENSMUSG00000042111; Expressed in primary oocyte and 130 other tissues.
DR Genevisible; Q8VE99; MM.
DR GO; GO:0030137; C:COPI-coated vesicle; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0042406; C:extrinsic component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IDA:MGI.
DR GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; ISS:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0006879; P:cellular iron ion homeostasis; ISS:UniProtKB.
DR GO; GO:0036295; P:cellular response to increased oxygen levels; ISS:UniProtKB.
DR GO; GO:0007042; P:lysosomal lumen acidification; ISS:UniProtKB.
DR GO; GO:1905146; P:lysosomal protein catabolic process; ISS:UniProtKB.
DR GO; GO:0070072; P:vacuolar proton-transporting V-type ATPase complex assembly; IEA:InterPro.
DR InterPro; IPR040357; Vma22/CCDC115.
DR PANTHER; PTHR31996; PTHR31996; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasmic vesicle; Endoplasmic reticulum; Endosome;
KW Lysosome; Reference proteome.
FT CHAIN 1..180
FT /note="Coiled-coil domain-containing protein 115"
FT /id="PRO_0000279404"
FT REGION 90..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 4..38
FT /evidence="ECO:0000255"
SQ SEQUENCE 180 AA; 19743 MW; BC2486DA366D705A CRC64;
MAVQALREEL DSKCLQLLSD LEELEAKRAA LNARVEEGWL SLAKARYAMG AKSVGPLQYA
SRMEPQVCVR ASEAQDGPQT FRVIKADAQT PEEVGPSEAS LRRRKGPTKT KELGSAVVPQ
DPLNWFGILV PHSLRQAQAS FRDGLQLAAD IASLQTRINW GQSQLRGLQK KLKELDPGPA
