位置:首页 > 蛋白库 > RBL7_ARATH
RBL7_ARATH
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   03-AUG-2022, entry version 120.
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   PRIDE; 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; locus:2127258; AT4G23070.
DR   eggNOG; KOG2289; Eukaryota.
DR   HOGENOM; CLU_011531_0_0_1; -.
DR   InParanoid; O82756; -.
DR   OMA; DCPHKSH; -.
DR   OrthoDB; 1253228at2759; -.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; -; 1.
DR   InterPro; IPR002610; Peptidase_S54_rhomboid.
DR   InterPro; IPR022764; Peptidase_S54_rhomboid_dom.
DR   InterPro; IPR035952; Rhomboid-like_sf.
DR   PANTHER; PTHR22936; PTHR22936; 1.
DR   Pfam; PF01694; Rhomboid; 1.
DR   SUPFAM; SSF144091; SSF144091; 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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2025