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S2P_ARATH
ID   S2P_ARATH               Reviewed;         513 AA.
AC   F4JUU5; O65444;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   04-MAR-2015, sequence version 2.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Membrane-bound transcription factor site-2 protease homolog;
DE            EC=3.4.24.-;
DE   AltName: Full=Endopeptidase S2P;
GN   Name=S2P; OrderedLocusNames=At4g20310 {ECO:0000312|Araport:AT4G20310};
GN   ORFNames=F1C12.220 {ECO:0000312|EMBL:CAA18255.1};
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=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(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   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=20876872; DOI=10.1126/scisignal.2001140;
RA   Che P., Bussell J.D., Zhou W., Estavillo G.M., Pogson B.J., Smith S.M.;
RT   "Signaling from the endoplasmic reticulum activates brassinosteroid
RT   signaling and promotes acclimation to stress in Arabidopsis.";
RL   Sci. Signal. 3:RA69-RA69(2010).
CC   -!- FUNCTION: Metalloprotease that catalyzes the second step (site-2
CC       cleavage) in the proteolytic activation of various factors, after site-
CC       1 cleavage. Part of a regulated intramembrane proteolysis (RIP)
CC       cascade. After ER stress, cleaves BZIP17 and BZIP28 proteins which
CC       functions as stress sensors and transducers in ER stress signaling
CC       pathway. The N-terminal bZIP component is translocated to the nucleus,
CC       where it activates the expression and production of ER chaperones, as
CC       well as proteins involved in brassinosteroid (BR) signaling, which is
CC       required for stress acclimation and growth.
CC       {ECO:0000269|PubMed:20876872}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000305|PubMed:20876872}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences. {ECO:0000305};
CC       Name=1;
CC         IsoId=F4JUU5-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Expressed in the vasculature of roots, cotyledons
CC       and leaves. {ECO:0000269|PubMed:20876872}.
CC   -!- DISRUPTION PHENOTYPE: Short root and increased root branching. Mutant
CC       plants have increased sensitivity to salt-induced osmotic stress and
CC       tunicamycin. {ECO:0000269|PubMed:20876872}.
CC   -!- SIMILARITY: Belongs to the peptidase M50A family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA18255.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB79031.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL022224; CAA18255.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161552; CAB79031.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; ANM67075.1; -; Genomic_DNA.
DR   PIR; T05339; T05339.
DR   RefSeq; NP_001328927.1; NM_001341413.1. [F4JUU5-1]
DR   AlphaFoldDB; F4JUU5; -.
DR   STRING; 3702.AT4G20310.2; -.
DR   MEROPS; M50.009; -.
DR   PaxDb; F4JUU5; -.
DR   PRIDE; F4JUU5; -.
DR   EnsemblPlants; AT4G20310.4; AT4G20310.4; AT4G20310. [F4JUU5-1]
DR   GeneID; 827778; -.
DR   Gramene; AT4G20310.4; AT4G20310.4; AT4G20310. [F4JUU5-1]
DR   KEGG; ath:AT4G20310; -.
DR   Araport; AT4G20310; -.
DR   TAIR; locus:2120352; AT4G20310.
DR   eggNOG; KOG2921; Eukaryota.
DR   InParanoid; F4JUU5; -.
DR   OMA; CMHYPYD; -.
DR   BRENDA; 3.4.24.85; 399.
DR   PRO; PR:F4JUU5; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; F4JUU5; baseline and differential.
DR   Genevisible; F4JUU5; AT.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IDA:UniProtKB.
DR   GO; GO:0071475; P:cellular hyperosmotic salinity response; IMP:UniProtKB.
DR   GO; GO:0031293; P:membrane protein intracellular domain proteolysis; IBA:GO_Central.
DR   GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IBA:GO_Central.
DR   GO; GO:1990440; P:positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR   GO; GO:1900457; P:regulation of brassinosteroid mediated signaling pathway; IMP:TAIR.
DR   GO; GO:1905897; P:regulation of response to endoplasmic reticulum stress; IMP:TAIR.
DR   GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR   InterPro; IPR001193; MBTPS2.
DR   InterPro; IPR008915; Peptidase_M50.
DR   PANTHER; PTHR13325; PTHR13325; 1.
DR   Pfam; PF02163; Peptidase_M50; 1.
DR   PRINTS; PR01000; SREBPS2PTASE.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Golgi apparatus; Hydrolase; Membrane; Metal-binding;
KW   Metalloprotease; Protease; Reference proteome; Transmembrane;
KW   Transmembrane helix; Zinc.
FT   CHAIN           1..513
FT                   /note="Membrane-bound transcription factor site-2 protease
FT                   homolog"
FT                   /id="PRO_0000431970"
FT   TOPO_DOM        1..60
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        61..81
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        82..107
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        108..128
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        129..137
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        138..158
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        159..182
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        183..203
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        204..437
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        438..458
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        459..485
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        486..506
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        507..513
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   ACT_SITE        126
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         125
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         129
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   513 AA;  56824 MW;  6544814A3813D122 CRC64;
     MEISGRRMRR FRMRFRRDHL TGGENIENEA SCCYCDLKIS NFNEPIFRLG RRFSGVLKVW
     FSIGLGFGVA SLILVTVFLL LQFHSNPLFS NRLTSAVFGF SPSTRVSLSG IAYVLVSTVI
     TVSVHELGHA LAAASEGIQM EYIAVFIAAI FPGGLVAFDN DVLQSLPSFN ALRIYCAGIW
     HNAVFCALCV FALFLLPVML SPFYKHGESL TVVDVPSVSP LFGYLSPGDV IVSLDGIQVH
     KPSEWLELAA ILDKENSKTS NGSLYLGGSR RFHHGKGYCV PISLIEEGYK GKMVENQFVC
     PGDLTAFRTM PCSNAAIREV SVCLDAKDIV KLQKCGDGWV TTSDTDNQSD CVCPQGDLCL
     QAMQSPGVLW TEITYKRTSS QDCSRLGLDF NTSNCLGTFV FVGDLIAMSH SVHLTAYQPR
     WLFNFFGKSF PNILERSLTC TFHVSLALVL LNSLPVYYLD GESILESSLQ SFTWLSPRKK
     KKALQVCLVG GSLLSFLAFF RIFLLGLPLS RRW
 
 
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