ID   KEX1_LACTC              Reviewed;         745 AA.
AC   C5DLM9;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 61.
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=KLTH0G01980g;
OS   Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS   (Yeast) (Kluyveromyces thermotolerans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=559295;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284;
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA   Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA   Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA   Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA   Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA   Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA   Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA   Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA   Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(2009).
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}.
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DR   EMBL; CU928171; CAR24690.1; -; Genomic_DNA.
DR   RefSeq; XP_002555127.1; XM_002555081.1.
DR   AlphaFoldDB; C5DLM9; -.
DR   SMR; C5DLM9; -.
DR   STRING; 559295.C5DLM9; -.
DR   ESTHER; lactc-kex1; Carboxypeptidase_S10.
DR   MEROPS; S10.007; -.
DR   GlyCosmos; C5DLM9; 3 sites, No reported glycans.
DR   GeneID; 8293386; -.
DR   KEGG; lth:KLTH0G01980g; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_11_2_1; -.
DR   InParanoid; C5DLM9; -.
DR   OMA; PLMFAGQ; -.
DR   OrthoDB; 1647009at2759; -.
DR   Proteomes; UP000002036; Chromosome G.
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   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.
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..47
FT                   /evidence="ECO:0000255"
FT   CHAIN           48..745
FT                   /note="Pheromone-processing carboxypeptidase KEX1"
FT                   /id="PRO_0000411922"
FT   TOPO_DOM        48..655
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        656..676
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        677..745
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          515..651
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          709..745
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        515..549
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        566..581
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        590..630
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        631..651
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        214
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        418
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        482
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        471
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        479
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        552
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   745 AA;  82855 MW;  ECAC755742FE5B2E CRC64;
     MSHFKYRNQT TDICNAAALD AFAMYSNYSV PLALLFALLL SFQTARALKA ADEYAVSPDL
     IPGLSQAEDR ALVPTMHAGH IPLDENNDEH TKNYFFWKFH DESGSASGPA RDTLIFWLNG
     GPGCSSMDGA LMESGALRID SDGKAYLNRG GWHTRGDIVF VDQPAGTGFS TVASDNDYDN
     DLKVVSEHFV AFLRNYFQVF PDDAGKQVVF AGESYAGQFI PYFARAVLDQ DEVQVNLQAL
     LIGNGWIDPN QQSLYYIPFA VEKGLITQDD PSFSYLLKQQ ENCQNKINSK ENDRFSFKEC
     ENILNNLLEV TRKIKDSEGK KVPSDQQCIN MYDLRLKDSY PSCGMNWPQD LPNLGKFFGT
     EGVLEALHLD PEHVSQWHEC DDKVSNYLKN PDSRASAAIL PGLLEAGLEV MLFNGDQDII
     CNNMGVEAVI SQMSWGGETG FSENVQLYDW VYRSPENSEI TPAGFVKYDR NLTFMSVYNA
     SHMVPFDNAL VSRGVVDLFL NDVDLVQIDG RDTLITDDVN KGKDGDASET DDTTELDCEG
     KDKLSEECKQ LNASKGQNGE SDKDEGEKGN EEDDNDDTED GKKDAGDEKD DGEKDDDEKD
     GDEKDGDEKD EEDDDDKDEN EKDEEDDDKD GDKPEGKNND GAEDEDDDHN SGSHLAVTMI
     CLLVSGTIIG GLYFTFRDRF RPRLRAILVD PTNRSEASKK TVSWAADLEQ DAADLSNPEN
     GAKKKGPYTS VPTQESRDSF ELDNL
//