ID   DYL4_CHLRE              Reviewed;         129 AA.
AC   Q39591;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 111.
DE   RecName: Full=Dynein 14 kDa light chain, flagellar outer arm;
OS   Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 15-32 AND 58-65.
RC   STRAIN=1132D;
RX   PubMed=8626422; DOI=10.1074/jbc.271.11.6283;
RA   Patel-King R.S., Benashski S.E., Harrison A., King S.M.;
RT   "Two functional thioredoxins containing redox-senesitive vicinal dithiols
RT   from the Chlamydomonas outer dynein arm.";
RL   J. Biol. Chem. 271:6283-6291(1996).
CC   -!- FUNCTION: May be involved in regulating the redox state of functionally
CC       important thiol groups within dynein.
CC   -!- SUBUNIT: Consists of at least 3 heavy chains (alpha, beta and gamma), 2
CC       intermediate chains and 8 light chains.
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum. Cytoplasm,
CC       cytoskeleton, flagellum axoneme.
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; U43609; AAB03681.1; -; mRNA.
DR   PIR; T08084; T08084.
DR   RefSeq; XP_001700453.1; XM_001700401.1.
DR   AlphaFoldDB; Q39591; -.
DR   SMR; Q39591; -.
DR   STRING; 3055.EDO98142; -.
DR   EnsemblPlants; PNW70304; PNW70304; CHLRE_17g714250v5.
DR   GeneID; 5725952; -.
DR   Gramene; PNW70304; PNW70304; CHLRE_17g714250v5.
DR   KEGG; cre:CHLRE_17g714250v5; -.
DR   eggNOG; KOG0907; Eukaryota.
DR   HOGENOM; CLU_090389_14_4_1; -.
DR   OMA; WEEMLCL; -.
DR   OrthoDB; 1482186at2759; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0030286; C:dynein complex; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0031514; C:motile cilium; IEA:UniProtKB-SubCell.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   1: Evidence at protein level;
KW   Cell projection; Cilium; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; Disulfide bond; Dynein; Electron transport;
KW   Flagellum; Microtubule; Motor protein; Redox-active center; Transport.
FT   CHAIN           1..129
FT                   /note="Dynein 14 kDa light chain, flagellar outer arm"
FT                   /id="PRO_0000120151"
FT   DOMAIN          2..109
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   REGION          107..129
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        34..37
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   129 AA;  14179 MW;  3E3F0B02E8C53E09 CRC64;
     MAFITEIANE AQWKTEVLET PGTLQVVEVF QSWCGPCKAV QSTFKKLYFD LNDRPLKFYS
     VSSERLSSLK EYVGKCKPIF LFFKDGKQVE KIEGVKAPQL NRIVTELSGK NPPPAAPAAA
     PAAPAAEAS