KEX1_PICPA
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 03-AUG-2022, entry version 76.
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}.
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DR EMBL; AF095574; AAC64191.1; -; Genomic_DNA.
DR AlphaFoldDB; O74702; -.
DR SMR; O74702; -.
DR ESTHER; picpa-KEX1; Carboxypeptidase_S10.
DR MEROPS; S10.007; -.
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; 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
