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   27-MAR-2024, entry version 103.
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 /
RC   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; 284590.Q6CKK4; -.
DR   ESTHER; klula-q6ckk4; Carboxypeptidase_S10.
DR   MEROPS; S10.007; -.
DR   GlyCosmos; Q6CKK4; 4 sites, No reported glycans.
DR   PaxDb; 284590-Q6CKK4; -.
DR   GeneID; 2895014; -.
DR   KEGG; kla:KLLA0_F09999g; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_11_2_1; -.
DR   InParanoid; Q6CKK4; -.
DR   OMA; PLMFAGQ; -.
DR   Proteomes; UP000000598; Chromosome F.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; alpha/beta hydrolase; 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:SF190; PHEROMONE-PROCESSING CARBOXYPEPTIDASE KEX1; 1.
DR   PANTHER; PTHR11802; SERINE PROTEASE FAMILY S10 SERINE CARBOXYPEPTIDASE; 1.
DR   Pfam; PF00450; Peptidase_S10; 1.
DR   PRINTS; PR00724; CRBOXYPTASEC.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 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
//