CCD61_RAT
ID CCD61_RAT Reviewed; 512 AA.
AC A0JPP8;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Centrosomal protein CCDC61 {ECO:0000250|UniProtKB:Q9Y6R9};
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:0000312|RGD:1307390};
GN Synonyms=VFL3 {ECO:0000250|UniProtKB:Q9Y6R9};
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=Testis;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-372 AND SER-375, AND
RP IDENTIFICATION BY 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: 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) (By similarity). Interacts
CC with CEP170 (By similarity). Interacts with PCM1 and CEP131 (By
CC similarity). Binds tubulin (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y6R9}.
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 domains are 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; BC127532; AAI27533.1; -; mRNA.
DR RefSeq; NP_001099699.1; NM_001106229.1.
DR AlphaFoldDB; A0JPP8; -.
DR SMR; A0JPP8; -.
DR STRING; 10116.ENSRNOP00000018495; -.
DR iPTMnet; A0JPP8; -.
DR PhosphoSitePlus; A0JPP8; -.
DR PaxDb; A0JPP8; -.
DR PRIDE; A0JPP8; -.
DR Ensembl; ENSRNOT00000018495; ENSRNOP00000018495; ENSRNOG00000013767.
DR GeneID; 292680; -.
DR KEGG; rno:292680; -.
DR UCSC; RGD:1307390; rat.
DR CTD; 729440; -.
DR RGD; 1307390; Ccdc61.
DR eggNOG; ENOG502QRAS; Eukaryota.
DR GeneTree; ENSGT00940000154133; -.
DR HOGENOM; CLU_038746_1_0_1; -.
DR InParanoid; A0JPP8; -.
DR OMA; THRIKDK; -.
DR OrthoDB; 1433381at2759; -.
DR PhylomeDB; A0JPP8; -.
DR TreeFam; TF329415; -.
DR PRO; PR:A0JPP8; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000013767; Expressed in thymus and 19 other tissues.
DR Genevisible; A0JPP8; RN.
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; ISS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; ISO:RGD.
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 Acetylation; Cell projection; Cilium biogenesis/degradation; Coiled coil;
KW Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome.
FT CHAIN 1..512
FT /note="Centrosomal protein CCDC61"
FT /id="PRO_0000311257"
FT REGION 1..142
FT /note="Head domain"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R9"
FT REGION 282..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 176..203
FT /evidence="ECO:0000255"
FT COILED 246..273
FT /evidence="ECO:0000255"
FT COMPBIAS 282..303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..360
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R9"
FT MOD_RES 282
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R9"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R9"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R9"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 447
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R9"
FT MOD_RES 473
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R9"
SQ SEQUENCE 512 AA; 57730 MW; 1FD0D07D29DB51D9 CRC64;
MEQPAGLQVD YMFRGVEHAV RVVVSGQVLE LEVEDRMTAD QWRGEFDANF IEDLTHKTGN
FKQFSIFCNM LESALTQSSE SVTLDLLTYT DLESLRSRKL GGRPGPCPRS AQLNSKRYLI
LIYSVEFDRI HYPLPLPYQG KPDPVVLQGI IRSLKEELGH LRGMNGGQDA RETEIWHLRE
QVTRLASEKR ELEAQLGRSR EEALAGRAAR QEAESLRGLV RGLELELRQE RGLGGRAAGR
RSQDCRRLAK ELEEVKASER NLRARLKTLN CELAMYRRGR RTLPAGARED RALSSRERST
SRGRTATRSS SRESNRGARS HGRPAHPSPS PTGSRVPRFD PTAFVKAKEK KQREIRMKRQ
QQQQQQRNRM GSGGSGDGPS VSWSHQTRPP AAVTGRGDAA NRSRNRSSSV DSFRSRCSSV
SSCSELEDFS QSVSKSRRCR GRGKPPSPIP WSGSKTKSTT RERNNHQRHL ASSGAWVPIK
EYSSDYQGAD MAEIDARLKA LQEYMNRLDT RS
