ID RBL7_ARATH Reviewed; 313 AA. AC O82756; DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 13-SEP-2023, entry version 125. DE RecName: Full=RHOMBOID-like protein 7 {ECO:0000303|PubMed:16223493, ECO:0000303|PubMed:17181860}; DE Short=AtRBL7 {ECO:0000303|PubMed:16223493, ECO:0000303|PubMed:17181860}; DE EC=3.4.21.- {ECO:0000305}; GN Name=RBL7 {ECO:0000303|PubMed:16223493, ECO:0000303|PubMed:17181860}; GN OrderedLocusNames=At4g23070 {ECO:0000312|Araport:AT4G23070}; GN ORFNames=F7H19.260 {ECO:0000312|EMBL:CAA19823.1}; 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 {ECO:0000312|Proteomes:UP000006548}; 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 GENE FAMILY, AND NOMENCLATURE. RC STRAIN=cv. Columbia; RX PubMed=16223493; DOI=10.1016/j.febslet.2005.09.049; RA Kanaoka M.M., Urban S., Freeman M., Okada K.; RT "An Arabidopsis Rhomboid homolog is an intramembrane protease in plants."; RL FEBS Lett. 579:5723-5728(2005). RN [4] RP GENE FAMILY, AND NOMENCLATURE. RX PubMed=16895613; DOI=10.1186/1471-2164-7-200; RA Tripathi L.P., Sowdhamini R.; RT "Cross genome comparisons of serine proteases in Arabidopsis and rice."; RL BMC Genomics 7:200-200(2006). RN [5] RP GENE FAMILY, AND NOMENCLATURE. RX PubMed=17181860; DOI=10.1186/1471-2229-6-30; RA Garcia-Lorenzo M., Sjodin A., Jansson S., Funk C.; RT "Protease gene families in Populus and Arabidopsis."; RL BMC Plant Biol. 6:30-30(2006). RN [6] RP GENE FAMILY, AND NOMENCLATURE. RX PubMed=17938163; DOI=10.1101/gr.6425307; RA Lemberg M.K., Freeman M.; RT "Functional and evolutionary implications of enhanced genomic analysis of RT rhomboid intramembrane proteases."; RL Genome Res. 17:1634-1646(2007). RN [7] RP REVIEW. RX PubMed=22007993; DOI=10.1111/j.1399-3054.2011.01532.x; RA Knopf R.R., Adam Z.; RT "Rhomboid proteases in plants - still in square one?"; RL Physiol. Plantarum 145:41-51(2012). CC -!- FUNCTION: Probable rhomboid-type serine protease that catalyzes CC intramembrane proteolysis. May function in embryo development. CC {ECO:0000303|PubMed:22007993}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane CC protein {ECO:0000255}. CC -!- SIMILARITY: Belongs to the peptidase S54 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; AL031018; CAA19823.1; -; Genomic_DNA. DR EMBL; AL161558; CAB79262.1; -; Genomic_DNA. DR EMBL; CP002687; AEE84702.1; -; Genomic_DNA. DR PIR; T05139; T05139. DR RefSeq; NP_194038.1; NM_118436.2. DR AlphaFoldDB; O82756; -. DR IntAct; O82756; 1. DR STRING; 3702.AT4G23070.1; -. DR MEROPS; S54.A03; -. DR PaxDb; O82756; -. DR EnsemblPlants; AT4G23070.1; AT4G23070.1; AT4G23070. DR GeneID; 828406; -. DR Gramene; AT4G23070.1; AT4G23070.1; AT4G23070. DR KEGG; ath:AT4G23070; -. DR Araport; AT4G23070; -. DR TAIR; AT4G23070; RBL7. DR eggNOG; KOG2289; Eukaryota. DR HOGENOM; CLU_011531_0_0_1; -. DR InParanoid; O82756; -. DR OMA; EWEENRV; -. DR OrthoDB; 3087653at2759; -. DR PhylomeDB; O82756; -. DR PRO; PR:O82756; -. DR Proteomes; UP000006548; Chromosome 4. DR ExpressionAtlas; O82756; baseline and differential. DR Genevisible; O82756; AT. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR Gene3D; 1.20.1540.10; Rhomboid-like; 1. DR InterPro; IPR002610; Peptidase_S54_rhomboid. DR InterPro; IPR022764; Peptidase_S54_rhomboid_dom. DR InterPro; IPR035952; Rhomboid-like_sf. DR PANTHER; PTHR22936:SF94; RHOMBOID-LIKE PROTEIN 7; 1. DR PANTHER; PTHR22936; RHOMBOID-RELATED; 1. DR Pfam; PF01694; Rhomboid; 1. DR SUPFAM; SSF144091; Rhomboid-like; 1. PE 3: Inferred from homology; KW Hydrolase; Membrane; Protease; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1..313 FT /note="RHOMBOID-like protein 7" FT /id="PRO_0000433328" FT TRANSMEM 31..51 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 112..132 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 143..163 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 166..186 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 196..216 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 221..241 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 269..289 FT /note="Helical" FT /evidence="ECO:0000255" FT REGION 1..24 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 171 FT /note="Nucleophile" FT /evidence="ECO:0000250|UniProtKB:P54493" FT ACT_SITE 223 FT /note="Charge relay system" FT /evidence="ECO:0000250|UniProtKB:P54493" SQ SEQUENCE 313 AA; 34532 MW; D7715F7DCA16E493 CRC64; MLSTAAEEDP EGGSRETNNG GETTPDMQWR SWIIPIVVIA NVVVFVVVMY YNDCPHKSHR CLAKFLGRFS FESFKSNPLL GPSSSTLEKM GALAWGKIVH KRQVWRLLTC MWLHAGVIHL LANMCCVAYI GVRLEQQFGF VRVGTIYLVS GFCGSILSCL FLEDAISVGA SSALFGLLGA MLSELLINWT TYDNKGVAIV MLLVIVGVNL GLGTLPPVDN FAHIGGFFGG FLLGFLLLIH PQFEWEENQV SLMPGTIVKP KYNTCQLVLC IVASIVFVAG FTSGLVILFR GDSLNRYCKW CHKLSYSSKS QWT //