RBD2_YEAST
ID RBD2_YEAST Reviewed; 262 AA.
AC Q12270; D6W3C5;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Rhomboid protein 2;
DE EC=3.4.21.-;
GN Name=RBD2; OrderedLocusNames=YPL246C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP GENE NAME.
RX PubMed=12774122; DOI=10.1038/nature01633;
RA McQuibban G.A., Saurya S., Freeman M.;
RT "Mitochondrial membrane remodelling regulated by a conserved rhomboid
RT protease.";
RL Nature 423:537-541(2003).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP INTERACTION WITH SNX3.
RX PubMed=15263065; DOI=10.1074/mcp.m400081-mcp200;
RA Vollert C.S., Uetz P.;
RT "The phox homology (PX) domain protein interaction network in yeast.";
RL Mol. Cell. Proteomics 3:1053-1064(2004).
RN [7]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
CC -!- FUNCTION: Probable serine protease. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with SNX3. {ECO:0000269|PubMed:15263065}.
CC -!- INTERACTION:
CC Q12270; P32912: VAM7; NbExp=3; IntAct=EBI-31471, EBI-20232;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:14562095}. Golgi apparatus, cis-Golgi network
CC membrane {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 7850 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the peptidase S54 family. {ECO:0000305}.
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DR EMBL; Z73602; CAA97967.1; -; Genomic_DNA.
DR EMBL; Z67751; CAA91598.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11191.1; -; Genomic_DNA.
DR PIR; S61018; S61018.
DR RefSeq; NP_015078.1; NM_001184060.1.
DR AlphaFoldDB; Q12270; -.
DR SMR; Q12270; -.
DR BioGRID; 35917; 125.
DR DIP; DIP-1734N; -.
DR IntAct; Q12270; 47.
DR MINT; Q12270; -.
DR STRING; 4932.YPL246C; -.
DR MaxQB; Q12270; -.
DR PaxDb; Q12270; -.
DR PRIDE; Q12270; -.
DR TopDownProteomics; Q12270; -.
DR EnsemblFungi; YPL246C_mRNA; YPL246C; YPL246C.
DR GeneID; 855830; -.
DR KEGG; sce:YPL246C; -.
DR SGD; S000006167; RBD2.
DR VEuPathDB; FungiDB:YPL246C; -.
DR eggNOG; KOG2632; Eukaryota.
DR HOGENOM; CLU_071084_0_0_1; -.
DR InParanoid; Q12270; -.
DR OMA; NTFPFIH; -.
DR BioCyc; YEAST:G3O-34132-MON; -.
DR PRO; PR:Q12270; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q12270; protein.
DR GO; GO:0005794; C:Golgi apparatus; HDA:SGD.
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:0034399; C:nuclear periphery; IDA:SGD.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1540.10; -; 1.
DR InterPro; IPR022764; Peptidase_S54_rhomboid_dom.
DR InterPro; IPR035952; Rhomboid-like_sf.
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..262
FT /note="Rhomboid protein 2"
FT /id="PRO_0000206193"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..57
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..89
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..112
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 134..151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..174
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..262
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 243..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 124
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 179
FT /evidence="ECO:0000250"
SQ SEQUENCE 262 AA; 29500 MW; 3A436E3FEAB7FD35 CRC64;
MNWKSYVFPG GHPPAALTTG LVVFLTAIYL LSFIFALRED LSLAPESLFK LQMSRLSLYP
LIHLSLPHLL FNVLAIWAPL NLFEETHGTV YTGVFLNLSA LFAGILYCLL GKLLYPEALV
AGASGWCFTL FAYYSFKESQ IRPRTRIFRT DYSIPTLYTP LVLLVAIAVV IPGSSFWGHF
FGLCVGYAIG YKESWFNKIT PPGWIITKIE KSLDGLIRLI PWGIKYYRDE DIDRTKDYEP
LMSTETPLPL HNDNSGTVLG TA
