ID A0A484DHM0_PERFV Unreviewed; 812 AA.
AC A0A484DHM0;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
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 ORFNames=EPR50_G00041870 {ECO:0000313|EMBL:TDH14170.1};
OS Perca flavescens (American yellow perch) (Morone flavescens).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Percoidei; Percidae; Percinae; Perca.
OX NCBI_TaxID=8167 {ECO:0000313|EMBL:TDH14170.1, ECO:0000313|Proteomes:UP000295070};
RN [1] {ECO:0000313|EMBL:TDH14170.1, ECO:0000313|Proteomes:UP000295070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YP-PL-M2 {ECO:0000313|EMBL:TDH14170.1};
RC TISSUE=Blood {ECO:0000313|EMBL:TDH14170.1};
RA Feron R., Morvezen R., Bestin A., Haffray P., Klopp C., Zahm M., Cabau C.,
RA Roques C., Donnadieu C., Bouchez O., Christie M., Larson W., Guiguen Y.;
RT "A chromosome-scale genome assembly of the yellow perch, Perca
RT flavescens.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TDH14170.1}.
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DR EMBL; SCKG01000004; TDH14170.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A484DHM0; -.
DR STRING; 8167.A0A484DHM0; -.
DR OrthoDB; 125937at2759; -.
DR Proteomes; UP000295070; Chromosome 4.
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.
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:UP000295070};
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..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..812
FT /note="DnaJ homolog subfamily C member 16"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019753188"
FT TRANSMEM 540..560
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 38..102
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT REGION 563..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..581
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..770
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 812 AA; 93518 MW; F954C1FFD9437F47 CRC64;
MTLRRTSRHP PPRTCPVLPA IFLLILSVQL VRAASEYDPY KVLGVSRSAS QAEIKRAYKN
LAKEWHPDKN KDPKAEDMFI KVSKSYEILS NEERRSNFDN YGQMDENQPF GQSQHHGFRG
FRNSFYFDES FFHFPRSRDF ADSKYLLHHA QFNSDVLPDS HKRPYLIKVT SEWCFACIHI
EPVWKETVQE LEPLGVGIGI VDLGYERRLA NQLGAHRAPS IIGLVNGRVT FFHQAVVREH
LRQFIEDLLP QKLVEKITDN NYLPFLDSWH VENKPSVLLF DQVPIVPLLF KLTAFAFKDY
VRFGYVDQGD THNTRLLRQF NINTYAPTML LFKEDTEKPV DIIQARGMKR QIMDEFVSNN
KFLQVPRLVN QQLFDELCPV KQFHRRRKYC VLLITGEDQA FLPGSKAFLD FASVNRKDVL
RFAYVYQRQQ QPLCQALLHN QAALAPQVVI LERRSHGGKV MYRSVSGGWN GSEEDKYRLH
EQLELLQKDP TYLSSDATLP ELNNEMAPIF IVQWMNAAYD YILQIYDDLL YSNWREMMPI
LSLIFSALFI LFGTVIIQAF SEPGESKPRK PKPKEQQQTE EDASSRASTS SRPPKKDFVE
VTELTDITYI SNLVKLRPGH INVVLVLTNT SKNALLRKFA KEVFSFSGTQ TLHFSFLNAD
KHRHWMPSLL HSTSDSMRSE GHSDVDEESP DYAGHVLALN GHKKYFCLFR PVFTGDDPND
SSSETSFSSD SRRKSRSRSR SSSSSHSRSR SHSREDGVGP RRGSSRATSI EVHHKLDRLG
LWMERLMEGT LPRLQVPAWP SLGETTNSST ET
//
