ID SCOP6_ARATH Reviewed; 93 AA. AC Q0WML3; DT 22-FEB-2023, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 1. DT 22-FEB-2023, entry version 85. DE RecName: Full=Serine rich endogenous peptide 6 {ECO:0000303|PubMed:33514716, ECO:0000303|PubMed:34535661}; DE Short=AtSCOOP6 {ECO:0000303|PubMed:33514716, ECO:0000303|PubMed:34535661}; DE AltName: Full=Phytocytokine SCOOP6 {ECO:0000303|PubMed:33514716, ECO:0000303|PubMed:34535661}; DE AltName: Full=Precursor of serine rich endogenous peptide phytocytokine 6 {ECO:0000303|PubMed:33514716, ECO:0000303|PubMed:34535661}; DE Flags: Precursor; GN Name=PROSCOOP6 {ECO:0000303|PubMed:33514716, ECO:0000303|PubMed:34535661}; GN Synonyms=SCOOP6 {ECO:0000303|PubMed:33514716, ECO:0000303|PubMed:34535661}; GN OrderedLocusNames=At5g44572 {ECO:0000312|Araport:AT5G44572}; GN ORFNames=K15C23 {ECO:0000312|EMBL:AB024024}; 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; RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H., RA Tabata S.; RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI."; RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases. 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; RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K., RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., RA Shinozaki K.; RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."; RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases. RN [4] RP GENE FAMILY. RC STRAIN=cv. Columbia, and cv. Wassilewskija; RX PubMed=30715439; DOI=10.1093/jxb/ery454; RA Gully K., Pelletier S., Guillou M.-C., Ferrand M., Aligon S., Pokotylo I., RA Perrin A., Vergne E., Fagard M., Ruelland E., Grappin P., Bucher E., RA Renou J.-P., Aubourg S.; RT "The SCOOP12 peptide regulates defense response and root elongation in RT Arabidopsis thaliana."; RL J. Exp. Bot. 70:1349-1365(2019). RN [5] RP FUNCTION, AND GENE FAMILY. RC STRAIN=cv. Columbia, and cv. Wassilewskija-2; RX PubMed=33514716; DOI=10.1038/s41467-021-20932-y; RA Rhodes J., Yang H., Moussu S., Boutrot F., Santiago J., Zipfel C.; RT "Perception of a divergent family of phytocytokines by the Arabidopsis RT receptor kinase MIK2."; RL Nat. Commun. 12:705-705(2021). RN [6] RP FUNCTION, TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE. RC STRAIN=cv. Columbia; RX PubMed=34535661; DOI=10.1038/s41467-021-25580-w; RA Hou S., Liu D., Huang S., Luo D., Liu Z., Xiang Q., Wang P., Mu R., Han Z., RA Chen S., Chai J., Shan L., He P.; RT "The Arabidopsis MIK2 receptor elicits immunity by sensing a conserved RT signature from phytocytokines and microbes."; RL Nat. Commun. 12:5494-5494(2021). RN [7] RP INDUCTION BY INSECT HERBIVORY AND WOUNDING. RC STRAIN=cv. Columbia, and cv. Wassilewskija; RX PubMed=35401621; DOI=10.3389/fpls.2022.852808; RA Stahl E., Fernandez Martin A., Glauser G., Guillou M.-C., Aubourg S., RA Renou J.-P., Reymond P.; RT "The MIK2/SCOOP signaling system contributes to Arabidopsis resistance RT against herbivory by modulating jasmonate and indole glucosinolate RT biosynthesis."; RL Front. Plant Sci. 13:852808-852808(2022). 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 (PubMed:33514716, PubMed:34535661). CC Inhibits root growth (PubMed:34535661). {ECO:0000269|PubMed:33514716, CC ECO:0000269|PubMed:34535661}. 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:0000250|UniProtKB:B3H7I1}. CC Secreted, extracellular space, apoplast {ECO:0000250|UniProtKB:B3H7I1}. CC Note=The precursor of SCOOP6, PROSCOOP6, accumulates at the plasma CC membrane and is proteolytically cleaved to release the SCOOP6 in the CC apoplasm. {ECO:0000250|UniProtKB:B3H7I1}. CC -!- TISSUE SPECIFICITY: Mostly expressed in seedlings shoots, and, to a CC lower extent, in roots. {ECO:0000269|PubMed:34535661}. CC -!- INDUCTION: Accumulates upon infection by generalist herbivores such as CC Spodoptera littoralis (PubMed:35401621). Induced by wounding CC (PubMed:35401621). {ECO:0000269|PubMed:35401621}. 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; AB024024; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CP002688; AED95129.1; -; Genomic_DNA. DR EMBL; AK229806; BAF01637.1; -; mRNA. DR RefSeq; NP_001078711.1; NM_001085242.2. DR AlphaFoldDB; Q0WML3; -. DR EnsemblPlants; AT5G44572.1; AT5G44572.1; AT5G44572. DR GeneID; 5008298; -. DR Gramene; AT5G44572.1; AT5G44572.1; AT5G44572. DR KEGG; ath:AT5G44572; -. DR Araport; AT5G44572; -. DR TAIR; locus:4010714043; AT5G44572. DR HOGENOM; CLU_2402689_0_0_1; -. DR OMA; MGIYMPN; -. DR OrthoDB; 5602178at2759; -. DR Proteomes; UP000006548; Chromosome 5. DR GO; GO:0048046; C:apoplast; ISS:UniProtKB. 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:0080027; P:response to herbivore; IEP:UniProtKB. DR GO; GO:0009625; P:response to insect; IEP:UniProtKB. DR GO; GO:0009611; P:response to wounding; IEP:UniProtKB. PE 2: Evidence at transcript level; KW Apoplast; Cell membrane; Cleavage on pair of basic residues; Membrane; KW Reference proteome; Repeat; Secreted; Signal. FT SIGNAL 1..27 FT /evidence="ECO:0000255" FT PROPEP 28..? FT /note="Removed in mature form" FT /evidence="ECO:0000250|UniProtKB:B3H7I1" FT /id="PRO_0000457224" FT PEPTIDE ?..93 FT /note="Serine rich endogenous peptide 6" FT /evidence="ECO:0000250|UniProtKB:B3H7I1" FT /id="PRO_0000457225" FT MOTIF 48..62 FT /note="SCOOP motif 1" FT /evidence="ECO:0000305|PubMed:34535661" FT MOTIF 54..56 FT /note="SxS motif essential for MIK2 binding" FT /evidence="ECO:0000250|UniProtKB:B3H7I1" FT MOTIF 73..87 FT /note="SCOOP motif 2" FT /evidence="ECO:0000305|PubMed:34535661" FT MOTIF 79..81 FT /note="SxS motif essential for MIK2 binding" FT /evidence="ECO:0000250|UniProtKB:B3H7I1" SQ SEQUENCE 93 AA; 9928 MW; 9FBCD3E04A0C5252 CRC64; MGTKCYSKLR YVVVLVLLLF VFPCSLSQSA PSSVTGRRLM GIYMPNGGII AGSSPSGQAP NINNNYHGRR LMISEARPSK SKKGGGREPE SPG //