KEX1A_KLULA
ID KEX1A_KLULA Reviewed; 756 AA.
AC P09231; Q6CQ47;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 25-MAY-2022, entry version 153.
DE RecName: Full=Protease KEX1;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=KEX1; OrderedLocusNames=KLLA0D19811g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 76492 / CBS 2359/152 / CLIB 210;
RX PubMed=3292294; DOI=10.1016/0014-5793(88)80139-x;
RA Tanguy-Rougeau C., Wesolowski-Louvel M., Fukuhara H.;
RT "The Kluyveromyces lactis KEX1 gene encodes a subtilisin-type serine
RT proteinase.";
RL FEBS Lett. 234:464-470(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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: Probably involved in the processing of the precursor of m1-
CC toxin and alpha-factor.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA30088.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X07038; CAA30088.1; ALT_FRAME; Genomic_DNA.
DR EMBL; CR382124; CAH01038.1; -; Genomic_DNA.
DR PIR; S01013; S01013.
DR RefSeq; XP_453942.1; XM_453942.1.
DR AlphaFoldDB; P09231; -.
DR SMR; P09231; -.
DR STRING; 28985.XP_453942.1; -.
DR EnsemblFungi; CAH01038; CAH01038; KLLA0_D19811g.
DR GeneID; 2893281; -.
DR KEGG; kla:KLLA0_D19811g; -.
DR eggNOG; KOG3525; Eukaryota.
DR HOGENOM; CLU_002976_2_1_1; -.
DR InParanoid; P09231; -.
DR OMA; AYEFDII; -.
DR Proteomes; UP000000598; Chromosome D.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005802; C:trans-Golgi network; IEA:EnsemblFungi.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:EnsemblFungi.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:EnsemblFungi.
DR GO; GO:0007323; P:peptide pheromone maturation; IEA:EnsemblFungi.
DR GO; GO:0016540; P:protein autoprocessing; IEA:EnsemblFungi.
DR CDD; cd04059; Peptidases_S8_Protein_convertases_Kexins_Furin-like; 1.
DR Gene3D; 3.40.50.200; -; 1.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR034182; Kexin/furin.
DR InterPro; IPR002884; P_dom.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR Pfam; PF01483; P_proprotein; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF52743; SSF52743; 1.
DR PROSITE; PS51829; P_HOMO_B; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Calcium; Disulfide bond; Glycoprotein; Hydrolase; Membrane; Protease;
KW Reference proteome; Serine protease; Signal; Transmembrane;
KW Transmembrane helix; Zymogen.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..756
FT /note="Protease KEX1"
FT /id="PRO_0000027040"
FT TRANSMEM 641..661
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 130..440
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 449..583
FT /note="P/Homo B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01173"
FT REGION 599..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 715..756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..628
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..756
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 164
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 202
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 373
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 392
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 538
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 218..365
FT /evidence="ECO:0000250"
FT DISULFID 310..340
FT /evidence="ECO:0000250"
FT CONFLICT 688
FT /note="S -> A (in Ref. 1; CAA30088)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 756 AA; 83713 MW; 7FA14CCB1B5D636F CRC64;
MILSSQLMLA LIAVSGYGKA MQVPKKDHEN RQYFAIESYD DVGNLLAEHS DWSFEHDVRG
LANHYVFSKP LQSLGKRDAI DTGYSENIID FHDLPPVQLH KRLPIGDSSM EQIQNARILF
NISDPLFDQQ WHLINPNYPG NDVNVTGLWK ENITGYGVVA ALVDDGLDYE NEDLKDNFCV
EGSWDFNDNN PLPKPRLKDD YHGTRCAGEI AAFRNDICGV GVAYNSKVSG IRILSGQITA
EDEAASLIYG LDVNDIYSCS WGPSDDGKTM QAPDTLVKKA IIKGVTEGRD AKGALYVFAS
GNGGMFGDSC NFDGYTNSIF SITVGAIDWK GLHPPYSESC SAVMVVTYSS GSGNYIKTTD
LDEKCSNTHG GTSAAAPLAA GIYTLVLEAN PNLTWRDVQY LSILSSEEIN PHDGKWQDTA
MGKRYSHTYG FGKLDAYNIV HMAKSWINVN PQGWLYLPTI VEKQSISNSD EVIESTVSVS
AEEFKQNNLK RLEHVTVTVD IDAPYRGHVL VDLISPDGVT STLATARRLD KNRYGFQNWT
FMSVAHWGSS GVGSWKLKVK STHDNEIVTL KSWRLKMFGE TIDAKKAKVI SYGNDKEDAE
VKSTESKTTT PTAQTSSFTT TSGEETSGAN KLPRPEQAAQ LYLAIFVIGA IVIIIYYLFF
LKSRRIIRRS RAEAYEFDII DTDSEYDSSI NQTAESISGE VNDDNLEDFN FDINEEELSP
RESSSNNPFG NESLESFDNS PDHTSNLLGQ NSIPNK
