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}.
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 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
//