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 27-MAR-2024, entry version 81.
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 function 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.F4JUU5; -.
DR MEROPS; M50.009; -.
DR PaxDb; 3702-AT4G20310-2; -.
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; AT4G20310; S2P.
DR eggNOG; KOG2921; Eukaryota.
DR InParanoid; F4JUU5; -.
DR OMA; FYSWGRW; -.
DR OrthoDB; 5181at2759; -.
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:0000139; C:Golgi membrane; IDA:UniProtKB.
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: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:SF3; MEMBRANE-BOUND TRANSCRIPTION FACTOR SITE-2 PROTEASE; 1.
DR PANTHER; PTHR13325; PROTEASE M50 MEMBRANE-BOUND TRANSCRIPTION FACTOR SITE 2 PROTEASE; 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
//
