DNAI7_MOUSE
ID DNAI7_MOUSE Reviewed; 730 AA.
AC Q6TDU8; Q3V0T6; Q64JA2; Q675B4; Q675B5; Q8BZM3;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Dynein axonemal intermediate chain 7 {ECO:0000305};
DE AltName: Full=Cancer susceptibility candidate gene 1 protein homolog;
DE Short=Protein CASC1;
DE AltName: Full=Cilia and flagella associated protein 94;
DE AltName: Full=Lung adenoma susceptibility protein 1 {ECO:0000303|PubMed:14583591};
GN Name=Dnai7;
GN Synonyms=Casc1, Cfap94 {ECO:0000312|MGI:MGI:2444480},
GN Las1 {ECO:0000303|PubMed:14583591};
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 [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=A/J; TISSUE=Lung;
RX PubMed=14583591; DOI=10.1073/pnas.2133947100;
RA Zhang Z., Futamura M., Vikis H.G., Wang M., Li J., Wang Y., Guan K.-L.,
RA You M.;
RT "Positional cloning of the major quantitative trait locus underlying lung
RT tumor susceptibility in mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12642-12647(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT SER-60.
RC STRAIN=A/J, and C57BL/6J; TISSUE=Lung;
RX PubMed=15064703; DOI=10.1038/sj.onc.1207584;
RA Manenti G., Galbiati F., Gianni-Barrera R., Pettinicchio A., Acevedo A.,
RA Dragani T.A.;
RT "Haplotype sharing suggests that a genomic segment containing six genes
RT accounts for the pulmonary adenoma susceptibility 1 (Pas1) locus activity
RT in mice.";
RL Oncogene 23:4495-4504(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANT
RP SER-60.
RC STRAIN=C57BL/6J; TISSUE=Diencephalon, 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=16862160; DOI=10.1038/ng1849;
RA Liu P., Wang Y., Vikis H., Maciag A., Wang D., Lu Y., Liu Y., You M.;
RT "Candidate lung tumor susceptibility genes identified through whole-genome
RT association analyses in inbred mice.";
RL Nat. Genet. 38:888-895(2006).
RN [6]
RP INTERACTION WITH TUBULIN, INTERACTION WITH MICROTUBULE, DEVELOPMENTAL
RP STAGE, SUBCELLULAR LOCATION, UBIQUITINATION, FUNCTION, AND CHARACTERIZATION
RP OF VARIANT SER-60.
RX PubMed=17974961; DOI=10.1158/0008-5472.can-07-2574;
RA Liu Y., Vikis H.G., Yi Y., Futamura M., Wang Y., You M.;
RT "Degradation of lung adenoma susceptibility 1, a major candidate mouse lung
RT tumor modifier, is required for cell cycle progression.";
RL Cancer Res. 67:10207-10213(2007).
RN [7]
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).
RN [8]
RP SUBUNIT, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=30060180; DOI=10.1093/jmcb/mjy043;
RA Zhang Y., Chen Y., Zheng J., Wang J., Duan S., Zhang W., Yan X., Zhu X.;
RT "Vertebrate Dynein-f depends on Wdr78 for axonemal localization and is
RT essential for ciliary beat.";
RL J. Mol. Cell Biol. 11:383-394(2019).
CC -!- FUNCTION: Via its association with the multisubunit axonemal dynein
CC complex, is potentially involved in the regulation of cilia function
CC (PubMed:30060180). May also act as a cell cycle regulator
CC (PubMed:17974961). {ECO:0000269|PubMed:17974961,
CC ECO:0000269|PubMed:30060180}.
CC -!- SUBUNIT: Part of the multisubunit axonemal dynein complex formed at
CC least of two heavy chains and a number of intermediate and light chains
CC (PubMed:30060180). Interacts with tubulin (PubMed:17974961). Associates
CC with microtubule (PubMed:17974961). {ECO:0000269|PubMed:17974961,
CC ECO:0000269|PubMed:30060180}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000269|PubMed:30060180}. Cytoplasm {ECO:0000269|PubMed:14583591}.
CC Note=Colocalizes with microtubules in interphase.
CC {ECO:0000269|PubMed:17974961}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6TDU8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6TDU8-2; Sequence=VSP_033384, VSP_033387;
CC Name=3;
CC IsoId=Q6TDU8-3; Sequence=VSP_033388, VSP_033385, VSP_033386;
CC -!- TISSUE SPECIFICITY: High expressed in lung, kidney, and testis.
CC {ECO:0000269|PubMed:14583591}.
CC -!- DEVELOPMENTAL STAGE: Cell cycle-dependent expression. Not detected in
CC G0 cells, starts to accumulate in early S phase, reaches the highest
CC level in the G2 phase, and drops to very low levels at mitosis.
CC {ECO:0000269|PubMed:17974961}.
CC -!- PTM: Ubiquitinated. Ubiquitination leads to its degradation through the
CC 26S proteasome. Ubiquitin-proteasome-mediated DNAI7 degradation occurs
CC in mitosis. {ECO:0000269|PubMed:17974961}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice display a higher susceptibility to
CC chemical induction of lung tumors. {ECO:0000269|PubMed:16862160}.
CC -!- SIMILARITY: Belongs to the DNAI7 family. {ECO:0000305}.
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DR EMBL; AY423542; AAQ93498.1; -; mRNA.
DR EMBL; AY485607; AAS55696.1; -; mRNA.
DR EMBL; AY485608; AAS55697.1; -; mRNA.
DR EMBL; AY490383; AAT72330.1; -; Genomic_DNA.
