CLXN_MOUSE
ID CLXN_MOUSE Reviewed; 212 AA.
AC Q9D3N2; Q8BSW3; Q8C982; Q8CAI0; Q9D527; Q9D5E7;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Calaxin {ECO:0000303|PubMed:31240264};
DE AltName: Full=EF-hand calcium-binding domain-containing protein 1;
GN Name=Clxn; Synonyms=Efcab1 {ECO:0000312|MGI:MGI:1914043};
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] (ISOFORMS 1; 2; 3 AND 4).
RC STRAIN=C57BL/6J;
RC TISSUE=Brain cortex, Cerebellum, Embryo, Head, Hypothalamus, Pituitary, and
RC 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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Eye;
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, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=31240264; DOI=10.1038/s42003-019-0462-y;
RA Sasaki K., Shiba K., Nakamura A., Kawano N., Satouh Y., Yamaguchi H.,
RA Morikawa M., Shibata D., Yanase R., Jokura K., Nomura M., Miyado M.,
RA Takada S., Ueno H., Nonaka S., Baba T., Ikawa M., Kikkawa M., Miyado K.,
RA Inaba K.;
RT "Calaxin is required for cilia-driven determination of vertebrate
RT laterality.";
RL Commun. Biol. 2:226-226(2019).
CC -!- FUNCTION: Component of the outer dynein arm-docking complex (ODA-DC)
CC that mediates outer dynein arms (ODA) binding onto the doublet
CC microtubule. Seems to regulate the assembly of both ODAs and their
CC axonemal docking complex onto ciliary microtubules (By similarity).
CC Regulates ciliary and flagellar motility and is required for cilia-
CC driven determination of body laterality (PubMed:31240264).
CC {ECO:0000250|UniProtKB:Q32L26, ECO:0000269|PubMed:31240264}.
CC -!- SUBUNIT: Component of the outer dynein arm-docking complex along with
CC ODAD1, ODAD2, ODAD3 and ODAD4. {ECO:0000250|UniProtKB:Q32L26}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000269|PubMed:31240264}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9D3N2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D3N2-2; Sequence=VSP_020830, VSP_020831;
CC Name=3;
CC IsoId=Q9D3N2-3; Sequence=VSP_020828, VSP_020829;
CC Name=4;
CC IsoId=Q9D3N2-4; Sequence=VSP_020827;
CC -!- DISRUPTION PHENOTYPE: Mice display typical phenotypes of primary
CC ciliary dyskinesia, including hydrocephalus, situs inversus, and
CC abnormal motility of trachea cilia and sperm flagella
CC (PubMed:31240264). Strikingly, both males and females are viable and
CC fertile (PubMed:31240264). The 9 + 2 axonemal structures of epithelial
CC multicilia and sperm flagella are normal, but the formation of 9 + 0
CC nodal cilia is significantly disrupted (PubMed:31240264).
CC {ECO:0000269|PubMed:31240264}.
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DR EMBL; AK015426; BAB29839.1; -; mRNA.
DR EMBL; AK015866; BAB30007.1; -; mRNA.
DR EMBL; AK017267; BAB30660.1; -; mRNA.
DR EMBL; AK030381; BAC26934.1; -; mRNA.
DR EMBL; AK038735; BAC30115.1; -; mRNA.
DR EMBL; AK042748; BAC31349.1; -; mRNA.
DR EMBL; AK043519; BAC31565.1; -; mRNA.
DR EMBL; AK077722; BAC36981.1; -; mRNA.
DR EMBL; BC085167; AAH85167.1; -; mRNA.
DR CCDS; CCDS27975.1; -. [Q9D3N2-1]
DR RefSeq; NP_080045.1; NM_025769.3. [Q9D3N2-1]
DR AlphaFoldDB; Q9D3N2; -.
DR SMR; Q9D3N2; -.
DR STRING; 10090.ENSMUSP00000087744; -.
DR PhosphoSitePlus; Q9D3N2; -.
DR MaxQB; Q9D3N2; -.
DR PaxDb; Q9D3N2; -.
DR PRIDE; Q9D3N2; -.
DR ProteomicsDB; 277723; -. [Q9D3N2-1]
DR ProteomicsDB; 277724; -. [Q9D3N2-2]
DR ProteomicsDB; 277725; -. [Q9D3N2-3]
DR ProteomicsDB; 277726; -. [Q9D3N2-4]
DR Antibodypedia; 11583; 71 antibodies from 18 providers.
DR DNASU; 66793; -.
