RBD2_DEBHA
ID RBD2_DEBHA Reviewed; 286 AA.
AC Q6BSA9;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Rhomboid protein 2;
DE EC=3.4.21.-;
GN Name=RBD2; OrderedLocusNames=DEHA2D10252g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Probable serine protease. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Multi-
CC pass membrane protein {ECO:0000250}. Golgi apparatus, cis-Golgi network
CC membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S54 family. {ECO:0000305}.
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DR EMBL; CR382136; CAG87065.2; -; Genomic_DNA.
DR RefSeq; XP_458911.2; XM_458911.1.
DR AlphaFoldDB; Q6BSA9; -.
DR STRING; 4959.XP_458911.2; -.
DR EnsemblFungi; CAG87065; CAG87065; DEHA2D10252g.
DR GeneID; 2901604; -.
DR KEGG; dha:DEHA2D10252g; -.
DR VEuPathDB; FungiDB:DEHA2D10252g; -.
DR eggNOG; KOG2632; Eukaryota.
DR HOGENOM; CLU_071084_0_0_1; -.
DR InParanoid; Q6BSA9; -.
DR OMA; NTFPFIH; -.
DR OrthoDB; 1588469at2759; -.
DR Proteomes; UP000000599; Chromosome D.
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: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; IPR022764; Peptidase_S54_rhomboid_dom.
DR InterPro; IPR035952; Rhomboid-like_sf.
DR Pfam; PF01694; Rhomboid; 1.
DR SUPFAM; SSF144091; SSF144091; 1.
PE 3: Inferred from homology;
KW Golgi apparatus; Hydrolase; Membrane; Protease; Reference proteome;
KW Serine protease; Transmembrane; Transmembrane helix.
FT CHAIN 1..286
FT /note="Rhomboid protein 2"
FT /id="PRO_0000206186"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 133
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 191
FT /evidence="ECO:0000250"
SQ SEQUENCE 286 AA; 31559 MW; B842098C27EC8DA2 CRC64;
MSSPSFINKL ALPNLATITQ YPALTVGLSV FTFLLLVIDL CSNQALSQKF SLYPNAPFEF
DLNRLSFYLL FHRGFTHWLL NVVGLFSPLA IFERTNGTVF TGVTLNVLAV TAGLQFCIVG
KLLYPNTQVI GLSGVVFSFM SFMAYKEHHT TPVIYTFKYQ GSEVSIPTLY SPFIFLIVCM
VLIPGSSFWG HLAGISSGYL LALGYIKFLY PPSKAILFIE RKLQTPINAL RSLVVYYKEE
EAIEQRGVSY NPLLSSDPES ALNDIPVTTG ARTNSFAGEG QVLGAT