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 03-AUG-2022, entry version 83.
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 -!- 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.ENSBTAP00000042324; -.
DR iPTMnet; Q1RMI8; -.
DR PaxDb; Q1RMI8; -.
DR PRIDE; Q1RMI8; -.
DR Ensembl; ENSBTAT00000044871; ENSBTAP00000042324; ENSBTAG00000013277.
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; 985190at2759; -.
DR TreeFam; TF325575; -.
DR Proteomes; UP000009136; Chromosome X.
DR Bgee; ENSBTAG00000013277; Expressed in choroid plexus and 105 other tissues.
DR ExpressionAtlas; Q1RMI8; baseline.
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 PANTHER; PTHR15668; PTHR15668; 2.
DR Pfam; PF05667; DUF812; 2.
PE 2: Evidence at transcript level;
KW Coiled coil; Endosome; Phosphoprotein; Protein transport;
KW 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
