GenomeNet

Database: UniProt
Entry: CCD22_BOVIN
LinkDB: CCD22_BOVIN
Original site: CCD22_BOVIN 
ID   CCD22_BOVIN             Reviewed;         595 AA.
AC   Q1RMI8;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   24-JAN-2024, entry version 89.
DE   RecName: Full=Coiled-coil domain-containing protein 22;
GN   Name=CCDC22;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thymus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
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       Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC       {ECO:0000250|UniProtKB:O60826}.
CC   -!- SIMILARITY: Belongs to the CCDC22 family. {ECO:0000305}.
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DR   EMBL; BC114868; AAI14869.1; -; mRNA.
DR   RefSeq; NP_001069484.1; NM_001076016.2.
DR   AlphaFoldDB; Q1RMI8; -.
DR   SMR; Q1RMI8; -.
DR   STRING; 9913.ENSBTAP00000066233; -.
DR   iPTMnet; Q1RMI8; -.
DR   PaxDb; 9913-ENSBTAP00000042324; -.
DR   Ensembl; ENSBTAT00000044871.2; ENSBTAP00000042324.1; ENSBTAG00000013277.5.
DR   GeneID; 534246; -.
DR   KEGG; bta:534246; -.
DR   CTD; 28952; -.
DR   VEuPathDB; HostDB:ENSBTAG00000013277; -.
DR   VGNC; VGNC:26886; CCDC22.
DR   eggNOG; KOG1937; Eukaryota.
DR   GeneTree; ENSGT00390000003809; -.
DR   HOGENOM; CLU_024231_1_0_1; -.
DR   InParanoid; Q1RMI8; -.
DR   OrthoDB; 9179at2759; -.
DR   TreeFam; TF325575; -.
DR   Reactome; R-BTA-8951664; Neddylation.
DR   Proteomes; UP000009136; Chromosome X.
DR   Bgee; ENSBTAG00000013277; Expressed in choroid plexus and 105 other cell types or tissues.
DR   ExpressionAtlas; Q1RMI8; baseline.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0097602; F:cullin family protein binding; IBA:GO_Central.
DR   GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR   GO; GO:2000060; P:positive regulation of ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR008530; CCDC22.
DR   InterPro; IPR048348; CCDC22_CC.
DR   InterPro; IPR048349; CCDC22_N.
DR   PANTHER; PTHR15668:SF4; COILED-COIL DOMAIN-CONTAINING PROTEIN 22; 1.
DR   PANTHER; PTHR15668; JM1 PROTEIN; 1.
DR   Pfam; PF05667; CCDC22_CC; 2.
DR   Pfam; PF21674; CCDC22_N; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Endosome; Phosphoprotein;
KW   Protein transport; Reference proteome; Transport; Ubl conjugation pathway.
FT   CHAIN           1..595
FT                   /note="Coiled-coil domain-containing protein 22"
FT                   /id="PRO_0000338399"
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   REGION          218..243
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          323..369
FT                   /evidence="ECO:0000255"
FT   COILED          447..484
FT                   /evidence="ECO:0000255"
FT   COILED          564..595
FT                   /evidence="ECO:0000255"
FT   MOD_RES         410
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O60826"
SQ   SEQUENCE   595 AA;  67042 MW;  8AB061A1E79362FB CRC64;
     MEEADRILIH SLRQAGTAVP PDVQTLRAFT TELVVEAVVR CLRVINPAVG SGLSPLLPLA
     MSARFRLAMS LAQACMDLGY PLELGYQNFL YPSEPDLRDL LLFLAERLPT DASEDADQSA
     GESAILLRAI GSRIRDHLAL PWVPPLLRTP KLQYLQGSAH QKPFHASRLV MPELSSRGES
     REFQAGPLLL PVPAQVPQPA ARAASLLEHH AIQLCQHTGR DRAGDEDWGH RTSRLPAQED
     TRAQRQRLQK HLAEHLRQTW GRPGPPQQAR DLGEVLQAWG AGARPGTPKG SRFTHSKKFT
     FHLEPEAQAA QVSDVPATSQ RPEQDTWAAQ EQELESLREQ LEGVNHNIEE VEANMKTLGI
     NLVQVETECR QSELSIVERE QALRLKSQAV ELLPDGAANL AKLQLVVESS AQRVIHLAGQ
     WEKHRVPLLA EYRHLRKLQD CRELESSRRL AEIQELHQSV RAAAEEARRK EEVYKQLVSE
     LETLPKDVSR LAYTQRILEI VGNIRKQKEE ITKDAKKDDA VRKAYKYLAA LHENCSQLIQ
     TIEDTGTIMR EVRDLEEQIE TEMGKKTLSN LDKIREDYRA LRQENAGLLG RVREA
//
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