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Database: UniProt
Entry: A0A2K5X604_MACFA
LinkDB: A0A2K5X604_MACFA
Original site: A0A2K5X604_MACFA 
ID   A0A2K5X604_MACFA        Unreviewed;       655 AA.
AC   A0A2K5X604;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   24-JAN-2024, entry version 26.
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|Ensembl:ENSMFAP00000044889.2};
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000044889.2, ECO:0000313|Proteomes:UP000233100};
RN   [1] {ECO:0000313|Ensembl:ENSMFAP00000044889.2, ECO:0000313|Proteomes:UP000233100}
RP   NUCLEOTIDE SEQUENCE.
RA   Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSMFAP00000044889.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   AlphaFoldDB; A0A2K5X604; -.
DR   Ensembl; ENSMFAT00000019190.2; ENSMFAP00000044889.2; ENSMFAG00000036417.2.
DR   VEuPathDB; HostDB:ENSMFAG00000036417; -.
DR   GeneTree; ENSGT00940000155851; -.
DR   Proteomes; UP000233100; Chromosome 1.
DR   Bgee; ENSMFAG00000036417; Expressed in skeletal muscle tissue and 13 other cell types or tissues.
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, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233100};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..655
FT                   /note="DnaJ homolog subfamily C member 16"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5030052604"
FT   TRANSMEM        536..559
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          29..93
FT                   /note="J"
FT                   /evidence="ECO:0000259|PROSITE:PS50076"
FT   DOMAIN          119..247
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   REGION          562..593
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        566..585
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   655 AA;  75908 MW;  80A954BF4E211419 CRC64;
     MEVRKLSISW QFLIVLVLIL QILSALDFDP YRVLGVSRTA SQADIKKAYK KLAREWHPDK
     NKDPGAEDKF IQISKAYEIL SNEEKRSNYD QYGDAGENQG YQKQQQQREY RFRHFHENFY
     FDESFFHFPF NSERRDSIDE KYLLHFSHYV NEVVPDSFKK PYLIKITSDW CFSCIHIEPV
     WKEVVQELEE LGVGIGVVHA GYERRLAHHL GAHSTPSILG IINGKISFFH NAVVRENLRQ
     FVESLLPGNL VEKVTNKNYV RFLSGWQQEN KPHVLLFDQT PIVPLLYKLT AFAYKDYLSF
     GYVYVGLRGT EEMTRRYNIN VYTPTLLIFK EHINKPADVI QARGMKKQII DDFITQNKYL
     LAARLTSQKL FHELCPVKRS HRQRKYCVVL LTAETAKLSK PFEAFLSFAL ANTQDTVRFV
     HVYSNRQQEF ADTLLPDSEA FQGKSAVSIL ERRNTAGRVV YKTLEDPWTG SESDKFILLG
     YLDQLRKDPA LLSSEAVLPD LTDELAPVFL LRWFYSASDY ISDCWDSIFH NNWREMMPLL
     SLIFSALFIL FGTVIVQAFS DSNDERESSP PGKEEAQEKT GKTEPSFTKE NSSKIPKKGF
     VEVTELTDVT YTSNLVRLRP GHMNVVLILS NSTKTSLLQK FALEVYTFTG KIIRW
//
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