CCD22_RAT
ID CCD22_RAT Reviewed; 627 AA.
AC P86182; A6KP98;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 2.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Coiled-coil domain-containing protein 22 {ECO:0000250|UniProtKB:O60826};
GN Name=Ccdc22 {ECO:0000250|UniProtKB:O60826};
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP IDENTIFICATION BY MASS SPECTROMETRY.
RA Maurya D.K., Bhargava P.;
RL Submitted (JAN-2009) to UniProtKB.
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 (By similarity). Interacts with
CC COMMD1, COMMD2 COMMD3, COMMD4, COMMD5, COMMD6, COMMD7, COMMD8, COMMD9,
CC COMMD10. Interacts with CUL1, CUL2, CUL3, SKP1, BTRC. Interacts with
CC CCDC93; proposed to be a component of the CCC (COMMD/CCDC22/CCDC93)
CC complex which contains at least COMMD1 (and possibly other COMM domain-
CC containing proteins), CCDC22 and CCDC93; in the complex interacts
CC directly with CCDC93. Interacts with VPS35L; associates with the
CC retriever complex. Interacts with SNX17 and SNX31 (By similarity).
CC {ECO:0000250|UniProtKB:O60826, ECO:0000250|UniProtKB:Q9JIG7}.
CC -!- SUBCELLULAR LOCATION: Endosome {ECO:0000250|UniProtKB:O60826}.
CC -!- SIMILARITY: Belongs to the CCDC22 family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDL83846.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH474078; EDL83846.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_001129309.1; NM_001135837.1.
DR AlphaFoldDB; P86182; -.
DR SMR; P86182; -.
DR IntAct; P86182; 2.
DR STRING; 10116.ENSRNOP00000015547; -.
DR iPTMnet; P86182; -.
DR PhosphoSitePlus; P86182; -.
DR jPOST; P86182; -.
DR PaxDb; P86182; -.
DR PRIDE; P86182; -.
DR Ensembl; ENSRNOT00000015546; ENSRNOP00000015547; ENSRNOG00000010846.
DR GeneID; 317381; -.
DR KEGG; rno:317381; -.
DR UCSC; RGD:1560910; rat.
DR CTD; 28952; -.
DR RGD; 1560910; Ccdc22.
DR eggNOG; KOG1937; Eukaryota.
DR GeneTree; ENSGT00390000003809; -.
DR HOGENOM; CLU_024231_1_0_1; -.
DR InParanoid; P86182; -.
DR OMA; KFEQHIQ; -.
DR OrthoDB; 985190at2759; -.
DR PhylomeDB; P86182; -.
DR TreeFam; TF325575; -.
DR Reactome; R-RNO-8951664; Neddylation.
DR PRO; PR:P86182; -.
DR Proteomes; UP000002494; Chromosome X.
DR Proteomes; UP000234681; Chromosome x.
DR Bgee; ENSRNOG00000010846; Expressed in pancreas and 20 other tissues.
DR Genevisible; P86182; RN.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0097602; F:cullin family protein binding; ISO:RGD.
DR GO; GO:0006878; P:cellular copper ion homeostasis; ISO:RGD.
DR GO; GO:0007253; P:cytoplasmic sequestering of NF-kappaB; ISO:RGD.
DR GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; ISO:RGD.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; ISO:RGD.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISO:RGD.
DR GO; GO:2000060; P:positive regulation of ubiquitin-dependent protein catabolic process; ISO:RGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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_0000365633"
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 321..384
FT /evidence="ECO:0000255"
FT COILED 448..535
FT /evidence="ECO:0000255"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60826"
SQ SEQUENCE 627 AA; 70855 MW; ECCF7CA8D891001D CRC64;
MEEADRILIH SLRQAGTAVP PEVQTLRAFT TELVVEAVVR CLRVINPDVG SGLSHLLPPA
MSARFRLAMS LAQACMDLGY PLELGYQNFL YPSEPDLRDL LLFLAERLPT DASEDADQPA
GDSAIFLRAI GSQIRDQLAL PWVPPLLRTP KVQRLQGSAL QQAFHSSRLV LPELNCRGEP
REFQASPLLL PAPSQVPQLL GRAASLLEHH AIQLCQHVNR DCPGDEDRVR WASRLPSQED
PRAPQQRLHK QLIEHLRQSW GPLGAPTQVR DLGEMLQAWG AKAMTGVPKG SRFTHSEKFT
FHLEPQVQAA QVADIPAASQ RPEQDTRAAQ EEELESLREQ LASVNHNIEE VEANMKSLGM
NLVQVETECR QSELSVAEQE QALRLKSRTV ELLPDGAANL TKLQLVVESS AQRLIHLASQ
WEKHRVPLLA EYRHLRKLQD CRELESSRRL VEIQELHQSV RAAAEEARRK EEVYKQLVSE
LETLPKDVSR LAYTQRILEI VGNIRKQKEE ITKILSDTKE LQKEINSLSG KLDRTFAVTD
ELVFKDAKKD DAVRKAYKYL AALHENCSQL IQTIEDTGTI MREVRDLEEQ IETEMGKKTL
SNLEKICEDY RALRQENAGL LGRVREV
