ID   KEX1_PICPA              Reviewed;         623 AA.
AC   O74702;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   22-FEB-2023, entry version 78.
DE   RecName: Full=Pheromone-processing carboxypeptidase KEX1;
DE            EC=3.4.16.6;
DE   AltName: Full=Carboxypeptidase D;
DE   Flags: Precursor;
GN   Name=KEX1;
OS   Komagataella pastoris (Yeast) (Pichia pastoris).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Komagataella.
OX   NCBI_TaxID=4922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=SMD1168;
RX   PubMed=10341419;
RX   DOI=10.1002/(sici)1097-0061(199905)15:7<563::aid-yea398>3.0.co;2-r;
RA   Boehm T., Pirie-Shepherd S., Trinh L.B., Shiloach J., Folkman J.;
RT   "Disruption of the KEX1 gene in Pichia pastoris allows expression of full-
RT   length murine and human endostatin.";
RL   Yeast 15:563-572(1999).
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       ECO:0000269|PubMed:10341419}.
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; AF095574; AAC64191.1; -; Genomic_DNA.
DR   AlphaFoldDB; O74702; -.
DR   SMR; O74702; -.
DR   ESTHER; picpa-KEX1; Carboxypeptidase_S10.
DR   MEROPS; S10.007; -.
DR   GlyCosmos; O74702; 6 sites, No reported glycans.
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; 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; PS00131; CARBOXYPEPT_SER_SER; 1.
PE   3: Inferred from homology;
KW   Apoptosis; Carboxypeptidase; Glycoprotein; Golgi apparatus; Hydrolase;
KW   Membrane; Protease; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..623
FT                   /note="Pheromone-processing carboxypeptidase KEX1"
FT                   /id="PRO_0000411939"
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
//