KEX1_PHANO
ID KEX1_PHANO Reviewed; 642 AA.
AC Q0USX0;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=SNOG_05144;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(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; CH445331; EAT87535.1; -; Genomic_DNA.
DR RefSeq; XP_001795554.1; XM_001795502.1.
DR AlphaFoldDB; Q0USX0; -.
DR SMR; Q0USX0; -.
DR STRING; 13684.SNOT_05144; -.
DR MEROPS; S10.007; -.
DR EnsemblFungi; SNOT_05144; SNOT_05144; SNOG_05144.
DR GeneID; 5972429; -.
DR KEGG; pno:SNOG_05144; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_11_0_1; -.
DR InParanoid; Q0USX0; -.
DR OMA; EMADQFV; -.
DR OrthoDB; 625787at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IBA:GO_Central.
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..30
FT /evidence="ECO:0000255"
FT CHAIN 31..642
FT /note="Pheromone-processing carboxypeptidase KEX1"
FT /id="PRO_0000411935"
FT TOPO_DOM 31..519
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 520..540
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 541..642
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 476..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..642
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 184
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 386
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 448
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 437
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 445
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 497
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 642 AA; 72415 MW; C4D96E313AEB1716 CRC64;
MLLTHTSSRW RTAAVCALAA TASWLPSVQA AEKTQADYFV SSLPGAPEGP LLKMHAGHIE
VDAEHNSNLF FWHYENRHIA DRQRTVLWLN GGPGCSSMDG AMMEIGPYRV KHGGHLEYNN
GSWDEFANML FIDQPVGTGF SYVNTDSYLT DLDQMAEHMM IFLEKWFKLF PEYENDDLYI
AGESYAGQHI PYIARAILNR NKNQNTDPKP WNLKGLLIGN GWISPADQYL AYLPFAYQNG
MIQADSDSAK RVEQQQSICI QKLQDGGHDK VDTSECEQIM VAILEETKDR KADRMNQCLN
MYDIRLRDDS SCGMNWPPDL TDVTPYLRRP DVIKALHINS DKKTGWSECN GAVSGHFRAK
NSVPTVKFLP ELLTEVPILL FSGDKDFICN HVGTEAMIEN MSWNGGKGWE VSPGVWAPKQ
DWTFEGEPAG TYQEVRNLTY VVFYNSSHMV PFDYPKRTRD MLDRFMNVDI SAIGGDPADS
RIDGEKGPLT SVGDHPNSTK AEEDKAQQLK EAEWKAYYRS GEVVLVILII VACLWGAFLW
RTRRSTSLYK GVDGDEGRES LLTGMGLDNF RRGARRHDVE AADFDERELD DLDDAPKKPA
NGYSNVNSEK ERQPHNDSTF SLGADSDDEA EGSERGRRKE HS
