ID   CCD66_CANLF             Reviewed;         919 AA.
AC   F1PZQ5; D0R7H6;
DT   20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2012, sequence version 2.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Coiled-coil domain-containing protein 66 {ECO:0000305};
GN   Name=CCDC66;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND INVOLVEMENT IN PROGRESSIVE RETINAL ATROPHY.
RC   TISSUE=Retina;
RX   PubMed=19777273; DOI=10.1007/s10048-009-0223-z;
RA   Dekomien G., Vollrath C., Petrasch-Parwez E., Boeve M.H., Akkad D.A.,
RA   Gerding W.M., Epplen J.T.;
RT   "Progressive retinal atrophy in Schapendoes dogs: mutation of the newly
RT   identified CCDC66 gene.";
RL   Neurogenetics 11:163-174(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Boxer;
RX   PubMed=16341006; DOI=10.1038/nature04338;
RA   Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA   Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E.,
RA   Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F.,
RA   Smith D.R., deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W.,
RA   Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S.,
RA   Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A.,
RA   Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P.,
RA   Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA   Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA   Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P.,
RA   Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B.,
RA   Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A.,
RA   Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M.,
RA   Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S.,
RA   Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L.,
RA   Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA   Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C.,
RA   Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G.,
RA   Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N.,
RA   Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A.,
RA   Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A.,
RA   Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M.,
RA   Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L.,
RA   LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A.,
RA   Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S.,
RA   Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T.,
RA   Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A.,
RA   Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA   Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S.,
RA   Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M.,
RA   Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F.,
RA   Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T.,
RA   Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C.,
RA   Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C.,
RA   Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D.,
RA   Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H.,
RA   Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA   Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J.,
RA   Zembek L., Zimmer A., Lander E.S.;
RT   "Genome sequence, comparative analysis and haplotype structure of the
RT   domestic dog.";
RL   Nature 438:803-819(2005).
CC   -!- FUNCTION: Microtubule-binding protein required for ciliogenesis. May
CC       function in ciliogenesis by mediating the transport of proteins like
CC       BBS4 to the cilium, but also through the organization of the centriolar
CC       satellites (By similarity). Plays a role in retina morphogenesis and/or
CC       homeostasis (PubMed:19777273). {ECO:0000250|UniProtKB:A2RUB6,
CC       ECO:0000269|PubMed:19777273}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked (By similarity). Interacts with
CC       CEP290 (By similarity). Interacts with PCM1 (By similarity). Interacts
CC       with ARMC9, TOGARAM1, CSPP1 and CEP104 (By similarity).
CC       {ECO:0000250|UniProtKB:A2RUB6, ECO:0000250|UniProtKB:Q6NS45}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome {ECO:0000250|UniProtKB:A2RUB6}. Cytoplasm,
CC       cytoskeleton, microtubule organizing center, centrosome, centriolar
CC       satellite {ECO:0000250|UniProtKB:A2RUB6}. Cell projection, cilium
CC       {ECO:0000250|UniProtKB:A2RUB6}. Cytoplasm, cytoskeleton, cilium basal
CC       body {ECO:0000250|UniProtKB:A2RUB6}. Photoreceptor inner segment
CC       {ECO:0000269|PubMed:19777273}. Cell projection, cilium, photoreceptor
CC       outer segment {ECO:0000269|PubMed:19777273}. Note=Restricted to the
CC       centrosomes and the spindle microtubules during mitosis (By
CC       similarity). Enriched in the inner segment of the photoreceptor
CC       (PubMed:19777273). {ECO:0000250|UniProtKB:A2RUB6,
CC       ECO:0000269|PubMed:19777273}.
CC   -!- TISSUE SPECIFICITY: Expressed in retina and blood (PubMed:19777273).
CC       Expressed in retina, mainly in photoreceptors but also in outer
CC       plexiform and ganglion cell layers (at protein level)
CC       (PubMed:19777273). {ECO:0000269|PubMed:19777273}.
CC   -!- DISEASE: Note=Defects in CCDC66 are the cause of generalized
CC       progressive retinal atrophy (gPRA), characterized by continuous
CC       degeneration of photoreceptor cells leading to night blindness and
CC       progressive vision loss. A homozygous mutation in the CCDC66 gene
CC       resulting in a frameshift and the production of a truncated protein is
CC       probably causing the disease. {ECO:0000269|PubMed:19777273}.
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DR   EMBL; FN433897; CBA13041.1; -; mRNA.
DR   EMBL; AAEX03012172; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAEX03012173; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001161484.1; NM_001168012.1.
