CCD61_MOUSE
ID CCD61_MOUSE Reviewed; 511 AA.
AC Q3UJV1;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
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|MGI:MGI:2685005};
GN Synonyms=Gm159, VFL3 {ECO:0000250|UniProtKB:Q9Y6R9};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-371 AND SER-374, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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}.
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; AK146297; BAE27054.1; -; mRNA.
DR CCDS; CCDS39791.1; -.
DR RefSeq; NP_001028486.1; NM_001033314.3.
DR RefSeq; XP_006539877.2; XM_006539814.3.
DR RefSeq; XP_006539878.1; XM_006539815.1.
DR RefSeq; XP_006539879.1; XM_006539816.1.
DR RefSeq; XP_006539881.1; XM_006539818.1.
DR AlphaFoldDB; Q3UJV1; -.
DR SMR; Q3UJV1; -.
DR STRING; 10090.ENSMUSP00000096377; -.
DR iPTMnet; Q3UJV1; -.
DR PhosphoSitePlus; Q3UJV1; -.
DR EPD; Q3UJV1; -.
DR jPOST; Q3UJV1; -.
DR MaxQB; Q3UJV1; -.
DR PaxDb; Q3UJV1; -.
DR PeptideAtlas; Q3UJV1; -.
DR PRIDE; Q3UJV1; -.
DR ProteomicsDB; 265712; -.
DR Antibodypedia; 49264; 124 antibodies from 18 providers.
DR DNASU; 232933; -.
DR Ensembl; ENSMUST00000098780; ENSMUSP00000096377; ENSMUSG00000074358.
DR GeneID; 232933; -.
DR KEGG; mmu:232933; -.
DR UCSC; uc009fjw.1; mouse.
DR CTD; 729440; -.
DR MGI; MGI:2685005; Ccdc61.
DR VEuPathDB; HostDB:ENSMUSG00000074358; -.
DR eggNOG; ENOG502QRAS; Eukaryota.
DR GeneTree; ENSGT00940000154133; -.
DR HOGENOM; CLU_038746_1_0_1; -.
DR InParanoid; Q3UJV1; -.
DR OMA; THRIKDK; -.
DR OrthoDB; 1433381at2759; -.
DR PhylomeDB; Q3UJV1; -.
DR TreeFam; TF329415; -.
DR BioGRID-ORCS; 232933; 1 hit in 73 CRISPR screens.
DR PRO; PR:Q3UJV1; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q3UJV1; protein.
DR Bgee; ENSMUSG00000074358; Expressed in indifferent gonad and 184 other tissues.
DR ExpressionAtlas; Q3UJV1; baseline and differential.
DR Genevisible; Q3UJV1; MM.
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:MGI.
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..511
FT /note="Centrosomal protein CCDC61"
FT /id="PRO_0000311256"
FT REGION 1..143
FT /note="Head domain"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R9"
FT REGION 284..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..476
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 344..362
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..413
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 283
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R9"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R9"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R9"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 374
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 446
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R9"
FT MOD_RES 472
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R9"
SQ SEQUENCE 511 AA; 57368 MW; 84DBB0F32986AF4F CRC64;
MDQPAGLQVD YIFRGVEHAV RVVVSGQVLE LEVEDRMTAD QWRGEFDANF IEDLTHKTGN
FKQFSIFCNM LESALTQSSE SVTLDLLTYT DLESLRSRKL GGRPGALAPR SAQLNSKRYL
ILIYSVEFDR IHYPLPLPYQ GKPDPVVLQG IIRSLKEELG HLRGLNGGQD ARETEIWHLR
EQVTRLTSEK RELEAQLGRS REEALAGRAA RQEAESLRGL VRGLELELRQ ERGLGGRAAG
RRSQDSRRLA KELEEVKASE RNLRARLKTL NSELAMYRRG RRTLPPVAVR EGRASSSRER
STSRGRAVTR SSSRESSRGA RGRGRPAHPS PSPTGSRAPR FDPTAFVKAK EKKQREIRMK
QQQQQRNRMG SGGSGDGPSV SWSQQTRPAA AVTGRGDAVN RSRNRSSSVD SFRSRCSSVS
SCSELEDFSH SVSRSRRCRG RGKPPSPTPW SRSKTKSTTQ ERSDHQRHLA SSGGWVPIKE
YSSDFQGADM AEIDARLKAL QEYMNRLDTR S