YKK0_YEAST
ID YKK0_YEAST Reviewed; 587 AA.
AC P34248; D6VXI7;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Probable intramembrane protease YKL100C;
DE EC=3.4.23.-;
GN OrderedLocusNames=YKL100C; ORFNames=YKL450;
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 [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8256524; DOI=10.1002/yea.320091016;
RA Pallier C., Valens M., Puzos V., Fukuhara H., Cheret G., Sor F.,
RA Bolotin-Fukuhara M.;
RT "DNA sequence analysis of a 17 kb fragment of yeast chromosome XI
RT physically localizes the MRB1 gene and reveals eight new open reading
RT frames, including a homologue of the KIN1/KIN2 and SNF1 protein kinases.";
RL Yeast 9:1149-1155(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [3]
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 [4]
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: May act as intramembrane protease. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- DOMAIN: The PAL motif is required for normal active site conformation.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase A22B family. {ECO:0000305}.
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DR EMBL; X71133; CAA50457.1; -; Genomic_DNA.
DR EMBL; Z28100; CAA81940.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09057.1; -; Genomic_DNA.
DR PIR; S37927; S37927.
DR RefSeq; NP_012822.1; NM_001179666.1.
DR AlphaFoldDB; P34248; -.
DR BioGRID; 34033; 39.
DR IntAct; P34248; 12.
DR MINT; P34248; -.
DR STRING; 4932.YKL100C; -.
DR MEROPS; A22.008; -.
DR iPTMnet; P34248; -.
DR MaxQB; P34248; -.
DR PaxDb; P34248; -.
DR PRIDE; P34248; -.
DR EnsemblFungi; YKL100C_mRNA; YKL100C; YKL100C.
DR GeneID; 853761; -.
DR KEGG; sce:YKL100C; -.
DR SGD; S000001583; YKL100C.
DR VEuPathDB; FungiDB:YKL100C; -.
DR eggNOG; KOG2443; Eukaryota.
DR GeneTree; ENSGT00940000156478; -.
DR HOGENOM; CLU_023799_3_0_1; -.
DR InParanoid; P34248; -.
DR OMA; TFWTGTL; -.
DR BioCyc; YEAST:G3O-31890-MON; -.
DR PRO; PR:P34248; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P34248; protein.
DR GO; GO:0071458; C:integral component of cytoplasmic side of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:1990578; C:perinuclear endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0042500; F:aspartic endopeptidase activity, intramembrane cleaving; IMP:SGD.
DR GO; GO:0009267; P:cellular response to starvation; IMP:SGD.
DR GO; GO:0033619; P:membrane protein proteolysis; IBA:GO_Central.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IMP:SGD.
DR GO; GO:0006465; P:signal peptide processing; IBA:GO_Central.
DR InterPro; IPR007369; Peptidase_A22B_SPP.
DR InterPro; IPR006639; Preselin/SPP.
DR PANTHER; PTHR12174; PTHR12174; 1.
DR Pfam; PF04258; Peptidase_A22B; 1.
DR SMART; SM00730; PSN; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Hydrolase; Membrane; Protease; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..587
FT /note="Probable intramembrane protease YKL100C"
FT /id="PRO_0000073915"
FT TOPO_DOM 1..85
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 107..156
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 178..192
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 214..303
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 325..328
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 350..351
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..372
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 373..401
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 423..450
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 451..471
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 472..475
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 476..496
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 497..587
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 561..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 477..479
FT /note="PAL"
FT ACT_SITE 366
FT /evidence="ECO:0000250"
FT ACT_SITE 411
FT /evidence="ECO:0000250"
SQ SEQUENCE 587 AA; 67525 MW; 40611E339C6FD388 CRC64;
MDKYLNSFVD HLSEWSSRAF RNNSSSANQS ASNKELEQVF EQINAIVENH NNKLTTAFDK
ISYRVAHKIT HLVESHSLVF NYATLVLIAS ALVVIGSFTS ISSIPFTALP PTREHSLFDP
TDFDVDHDCH VIYRENDEDK KKKKKSKRFF DMMDEKHAII LPLTSGCTLL ALYFVIKKLH
LNWLKYVVKI LNFNITLLNI PAGTFVYSYF LNSLFRNLSH LASWNPLVVL PRYRVTIADD
NEDLNKIGGF VTNLNYKDGL TNSVVHKKTL DEIEKDHWMK HFYRRELVEP KDIKSKRQIS
NMYLNSALIV SFVLSIVSTV YFYLSPNDWL ISNAVSMNMA IWSIAQLKLK NLKSGALILI
ALFFYDICFV FGTDVMVTVA TNLDIPVKLS LPVKFNTAQN NFNFSILGLG DIALPGMFIA
MCYKYDIWKW HLDHDDTEFH FLNWSYVGKY FITAMVSYVA SLVSAMVSLS IFNTAQPALL
YIVPSLLIST ILVACWNKDF KQFWNFQYDT IEVDKSLKKA IEKKENSITY STFILSEYYN
DADKYALLGD DVNENFDDDE EFVQEEDLSD SSEEELSEED LLDDESS
