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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
 
 
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