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CLXN_BOVIN
ID   CLXN_BOVIN              Reviewed;         212 AA.
AC   Q32L26;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 93.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0007744|PDB:7RRO}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS), SUBUNIT, FUNCTION,
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=34715025; DOI=10.1016/j.cell.2021.10.007;
RA   Gui M., Farley H., Anujan P., Anderson J.R., Maxwell D.W., Whitchurch J.B.,
RA   Botsch J.J., Qiu T., Meleppattu S., Singh S.K., Zhang Q., Thompson J.,
RA   Lucas J.S., Bingle C.D., Norris D.P., Roy S., Brown A.;
RT   "De novo identification of mammalian ciliary motility proteins using cryo-
RT   EM.";
RL   Cell 184:5791-5806.e19(2021).
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 (PubMed:34715025).
CC       Regulates ciliary and flagellar motility and is required for cilia-
CC       driven determination of body laterality (By similarity).
CC       {ECO:0000250|UniProtKB:Q9D3N2, ECO:0000269|PubMed:34715025}.
CC   -!- SUBUNIT: Component of the outer dynein arm-docking complex along with
CC       ODAD1, ODAD2, ODAD3 and ODAD4. {ECO:0000269|PubMed:34715025}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC       {ECO:0000250|UniProtKB:Q96M63}.
CC   -!- TISSUE SPECIFICITY: Expressed in trachea multiciliated cells.
CC       {ECO:0000269|PubMed:34715025}.
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DR   EMBL; BC109799; AAI09800.1; -; mRNA.
DR   RefSeq; NP_001032674.1; NM_001037585.2.
DR   PDB; 7RRO; EM; 3.40 A; I3/I4=1-212.
DR   PDBsum; 7RRO; -.
DR   AlphaFoldDB; Q32L26; -.
DR   SMR; Q32L26; -.
DR   STRING; 9913.ENSBTAP00000011457; -.
DR   PaxDb; Q32L26; -.
DR   Ensembl; ENSBTAT00000011457; ENSBTAP00000011457; ENSBTAG00000008693.
DR   Ensembl; ENSBTAT00000066916; ENSBTAP00000073883; ENSBTAG00000008693.
DR   GeneID; 505272; -.
DR   KEGG; bta:505272; -.
DR   CTD; 79645; -.
DR   VEuPathDB; HostDB:ENSBTAG00000008693; -.
DR   VGNC; VGNC:28339; CLXN.
DR   eggNOG; KOG0044; Eukaryota.
DR   GeneTree; ENSGT00940000159968; -.
DR   HOGENOM; CLU_061288_3_2_1; -.
DR   InParanoid; Q32L26; -.
DR   OMA; FTENIRH; -.
DR   OrthoDB; 1331864at2759; -.
DR   TreeFam; TF323358; -.
DR   Proteomes; UP000009136; Chromosome 14.
DR   Bgee; ENSBTAG00000008693; Expressed in olfactory segment of nasal mucosa and 67 other tissues.
DR   GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR   GO; GO:0120228; C:outer dynein arm docking complex; ISS:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0003341; P:cilium movement; IDA:UniProtKB.
DR   GO; GO:0036158; P:outer dynein arm assembly; IDA: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; 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; 2.
DR   PROSITE; PS50222; EF_HAND_2; 3.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium; Cell projection; Cytoplasm; Cytoskeleton;
KW   Metal-binding; Reference proteome; Repeat.
FT   CHAIN           1..212
FT                   /note="Calaxin"
FT                   /id="PRO_0000251968"
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:0000305"
FT   BINDING         116
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   BINDING         118
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   BINDING         125
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
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"
SQ   SEQUENCE   212 AA;  24635 MW;  BC72F75EEBC664A4 CRC64;
     MNRKKLQKLT DSLTKNCKHF SKFEVKCLIN LFYNLVGEVT ERQGVIIGLD RNAFRNILHM
     TFGMTDDMIM DRVFRGFDKD NDGCISVTEW VYGLSVFLRG TLEEKMKYCF EVFDLNGDSF
     ISKEEMFHML KNSLLKQPSE EDPDEGIKDL VEITLKKMDH DHDGKLSFAD YEQAVREETL
     LLEAFGPCLP DPKSQSEFEA QVFKDPNEFN EV
 
 
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