DR Ensembl; ENSMUST00000090277; ENSMUSP00000087744; ENSMUSG00000068617. [Q9D3N2-1]
DR Ensembl; ENSMUST00000228998; ENSMUSP00000155377; ENSMUSG00000068617. [Q9D3N2-3]
DR Ensembl; ENSMUST00000229121; ENSMUSP00000155692; ENSMUSG00000068617. [Q9D3N2-2]
DR Ensembl; ENSMUST00000229825; ENSMUSP00000155853; ENSMUSG00000068617. [Q9D3N2-4]
DR GeneID; 66793; -.
DR KEGG; mmu:66793; -.
DR UCSC; uc007yhn.1; mouse. [Q9D3N2-1]
DR CTD; 66793; -.
DR MGI; MGI:1914043; Efcab1.
DR VEuPathDB; HostDB:ENSMUSG00000068617; -.
DR eggNOG; KOG0044; Eukaryota.
DR GeneTree; ENSGT00940000159968; -.
DR HOGENOM; CLU_061288_3_2_1; -.
DR InParanoid; Q9D3N2; -.
DR OMA; FTENIRH; -.
DR OrthoDB; 1331864at2759; -.
DR PhylomeDB; Q9D3N2; -.
DR TreeFam; TF323358; -.
DR BioGRID-ORCS; 66793; 2 hits in 71 CRISPR screens.
DR PRO; PR:Q9D3N2; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9D3N2; protein.
DR Bgee; ENSMUSG00000068617; Expressed in islet of Langerhans and 128 other tissues.
DR Genevisible; Q9D3N2; MM.
DR GO; GO:0097729; C:9+2 motile cilium; ISO:MGI.
DR GO; GO:0005930; C:axoneme; ISO:MGI.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0048487; F:beta-tubulin binding; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:0120152; F:calcium-dependent outer dynein arm binding; ISO:MGI.
DR GO; GO:0140659; F:cytoskeletal motor regulator activity; ISO:MGI.
DR GO; GO:0045504; F:dynein heavy chain binding; ISO:MGI.
DR GO; GO:0060326; P:cell chemotaxis; ISO:MGI.
DR GO; GO:0003341; P:cilium movement; ISS:UniProtKB.
DR GO; GO:0036158; P:outer dynein arm assembly; ISS:UniProtKB.
DR GO; GO:0003352; P:regulation of cilium movement; IMP:UniProtKB.
DR GO; GO:1901317; P:regulation of flagellated sperm motility; IMP:UniProtKB.
DR CDD; cd00051; EFh; 2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR028846; Recoverin.
DR PANTHER; PTHR23055; PTHR23055; 1.
DR Pfam; PF00036; EF-hand_1; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00054; EFh; 3.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 3.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 2: Evidence at transcript level;
KW Alternative splicing; Calcium; Cell projection; Cytoplasm; Cytoskeleton;
KW Metal-binding; Reference proteome; Repeat.
FT CHAIN 1..212
FT /note="Calaxin"
FT /id="PRO_0000251970"
FT DOMAIN 65..100
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 101..136
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 146..181
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 78
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 80
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 82
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 84
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 89
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 114
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 116
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 118
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 125
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 159
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 161
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 163
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 165
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 170
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT VAR_SEQ 108..212
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020827"
FT VAR_SEQ 159..169
FT /note="DHDHDGKLSFV -> CAFAARMPCSD (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020828"
FT VAR_SEQ 170..212
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020829"
FT VAR_SEQ 194..195
FT /note="SQ -> LK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020830"
FT VAR_SEQ 196..212
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020831"
FT CONFLICT 6
FT /note="L -> Q (in Ref. 1; BAB29839)"
FT /evidence="ECO:0000305"
FT CONFLICT 35
FT /note="L -> W (in Ref. 1; BAC30115)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="K -> R (in Ref. 1; BAC26934)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 212 AA; 24606 MW; F85651A9D0343F43 CRC64;
MNRKKLQKLT DTLTKNCKHF DKFEVKCLIT LFYNLVGDVA ERPGVVTGLD RNVFRNILHV
TFGMTDDMIM DRVFRGFDKD NDGCISVSEW IHGLSLFLRG TLDEKMKYCF EVFDLNGDGF
ISKEEMFHML KNSLLKQPSE EDPDEGIKDL VEITLKKMDH DHDGKLSFVD YEKAVREENL
LLEAFGPCLP DPKSQMEFEA QVFKDPNEFN DM
