ID DJC16_RAT Reviewed; 771 AA. AC Q5FVM7; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2005, sequence version 1. DT 02-SEP-2026, entry version 129. DE RecName: Full=DnaJ homolog subfamily C member 16; DE AltName: Full=Endoplasmic reticulum DNA J domain-containing protein 8 {ECO:0000250|UniProtKB:Q9Y2G8}; DE Short=ER-resident protein ERdj8; DE Short=ERdj8; DE Flags: Precursor; GN Name=Dnajc16; Synonyms=Erdj8; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Plays an important role in regulating the size of CC autophagosomes during the formation process. CC {ECO:0000250|UniProtKB:Q9Y2G8}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000250|UniProtKB:Q9Y2G8}; Single-pass type IV membrane protein CC {ECO:0000305}. 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; BC089875; AAH89875.1; -; mRNA. DR RefSeq; NP_001014216.1; NM_001014194.1. DR AlphaFoldDB; Q5FVM7; -. DR SMR; Q5FVM7; -. DR FunCoup; Q5FVM7; 4027. DR STRING; 10116.ENSRNOP00000017247; -. DR GlyCosmos; Q5FVM7; 1 site, No reported glycans. DR GlyGen; Q5FVM7; 1 site. DR PhosphoSitePlus; Q5FVM7; -. DR PaxDb; 10116-ENSRNOP00000017247; -. DR Ensembl; ENSRNOT00055041378; ENSRNOP00055033672; ENSRNOG00055024093. DR Ensembl; ENSRNOT00060035048; ENSRNOP00060028798; ENSRNOG00060020245. DR Ensembl; ENSRNOT00065045624; ENSRNOP00065037411; ENSRNOG00065026432. DR GeneID; 362652; -. DR KEGG; rno:362652; -. DR UCSC; RGD:1359395; rat. DR AGR; RGD:1359395; -. DR CTD; 23341; -. DR RGD; 1359395; Dnajc16. DR eggNOG; KOG0715; Eukaryota. DR HOGENOM; CLU_020140_0_1_1; -. DR InParanoid; Q5FVM7; -. DR OMA; QPEFAST; -. DR OrthoDB; 10065037at2759; -. DR PhylomeDB; Q5FVM7; -. DR PRO; PR:Q5FVM7; -. DR Proteomes; UP000002494; Chromosome 5. DR Bgee; ENSRNOG00000012503; Expressed in skeletal muscle tissue and 18 other cell types or tissues. DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB. DR GO; GO:0016243; P:regulation of autophagosome size; ISS:UniProtKB. 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; IPR060274; DJC16_2nd. DR InterPro; IPR060272; DJC16_3rd. DR InterPro; IPR060275; DJC16_C. DR InterPro; IPR052448; DnaJ_C16_autophagy_reg. 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; PF26976; DJC16_C; 1. DR Pfam; PF00226; DnaJ; 1. DR Pfam; PF00085; Thioredoxin; 1. DR Pfam; PF26973; Thioredoxin-like_DJC16_2nd; 1. DR Pfam; PF26968; Thioredoxin-like_DJC16_3rd; 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 2: Evidence at transcript level; KW Autophagy; Endoplasmic reticulum; Glycoprotein; Membrane; KW Reference proteome; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1..25 FT /evidence="ECO:0000255" FT CHAIN 26..771 FT /note="DnaJ homolog subfamily C member 16" FT /id="PRO_0000236686" FT TOPO_DOM 26..532 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 533..553 FT /note="Helical; Anchor for type IV membrane protein" FT /evidence="ECO:0000255" FT TOPO_DOM 554..771 FT /note="Extracellular" FT /evidence="ECO:0000255" FT DOMAIN 29..93 FT /note="J" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286" FT DOMAIN 116..244 FT /note="Thioredoxin" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691" FT REGION 559..590 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 560..579 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 628 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" SQ SEQUENCE 771 AA; 88870 MW; F9B65C08A01D4C63 CRC64; MELKRLSISW QFLIVLVLIL QSLSALDFDP YRVLGVSRTA SQADIKKAYK KLAREWHPDK NKDPGAEDKF IQISKAYEIL SNEEKRTNYD HYGDAGENQG YQQQREYRFR HFHENFYFDE SFFHFPFNSE RRDSIDEKYL LHFSHYVNEV VPDSFKKPYL IKITSDWCFS CIHIEPIWKE VVQELEGLGV GIGVVHAGYE RRLAHHLGAH STPSILGIIN GKISFFHNAV VHENLRQFVE SLLPGNLVEK VTNKNYVRFL SGWQQENKPH ALLFGQTPAA PLLYKLTAFA YKDYVSFGYV YVGLRGVEEM TRQYNVNIYA PTMLIFKEHI NKPADAIQAR GLKKQVIEDF ITQNKYLLAS RLTSQKLFHE LCPVKRSHRQ RKYCVVLLTA EANKLSKPFD AFLSFALANT QDTVRFVHVY SSRQQEFAST LLPDIEAFQG KSGVSILERR NTAGRVVFKT LEDPWTGSES DKFVLLGYLD QLRKDPAFLS SEAVLPDLTD ELAPVFLLRW LYSVSDYLSD FWESLLHSNW REMMPLLSLI FSALFILFGT VIVQAFSDSN EERESHPPDK EEVPEKAGKT EPSFTKESSS KIPKKGFVEV TELTDVTYTS NLVRLRPGHM NVVLILSNST KTSLLQKFAL EVYTFTGSSS LHFSFLTLDK HREWLEYLLE FAQDAAPIPN QYDKHFMERD YTGYVLALNG HKKYFCLFKP LKTVDEETVG SCDLDSSRGK PPCGLGPKPL KGKLSKLSLW MERLLEGSLQ RFYIPSWPEL D //