KEX1_KLULA
ID KEX1_KLULA Reviewed; 642 AA.
AC Q6CKK4;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Pheromone-processing carboxypeptidase KEX1;
DE EC=3.4.16.6;
DE AltName: Full=Carboxypeptidase D;
DE Flags: Precursor;
GN Name=KEX1; OrderedLocusNames=KLLA0F09999g;
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 [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: Protease with a carboxypeptidase B-like function involved in
CC the C-terminal processing of the lysine and arginine residues from
CC protein precursors. Promotes cell fusion and is involved in the
CC programmed cell death (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential release of a C-terminal arginine or lysine
CC residue.; EC=3.4.16.6;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR382126; CAG98243.1; -; Genomic_DNA.
DR RefSeq; XP_455535.1; XM_455535.1.
DR AlphaFoldDB; Q6CKK4; -.
DR SMR; Q6CKK4; -.
DR STRING; 28985.XP_455535.1; -.
DR ESTHER; klula-q6ckk4; Carboxypeptidase_S10.
DR MEROPS; S10.007; -.
DR EnsemblFungi; CAG98243; CAG98243; KLLA0_F09999g.
DR GeneID; 2895014; -.
DR KEGG; kla:KLLA0_F09999g; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_11_2_1; -.
DR OMA; NGWIDPD; -.
DR Proteomes; UP000000598; Chromosome F.
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:0004185; F:serine-type carboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001563; Peptidase_S10.
DR InterPro; IPR033124; Ser_caboxypep_his_AS.
DR InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR PANTHER; PTHR11802; PTHR11802; 1.
DR Pfam; PF00450; Peptidase_S10; 1.
DR PRINTS; PR00724; CRBOXYPTASEC.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1.
DR PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE 3: Inferred from homology;
KW Apoptosis; Carboxypeptidase; Glycoprotein; Golgi apparatus; Hydrolase;
KW Membrane; Protease; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..642
FT /note="Pheromone-processing carboxypeptidase KEX1"
FT /id="PRO_0000411921"
FT TOPO_DOM 20..544
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 545..565
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 566..642
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 515..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 189
FT /evidence="ECO:0000250"
FT ACT_SITE 406
FT /evidence="ECO:0000250"
FT ACT_SITE 470
FT /evidence="ECO:0000250"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 425
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 459
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 467
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 642 AA; 72916 MW; 72DB7F3D4A858215 CRC64;
MSLWLFFVQT VLLIQCALGG LPNAKDYLVA PDLLPGLNDV KDKELIPEMH AGHIPLDDGD
DDDDDDEKNY FFWKFHDLAN QTSVVASKTL IIWLNGGPGC SSLDGALMES GALRIDDDGE
AYLNPGSWHT RGDIVFVDQP AGTGFSTVGD SKYDKDLNQV SKHFMKFLKN YFKIFPDDLD
KDLVLAGESY AGQYIPFFAN EILKFNSKLD KDDNEEESRS GKKYNLKSLL IGNGWIDPDQ
QSLSYIPFAL ENNLISTKAD YFPDLLNMHS RCQNLVNNNG GKKFSFDECE DILTKILYYT
RRKTDENGNK VPSNQECTNI YDFRLFDSYP ACGSNWPDDL PSVSKFLGKP GVMDSLHLDV
DKVPHWRECD SKVSSHLKNK NTQPSIHLLP NLLKHMQIFL FNGDKDIICN SRGVQDLIKN
MKWNNHTGFT NDAEYYDWQY YDQFTDDTIS AGFVKHESNL TYVSVYNASH MVPYDNALIS
RGIMDIYLKD VELVVGKDNQ DDVIISKDFV VHSDHSTGEE ELSADQKQDE DENSHKDRHR
NSDKFEIAVI LLVVFSITGT IAYYFLRERF RKQIHAILID PENRPPSSNK SVAWADDIEN
QGDDFKLSID EAPSTADKPA KNKSGYTKVP NTDDDSFELD NL
