CLXN_XENLA
ID CLXN_XENLA Reviewed; 208 AA.
AC Q3KQ77;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Calaxin {ECO:0000250|UniProtKB:Q9D3N2};
DE AltName: Full=EF-hand calcium-binding domain-containing protein 1;
GN Name=clxn; Synonyms=efcab1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC {ECO:0000250|UniProtKB:Q32L26, ECO:0000250|UniProtKB:Q9D3N2}.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC106351; AAI06352.1; -; mRNA.
DR RefSeq; NP_001089695.1; NM_001096226.1.
DR AlphaFoldDB; Q3KQ77; -.
DR SMR; Q3KQ77; -.
DR DNASU; 734757; -.
DR GeneID; 734757; -.
DR KEGG; xla:734757; -.
DR CTD; 734757; -.
DR Xenbase; XB-GENE-5727581; efcab1.S.
DR OrthoDB; 1331864at2759; -.
DR Proteomes; UP000186698; Chromosome 6S.
DR Bgee; 734757; Expressed in testis and 19 other tissues.
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; ISS:UniProtKB.
DR GO; GO:0036158; P:outer dynein arm assembly; ISS:UniProtKB.
DR GO; GO:0003352; P:regulation of cilium movement; ISS:UniProtKB.
DR GO; GO:1901317; P:regulation of flagellated sperm motility; 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; PF13499; EF-hand_7; 1.
DR SMART; SM00054; EFh; 3.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
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..208
FT /note="Calaxin"
FT /id="PRO_0000251971"
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:0000305"
FT BINDING 79
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 81
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 113
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 115
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 117
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 119
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 124
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 158
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000305"
FT BINDING 160
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000305"
FT BINDING 162
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000305"
FT BINDING 164
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000305"
FT BINDING 169
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000305"
SQ SEQUENCE 208 AA; 24165 MW; 56B92E23489AD25C CRC64;
MNRKNLQKQA EALSRLIKHF SKSEVESLIR LYHTLVGRPG DPNTRRGIDR NTFRNILHNT
FGMTDDMIMD RVFRGFDKDN DSFISVTEWV EGLSVFLHGT LEEKIKYCFG VYDLNGDGYI
SREEMFHMLK NSLLKQPSEE DPDEGVKDLV EIALKKMDYD HDSKLSYTDF EKAVQEENLL
LEAFGTCLPD SKCIMAFERQ AFTEMNDI
