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PDI22_ORYSJ
ID   PDI22_ORYSJ             Reviewed;         371 AA.
AC   Q942L2; A0A0P0V205;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Protein disulfide isomerase-like 2-2;
DE            Short=OsPDIL2-2;
DE            EC=5.3.4.1;
DE   AltName: Full=Protein disulfide isomerase-like 4-2;
DE            Short=OsPDIL4-2;
DE   Flags: Precursor;
GN   Name=PDIL2-2; Synonyms=PDIL4-2;
GN   OrderedLocusNames=Os01g0339900, LOC_Os01g23740;
GN   ORFNames=B1088D01.21, OsJ_01619;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12447438; DOI=10.1038/nature01184;
RA   Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA   Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA   Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA   Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA   Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA   Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA   Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA   Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA   Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA   Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA   Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA   Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA   Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT   "The genome sequence and structure of rice chromosome 1.";
RL   Nature 420:312-316(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
RN   [7]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=15684019; DOI=10.1104/pp.104.056507;
RA   Houston N.L., Fan C., Xiang J.Q., Schulze J.M., Jung R., Boston R.S.;
RT   "Phylogenetic analyses identify 10 classes of the protein disulfide
RT   isomerase family in plants, including single-domain protein disulfide
RT   isomerase-related proteins.";
RL   Plant Physiol. 137:762-778(2005).
RN   [8]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=20525253; DOI=10.1186/1471-2229-10-101;
RA   d'Aloisio E., Paolacci A.R., Dhanapal A.P., Tanzarella O.A., Porceddu E.,
RA   Ciaffi M.;
RT   "The protein disulfide isomerase gene family in bread wheat (T. aestivum
RT   L.).";
RL   BMC Plant Biol. 10:101-101(2010).
CC   -!- FUNCTION: Acts as a protein-folding catalyst that interacts with
CC       nascent polypeptides to catalyze the formation, isomerization, and
CC       reduction or oxidation of disulfide bonds. May play a role in storage
CC       protein biogenesis (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC         EC=5.3.4.1;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; AP003331; BAB67990.1; -; Genomic_DNA.
DR   EMBL; AP008207; BAF04863.1; -; Genomic_DNA.
DR   EMBL; AP014957; BAS71966.1; -; Genomic_DNA.
DR   EMBL; CM000138; EAZ11750.1; -; Genomic_DNA.
DR   EMBL; AK066111; BAG89827.1; -; mRNA.
DR   RefSeq; XP_015622515.1; XM_015767029.1.
DR   AlphaFoldDB; Q942L2; -.
DR   SMR; Q942L2; -.
DR   STRING; 4530.OS01T0339900-01; -.
DR   PaxDb; Q942L2; -.
DR   PRIDE; Q942L2; -.
DR   EnsemblPlants; Os01t0339900-01; Os01t0339900-01; Os01g0339900.
DR   GeneID; 4326806; -.
DR   Gramene; Os01t0339900-01; Os01t0339900-01; Os01g0339900.
DR   KEGG; osa:4326806; -.
DR   eggNOG; KOG0191; Eukaryota.
DR   HOGENOM; CLU_038617_1_0_1; -.
DR   InParanoid; Q942L2; -.
DR   OMA; FINEHAG; -.
DR   OrthoDB; 840943at2759; -.
DR   Proteomes; UP000000763; Chromosome 1.
DR   Proteomes; UP000007752; Chromosome 1.
DR   Proteomes; UP000059680; Chromosome 1.
DR   Genevisible; Q942L2; OS.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   CDD; cd00238; ERp29c; 1.
DR   Gene3D; 1.20.1150.12; -; 1.
DR   InterPro; IPR005788; Disulphide_isomerase.
DR   InterPro; IPR011679; ERp29_C.
DR   InterPro; IPR036356; ERp29_C_sf.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF07749; ERp29; 1.
DR   Pfam; PF00085; Thioredoxin; 2.
DR   SUPFAM; SSF47933; SSF47933; 1.
DR   SUPFAM; SSF52833; SSF52833; 2.
DR   TIGRFAMs; TIGR01126; pdi_dom; 2.
DR   PROSITE; PS00194; THIOREDOXIN_1; 2.
DR   PROSITE; PS51352; THIOREDOXIN_2; 2.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Isomerase; Redox-active center; Reference proteome; Repeat;
KW   Secreted; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..371
FT                   /note="Protein disulfide isomerase-like 2-2"
FT                   /id="PRO_0000400034"
FT   DOMAIN          28..143
FT                   /note="Thioredoxin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DOMAIN          147..262
FT                   /note="Thioredoxin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   ACT_SITE        64
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        67
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        183
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        186
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   SITE            65
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            66
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            129
FT                   /note="Lowers pKa of C-terminal Cys of first active site"
FT                   /evidence="ECO:0000250"
FT   SITE            184
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            185
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            248
FT                   /note="Lowers pKa of C-terminal Cys of second active site"
FT                   /evidence="ECO:0000250"
FT   DISULFID        64..67
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        183..186
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   371 AA;  40741 MW;  725F6DB1C8BDA87C CRC64;
     MAIPRISPRK TLPLFAALAL ALAWAFAAPA FADGDDVVAL TESTFEKEVG QDRGALVEFY
     APWCGHCKKL APEYEKLGAS FKKAKSVFIA KVDCDEHKSV CSKYGVSGYP TIQWFPKGSL
     EPKKYEGQRS AEALAEFVNT EGGTNVKLAT IPSSVVVLGP DNFDSIVLDE NKDILVEFYA
     PWCGHCKHLA PIYEKLASVY KLDDGVVIAN LDADKHKDLA EKYGVSGYPT LKFFPKGNKA
     GEDYDGGREL DDFVKFINEK CGTSRDTKGQ LTSEAGRIAS LDALAKEFLG AANDKRKEIL
     SNMEEEVVKL SGSAAKHGKV YIAIAKKILD KGHDYTKKET ERLERMLEKS ISPSKADEFI
     IKKNVLSTFS S
 
 
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