ID A0A5K4F1J9_SCHMA Unreviewed; 966 AA.
AC A0A5K4F1J9;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, sequence version 1.
DT 24-JAN-2024, entry version 15.
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};
OS Schistosoma mansoni (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6183 {ECO:0000313|Proteomes:UP000008854, ECO:0000313|WBParaSite:Smp_243870.1};
RN [1] {ECO:0000313|Proteomes:UP000008854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Puerto Rican {ECO:0000313|Proteomes:UP000008854};
RX PubMed=22253936; DOI=10.1371/journal.pntd.0001455;
RA Protasio A.V., Tsai I.J., Babbage A., Nichol S., Hunt M., Aslett M.A.,
RA De Silva N., Velarde G.S., Anderson T.J., Clark R.C., Davidson C.,
RA Dillon G.P., Holroyd N.E., LoVerde P.T., Lloyd C., McQuillan J.,
RA Oliveira G., Otto T.D., Parker-Manuel S.J., Quail M.A., Wilson R.A.,
RA Zerlotini A., Dunne D.W., Berriman M.;
RT "A systematically improved high quality genome and transcriptome of the
RT human blood fluke Schistosoma mansoni.";
RL PLoS Negl. Trop. Dis. 6:E1455-E1455(2012).
RN [2] {ECO:0000313|WBParaSite:Smp_243870.1}
RP IDENTIFICATION.
RC STRAIN=Puerto Rican {ECO:0000313|WBParaSite:Smp_243870.1};
RG WormBaseParasite;
RL Submitted (NOV-2019) 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; A0A5K4F1J9; -.
DR STRING; 6183.A0A5K4F1J9; -.
DR EnsemblMetazoa; Smp_243870.1; Smp_243870.1; Smp_243870.
DR WBParaSite; Smp_243870.1; Smp_243870.1; Smp_243870.
DR InParanoid; A0A5K4F1J9; -.
DR Proteomes; UP000008854; Unassembled WGS sequence.
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 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; 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|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008854};
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..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..966
FT /note="DnaJ homolog subfamily C member 16"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5024353143"
FT TRANSMEM 637..660
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 19..83
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT DOMAIN 115..235
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 670..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..708
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 966 AA; 110664 MW; 510D086ED1B46E79 CRC64;
MKLSLFIQLA LFIRYTTCDY YDVLGVSKSA SNLEIKTAYR KLAKKWHPDK NPTEKANKKF
IEINEAYEVL SNSKKRHEYD TFGKVHSDGS QPPPGHYPYR HEFVHPSFEE LFDFFPGFNS
APQFSVNVLN IDFRSYRLTH LPRSRTVPLF IYGYSDFCFP CRQVRPIWSQ LADELTPLGI
TVASVNLEHD SALREELRVL HVPSVTIVVD GQVTYYSRGD FSHNSLIDAL RNAIMKSNPS
HSKALPTFLS TTIDTPLIQS INDYDTFVNT FHYGWRRDSR PRMVLIKPLT LPPLRYCVAA
FRAADHLAAG YINSETGSNY NFVKKFNVNP NEETLLIYHE DSSIPVYRQS ATKLSPTLLD
SAMLAYSQLN IPRIYSRARL LDLCPTDGSK PTSKYALESD KRYNDHSNHR HLCLVLLLNS
KQSNVEQINS WGDIWLTMLR RTLQLSQADL SKLYHTNQHS YHFMPVHIYV DRQISLMQKL
STSSTCSNES CNLLNEDNIG RLALIWRISS TETVYQLFPT NSMSHPRTHL NEKMLKPNDL
KTLILKSTEQ MHTALMNDLK NVIQMVSTTD KLTSPSNHLT HSIDKVTSQW YLLKDCMIEE
LMIDELVASI WIRMRNRLLQ ILVDIGHSMF DLVNHPLAFV FSSFMIIIGL LLFSLISTLI
QATKNEQKNK CTTEKHYNET NQGVNTSLSS NSNINDKNNN NNSSSSQCRI PEGSFALTPI
VSLNPSTYDR LVRDAPKGFR LLVLCVRGTT QDNRLRDQFD FKTRRVCGSQ IQRACLSMDR
YSGWLAKLLE STRPNLPIHI RSNKTMQKNR NVNDTTDNNN SGVLFINPVN CVGTVIAVNG
YRRYFNLYHP LIPGSQSSSD ENSESDVDES LSIEKQGNRL RRRHIFGRAF GLESDDEEDL
HQSNINNNHS HLKSRHQITD GVLFDSELLD GLSNWLDRLF EGSLPRYNIA EWPIGLLGDD
DDDDDD
//