DR EMBL; AY490384; AAT72331.1; -; Genomic_DNA.
DR EMBL; AK034148; BAC28607.1; -; mRNA.
DR EMBL; AK132912; BAE21417.1; -; mRNA.
DR EMBL; BC120743; AAI20744.1; -; mRNA.
DR EMBL; BC125423; AAI25424.1; -; mRNA.
DR CCDS; CCDS39705.1; -. [Q6TDU8-1]
DR RefSeq; NP_796196.3; NM_177222.4.
DR AlphaFoldDB; Q6TDU8; -.
DR SMR; Q6TDU8; -.
DR BioGRID; 236199; 1.
DR STRING; 10090.ENSMUSP00000062279; -.
DR PhosphoSitePlus; Q6TDU8; -.
DR MaxQB; Q6TDU8; -.
DR PaxDb; Q6TDU8; -.
DR PRIDE; Q6TDU8; -.
DR ProteomicsDB; 265666; -. [Q6TDU8-1]
DR ProteomicsDB; 265667; -. [Q6TDU8-2]
DR ProteomicsDB; 265668; -. [Q6TDU8-3]
DR GeneID; 320662; -.
DR KEGG; mmu:320662; -.
DR UCSC; uc009erb.1; mouse. [Q6TDU8-1]
DR UCSC; uc009ere.2; mouse. [Q6TDU8-3]
DR UCSC; uc012evn.1; mouse. [Q6TDU8-2]
DR CTD; 320662; -.
DR MGI; MGI:2444480; Casc1.
DR eggNOG; ENOG502QQM9; Eukaryota.
DR InParanoid; Q6TDU8; -.
DR OrthoDB; 526857at2759; -.
DR PhylomeDB; Q6TDU8; -.
DR TreeFam; TF326474; -.
DR BioGRID-ORCS; 320662; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Casc1; mouse.
DR PRO; PR:Q6TDU8; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q6TDU8; protein.
DR GO; GO:0005858; C:axonemal dynein complex; IDA:UniProtKB.
DR GO; GO:0005930; C:axoneme; IBA:GO_Central.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005881; C:cytoplasmic microtubule; IDA:MGI.
DR GO; GO:0036156; C:inner dynein arm; ISO:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
DR GO; GO:0043014; F:alpha-tubulin binding; ISO:MGI.
DR GO; GO:0048487; F:beta-tubulin binding; IDA:MGI.
DR GO; GO:0008017; F:microtubule binding; IDA:MGI.
DR GO; GO:0051012; P:microtubule sliding; ISO:MGI.
DR InterPro; IPR031826; IC97/Casc1_N.
DR InterPro; IPR023247; IC97/Dnai7-like.
DR PANTHER; PTHR20929; PTHR20929; 1.
DR Pfam; PF15927; Casc1_N; 1.
DR PRINTS; PR02043; CANCERSCCP1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cytoplasm; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..730
FT /note="Dynein axonemal intermediate chain 7"
FT /id="PRO_0000332733"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..206
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033388"
FT VAR_SEQ 1..13
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033384"
FT VAR_SEQ 342..359
FT /note="TSDSEGEDSQTTQLELEM -> VGYSVSLSVCLSSVYIPG (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033385"
FT VAR_SEQ 360..730
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033386"
FT VAR_SEQ 604..641
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033387"
FT VARIANT 60
FT /note="N -> S (in strain: C57BL/6J; could be associated
FT with tumor susceptibility; does not affect binding with
FT tubulin; more unstable)"
FT /evidence="ECO:0000269|PubMed:15064703,
FT ECO:0000269|PubMed:16141072, ECO:0000269|PubMed:17974961"
SQ SEQUENCE 730 AA; 84966 MW; 3F3F622B1E1B7344 CRC64;
MAPKSKKAPS KKKMTKAERL RLMQEEEERR LKEEEEARLK FEKEEQERLE IQRIEREKWN
LLEKKDLERR SQELEELALL EGCFPEAEKQ KREIRALAQW KHYTECDGSP DPWVAQEMNT
FISLWEEEKN QAFEQVMEKS KLVLSLIEKV KLILLETPTY ELDHRTVLQH QGSILRLQEL
LSLKINVATE LLLRQASNLA DLDTGNMEKI IKDENVTLYV WANLKKNPRH RSVRFSETQI
GFEIPRILAT SNVALRLLHT RYDHITPLFP IAVTEQNQNP VGAEQVNVEE STEKAMTEEK
LFTEEKAANE DEQPKAEQER ELNLVQEENK YEAIENTVLQ RTSDSEGEDS QTTQLELEMK
LLSEAVLAAQ LCLVENVVEL PEASQAYKVD LCHFSTLGGV YHLDVLELPP QCKPVKGWVL
VEILQEGLQR FIYPPDTTEE PDPDVTFPPI EVTLEIHKSV IFFERPRVVR WDNEGKFWRS
DGISSVYYNR EDRLLTFSMD TLGPVTLIQD AHVNMPYQSW EMSPCGMNKV LLIVKTVFME
LQIYIKENLC MLASVKLRGK GLEFHLKGKW MAPIPFILAL KEAGLNIFPA VYSHFYVVIN
NKVPQVELKA YRQMALLSSA FSFGWSKWNM VCNSTRVVIR VREQLSEETE HHTWSLLMFS
GDRAQMLKMQ EENDKFSEAL REGTEFHSTL YHMMKDFASP VAMERVRHSN CQFIDSVCYM
LLSIRVLSYS
