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Database: UniProt
Entry: W5MIA0_LEPOC
LinkDB: W5MIA0_LEPOC
Original site: W5MIA0_LEPOC 
ID   W5MIA0_LEPOC            Unreviewed;       801 AA.
AC   W5MIA0;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=DnaJ homolog subfamily C member 10 {ECO:0000256|ARBA:ARBA00020920};
OS   Lepisosteus oculatus (Spotted gar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC   Lepisosteus.
OX   NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000008109.1, ECO:0000313|Proteomes:UP000018468};
RN   [1] {ECO:0000313|Proteomes:UP000018468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT   "The Draft Genome of Lepisosteus oculatus.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLOCP00000008109.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   EMBL; AHAT01020114; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; W5MIA0; -.
DR   Ensembl; ENSLOCT00000008119.1; ENSLOCP00000008109.1; ENSLOCG00000006697.1.
DR   GeneTree; ENSGT00940000155558; -.
DR   Proteomes; UP000018468; Linkage group LG12.
DR   Bgee; ENSLOCG00000006697; Expressed in embryo and 13 other cell types or tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   CDD; cd06257; DnaJ; 1.
DR   CDD; cd03004; PDI_a_ERdj5_C; 3.
DR   CDD; cd03003; PDI_a_ERdj5_N; 1.
DR   CDD; cd02961; PDI_a_family; 1.
DR   Gene3D; 1.10.287.110; DnaJ domain; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 6.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR035674; ERdj5_TRX_C.
DR   InterPro; IPR035673; ERdj5_TRX_N.
DR   InterPro; IPR036869; J_dom_sf.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR44340; DNAJ HOMOLOG SUBFAMILY C MEMBER 10; 1.
DR   PANTHER; PTHR44340:SF1; DNAJ HOMOLOG SUBFAMILY C MEMBER 10; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF00085; Thioredoxin; 4.
DR   PRINTS; PR00625; JDOMAIN.
DR   PRINTS; PR00421; THIOREDOXIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; Chaperone J-domain; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 6.
DR   PROSITE; PS50076; DNAJ_2; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 3.
DR   PROSITE; PS51352; THIOREDOXIN_2; 3.
PE   4: Predicted;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          40..105
FT                   /note="J"
FT                   /evidence="ECO:0000259|PROSITE:PS50076"
FT   DOMAIN          126..240
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DOMAIN          425..558
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DOMAIN          652..784
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   801 AA;  91894 MW;  B175D779CD542E13 CRC64;
     MESALLAEQT CCVYRRQSSR TFLYFFVIIC LAAVISCNDD YYELLGVSRE ASNREIRQAF
     KKLALTMHPD KNPNDQDAHD KFLKINRAYE VLKDEDLRKK YDKYGEKGLQ DNQEGGRYES
     WNYYRYDFGI YDDDLEIITL DRGDFDAAVN SGELWFVNFY FPRCSHCHDL APTWREFAKE
     MDGVIRIGAV NCGDNRMLCR SKGITSYPSL HIFKAGMNSE KYYGDRSKES LQNFAMQFVK
     SKVTELWSGN FFNAIESAFA SRIGWLITFC AETGDCLSSE TRHKLAGMLD GLVNLGWMDC
     STQAQLCDSF DIKSSTTTYF PPGSSLRDKG GVLFLKSLDA KEIYNEVMQH LPDLEVLTKE
     TIKDKLAHHR WLVSFTFGEN QLGSHEYKKL KSLLKEDHIQ VGKIDCLLEL DLCNSFYIHK
     PSIAVFKGFG INDFEIHHGK DVLYNIVAFA KDSVHAYVTT LRPENFPNNE KEPWLVDFFA
     PWCPPCRALL PELRKASKQL FGQLKFGTLD CTVHDGICSM YNIQAYPTTV IFNQSNIHEY
     EGHHSADGIL EFIEDLINPS VVTLSPESFE ELVKKRKRSE TWMVDFYAPW CGPCQALLPE
     WRRMARLLNG MISVGSVDCQ KYHSFCHGEN VRAYPEIRLF LQNSNRRDQY QSYNGWHRDA
     YSLRTWALGS LPRASVDLSP EDFKQKVLNG KDHWVIDFYA PWCGPCQNFA PEFEILARTV
     KGKVKAGKVD CQAYGQTCQS AGIRAYPTVK FYPFLGKKKR NAEGEYINSR DAGAIADLVS
     QRLQQISSQL QDKSSSKKDE K
//
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