CFA45_MOUSE
ID CFA45_MOUSE Reviewed; 551 AA.
AC Q9D9U9;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Cilia- and flagella-associated protein 45 {ECO:0000303|PubMed:33139725};
DE AltName: Full=Coiled-coil domain-containing protein 19;
DE AltName: Full=Nasopharyngeal epithelium-specific protein 1 {ECO:0000303|PubMed:16141072};
GN Name=Cfap45;
GN Synonyms=Ccdc19 {ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072},
GN Nesg1;
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 {ECO:0000312|EMBL:BAB24596.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB24596.1};
RC TISSUE=Testis {ECO:0000312|EMBL:BAB24596.1};
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain {ECO:0000312|EMBL:AAI50930.1};
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 [4]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=33139725; DOI=10.1038/s41467-020-19113-0;
RA Dougherty G.W., Mizuno K., Noethe-Menchen T., Ikawa Y., Boldt K.,
RA Ta-Shma A., Aprea I., Minegishi K., Pang Y.P., Pennekamp P., Loges N.T.,
RA Raidt J., Hjeij R., Wallmeier J., Mussaffi H., Perles Z., Elpeleg O.,
RA Rabert F., Shiratori H., Letteboer S.J., Horn N., Young S., Struenker T.,
RA Stumme F., Werner C., Olbrich H., Takaoka K., Ide T., Twan W.K.,
RA Biebach L., Grosse-Onnebrink J., Klinkenbusch J.A., Praveen K.,
RA Bracht D.C., Hoeben I.M., Junger K., Guetzlaff J., Cindric S., Aviram M.,
RA Kaiser T., Memari Y., Dzeja P.P., Dworniczak B., Ueffing M., Roepman R.,
RA Bartscherer K., Katsanis N., Davis E.E., Amirav I., Hamada H., Omran H.;
RT "CFAP45 deficiency causes situs abnormalities and asthenospermia by
RT disrupting an axonemal adenine nucleotide homeostasis module.";
RL Nat. Commun. 11:5520-5520(2020).
CC -!- FUNCTION: Microtubule inner protein (MIP) part of the dynein-decorated
CC doublet microtubules (DMTs) in cilia axoneme, which is required for
CC motile cilia beating (By similarity). It is an AMP-binding protein that
CC may facilitate dynein ATPase-dependent ciliary and flagellar beating
CC via adenine nucleotide homeostasis. May function as a donor of AMP to
CC AK8 and hence promote ADP production (PubMed:33139725).
CC {ECO:0000250|UniProtKB:Q32LN4, ECO:0000269|PubMed:33139725}.
CC -!- SUBUNIT: Interacts with AK8; dimerization with AK8 may create a cavity
CC at the interface of the dimer that can accommodate AMP (By similarity).
CC Interacts with CFAP52 (By similarity). Interacts with ENKUR (By
CC similarity). Directly interacts with DNALI1 (By similarity). Interacts
CC with DNAH11 (By similarity). Interacts with DNAI1 (By similarity).
CC {ECO:0000250|UniProtKB:Q9UL16}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000269|PubMed:33139725}. Cytoplasm, cytoskeleton, flagellum
CC axoneme {ECO:0000269|PubMed:33139725}. Note=Located in the proximal
CC region of respiratory cilia. {ECO:0000269|PubMed:33139725}.
CC -!- TISSUE SPECIFICITY: Expressed in respiratory cells and in sperm (at
CC protein level). {ECO:0000269|PubMed:33139725}.
CC -!- DISRUPTION PHENOTYPE: Knockout animals display left-right asymmetry
CC abnormalities, including situs inversus totalis. Nodal cilia rotational
CC speed is reduced compared to heterozyous littermates. Mutant males also
CC exhibit asthenospermia and are infertile.
CC {ECO:0000269|PubMed:33139725}.
CC -!- SIMILARITY: Belongs to the CFAP45 family. {ECO:0000305}.
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DR EMBL; AK006449; BAB24596.1; -; mRNA.
DR EMBL; BC150929; AAI50930.1; -; mRNA.
DR EMBL; BC151048; AAI51049.1; -; mRNA.
DR EMBL; BC151055; AAI51056.1; -; mRNA.
DR CCDS; CCDS48447.1; -.
DR RefSeq; NP_082248.1; NM_027972.1.
DR AlphaFoldDB; Q9D9U9; -.
