ID STMP6_ARATH Reviewed; 86 AA. AC O04468; DT 22-FEB-2023, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 22-FEB-2023, entry version 119. DE RecName: Full=Secreted transmembrane peptide 6 {ECO:0000303|PubMed:31001913}; DE AltName: Full=Phytocytokine STMP6 {ECO:0000305}; DE AltName: Full=Precursor of secreted transmembrane peptide 6 {ECO:0000305}; DE Flags: Precursor; GN Name=STMP6 {ECO:0000303|PubMed:31001913}; GN OrderedLocusNames=At1g65500 {ECO:0000312|Araport:AT1G65500}; GN ORFNames=F5I14.4 {ECO:0000312|EMBL:AAB60905.1}; 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=11130712; DOI=10.1038/35048500; RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L., RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., RA Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."; RL Nature 408:816-820(2000). 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, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, RP INDUCTION BY BIOTIC AND ABIOTIC STRESSES, GENE FAMILY, AND NOMENCLATURE. RC STRAIN=cv. Columbia; RX PubMed=31001913; DOI=10.1111/jipb.12817; RA Yu Z., Xu Y., Zhu L., Zhang L., Liu L., Zhang D., Li D., Wu C., Huang J., RA Yang G., Yan K., Zhang S., Zheng C.; RT "The Brassicaceae-specific secreted peptides, STMPs, function in plant RT growth and pathogen defense."; RL J. Integr. Plant Biol. 62:403-420(2020). CC -!- FUNCTION: Brassicaceae-specific phytocytokine (plant endogenous peptide CC released into the apoplast) perceived by MIK2 in a BAK1/SERK3 and SERK4 CC coreceptors-dependent manner, that modulates various physiological and CC antimicrobial processes including growth prevention and reactive oxygen CC species (ROS) response regulation (By similarity). Prevents general CC growth and development (PubMed:31001913). CC {ECO:0000250|UniProtKB:B3H7I1, ECO:0000269|PubMed:31001913}. CC -!- SUBUNIT: Interacts with MIK2 (via extracellular leucine-rich repeat CC domain); this interaction triggers the formation of complex between CC MIK2 and the BAK1/SERK3 and SERK4 coreceptors, and subsequent BAK1 CC activation by phosphorylation. {ECO:0000250|UniProtKB:B3H7I1}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:31001913}. CC Secreted, extracellular space, apoplast {ECO:0000269|PubMed:31001913}. CC Note=The precursor of STMP6 accumulates at the plasma membrane and is CC proteolytically cleaved to release the STMP6 in the apoplasm. CC {ECO:0000269|PubMed:31001913}. CC -!- TISSUE SPECIFICITY: Mostly expressed in leaves, and, to a lower extent, CC in roots, stems, siliques, seeds and flowers. CC {ECO:0000269|PubMed:31001913}. CC -!- INDUCTION: Induced by cold, drought and salt stress, but repressed by CC pathogenic bacteria Pseudomonas syringae pv. tomato (Pst) DC3000, CC jasmonate (MeJA), ethylene (ET) and salicylic acid (SA), mainly in CC shoots. {ECO:0000269|PubMed:31001913}. CC -!- DISRUPTION PHENOTYPE: Slightly increased growth and fresh weight. CC {ECO:0000269|PubMed:31001913}. CC -!- SIMILARITY: Belongs to the serine rich endogenous peptide (SCOOP) CC phytocytokine family. {ECO:0000305}. 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; AC001229; AAB60905.1; -; Genomic_DNA. DR EMBL; CP002684; AEE34390.1; -; Genomic_DNA. DR PIR; H96679; H96679. DR RefSeq; NP_564855.1; NM_105224.3. DR AlphaFoldDB; O04468; -. DR EnsemblPlants; AT1G65500.1; AT1G65500.1; AT1G65500. DR GeneID; 842862; -. DR Gramene; AT1G65500.1; AT1G65500.1; AT1G65500. DR KEGG; ath:AT1G65500; -. DR Araport; AT1G65500; -. DR TAIR; locus:2034173; AT1G65500. DR HOGENOM; CLU_194966_0_0_1; -. DR OMA; MKSPNIA; -. DR OrthoDB; 686926at2759; -. DR Proteomes; UP000006548; Chromosome 1. DR GO; GO:0048046; C:apoplast; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:TAIR. DR GO; GO:0030275; F:LRR domain binding; ISS:UniProtKB. DR GO; GO:0033612; F:receptor serine/threonine kinase binding; ISS:UniProtKB. DR GO; GO:0009617; P:response to bacterium; IEP:UniProtKB. DR GO; GO:0009409; P:response to cold; IEP:UniProtKB. DR GO; GO:0009723; P:response to ethylene; IEP:UniProtKB. DR GO; GO:0009753; P:response to jasmonic acid; IEP:UniProtKB. DR GO; GO:0009751; P:response to salicylic acid; IEP:UniProtKB. DR GO; GO:0009651; P:response to salt stress; IEP:UniProtKB. DR GO; GO:0009414; P:response to water deprivation; IEP:UniProtKB. PE 2: Evidence at transcript level; KW Apoplast; Cell membrane; Cleavage on pair of basic residues; Membrane; KW Reference proteome; Secreted; Signal. FT SIGNAL 1..31 FT /evidence="ECO:0000255" FT PROPEP 32..? FT /note="Removed in mature form" FT /evidence="ECO:0000250|UniProtKB:B3H7I1" FT /id="PRO_0000457266" FT PEPTIDE ?..86 FT /note="Secreted transmembrane peptide 6" FT /evidence="ECO:0000250|UniProtKB:B3H7I1" FT /id="PRO_0000457267" FT MOTIF 45..58 FT /note="SCOOP motif" FT /evidence="ECO:0000250|UniProtKB:A0A1P8AQ95" FT MOTIF 51..53 FT /note="SxS motif essential for MIK2 binding" FT /evidence="ECO:0000250|UniProtKB:B3H7I1" SQ SEQUENCE 86 AA; 9352 MW; 72778DB73973C0E5 CRC64; MGMKSPNIAA FMLPLLLILF TLSSQLKVVE STGRKLAWGF SGTPIVYTPP SRSCGTSPAV FTSKWRRPRP CRLPPGSYIP ASDQSP //