ID A0A2I3T3Z4_PANTR Unreviewed; 747 AA.
AC A0A2I3T3Z4; A0A2J8PRN5;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=DnaJ homolog subfamily C member 10 {ECO:0000256|ARBA:ARBA00020920};
GN Name=DNAJC10 {ECO:0000313|Ensembl:ENSPTRP00000083948.1,
GN ECO:0000313|VGNC:VGNC:6364};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000083948.1, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000083948.1, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000083948.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AACZ04058588; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04058589; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04058590; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04058591; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04058592; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2I3T3Z4; -.
DR Ensembl; ENSPTRT00000091625.1; ENSPTRP00000083948.1; ENSPTRG00000012707.6.
DR VGNC; VGNC:6364; DNAJC10.
DR GeneTree; ENSGT00940000155558; -.
DR OMA; APTWRKF; -.
DR Proteomes; UP000002277; Chromosome 2B.
DR Bgee; ENSPTRG00000012707; Expressed in pituitary gland and 21 other cell types or tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:InterPro.
DR GO; GO:0034975; P:protein folding in endoplasmic reticulum; IEA:InterPro.
DR CDD; cd06257; DnaJ; 1.
DR CDD; cd03004; PDI_a_ERdj5_C; 3.
DR CDD; cd03003; PDI_a_ERdj5_N; 1.
DR Gene3D; 1.10.287.110; DnaJ domain; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 6.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR021170; ERdj5.
DR InterPro; IPR035674; ERdj5_TRX_C.
DR InterPro; IPR035673; ERdj5_TRX_N.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR44340; DNAJ HOMOLOG SUBFAMILY C MEMBER 10; 1.
DR PANTHER; PTHR44340:SF1; DNAJ HOMOLOG SUBFAMILY C MEMBER 10; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF00085; Thioredoxin; 4.
DR PIRSF; PIRSF037293; DnaJ_homolog_subfam-C; 2.
DR PRINTS; PR00625; JDOMAIN.
DR PRINTS; PR00421; THIOREDOXIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 5.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 3.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR037293-1};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 14..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 35..100
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT DOMAIN 113..234
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 391..509
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 579..747
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DISULFID 158..161
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR037293-1"
FT DISULFID 434..437
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR037293-1"
FT DISULFID 542..545
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR037293-1"
FT DISULFID 654..657
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR037293-1"
SQ SEQUENCE 747 AA; 86085 MW; D9EAF81FC7BCCC00 CRC64;
MGVWLNKDDY IRDLKRIILC FLIVYMAILV GTDQDFYSLL GVSKTASSRE IRQAFKKLAL
KLHPDKNPNN PNAHGDFLKI NRAYEVLKDE DLRKKYDKYG EKGLEDNQGG QYESWNYYRY
DFGIYDDDPE IITLERREFD AAVNSGELWF VNFYSPGCSH CHDLAPTWRD FAKEVDGLLR
IGAVNCGDDR MLCRMKGVNS YPSLFIFRSG MAPVKYHGDR SKDSLVSFAM QHVRSTVTEL
WTGNFVNSIQ TAFAAGIGWL ITFCSKGGDC LTSQTRLRLS GMLFLNSLDA KEIYLEVIHN
LPDFELLSAN TLEDRLAHHR WLLFFHFGKN ENSNDPELKK LKTLLKNDHI QVGRFDCSSA
PDICSNLYVF QPSLAVFKGQ GTKEYEIHHG KKILYDILAF AKESVNSHVT TLGPQNFPAN
DKEPWLVDFF APWCPPCRAL LPELRRASNL LYGQLKFGTL DCTVHEGLCN MYNIQAYPTT
VVFNQSNIHE YEGHHSAEQI LEFIEDLMNP SVVSLTPTTF NELVTQRKHN EVWMVDFYSP
WCHPCQVLMP EWKRMARTLT GLINVGSIDC QQYHSFCAQE NVQRYPEIRF FPPKSNKAYQ
YHSYNGWNRD AYSLRIWGLG FLPQVSTDLT PQTFSEKVLQ GKNHWVIDFY APWCGPCQNF
APEFELLARM IKGKVKAGKV DCQAYAQTCQ KAGIRAYPTV KFYFYERAKR NFQEEQINTR
DAKAIAALIS EKLETLQNQG KRNKDEL
//
