RBL2_ARATH
ID RBL2_ARATH Reviewed; 317 AA.
AC Q9CAN1;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=RHOMBOID-like protein 2 {ECO:0000303|PubMed:16223493, ECO:0000303|PubMed:17181860};
DE Short=AtRBL2 {ECO:0000303|PubMed:16223493, ECO:0000303|PubMed:17181860};
DE EC=3.4.21.105 {ECO:0000269|PubMed:16223493};
GN Name=RBL2 {ECO:0000303|PubMed:16223493, ECO:0000303|PubMed:17181860};
GN OrderedLocusNames=At1g63120 {ECO:0000312|Araport:AT1G63120};
GN ORFNames=F16M19.4 {ECO:0000312|EMBL:AAG51610.1};
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 [MRNA], GENE FAMILY, NOMENCLATURE, TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION
RP PHENOTYPE.
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 [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
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 [6]
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 [7]
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 [8]
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: Rhomboid-type serine protease that catalyzes intramembrane
CC proteolysis. Can cleave the Drosophila proteins Spitz and Keren
CC (PubMed:16223493). May function in pollen elongation (PubMed:22007993).
CC {ECO:0000269|PubMed:16223493, ECO:0000303|PubMed:22007993}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleaves type-1 transmembrane domains using a catalytic dyad
CC composed of serine and histidine that are contributed by different
CC transmembrane domains.; EC=3.4.21.105;
CC Evidence={ECO:0000269|PubMed:16223493};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:16223493}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, seedlings, leaves, stems and
CC flowers. {ECO:0000269|PubMed:16223493}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000305|PubMed:16223493}.
CC -!- SIMILARITY: Belongs to the peptidase S54 family. {ECO:0000305}.
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DR EMBL; AB195671; BAE46871.1; -; mRNA.
DR EMBL; AC010795; AAG51610.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34058.1; -; Genomic_DNA.
DR EMBL; BT004076; AAO42103.1; -; mRNA.
DR EMBL; BT005121; AAO50654.1; -; mRNA.
DR PIR; F96656; F96656.
DR RefSeq; NP_176500.1; NM_104990.4.
DR AlphaFoldDB; Q9CAN1; -.
DR IntAct; Q9CAN1; 35.
DR STRING; 3702.AT1G63120.1; -.
DR MEROPS; S54.015; -.
DR PaxDb; Q9CAN1; -.
DR PRIDE; Q9CAN1; -.
DR ProteomicsDB; 236491; -.
DR EnsemblPlants; AT1G63120.1; AT1G63120.1; AT1G63120.
DR GeneID; 842616; -.
DR Gramene; AT1G63120.1; AT1G63120.1; AT1G63120.
DR KEGG; ath:AT1G63120; -.
DR Araport; AT1G63120; -.
DR TAIR; locus:2015193; AT1G63120.
DR eggNOG; KOG2289; Eukaryota.
DR HOGENOM; CLU_011531_0_0_1; -.
DR InParanoid; Q9CAN1; -.
DR OMA; CPKKITG; -.
DR OrthoDB; 1253228at2759; -.
DR PhylomeDB; Q9CAN1; -.
DR PRO; PR:Q9CAN1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9CAN1; baseline and differential.
DR Genevisible; Q9CAN1; AT.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:TAIR.
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 1: Evidence at protein level;
KW Golgi apparatus; Hydrolase; Membrane; Protease; Reference proteome;
KW Serine protease; Transmembrane; Transmembrane helix.
FT CHAIN 1..317
FT /note="RHOMBOID-like protein 2"
FT /id="PRO_0000433323"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 177
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P54493"
FT ACT_SITE 229
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P54493"
SQ SEQUENCE 317 AA; 35413 MW; 56265BE6BBA90451 CRC64;
MANRDVERVG KKNRGANNNY FYEESSGETH WTSWLIPAIV VANLAVFIAV MFVNDCPKKI
TGPNKECVAR FLGRFSFQPL KENPLFGPSS STLEKMGALE WRKVVHEHQG WRLLSCMWLH
AGIIHLLTNM LSLIFIGIRL EQQFGFIRVG LIYLISGLGG SILSSLFLQE SISVGASGAL
FGLLGAMLSE LLTNWTIYAN KAAALITLLF IIAINLALGM LPRVDNFAHI GGFLTGFCLG
FVLLVRPQYG WEASRTNTSR TKRKYSMYQY VLFVVSVVLL VVGLTVALVM LFKGENGNKH
CKWCHYLSCF PTSKWTC