DR SMR; Q9D9U9; -.
DR STRING; 10090.ENSMUSP00000083057; -.
DR PhosphoSitePlus; Q9D9U9; -.
DR jPOST; Q9D9U9; -.
DR MaxQB; Q9D9U9; -.
DR PaxDb; Q9D9U9; -.
DR PRIDE; Q9D9U9; -.
DR ProteomicsDB; 333100; -.
DR Antibodypedia; 34262; 152 antibodies from 21 providers.
DR Ensembl; ENSMUST00000085894; ENSMUSP00000083057; ENSMUSG00000026546.
DR GeneID; 71870; -.
DR KEGG; mmu:71870; -.
DR UCSC; uc007dqq.2; mouse.
DR CTD; 25790; -.
DR MGI; MGI:1919120; Cfap45.
DR VEuPathDB; HostDB:ENSMUSG00000026546; -.
DR eggNOG; ENOG502QPRZ; Eukaryota.
DR GeneTree; ENSGT00730000111174; -.
DR HOGENOM; CLU_026959_1_1_1; -.
DR InParanoid; Q9D9U9; -.
DR OMA; MRENCLP; -.
DR OrthoDB; 1428717at2759; -.
DR PhylomeDB; Q9D9U9; -.
DR TreeFam; TF327685; -.
DR BioGRID-ORCS; 71870; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Cfap45; mouse.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9D9U9; protein.
DR Bgee; ENSMUSG00000026546; Expressed in spermatid and 77 other tissues.
DR ExpressionAtlas; Q9D9U9; baseline and differential.
DR GO; GO:0097728; C:9+0 motile cilium; IDA:MGI.
DR GO; GO:0097729; C:9+2 motile cilium; ISO:MGI.
DR GO; GO:0005879; C:axonemal microtubule; ISS:UniProtKB.
DR GO; GO:0005930; C:axoneme; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:GOC.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0016208; F:AMP binding; ISO:MGI.
DR GO; GO:0090660; P:cerebrospinal fluid circulation; IMP:MGI.
DR GO; GO:0060287; P:epithelial cilium movement involved in determination of left/right asymmetry; IMP:MGI.
DR GO; GO:0061966; P:establishment of left/right asymmetry; ISO:MGI.
DR GO; GO:0030317; P:flagellated sperm motility; IMP:MGI.
DR GO; GO:0060296; P:regulation of cilium beat frequency involved in ciliary motility; IMP:MGI.
DR InterPro; IPR033253; CFAP45.
DR InterPro; IPR043597; TPH_dom.
DR PANTHER; PTHR15504; PTHR15504; 1.
DR Pfam; PF13868; TPH; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cilium; Coiled coil; Cytoplasm; Cytoskeleton; Flagellum;
KW Reference proteome.
FT CHAIN 1..551
FT /note="Cilia- and flagella-associated protein 45"
FT /id="PRO_0000454202"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 276..524
FT /evidence="ECO:0000255"
SQ SEQUENCE 551 AA; 65826 MW; 6FA1D798D877977E CRC64;
MPLRPGDASS SASTASNRSR TRTRYRTKAM NSEVDESLFG GVKPSSQGKS DSPIVVIHDK
HAIRKTLSAL GLEHKTETIQ LITRDMVREL IVPTEDPSGE SLIISPEEFE RIKWASQVLT
KEELNAREQA LKKEKEGILE AVTIRKKIMK QKEMTWNNNK KLSDLEEVAR ERAQNLLQRA
DKLRMEQEEE LKDMSKIILN AKCHAIRDAQ ILEKQQIQKE LDEEERRLDH MMEIDRRESL
QRQEDRERKR REERVRGKRH IVEQIKKNEE ERSLQAEHRE QEKEQMLAYL DRLQEEDLQD
LERRHQEKLK MQAEIKRIND ENQRQKAEML AQERLADQMV MEFTKKKMAR EAEYEAEQEK
IRREKEKEIA RLRALQEKAQ DYQAEQDALR AKRNQEVADR EWRRKEKENA QKKIETEEKL
RKSRLEQVAF KEHTLAVQVQ RDRDEFERIL RAQREQIERE KQEQEKKAKG CLQHANELRR
QVRENQQKHV QNRLATFEEG RRLKEEAEKR RERIEDIKKQ KLEELRATGL PEKYCIEVER
KANILPATSV N
