CCD22_MOUSE
ID CCD22_MOUSE Reviewed; 627 AA.
AC Q9JIG7; B1AVA1; Q8BYH4;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Coiled-coil domain-containing protein 22;
GN Name=Ccdc22; Synonyms=DXImx40e;
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 [MRNA].
RX PubMed=10857745; DOI=10.1006/geno.2000.6173;
RA Means G.D., Toy D.Y., Baum P.R., Derry J.M.J.;
RT "A transcript map of a 2-Mb BAC contig in the proximal portion of the mouse
RT X chromosome and regional mapping of the scurfy mutation.";
RL Genomics 65:213-223(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Spinal cord;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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 [5]
RP INTERACTION WITH CPNE1 AND CPNE4.
RX PubMed=12522145; DOI=10.1074/jbc.m212632200;
RA Tomsig J.L., Snyder S.L., Creutz C.E.;
RT "Identification of targets for calcium signaling through the copine family
RT of proteins. Characterization of a coiled-coil copine-binding motif.";
RL J. Biol. Chem. 278:10048-10054(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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: Involved in regulation of NF-kappa-B signaling. Promotes
CC ubiquitination of I-kappa-B-kinase subunit IKBKB and its subsequent
CC proteasomal degradation leading to NF-kappa-B activation; the function
CC may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin
CC ligase complex. May down-regulate NF-kappa-B activity via association
CC with COMMD1 and involving a CUL2-dependent E3 ubiquitin ligase complex.
CC Regulates the cellular localization of COMM domain-containing proteins,
CC such as COMMD1 and COMMD10. Component of the CCC complex, which is
CC involved in the regulation of endosomal recycling of surface proteins,
CC including integrins, signaling receptor and channels. The CCC complex
CC associates with SNX17, retriever and WASH complexes to prevent
CC lysosomal degradation and promote cell surface recycling of numerous
CC cargos such as integrins ITGA5:ITGB1. Plays a role in copper ion
CC homeostasis. Involved in copper-dependent ATP7A trafficking between the
CC trans-Golgi network and vesicles in the cell periphery; the function is
CC proposed to depend on its association within the CCC complex and
CC cooperation with the WASH complex on early endosomes.
CC {ECO:0000250|UniProtKB:O60826}.
CC -!- SUBUNIT: Interacts with CPNE1 and CPNE4 (PubMed:12522145). Interacts
CC with COMMD1, COMMD2 COMMD3, COMMD4, COMMD5, COMMD6, COMMD7, COMMD8,
CC COMMD9, COMMD10. Interacts with CUL1, CUL2, CUL3, SKP1, BTRC. Interacts
CC with CCDC93; proposed to be a component of the CCC
CC (COMMD/CCDC22/CCDC93) complex which contains at least COMMD1 (and
CC possibly other COMM domain-containing proteins), CCDC22 and CCDC93; in
CC the complex interacts directly with CCDC93. Interacts with VPS35L;
CC associates with the retriever complex. Interacts with SNX17 and SNX31
CC (By similarity). {ECO:0000250|UniProtKB:O60826,
CC ECO:0000269|PubMed:12522145}.
CC -!- SUBCELLULAR LOCATION: Endosome {ECO:0000250|UniProtKB:O60826}.
CC -!- SIMILARITY: Belongs to the CCDC22 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; AF229637; AAF66951.1; -; mRNA.
DR EMBL; AK010536; BAB27013.1; -; mRNA.
DR EMBL; AK039573; BAC30390.1; -; mRNA.
DR EMBL; AL672231; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC011195; AAH11195.1; -; mRNA.
DR CCDS; CCDS29966.1; -.
DR RefSeq; NP_613069.3; NM_138603.3.
DR AlphaFoldDB; Q9JIG7; -.
DR SMR; Q9JIG7; -.
DR BioGRID; 207701; 16.
DR IntAct; Q9JIG7; 5.
DR MINT; Q9JIG7; -.
DR STRING; 10090.ENSMUSP00000033483; -.
DR iPTMnet; Q9JIG7; -.
DR PhosphoSitePlus; Q9JIG7; -.
DR EPD; Q9JIG7; -.
DR MaxQB; Q9JIG7; -.
DR PaxDb; Q9JIG7; -.
DR PeptideAtlas; Q9JIG7; -.
DR PRIDE; Q9JIG7; -.
DR ProteomicsDB; 281416; -.
DR Antibodypedia; 368; 186 antibodies from 30 providers.
