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Database: UniProt
Entry: A0A340XJ84_LIPVE
LinkDB: A0A340XJ84_LIPVE
Original site: A0A340XJ84_LIPVE 
ID   A0A340XJ84_LIPVE        Unreviewed;       779 AA.
AC   A0A340XJ84;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: 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   Name=DNAJC16 {ECO:0000313|RefSeq:XP_007459349.1};
OS   Lipotes vexillifer (Yangtze river dolphin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Lipotidae; Lipotes.
OX   NCBI_TaxID=118797 {ECO:0000313|Proteomes:UP000265300, ECO:0000313|RefSeq:XP_007459349.1};
RN   [1] {ECO:0000313|RefSeq:XP_007459349.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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}.
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DR   RefSeq; XP_007459349.1; XM_007459287.1.
DR   AlphaFoldDB; A0A340XJ84; -.
DR   STRING; 118797.A0A340XJ84; -.
DR   GeneID; 103086275; -.
DR   KEGG; lve:103086275; -.
DR   CTD; 23341; -.
DR   InParanoid; A0A340XJ84; -.
DR   OrthoDB; 125937at2759; -.
DR   Proteomes; UP000265300; Unplaced.
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   CDD; cd02963; TRX_DnaJ; 1.
DR   Gene3D; 1.10.287.110; DnaJ domain; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR018253; DnaJ_domain_CS.
DR   InterPro; IPR043361; DNAJC16_TRX.
DR   InterPro; IPR036869; J_dom_sf.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR44303; DNAJ HOMOLOG SUBFAMILY C MEMBER 16; 1.
DR   PANTHER; PTHR44303:SF2; DNAJ HOMOLOG SUBFAMILY C MEMBER 16; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
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; PS51352; THIOREDOXIN_2; 1.
PE   4: Predicted;
KW   Autophagy {ECO:0000256|ARBA:ARBA00023006};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265300};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..779
FT                   /note="DnaJ homolog subfamily C member 16"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016427590"
FT   DOMAIN          29..93
FT                   /note="J"
FT                   /evidence="ECO:0000259|PROSITE:PS50076"
FT   DOMAIN          117..245
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   REGION          560..592
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        563..583
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   779 AA;  89958 MW;  1858FB940D4BADE1 CRC64;
     MEVKKLSISW QFLIVLVLIL QILSALDFDP YRVLGVSRTA SQADIKKAYK KLAREWHPDK
     NKDPGAEDKF IQISKAYEIL SNEEKRSHYD HYGDAGENQG HQKQQREYRF RHFHENFYFD
     EPFFHFPFNS ERRDSIDEKY LLHFSHYVNE VVPDSFKKPY LVKITSDWCF SCIHIEPVWK
     EAVEELEGLG VGIGVVHAGY ERRLAHHLGA HSTPAILGII NGKISFFHNA VVRENLRQFV
     ESLLPGNLVE KVTNKNYVRF LSGWQQENKP HVLLFDQMPV VPLLYKLTAF AYKDYLSFGY
     VYVGLRGAEE MTRQYNVNVY APTILIFKEH IHKPADVIQA RGMKKQVIDD FITQNKYLLA
     ARLTSQKLFH ELCPVKRSHR QRKYCVVLLT TEATKLSKPF EAFLSFALAN TQDTVRFVHV
     YSNRQQEFAN TLLPDSDTFQ GKSAVSILER RNTAGRVVYK TLEDPWTGSE SDKFILLGYL
     DQLRKDPALL SSEAVLPDLT DELAPIFLLR WLYSASDYIS DSWDSIFHSN WREMMPLLSL
     VFSALFILFG TVIIQAFSDS NEERESSPPD KEEAHEKTGR TEPSFTKEPS SKIPKKGFVE
     VTELTDVTYT SNLVRLRPGH MNVVLILSNS TKTSLLQKFA LEVYTFTGSS CLHFSFLSLD
     KHREWLEYLL EFAQDVAPIP NQYDKHFMER DYTGYVLALN GHKKYFCLFK PQKTVEEEEA
     MGSCSDLDSS LHLGESRGKS SGLGSRPIKG KLSKLSLWME RLLEGSLQRF YIPSWPELD
//
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