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   27-MAR-2024, entry version 159.
DE   RecName: Full=Rhomboid-type serine protease 2 {ECO:0000305};
DE            EC=3.4.21.105 {ECO:0000250|UniProtKB:O74926};
DE   AltName: Full=Rhomboid protein 2 {ECO:0000305};
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 rhomboid-type serine protease that catalyzes
CC       intramembrane proteolysis. {ECO:0000250|UniProtKB:O74926}.
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:0000250|UniProtKB:O74926};
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; 147.
DR   DIP; DIP-1734N; -.
DR   IntAct; Q12270; 47.
DR   MINT; Q12270; -.
DR   STRING; 4932.YPL246C; -.
DR   MaxQB; Q12270; -.
DR   PaxDb; 4932-YPL246C; -.
DR   PeptideAtlas; Q12270; -.
DR   TopDownProteomics; Q12270; -.
DR   EnsemblFungi; YPL246C_mRNA; YPL246C; YPL246C.
DR   GeneID; 855830; -.
DR   KEGG; sce:YPL246C; -.
DR   AGR; SGD:S000006167; -.
DR   SGD; S000006167; RBD2.
DR   VEuPathDB; FungiDB:YPL246C; -.
DR   eggNOG; KOG2632; Eukaryota.
DR   HOGENOM; CLU_071084_0_0_1; -.
DR   InParanoid; Q12270; -.
DR   OMA; NTYPIVH; -.
DR   OrthoDB; 2718371at2759; -.
DR   BioCyc; YEAST:G3O-34132-MONOMER; -.
DR   BioGRID-ORCS; 855830; 1 hit in 10 CRISPR screens.
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: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; Rhomboid-like; 1.
DR   InterPro; IPR022764; Peptidase_S54_rhomboid_dom.
DR   InterPro; IPR035952; Rhomboid-like_sf.
DR   PANTHER; PTHR43066:SF1; RHOMBOID PROTEIN 2; 1.
DR   PANTHER; PTHR43066; RHOMBOID-RELATED PROTEIN; 1.
DR   Pfam; PF01694; Rhomboid; 1.
DR   SUPFAM; SSF144091; Rhomboid-like; 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-type serine protease 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|UniProtKB:O74926"
FT   ACT_SITE        179
FT                   /evidence="ECO:0000250|UniProtKB:O74926"
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
//