DR DNASU; 54638; -.
DR Ensembl; ENSMUST00000033483; ENSMUSP00000033483; ENSMUSG00000031143.
DR GeneID; 54638; -.
DR KEGG; mmu:54638; -.
DR UCSC; uc009sln.1; mouse.
DR CTD; 28952; -.
DR MGI; MGI:1859608; Ccdc22.
DR VEuPathDB; HostDB:ENSMUSG00000031143; -.
DR eggNOG; KOG1937; Eukaryota.
DR GeneTree; ENSGT00390000003809; -.
DR HOGENOM; CLU_024231_1_0_1; -.
DR InParanoid; Q9JIG7; -.
DR OMA; KFEQHIQ; -.
DR OrthoDB; 985190at2759; -.
DR PhylomeDB; Q9JIG7; -.
DR TreeFam; TF325575; -.
DR Reactome; R-MMU-8951664; Neddylation.
DR BioGRID-ORCS; 54638; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Ccdc22; mouse.
DR PRO; PR:Q9JIG7; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9JIG7; protein.
DR Bgee; ENSMUSG00000031143; Expressed in interventricular septum and 250 other tissues.
DR Genevisible; Q9JIG7; MM.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0097602; F:cullin family protein binding; ISO:MGI.
DR GO; GO:0006878; P:cellular copper ion homeostasis; ISO:MGI.
DR GO; GO:0042632; P:cholesterol homeostasis; ISO:MGI.
DR GO; GO:0007253; P:cytoplasmic sequestering of NF-kappaB; ISO:MGI.
DR GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; ISO:MGI.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; ISO:MGI.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISO:MGI.
DR GO; GO:2000060; P:positive regulation of ubiquitin-dependent protein catabolic process; ISO:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0097006; P:regulation of plasma lipoprotein particle levels; ISO:MGI.
DR InterPro; IPR008530; CCDC22.
DR PANTHER; PTHR15668; PTHR15668; 1.
DR Pfam; PF05667; DUF812; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Endosome; Phosphoprotein; Protein transport;
KW Reference proteome; Transport; Ubl conjugation pathway.
FT CHAIN 1..627
FT /note="Coiled-coil domain-containing protein 22"
FT /id="PRO_0000076200"
FT REGION 1..447
FT /note="Sufficicient and required for interaction with
FT CCDC93"
FT /evidence="ECO:0000250|UniProtKB:O60826"
FT REGION 1..321
FT /note="Sufficient for interaction with COMMD1"
FT /evidence="ECO:0000250|UniProtKB:O60826"
FT COILED 448..535
FT /evidence="ECO:0000255"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60826"
FT CONFLICT 117
FT /note="D -> N (in Ref. 2; BAC30390)"
FT /evidence="ECO:0000305"
FT CONFLICT 529
FT /note="S -> F (in Ref. 2; BAC30390)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 627 AA; 70844 MW; 3710732B4CD90A2E CRC64;
MEEADRILIH SLRQAGTAVP PEVQTLRAFT TELVVEAVVR CLRVINPDVG SGLSHLLPPA
MSARFRLAMS LAQACMDLGY PLELGYQNFL YPSEPDLRDL LLFLAERLPS DASEDADQPA
GDSAIFLRAI GSQIRDQLAL PWVPPLLRTP KVQRLQGSAL QQPFHSSRLV LPELNSSGEL
WEFQASPLLL PAPTQVPQLQ GRAASLLEHH ASQLCQHVNR DCPGDEDRVR WASRVPSQED
SRAPQQRLHK QLIEHLRQSW GPLGAPTQVR DLGEMLQTWG ARAMTGVPKG SRFTHSEKFT
FHLEPQVQAA QVADVPATSQ RLEQDTRAAQ EQELESLREQ LASVNHNIEE VEADMKTLGI
NLVQVETECR QSELSVAEQE QALRLKSRTV ELLPDGAANL AKLQLVVESS AQRLIHLASQ
WEKHRVPLLA EYRHLRRLQD CRELESSRRL AEIQELHHSV RAAAEEARRK EEVYKQLVSE
LETLPKDVSR LAYTQRILEI VGNIRKQKEE ITKILSDTKE LQKEINSLSG KLDRTFAVTD
ELVFKDAKKD DAVRKAYKYL AALHENCSQL IQTIEDTGTI MREVRDLEEQ IETEMGKKTL
SNLEKICEDY RALRQENAGL LGRVREA
