KEX1_VANPO
ID KEX1_VANPO Reviewed; 713 AA.
AC A7TLB3;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Pheromone-processing carboxypeptidase KEX1;
DE EC=3.4.16.6;
DE AltName: Full=Carboxypeptidase D;
DE Flags: Precursor;
GN Name=KEX1; ORFNames=Kpol_1041p46;
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC Y-8283 / UCD 57-17;
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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; DS480413; EDO16988.1; -; Genomic_DNA.
DR RefSeq; XP_001644846.1; XM_001644796.1.
DR AlphaFoldDB; A7TLB3; -.
DR SMR; A7TLB3; -.
DR STRING; 436907.A7TLB3; -.
DR MEROPS; S10.007; -.
DR PRIDE; A7TLB3; -.
DR EnsemblFungi; EDO16988; EDO16988; Kpol_1041p46.
DR GeneID; 5545175; -.
DR KEGG; vpo:Kpol_1041p46; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_11_2_1; -.
DR InParanoid; A7TLB3; -.
DR OMA; NGWIDPD; -.
DR OrthoDB; 607679at2759; -.
DR PhylomeDB; A7TLB3; -.
DR Proteomes; UP000000267; Unassembled WGS sequence.
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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..713
FT /note="Pheromone-processing carboxypeptidase KEX1"
FT /id="PRO_0000411951"
FT TOPO_DOM 23..616
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 617..637
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 638..713
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 500..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..524
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..550
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..603
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..667
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 404
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 468
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT CARBOHYD 457
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 713 AA; 80063 MW; 3C8951CB2FB6041C CRC64;
MMVSYKLLSL ITLLFVAQCT TGLLKQDDYV VRPDLLPGIS SIKDKALIPK MYAGHIPLNL
QKTTDENENT DESDSNSNTN YFFWKFQHQS VESPNLIFWL NGGPGCSSMD GALVETGPFR
VDKNGKLYPN EGSWHSRGDL VYIDQPIGTG LSTSAAIPNL LDDLKEVSDN FILFLENYFT
IFPNDLDKDI IIAGESYAGQ YIPFFAKAIK EYNQKISDNK KKINLRMLLI GNGWIDPITQ
SLSYLPFAIE KNLVGKDTPD FETLLKAHEK CQNKINSISE DDNSFSHEEC ESIINMLVSV
TKDNSPNVKS NEVCINIYDF NLRDSFPACG ANWPIDVSHV AKFFSTPGVI EALNLNAEEV
PRWKECNYDV LNHLTNPVSK PSVRLLPELL ESGIEIILFN GENDLVCNNK GITDMISKLT
WNGATGFSDK VQKYEWLFRD LTKDTEEPAG TVTFDRNLTF ISVYNASHMV AYDKSIVARG
ILDIYLDNVM LVEKETDSPD VLISTNEPTF SDIEEEELDG EKEDEKDGVT EGDGEKSDTD
EGKDTDKGKD EKNDDDDDDD DDSDDDSDDD DDDDDDDDDD DDDDDDSDDD DDDDDDSDDN
EKDDKSESET KTHPKAKIAL LLLLFISVFG ITGSQALRQR NFQFRRAPLT SNSFSSSSSP
NDPSNWDSND DFDFDIENDP LPSTNNKHKA AKKKKDYVSI PSDIDESFEL AEI
