CLXN_DANRE
ID CLXN_DANRE Reviewed; 210 AA.
AC Q1LWZ0;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Calaxin {ECO:0000250|UniProtKB:Q9D3N2};
DE AltName: Full=EF-hand calcium-binding domain-containing protein 1;
GN Name=clxn; Synonyms=efcab1, si:ch211-173p18.9;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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 -!- FUNCTION: Regulates ciliary motility and is required for cilia-driven
CC determination of body laterality. {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:0000250|UniProtKB:Q96M63}.
CC -!- DISRUPTION PHENOTYPE: Knockout mutants show situs invertus but normal
CC formation of Kupffer's vesicle (KV) cilia (PubMed:31240264). However,
CC many of the KV cilia in the mutant beat with an irregular cycle in
CC contrast to the smooth rotary movement in wild-type fish
CC (PubMed:31240264). {ECO:0000269|PubMed:31240264}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI71473.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI71475.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BX510986; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC171473; AAI71473.1; ALT_INIT; mRNA.
DR EMBL; BC171475; AAI71475.1; ALT_INIT; mRNA.
DR RefSeq; NP_001038325.1; NM_001044860.1.
DR AlphaFoldDB; Q1LWZ0; -.
DR STRING; 7955.ENSDARP00000081908; -.
DR PaxDb; Q1LWZ0; -.
DR GeneID; 558421; -.
DR KEGG; dre:558421; -.
DR CTD; 66793; -.
DR ZFIN; ZDB-GENE-040914-40; efcab1.
DR eggNOG; KOG0044; Eukaryota.
DR HOGENOM; CLU_061288_3_2_1; -.
DR InParanoid; Q1LWZ0; -.
DR OMA; TWERGAN; -.
DR OrthoDB; 1331864at2759; -.
DR PhylomeDB; Q1LWZ0; -.
DR TreeFam; TF323358; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR Bgee; ENSDARG00000061377; Expressed in testis and 18 other tissues.
DR ExpressionAtlas; Q1LWZ0; baseline.
DR GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0003341; P:cilium movement; IMP:ZFIN.
DR GO; GO:0036158; P:outer dynein arm assembly; ISS: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; PF13202; EF-hand_5; 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 Calcium; Cell projection; Cytoplasm; Cytoskeleton; Metal-binding;
KW Reference proteome; Repeat.
FT CHAIN 1..210
FT /note="Calaxin"
FT /id="PRO_0000453980"
FT DOMAIN 64..99
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 100..135
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 145..180
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 77
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 79
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 81
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 83
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 88
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 113
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 115
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 117
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 119
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 124
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 158
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 160
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 162
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 164
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 169
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
SQ SEQUENCE 210 AA; 24535 MW; ACA2E92D65F425B6 CRC64;
MNRKLIQNLA ETLCRQVKHF NKTETECLIR LFNSLLGEQA ERKTTIGVDR AKFRNILHHT
FGMTDDMMTD RVCRVIDKDN DGYLSVKEWV EALSVFLRGT LDEKMKYCFE VYDLNGDGYI
SREEMFQMLK DSLIRQPTEE DPDEGIKDIV EIALKKMDYD HDGRVSYADF EKTVMDENLL
LEAFGNCLPD AKSVLAFEQQ AFQKHEHCKE
