位置:首页 > 蛋白库 > SDF2_ARATH
SDF2_ARATH
ID   SDF2_ARATH              Reviewed;         218 AA.
AC   Q93ZE8; O81720; Q9SEZ5;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 129.
DE   RecName: Full=Stromal cell-derived factor 2-like protein;
DE            Short=AtSDF2;
DE            Short=SDF2-like protein;
DE   Flags: Precursor;
GN   Name=SDF2; OrderedLocusNames=At2g25110; ORFNames=F13D4.70;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   FUNCTION, INTERACTION WITH ERDJ3B, SUBCELLULAR LOCATION, DISRUPTION
RP   PHENOTYPE, AND MUTAGENESIS OF GLY-64.
RX   PubMed=19763086; DOI=10.1038/emboj.2009.262;
RA   Nekrasov V., Li J., Batoux M., Roux M., Chu Z.H., Lacombe S., Rougon A.,
RA   Bittel P., Kiss-Papp M., Chinchilla D., van Esse H.P., Jorda L.,
RA   Schwessinger B., Nicaise V., Thomma B.P., Molina A., Jones J.D., Zipfel C.;
RT   "Control of the pattern-recognition receptor EFR by an ER protein complex
RT   in plant immunity.";
RL   EMBO J. 28:3428-3438(2009).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 24-218, FUNCTION, AND INDUCTION.
RX   PubMed=20378538; DOI=10.1074/jbc.m110.117176;
RA   Schott A., Ravaud S., Keller S., Radzimanowski J., Viotti C., Hillmer S.,
RA   Sinning I., Strahl S.;
RT   "Arabidopsis stromal-derived Factor2 (SDF2) is a crucial target of the
RT   unfolded protein response in the endoplasmic reticulum.";
RL   J. Biol. Chem. 285:18113-18121(2010).
CC   -!- FUNCTION: Involved in the endoplasmic reticulum (ER) protein quality
CC       control and unfolded protein response. May be involved in the quality
CC       control of glycoproteins. Forms a complex in the ER with ERDJ3B and
CC       MED37A/BIP1 which is required for the proper accumulation and function
CC       of the surface-exposed leucine-rich repeat receptor kinases EFR
CC       involved in pathogen-associated molecular pattern (PAMP) triggered
CC       immunity. {ECO:0000269|PubMed:19763086, ECO:0000269|PubMed:20378538}.
CC   -!- SUBUNIT: Interacts with ERDJ3B. {ECO:0000269|PubMed:19763086}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000269|PubMed:19763086}.
CC   -!- INDUCTION: By tunicamycin. {ECO:0000269|PubMed:20378538}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC       conditions, but mutant plants are insensitive to seedling growth
CC       inhibition in response to the pathogen-associated molecular pattern
CC       (PAMP) elf18 and show increased susceptibility to phytopathogenic
CC       bacteria. {ECO:0000269|PubMed:19763086}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002685; AEC07659.1; -; Genomic_DNA.
DR   EMBL; AY057588; AAL14383.1; -; mRNA.
DR   EMBL; AY143822; AAN28761.1; -; mRNA.
DR   EMBL; AY088079; AAM65625.1; -; mRNA.
DR   PIR; D84644; D84644.
DR   RefSeq; NP_565585.1; NM_128068.3.
DR   PDB; 3MAL; X-ray; 1.95 A; A/B=24-218.
DR   PDBsum; 3MAL; -.
DR   AlphaFoldDB; Q93ZE8; -.
DR   SMR; Q93ZE8; -.
DR   BioGRID; 2401; 1.
DR   IntAct; Q93ZE8; 1.
DR   MINT; Q93ZE8; -.
DR   STRING; 3702.AT2G25110.1; -.
DR   PaxDb; Q93ZE8; -.
DR   PRIDE; Q93ZE8; -.
DR   ProteomicsDB; 232857; -.
DR   DNASU; 817049; -.
DR   EnsemblPlants; AT2G25110.1; AT2G25110.1; AT2G25110.
DR   GeneID; 817049; -.
DR   Gramene; AT2G25110.1; AT2G25110.1; AT2G25110.
DR   KEGG; ath:AT2G25110; -.
DR   Araport; AT2G25110; -.
DR   TAIR; locus:2040199; AT2G25110.
DR   eggNOG; KOG3358; Eukaryota.