DR   AlphaFoldDB; F1PZQ5; -.
DR   SMR; F1PZQ5; -.
DR   STRING; 9615.ENSCAFP00000011951; -.
DR   PaxDb; F1PZQ5; -.
DR   GeneID; 476582; -.
DR   KEGG; cfa:476582; -.
DR   CTD; 285331; -.
DR   eggNOG; ENOG502R1PQ; Eukaryota.
DR   HOGENOM; CLU_016964_0_0_1; -.
DR   InParanoid; F1PZQ5; -.
DR   OMA; QVEYNAS; -.
DR   OrthoDB; 1468611at2759; -.
DR   TreeFam; TF350489; -.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0034451; C:centriolar satellite; ISS:UniProtKB.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR   GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; ISS:UniProtKB.
DR   GO; GO:0001917; C:photoreceptor inner segment; IDA:UniProtKB.
DR   GO; GO:0001750; C:photoreceptor outer segment; IEA:UniProtKB-SubCell.
DR   GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR   GO; GO:0001578; P:microtubule bundle formation; ISS:UniProtKB.
DR   GO; GO:1903564; P:regulation of protein localization to cilium; ISS:UniProtKB.
DR   GO; GO:0001895; P:retina homeostasis; IMP:UniProtKB.
DR   InterPro; IPR039183; CCD66.
DR   InterPro; IPR040467; CCDC66_dom.
DR   PANTHER; PTHR22736; PTHR22736; 1.
DR   Pfam; PF15236; CCDC66; 1.
PE   1: Evidence at protein level;
KW   Cell projection; Cilium; Cilium biogenesis/degradation; Coiled coil;
KW   Cytoplasm; Cytoskeleton; Disulfide bond; Reference proteome.
FT   CHAIN           1..919
FT                   /note="Coiled-coil domain-containing protein 66"
FT                   /id="PRO_0000444602"
FT   REGION          145..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          456..505
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          724..744
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          762..816
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          467..558
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        726..741
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        762..778
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        779..812
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        169
FT                   /note="G -> GV (in Ref. 1; CBA13041)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        770..773
FT                   /note="KKKN -> E (in Ref. 1; CBA13041)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   919 AA;  106504 MW;  23E11D4C91111185 CRC64;
     MGSKNKIAKC PIRTKQTGYI LKSTQNTCIR SGKLLQKKRM GSETSLAKGE KSSMIFSPTK
     DLCKQYVDKD CLYVQKEISP ATPTIQKTRN TINTSVVAKQ KHCKKHITAE NTKSGLVCLT
     QDQLQQILMT VNQGNKSISA IENGKEETSQ DSLHLNNTSN QPKDENIMGF QKNEALSSVL
     DENKSTLNKN QETSKQYEQK IAIENVWKPA DIFSTLGERE RDRSLLEAKK AQWKKELDEQ
     VALKKKEKEA SEKWNNPWKK FESDKIVWEK FQTLGQSKTS LSSSNILSQS PSQITVVQAD
     DYPLCRASQI LEETVPLERP LSTVKQEQQR KWIEDLNKQI EDDRQRKIEE KITSSKGEEH
     DRWAMHFDSL KNYPASQSQL SSRSIHNQPE YFCVSPDTQE LSDISNVYTP TTGSQVEPSE
     EEHIAKPVRD MAMANSQKTN FLRSMTALLD PAQIEERDRR RQKQLEHQKA ITAQVEEKRR
     KKQLEEQQRK KEEQEEERRL AREREEMQKQ YEEDILKQKQ KEEIMTLKTN ELFQTMQRAQ
     ELAQRLKQEQ RIRELAQKGH DTSGLIKNLG GYGLDDVSGK MNTCINSTTS PKKDTAVQTD
     DLNTGMFTIA ESCCGSIIER EILNCSSPEI PAEFNDQFKK DKQELINQDK AANLEKENSW
     YNDQYEFART EKKHMKKCPK RPDWNINKPL KRYIPASEKY PKQLQKQREE KKVRRQMELL
     NLVERNNPGH LSQNRGTSPV LPSPQEAEAR FRWHLIRKEE PLKSDSFSKK KKNRSQSPLE
     LVKNRTQQTQ TLKNRENLIL GDSQTETSPG ASEPSHFIPY VRTNEIYHLD PDAPLSRPLT
     QDLQYQNPHD CDQEQWQLFE SDVRDPLLNP NLVKNRDRQQ AILKGLSELR QGLLQKQREL
     ETNLMPLAAN QEENFNSSF