CCD93_RAT
ID CCD93_RAT Reviewed; 629 AA.
AC Q5BJT7;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Coiled-coil domain-containing protein 93;
GN Name=Ccdc93;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 PROTEIN SEQUENCE OF 260-269; 297-308; 353-358 AND 527-532, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-305, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Component of the CCC complex, which is involved in the
CC regulation of endosomal recycling of surface proteins, including
CC integrins, signaling receptor and channels. The CCC complex associates
CC with SNX17, retriever and WASH complexes to prevent lysosomal
CC degradation and promote cell surface recycling of numerous cargos such
CC as integrins ITGA5:ITGB1. Involved in copper-dependent ATP7A
CC trafficking between the trans-Golgi network and vesicles in the cell
CC periphery; the function is proposed to depend on its association within
CC the CCC complex and cooperation with the WASH complex on early
CC endosomes and is dependent on its interaction with WASHC2C.
CC {ECO:0000250|UniProtKB:Q567U6}.
CC -!- SUBUNIT: Interacts with COMMD1, COMMD2 COMMD3, COMMD4, COMMD5, COMMD6,
CC COMMD7, COMMD8, COMMD9, COMMD10, WASHC1. Interacts directly with
CC WASHC2C. Interacts 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 CCDC22. Interacts with VPS35L;
CC associates with the retriever complex. Interacts with SNX17 and SNX31.
CC {ECO:0000250|UniProtKB:Q567U6}.
CC -!- SUBCELLULAR LOCATION: Early endosome {ECO:0000250|UniProtKB:Q567U6}.
CC -!- SIMILARITY: Belongs to the CCDC93 family. {ECO:0000305}.
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DR EMBL; BC091337; AAH91337.1; -; mRNA.
DR RefSeq; NP_001020168.1; NM_001024997.1.
DR AlphaFoldDB; Q5BJT7; -.
DR SMR; Q5BJT7; -.
DR BioGRID; 257965; 1.
DR IntAct; Q5BJT7; 5.
DR STRING; 10116.ENSRNOP00000003435; -.
DR iPTMnet; Q5BJT7; -.
DR PhosphoSitePlus; Q5BJT7; -.
DR jPOST; Q5BJT7; -.
DR PaxDb; Q5BJT7; -.
DR PRIDE; Q5BJT7; -.
DR Ensembl; ENSRNOT00000003435; ENSRNOP00000003435; ENSRNOG00000002514.
DR GeneID; 304743; -.
DR KEGG; rno:304743; -.
DR UCSC; RGD:1560504; rat.
DR CTD; 54520; -.
DR RGD; 1560504; Ccdc93.
DR eggNOG; KOG2701; Eukaryota.
DR GeneTree; ENSGT00390000011294; -.
DR HOGENOM; CLU_016588_0_0_1; -.
DR InParanoid; Q5BJT7; -.
DR OMA; QYYTLYN; -.
DR OrthoDB; 1091136at2759; -.
DR PhylomeDB; Q5BJT7; -.
DR TreeFam; TF323318; -.
DR PRO; PR:Q5BJT7; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000002514; Expressed in duodenum and 19 other tissues.
DR Genevisible; Q5BJT7; RN.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; ISO:RGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR039116; CCDC93.
DR InterPro; IPR019159; CCDC93_CC.
DR PANTHER; PTHR16441; PTHR16441; 1.
DR Pfam; PF09762; CCDC93_CC; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Direct protein sequencing; Endosome; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..629
FT /note="Coiled-coil domain-containing protein 93"
FT /id="PRO_0000234606"
FT REGION 1..428
FT /note="Sufficient for interaction with CCDC22"
FT /evidence="ECO:0000250|UniProtKB:Q567U6"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..629
FT /note="Sufficient for interaction with WASHC2C"
FT /evidence="ECO:0000250|UniProtKB:Q567U6"
FT COILED 231..430
FT /evidence="ECO:0000255"
FT COILED 558..599
FT /evidence="ECO:0000255"
FT COMPBIAS 209..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q567U6"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q567U6"
FT MOD_RES 305
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 629 AA; 72636 MW; AF43FFE68DBC782F CRC64;
MGLPKGPEGQ GLPEVETRED EEQNVKLTEI LELLVAAGYF RARIKGLSPF DKVVGGMTWC
ITTCSFDVDV DLLFQENSTI GQKIALSEKI VSVLPRMKCP HQLEPHQIQG MDFIHIFPVV
QWLVKRAIET KEEMGDYIRS YSISQFQKTY SLPEDDDFIK RKDKAIQTVV DLSDAYKPRR
KYRRQQGAEE LLDEESRVHS TLLEYGRRHG FSRQSKTEKA EDKKTALAAG LSAAEKTDAH
EEDELQAAEE QRIQSLMTKM TAMANEESRL TASSVGQIVG LCSAEIKQIV SEYEGKQSEL
SAEESPEKLG TSQLHQRKVI SLNKQILQKT KHLEELQANH TSLQAKYSDK KKTLTELKNH
GEKLDQEQAA LEKLEAKADP SILQNLRALV AMNESLKSQE QEFKAHCREE MARLQQEIEI
LKAERAPGEK TISSGEPQGA LTSTMTHNED LDRRYNMEKE KLYKIRLLQA RRNREIAILH
RKIDEVPSRA ELIQYQKRFI ELYRQISAVH KETKQFFTLY NTLDDKKVYL EKEISLLNSI
HENFSQAMAS PAARDQFLRQ MEQIVEGIKQ SRMKMEKKKQ ENKMRRDQLN DQYLELLEKQ
RLYFKTVKEF KEEGRKNELL LSKIKAKAS
