ID   CCD61_DANRE             Reviewed;         511 AA.
AC   Q08CF3;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Centrosomal protein CCDC61 {ECO:0000303|PubMed:32375023};
DE   AltName: Full=Coiled-coil domain-containing protein 61 {ECO:0000250|UniProtKB:Q9Y6R9};
DE   AltName: Full=VFL3 homolog {ECO:0000250|UniProtKB:Q9Y6R9};
GN   Name=ccdc61 {ECO:0000250|UniProtKB:Q9Y6R9}; ORFNames=zgc:153153;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Olfactory epithelium;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0007744|PDB:6HXV, ECO:0007744|PDB:6HXY}
RP   X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF 1-168, MUTAGENESIS OF
RP   129-PHE-ASP-130, AND SUBUNIT.
RX   PubMed=32375023; DOI=10.1016/j.str.2020.04.010;
RA   Ochi T., Quarantotti V., Lin H., Jullien J., Rosa e Silva I., Boselli F.,
RA   Barnabas D.D., Johnson C.M., McLaughlin S.H., Freund S.M.V.,
RA   Blackford A.N., Kimata Y., Goldstein R.E., Jackson S.P., Blundell T.L.,
RA   Dutcher S.K., Gergely F., van Breugel M.;
RT   "CCDC61/VFL3 Is a Paralog of SAS6 and Promotes Ciliary Functions.";
RL   Structure 28:674-689(2020).
CC   -!- FUNCTION: Microtubule-binding centrosomal protein required for
CC       centriole cohesion, independently of the centrosome-associated
CC       protein/CEP250 and rootletin/CROCC linker. In interphase, required for
CC       anchoring microtubule at the mother centriole subdistal appendages and
CC       for centrosome positioning. During mitosis, may be involved in spindle
CC       assembly and chromatin alignment by regulating the organization of
CC       spindle microtubules into a symmetrical structure. Plays a non-
CC       essential role in ciliogenesis. {ECO:0000250|UniProtKB:Q9Y6R9}.
CC   -!- SUBUNIT: Forms homodimers (via head domain).
CC       {ECO:0000269|PubMed:32375023}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome {ECO:0000250|UniProtKB:Q9Y6R9}. Cytoplasm,
CC       cytoskeleton, microtubule organizing center, centrosome, centriolar
CC       satellite {ECO:0000250|UniProtKB:Q9Y6R9}. Cytoplasm, cytoskeleton,
CC       cilium basal body {ECO:0000250|UniProtKB:Q9Y6R9}. Note=Localization at
CC       the centriolar satellite is dependent on intact microtubule network.
CC       Localizes at the centriole subdistal appendages and proximal ends.
CC       Localized to centrosomal/satellite-like structures with the onset of
CC       centrosome separation in early G2. {ECO:0000250|UniProtKB:Q9Y6R9}.
CC   -!- DOMAIN: The coiled-coil domain is involved in microtubule-binding.
CC       {ECO:0000250|UniProtKB:Q9Y6R9}.
CC   -!- MISCELLANEOUS: The N-terminal 3D structure (head domain) resembles that
CC       of NHEJ1/XLF, PAXX, SASS6 and XRCC4. {ECO:0000250|UniProtKB:Q9Y6R9}.
CC   -!- SIMILARITY: Belongs to the CCDC61 family. {ECO:0000305}.
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DR   EMBL; BC124262; AAI24263.1; -; mRNA.
DR   RefSeq; NP_001070634.1; NM_001077166.1.
DR   PDB; 6HXV; X-ray; 1.97 A; A/B=1-168.
DR   PDB; 6HXY; X-ray; 2.90 A; A/B=1-170.
DR   PDBsum; 6HXV; -.
DR   PDBsum; 6HXY; -.
DR   AlphaFoldDB; Q08CF3; -.
DR   SMR; Q08CF3; -.
DR   STRING; 7955.ENSDARP00000098205; -.
DR   PaxDb; Q08CF3; -.
DR   PRIDE; Q08CF3; -.
DR   GeneID; 798766; -.
DR   KEGG; dre:798766; -.
