CCD66_PONAB
ID CCD66_PONAB Reviewed; 949 AA.
AC Q5RBD6;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 52.
DE RecName: Full=Coiled-coil domain-containing protein 66 {ECO:0000305};
GN Name=CCDC66 {ECO:0000250|UniProtKB:A2RUB6};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250|UniProtKB:A2RUB6,
CC ECO:0000250|UniProtKB:Q6NS45}.
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:0000250|UniProtKB:A2RUB6}. Cell projection, cilium, photoreceptor
CC outer segment {ECO:0000250|UniProtKB:A2RUB6}. Note=Restricted to the
CC centrosomes and the spindle microtubules during mitosis. Enriched in
CC the inner segment of the photoreceptor. {ECO:0000250|UniProtKB:A2RUB6}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR858715; CAH90924.1; -; mRNA.
DR RefSeq; NP_001125528.1; NM_001132056.1.
DR AlphaFoldDB; Q5RBD6; -.
DR SMR; Q5RBD6; -.
DR STRING; 9601.ENSPPYP00000015416; -.
DR GeneID; 100172440; -.
DR KEGG; pon:100172440; -.
DR CTD; 285331; -.
DR eggNOG; ENOG502R1PQ; Eukaryota.
DR InParanoid; Q5RBD6; -.
DR Proteomes; UP000001595; 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; ISS: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; ISS:UniProtKB.
DR InterPro; IPR039183; CCD66.
DR InterPro; IPR040467; CCDC66_dom.
DR PANTHER; PTHR22736; PTHR22736; 1.
DR Pfam; PF15236; CCDC66; 1.
PE 2: Evidence at transcript level;
KW Cell projection; Cilium; Cilium biogenesis/degradation; Coiled coil;
KW Cytoplasm; Cytoskeleton; Disulfide bond; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..949
FT /note="Coiled-coil domain-containing protein 66"
FT /id="PRO_0000320039"
FT REGION 691..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 789..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 474..558
FT /evidence="ECO:0000255"
FT COMPBIAS 691..707
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..809
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 115
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:A2RUB6"
FT MOD_RES 121
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:A2RUB6"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NS45"
FT MOD_RES 606
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NS45"
SQ SEQUENCE 949 AA; 109454 MW; D433C6483CEAFDE2 CRC64;
MNLGDGLKLE TELLDGKTKL ILSPYEHKSK ISVKMGNKAK IAKCPLRTKT GHILKSTQDT
CIGSEKLLQK KTVGSETSQA KGEKNGMTFS STKDLCKQCI DKDCLHIQKE ISPATPNMQK
TRNTVNTSLV GKQKPHKKHI TAENMKSNLV CLTQEQLQQI LMTVNQGNRS LSLTENGKEA
KSQYSLHLNS ISNQPKDENI MGLFKKTEMV SSVPAENKSV LNEHQETSKQ CEQKIAIENE
WKPADIFSTL GERERDRSLL EAKKAQWRKE LDEQVALKKK EKEVSEKWND PWKKSESDKI
IWEKHQILDQ SRETVLLEHA FSAVKQELQR KWIEELNKQI EDDRQRKIEE KIIYSKGEEH
DRWAMHFDSL KSYPGSQSQL SSRSTHKQPE YFCVSPDTQE LADVSSVCTP TTGSQVEPSE
EEHIAKPIKD VVMANSKKTN FLRSMTALLD PAQIEERDRR RQKQLEHQKA ITAQVEEKCR
KKQLEEEQRK KEEQEEELRL AQEREEMQKQ YEEDILKQKQ KEEIMTLKTN ELFQTMQRAQ
ELAQRLKQEQ RIRELAQKGH DTSRLIKNLG VDTIQIEYNA SNISNSRHDS DEVSGKMNTY
MNSTTSPKKD TGVQTDDLNI GIFTNAESHC GSLMERDITN CSSPEISAEL IGQFSTKKNK
QELTQDKGAS LEKENNRCND QCNQFTRIDK QTKHMKKYPK RPDWNINKPP KRYIPASEKY
PKQLQKQREE KEVRRQMELL HLVEKNNPGH LSQNRGISPE IFHSSHQETE SKFRWHLVKK
EEEPLNIHSF SKERSPSSPV PAVKNRTQQT QNTLHLPLKN SSYERENLIS GGNQTELSSG
ISESSHFIPY VRTNEIYYLD PDAPLSGPST QDPQYQNSQD CGQERQLFDS DCVRDPLLNP
NMVKNRDRQQ AILKGLSELR QGLLQKQKEL ESSLLPLAEN QEENFGSSF
