ID   KEX1_KOMPG              Reviewed;         623 AA.
AC   C4QZV7;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 60.
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=PAS_chr2-1_0174;
OS   Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Komagataella.
OX   NCBI_TaxID=644223;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GS115 / ATCC 20864;
RX   PubMed=19465926; DOI=10.1038/nbt.1544;
RA   De Schutter K., Lin Y.-C., Tiels P., Van Hecke A., Glinka S.,
RA   Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.;
RT   "Genome sequence of the recombinant protein production host Pichia
RT   pastoris.";
RL   Nat. Biotechnol. 27:561-566(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}.
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; FN392320; CAY68781.1; -; Genomic_DNA.
DR   RefSeq; XP_002491061.1; XM_002491016.1.
DR   AlphaFoldDB; C4QZV7; -.
DR   SMR; C4QZV7; -.
DR   STRING; 644223.C4QZV7; -.
DR   ESTHER; picpa-KEX1; Carboxypeptidase_S10.
DR   MEROPS; S10.007; -.
DR   EnsemblFungi; CAY68781; CAY68781; PAS_chr2-1_0174.
DR   GeneID; 8198557; -.
DR   KEGG; ppa:PAS_chr2-1_0174; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_11_2_1; -.
DR   InParanoid; C4QZV7; -.
DR   OMA; NGWIDPD; -.
DR   Proteomes; UP000000314; Chromosome 2.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of 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; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001563; Peptidase_S10.
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; 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..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..623
FT                   /note="Pheromone-processing carboxypeptidase KEX1"
FT                   /id="PRO_0000411940"
FT   TOPO_DOM        17..512
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        513..533
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        534..623
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          597..623
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        605..623
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        177
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        383
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        441
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   CARBOHYD        54
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        258
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        430
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        438
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        469
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        483
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   623 AA;  70018 MW;  CC7B0683829D8FDB CRC64;
     MLKLLCLLLP LVAVSASPID LGSQKDYLVL DLPGLSHLSE TQRPTMHAGL LPLNLSFVAD
     DDTEYFFWRF SKQDVDRADI VFWLNGGPGC SSMDGALMEL GPFVINPKQE VEYNEGTWVE
     AADVVFVDQP GGTGFSSTTN YLTELTEVAD GFVTFLARYF HLFPADVYKK FTLGGESYAG
     QYVPYILKAI MDDLKSDSGQ LPKELYLKGA LIGNGWIDPN EQSLSYLEFF IKKELIDIHG
     SYMPGLLQQQ EKCQNLINHS SGEASESQIS YSACEKILND ALRFTRDKKA PLDQQCINMY
     DYTLRDTYPS CGMSWPPYLP DVTAFLQKKS VLEALHLDSS ASWSECSARV GSHLKNKISV
     PSVDILPDLL QEIPIILFNG DHDIICNCIG TERMIDKLEF NGDQGFTEGT EYIPWFYNEV
     NVGKVISERN LTYVRVYNSS HMVPFDNTPV SRGLLDIYFD NFEDVEYNNV SGIATPVYDV
     DKNITYIDSN DPRLQNGPKS SSTDDSAAHG NPFFYYVFEL FVIVLLLCGL VYLYQYYSNS
     APHSILADKH KKKSKNKSKN VRFLDDLESN LDLDNTDDKK DNSVMSKLLS SMGYQAQEPY
     KPLDKGANAD LDIEMDSHGT SEK