DR   CTD; 729440; -.
DR   ZFIN; ZDB-GENE-060929-348; ccdc61.
DR   eggNOG; ENOG502QRAS; Eukaryota.
DR   InParanoid; Q08CF3; -.
DR   PRO; PR:Q08CF3; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0034451; C:centriolar satellite; ISS:UniProtKB.
DR   GO; GO:0120103; C:centriolar subdistal appendage; ISS:UniProtKB.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005815; C:microtubule organizing center; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IMP:UniProtKB.
DR   GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR   GO; GO:0098534; P:centriole assembly; ISS:UniProtKB.
DR   GO; GO:0090307; P:mitotic spindle assembly; ISS:UniProtKB.
PE   1: Evidence at protein level;
KW   3D-structure; Cell projection; Cilium biogenesis/degradation; Coiled coil;
KW   Cytoplasm; Cytoskeleton; Reference proteome.
FT   CHAIN           1..511
FT                   /note="Centrosomal protein CCDC61"
FT                   /id="PRO_0000311259"
FT   REGION          1..144
FT                   /note="Head domain"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y6R9"
FT   REGION          306..403
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          447..486
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          147..272
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        306..336
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        337..351
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        363..402
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         129..130
FT                   /note="FD->EA: Abolishes dimerization."
FT                   /evidence="ECO:0000269|PubMed:32375023"
FT   STRAND          6..13
FT                   /evidence="ECO:0007829|PDB:6HXV"
FT   STRAND          16..25
FT                   /evidence="ECO:0007829|PDB:6HXV"
FT   STRAND          28..35
FT                   /evidence="ECO:0007829|PDB:6HXV"
FT   TURN            36..38
FT                   /evidence="ECO:0007829|PDB:6HXV"
FT   STRAND          41..46
FT                   /evidence="ECO:0007829|PDB:6HXV"
FT   HELIX           48..58
FT                   /evidence="ECO:0007829|PDB:6HXV"
FT   HELIX           64..76
FT                   /evidence="ECO:0007829|PDB:6HXV"
FT   STRAND          82..87
FT                   /evidence="ECO:0007829|PDB:6HXV"
FT   HELIX           89..99
FT                   /evidence="ECO:0007829|PDB:6HXV"
FT   HELIX           113..117
FT                   /evidence="ECO:0007829|PDB:6HXV"
FT   STRAND          119..127
FT                   /evidence="ECO:0007829|PDB:6HXV"
FT   STRAND          130..138
FT                   /evidence="ECO:0007829|PDB:6HXV"
FT   STRAND          140..142
FT                   /evidence="ECO:0007829|PDB:6HXV"
FT   HELIX           146..163
FT                   /evidence="ECO:0007829|PDB:6HXV"
SQ   SEQUENCE   511 AA;  57554 MW;  4754BFBC28FB36CB CRC64;
     MEVGTVVQEE MKFRGSEFAV KVEMAERLLI VEISDVVTAD QWRGEFGPAY IEDLTRKTGN
     FKQFPVFCSM LESAVHKSSD SVTLDLLTYS DLELLRNRKA GVVGRPRAQP QSPALSAKRY
     LILIYTVEFD RIHYPLPLPY LGKPDPAELQ KEIRALRSEL KTLGLRGDHK VSDQETRKLR
     TELALVRDEK EALAKALDRL QMVGSGSAPG ARGLREAVHS LEEQLLKERA KSQRSAIKKS
     QEQRLLVEQL EELRASERAL RIRVKSLTTE LALLRRGRAT PVLSDRGGLR GDGVVHRSLS
     RERSLTRVGI RARSGSRERI EDRGRRSEER VRRADSSGSR NCITRPSPSP TGSRVPRFDP
     TAYIQDRQRR QKEAELKSQR KIRRDMLASP SLMERGRSRS REPVPQLMRA GSAGRGRSVS
     VESRRSRCSS EGSVAEFEEL AKPLNSRGRK LMSNGPAVSR GRHINKKPMC STPAQRMRAG
     DTSMDTGADL SEIDARLQAL QDYMRDLDTG H