DR   HOGENOM; CLU_078126_0_0_1; -.
DR   InParanoid; Q93ZE8; -.
DR   OMA; KPQHGTR; -.
DR   OrthoDB; 1534407at2759; -.
DR   PhylomeDB; Q93ZE8; -.
DR   PRO; PR:Q93ZE8; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q93ZE8; baseline and differential.
DR   Genevisible; Q93ZE8; AT.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR   GO; GO:0005773; C:vacuole; HDA:TAIR.
DR   GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR   GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR   GO; GO:0002221; P:pattern recognition receptor signaling pathway; IMP:TAIR.
DR   InterPro; IPR036300; MIR_dom_sf.
DR   InterPro; IPR016093; MIR_motif.
DR   Pfam; PF02815; MIR; 1.
DR   SMART; SM00472; MIR; 3.
DR   SUPFAM; SSF82109; SSF82109; 1.
DR   PROSITE; PS50919; MIR; 3.
PE   1: Evidence at protein level;
KW   3D-structure; Endoplasmic reticulum; Glycoprotein; Plant defense;
KW   Reference proteome; Repeat; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..218
FT                   /note="Stromal cell-derived factor 2-like protein"
FT                   /id="PRO_0000031959"
FT   DOMAIN          34..88
FT                   /note="MIR 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT   DOMAIN          96..151
FT                   /note="MIR 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT   DOMAIN          154..208
FT                   /note="MIR 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT   CARBOHYD        214
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         64
FT                   /note="G->D: In sdf2-3; decreased response to the PAMP
FT                   elf18."
FT                   /evidence="ECO:0000269|PubMed:19763086"
FT   CONFLICT        203
FT                   /note="W -> C (in Ref. 4; AAM65625)"
FT                   /evidence="ECO:0000305"
FT   STRAND          42..47
FT                   /evidence="ECO:0007829|PDB:3MAL"
FT   TURN            48..50
FT                   /evidence="ECO:0007829|PDB:3MAL"
FT   STRAND          53..60
FT                   /evidence="ECO:0007829|PDB:3MAL"
FT   STRAND          68..73
FT                   /evidence="ECO:0007829|PDB:3MAL"
FT   HELIX           79..81
FT                   /evidence="ECO:0007829|PDB:3MAL"
FT   STRAND          83..86
FT                   /evidence="ECO:0007829|PDB:3MAL"
FT   STRAND          104..109
FT                   /evidence="ECO:0007829|PDB:3MAL"
FT   TURN            110..112
FT                   /evidence="ECO:0007829|PDB:3MAL"
FT   STRAND          115..122
FT                   /evidence="ECO:0007829|PDB:3MAL"
FT   TURN            124..126
FT                   /evidence="ECO:0007829|PDB:3MAL"
FT   STRAND          128..134
FT                   /evidence="ECO:0007829|PDB:3MAL"
FT   HELIX           142..144
FT                   /evidence="ECO:0007829|PDB:3MAL"
FT   STRAND          146..153
FT                   /evidence="ECO:0007829|PDB:3MAL"
FT   STRAND          162..167
FT                   /evidence="ECO:0007829|PDB:3MAL"
FT   TURN            168..170
FT                   /evidence="ECO:0007829|PDB:3MAL"
FT   STRAND          173..180
FT                   /evidence="ECO:0007829|PDB:3MAL"
FT   STRAND          183..185
FT                   /evidence="ECO:0007829|PDB:3MAL"
FT   STRAND          189..196
FT                   /evidence="ECO:0007829|PDB:3MAL"
FT   HELIX           199..201
FT                   /evidence="ECO:0007829|PDB:3MAL"
FT   STRAND          203..209
FT                   /evidence="ECO:0007829|PDB:3MAL"
SQ   SEQUENCE   218 AA;  23935 MW;  575F683AC0C3BC87 CRC64;
     MALGFFCLAI FLYLSLDPDS GYTSASAAAS GKEGVEITYG SAIKLMHEKT KFRLHSHDVP
     YGSGSGQQSV TGFPGVVDSN SYWIVKPVPG TTEKQGDAVK SGATIRLQHM KTRKWLHSHL
     HASPISGNLE VSCFGDDTNS DTGDHWKLII EGSGKTWKQD QRVRLQHIDT SGYLHSHDKK
     YQRIAGGQQE VCGIREKKAD NIWLAAEGVY LPLNESSK
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024