CC181_MOUSE
ID CC181_MOUSE Reviewed; 509 AA.
AC Q80ZU5; Q3UF07; Q8C631; Q9CUL9;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Coiled-coil domain-containing protein 181 {ECO:0000305};
GN Name=Ccdc181 {ECO:0000312|MGI:MGI:1922145};
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=C57BL/6J; TISSUE=Sympathetic ganglion, and Testis;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Olfactory epithelium;
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 [3]
RP FUNCTION, SUBUNIT, INTERACTION WITH HOOK1; HOOK2 AND HOOK3, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=28283191; DOI=10.1016/j.ejcb.2017.02.003;
RA Schwarz T., Prieler B., Schmid J.A., Grzmil P., Neesen J.;
RT "Ccdc181 is a microtubule-binding protein that interacts with Hook1 in
RT haploid male germ cells and localizes to the sperm tail and motile cilia.";
RL Eur. J. Cell Biol. 96:276-288(2017).
CC -!- FUNCTION: Microtubule-binding protein that localizes to the
CC microtubular manchette of elongating spermatids.
CC {ECO:0000305|PubMed:28283191}.
CC -!- SUBUNIT: Homodimer (PubMed:28283191). Interacts with HOOK1
CC (PubMed:28283191). Interacts with HOOK2 (PubMed:28283191). Interacts
CC with HOOK3 (PubMed:28283191). {ECO:0000269|PubMed:28283191}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:28283191}. Cell projection, cilium, flagellum
CC {ECO:0000269|PubMed:28283191}. Note=Localizes to the microtubular
CC manchette of elongating spermatids (PubMed:28283191). Localizes to the
CC sperm flagella and to the basal half of motile cilia (PubMed:28283191).
CC {ECO:0000269|PubMed:28283191}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in testis
CC (PubMed:28283191). Expressed at lower level in brain, eye, trachea and
CC lung (PubMed:28283191). Barely expressed in tongue, heart, liver,
CC kidney, spleen and muscle (PubMed:28283191). Present at high level in
CC elongating spermatids, whereas lower levels are observed in round
CC spermatids (at protein level) (PubMed:28283191).
CC {ECO:0000269|PubMed:28283191}.
CC -!- DEVELOPMENTAL STAGE: In testis, expressed at low level until day 20,
CC when round spermatids appear for the first time. After day 20, a sharp
CC and constant increase of expression is observed.
CC {ECO:0000269|PubMed:28283191}.
CC -!- SIMILARITY: Belongs to the CCDC181 family. {ECO:0000305}.
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DR EMBL; AK015464; BAB29858.1; -; mRNA.
DR EMBL; AK076640; BAC36430.1; -; mRNA.
DR EMBL; AK149168; BAE28754.1; -; mRNA.
DR EMBL; BC048086; AAH48086.1; -; mRNA.
DR CCDS; CCDS15434.1; -.
DR RefSeq; NP_083391.2; NM_029115.3.
DR AlphaFoldDB; Q80ZU5; -.
DR SMR; Q80ZU5; -.
DR BioGRID; 217061; 1.
DR STRING; 10090.ENSMUSP00000027867; -.
DR iPTMnet; Q80ZU5; -.
DR PhosphoSitePlus; Q80ZU5; -.
DR MaxQB; Q80ZU5; -.
DR PaxDb; Q80ZU5; -.
DR PRIDE; Q80ZU5; -.
DR ProteomicsDB; 265586; -.
DR Antibodypedia; 34357; 98 antibodies from 13 providers.
DR DNASU; 74895; -.
DR Ensembl; ENSMUST00000027867; ENSMUSP00000027867; ENSMUSG00000026578.
DR GeneID; 74895; -.
DR KEGG; mmu:74895; -.
DR UCSC; uc007dif.2; mouse.
DR CTD; 57821; -.
DR MGI; MGI:1922145; Ccdc181.
DR VEuPathDB; HostDB:ENSMUSG00000026578; -.
DR eggNOG; ENOG502QV5R; Eukaryota.
DR GeneTree; ENSGT00390000018244; -.
DR HOGENOM; CLU_040811_0_0_1; -.
DR InParanoid; Q80ZU5; -.
DR OMA; FKAWLMR; -.
DR OrthoDB; 1520743at2759; -.
DR PhylomeDB; Q80ZU5; -.
DR TreeFam; TF331115; -.
DR BioGRID-ORCS; 74895; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Ccdc181; mouse.
DR PRO; PR:Q80ZU5; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q80ZU5; protein.
DR Bgee; ENSMUSG00000026578; Expressed in seminiferous tubule of testis and 219 other tissues.
DR Genevisible; Q80ZU5; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0002177; C:manchette; IDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0036126; C:sperm flagellum; IDA:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR InterPro; IPR026687; CCDC181.
DR PANTHER; PTHR14320; PTHR14320; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cilium; Coiled coil; Cytoplasm; Cytoskeleton; Flagellum;
KW Microtubule; Reference proteome.
FT CHAIN 1..509
FT /note="Coiled-coil domain-containing protein 181"
FT /id="PRO_0000279467"
FT REGION 1..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 335..377
FT /evidence="ECO:0000255"
FT COILED 418..488
FT /evidence="ECO:0000255"
FT COMPBIAS 1..22
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 2
FT /note="D -> N (in Ref. 1; BAB29858)"
FT /evidence="ECO:0000305"
FT CONFLICT 39
FT /note="E -> K (in Ref. 1; BAE28754)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="N -> H (in Ref. 1; BAC36430)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="M -> I (in Ref. 1; BAC36430)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 509 AA; 59241 MW; 79D5F7ECBBCE5035 CRC64;
MDEDKDIDSK ESGEYEDDFE KDLEWLINDK EKSNGSTIEM ACKKEDDLDQ VLKENETETE
LGQQLSDPDN SPKDEALPRR NDFISVPSIQ PLDPISDSDS ENSFQDSKPE NQKDLEDEED
EEVRRYIMEK IIEANKLLQT QEPVNDKRER KLKFKDKLVD LEVPPLEDSD TCKALLENET
NMSGKLSQLC ISGDLEQESV LVSVTDGSCE ENDRKILVER DGKFELMNLQ DIESQGFLPP
ISSANSVEHE SSQLPLRAPN PSVGGIKKEE SEAKGHVLPI SPAGEPLAQV PQLLPNPKNR
PSSAANPDVT KKARRSNHRI QSAGVSPVTS TYCLSPRQKE LQKQLERKRE KLKREEEQRK
LEEENEKKKE NEMVFKAWLQ KKREQVIEMR RVQRAKQIED MSSRQVNRDP QQAFRLWLKK
KHEEQMKERK TEELRKQEEC LFFLRGTEGR ERAFRQWLRR KQIEKIAEQQ AVKERARQLR
LEARRSKQLQ SSLYSIPEAK AFRFTDHYN
