ID A0A250WV28_9CHLO Unreviewed; 460 AA.
AC A0A250WV28;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=DnaJ homolog subfamily C member 10 {ECO:0000256|ARBA:ARBA00020920};
DE AltName: Full=DnaJ homolog subfamily C member 16 {ECO:0000256|ARBA:ARBA00020921};
DE AltName: Full=Endoplasmic reticulum DNA J domain-containing protein 8 {ECO:0000256|ARBA:ARBA00035043};
GN ORFNames=CEUSTIGMA_g2103.t1 {ECO:0000313|EMBL:GAX74655.1};
OS Chlamydomonas eustigma.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=1157962 {ECO:0000313|EMBL:GAX74655.1, ECO:0000313|Proteomes:UP000232323};
RN [1] {ECO:0000313|EMBL:GAX74655.1, ECO:0000313|Proteomes:UP000232323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2499 {ECO:0000313|EMBL:GAX74655.1,
RC ECO:0000313|Proteomes:UP000232323};
RA Hirooka S., Hirose Y., Kanesaki Y., Higuchi S., Fujiwara T., Onuma R.,
RA Era A., Ohbayashi R., Uzuka A., Nozaki H., Yoshikawa H., Miyagishima S.Y.;
RT "Acidophilic green algal genome provides insights into adaptation to an
RT acidic environment.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays an important role in regulating the size of
CC autophagosomes during the formation process.
CC {ECO:0000256|ARBA:ARBA00035002}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004163}; Single-pass type IV membrane protein
CC {ECO:0000256|ARBA:ARBA00004163}. Membrane
CC {ECO:0000256|ARBA:ARBA00004211}; Single-pass type IV membrane protein
CC {ECO:0000256|ARBA:ARBA00004211}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAX74655.1}.
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DR EMBL; BEGY01000008; GAX74655.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A250WV28; -.
DR STRING; 1157962.A0A250WV28; -.
DR OrthoDB; 276281at2759; -.
DR Proteomes; UP000232323; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; DnaJ domain; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 2.
DR Gene3D; 1.10.720.30; SAP domain; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR036361; SAP_dom_sf.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR45815; PROTEIN DISULFIDE-ISOMERASE A6; 1.
DR PANTHER; PTHR45815:SF3; PROTEIN DISULFIDE-ISOMERASE A6; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Autophagy {ECO:0000256|ARBA:ARBA00023006};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000232323}.
FT DOMAIN 8..73
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT DOMAIN 163..269
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 460 AA; 50064 MW; EC1D6F5CE4CF8E18 CRC64;
MLYVNLLDAG YLLTFWQVLR KMQRKNRSRR LTESKLYRNM DNKKEAEEKF KDIAAAYETL
SDPEKRKLYD SYGEEGLRSG GPGGPGFGGA DPFEMFNMFM GGMGGMGGMG SGGHQRMHFQ
FSGSADSSMG GGGFGGFGGG GFGGGMGGGG FQVEEEGFYD NDPYVIDVNP SNFPADSTLS
IVWVLEFYSP GCGHCQQLAP KYKQVASALA GIVKLGAVNC DLHKKLCSKE AVKGYPTIKA
YIPEQTGSKF YKGERTAKAI NDWILSLIPN HVNLISSDSD TTQLLQSCAG GSRSKRRSSS
SDMTERASWD VCVVLVTDKE KTAASYKSLS SQFKGKITFG EVRAANKPQL DGSALGLKPD
TDMPVVVAYC NGNTKLRLEY EGSMKGEALK RWLGEFEGGR KCSAMMPLDS TTDLKALSSK
VLKQLVKSHN VECKGAVEKE DFIVCLERQI HLEAQTKTDL
//
