ID A0A2K1J9T8_PHYPA Unreviewed; 603 AA.
AC A0A2K1J9T8;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|Pfam:PF00085};
GN ORFNames=PHYPA_021404 {ECO:0000313|EMBL:PNR38293.1};
OS Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX NCBI_TaxID=3218 {ECO:0000313|EMBL:PNR38293.1};
RN [1] {ECO:0000313|EMBL:PNR38293.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c16_23880V3.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=18079367; DOI=10.1126/science.1150646;
RA Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA Boore J.L.;
RT "The Physcomitrella genome reveals evolutionary insights into the conquest
RT of land by plants.";
RL Science 319:64-69(2008).
RN [2] {ECO:0000313|EMBL:PNR38293.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c16_23880V3.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=29237241; DOI=10.1111/tpj.13801;
RA Lang D., Ullrich K.K., Murat F., Fuchs J., Jenkins J., Haas F.B.,
RA Piednoel M., Gundlach H., Van Bel M., Meyberg R., Vives C., Morata J.,
RA Symeonidi A., Hiss M., Muchero W., Kamisugi Y., Saleh O., Blanc G.,
RA Decker E.L., van Gessel N., Grimwood J., Hayes R.D., Graham S.W.,
RA Gunter L.E., McDaniel S.F., Hoernstein S.N.W., Larsson A., Li F.W.,
RA Perroud P.F., Phillips J., Ranjan P., Rokshar D.S., Rothfels C.J.,
RA Schneider L., Shu S., Stevenson D.W., Thummler F., Tillich M.,
RA Villarreal Aguilar J.C., Widiez T., Wong G.K., Wymore A., Zhang Y.,
RA Zimmer A.D., Quatrano R.S., Mayer K.F.X., Goodstein D., Casacuberta J.M.,
RA Vandepoele K., Reski R., Cuming A.C., Tuskan G.A., Maumus F., Salse J.,
RA Schmutz J., Rensing S.A.;
RT "The Physcomitrella patens chromosome-scale assembly reveals moss genome
RT structure and evolution.";
RL Plant J. 93:515-533(2018).
RN [3] {ECO:0000313|EnsemblPlants:Pp3c16_23880V3.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (DEC-2020) to UniProtKB.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000256|ARBA:ARBA00006347}.
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DR EMBL; ABEU02000016; PNR38293.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K1J9T8; -.
DR STRING; 3218.A0A2K1J9T8; -.
DR PaxDb; 3218-PP1S4_328V6-1; -.
DR EnsemblPlants; Pp3c16_23880V3.1; Pp3c16_23880V3.1; Pp3c16_23880.
DR EnsemblPlants; Pp3c16_23880V3.2; Pp3c16_23880V3.2; Pp3c16_23880.
DR Gramene; Pp3c16_23880V3.1; Pp3c16_23880V3.1; Pp3c16_23880.
DR Gramene; Pp3c16_23880V3.2; Pp3c16_23880V3.2; Pp3c16_23880.
DR InParanoid; A0A2K1J9T8; -.
DR OMA; SNENLAM; -.
DR OrthoDB; 314307at2759; -.
DR Proteomes; UP000006727; Chromosome 16.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IBA:GO_Central.
DR CDD; cd02961; PDI_a_family; 1.
DR CDD; cd02995; PDI_a_PDI_a'_C; 1.
DR CDD; cd02982; PDI_b'_family; 1.
DR CDD; cd02981; PDI_b_family; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 4.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR18929; PROTEIN DISULFIDE ISOMERASE; 1.
DR PANTHER; PTHR18929:SF189; PROTEIN DISULFIDE ISOMERASE-LIKE 1-5-RELATED; 1.
DR Pfam; PF00085; Thioredoxin; 2.
DR Pfam; PF13848; Thioredoxin_6; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 4.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000006727};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..603
FT /note="Thioredoxin domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5036318938"
FT DOMAIN 81..182
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|Pfam:PF00085"
FT DOMAIN 415..506
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|Pfam:PF00085"
FT REGION 45..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..62
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 603 AA; 67535 MW; 13CFA56690B82111 CRC64;
MARRWFRLLL LLLALVSVVV HCCRALEEED SQGLVKEDVV SLEGEELDDE DELEDLDEGL
EDGGGGSDSF SSVETMAASK VVNVNDRDVE RVVARFEYVL LLGYAPWCTQ SQKLLPEFAA
AALNLVQLGN PTVFAKVDAI NNLATSSRYG IRGYPTLIFF VNGSRQAYSG GHSREEISLW
VRKKTDNAVT TIRSEEEAEI ILKKNLTTVL GYFDKLEGPE HEAFVAAAKS EMNTEFVQTT
VAEVAQVFIR PPFVALRKPE PEYFSAFDGN FSPKEISLFV EMNKRPLLTV LNSKNANMVY
SSPLKLHVLL FAETKDYESI KPLYMEAAQD FKSKVMFVVV DMEDKDFAMP MLAVYGLDRN
KPVVAGLNNE DGSKYLMESD LTVENLKKFA ADFYSRKLPL YFKSQPVPVE NGLVKIVVGK
TFDEVVMDDW KDVFLQVHAP WCPSCEKVNR VFEKLARHVQ KVPSLLMAKF DAQANEHPSL
MDVHSYPLLL LYPAGRKSSK PIVAQSQASW KKLLVFLKEN VAIPFPVSNG DEIVPKAHGV
NDVARLDAEQ VKEINDPLSV ENLEKEPVDE ASGSQEVAEK LYLSSQSGNN VEDLYFAELN
DEL
//
