ID   KEX1_ASPTN              Reviewed;         625 AA.
AC   Q0CCR9;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   22-FEB-2023, entry version 70.
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=ATEG_08515;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476606; EAU30647.1; -; Genomic_DNA.
DR   RefSeq; XP_001217101.1; XM_001217100.1.
DR   AlphaFoldDB; Q0CCR9; -.
DR   SMR; Q0CCR9; -.
DR   STRING; 341663.Q0CCR9; -.
DR   ESTHER; asptn-kex1; Carboxypeptidase_S10.
DR   MEROPS; S10.007; -.
DR   GlyCosmos; Q0CCR9; 4 sites, No reported glycans.
DR   EnsemblFungi; EAU30647; EAU30647; ATEG_08515.
DR   GeneID; 4323538; -.
DR   VEuPathDB; FungiDB:ATEG_08515; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_11_0_1; -.
DR   OMA; EMADQFV; -.
DR   OrthoDB; 1647009at2759; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
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   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.
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..38
FT                   /evidence="ECO:0000255"
FT   CHAIN           39..625
FT                   /note="Pheromone-processing carboxypeptidase kex1"
FT                   /id="PRO_0000411906"
FT   TOPO_DOM        39..522
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        523..543
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        544..625
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          479..510
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          588..625
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        588..616
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        190
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        389
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        451
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        119
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        440
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        448
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        500
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   625 AA;  70454 MW;  3FC518DD043A26D0 CRC64;
     MVSLSLRGAR RTAKDAASLP FLSWTLSLLA LNPLLVSAKS AADYYVRSLP GAPEGPLLKM
     HAGHIEVDPE NHGNLFFWHF QNRHIANRQR TVIWLNGGPG CSSMDGALME VGPYRLKDNS
     TLEYNEGSWD EFGNLLFVDQ PVGTGFSYVN GNQYLHEMDE MAAHFITFLE NWFDIFPEYE
     RDDIYIAGES FAGQHIPYIA KAIQERNEKA QMKPKWSLRG LLIGNGWISP KDQYPSYLTF
     AYEEGLITKD SRTAKNLEVL QSVCESRLEA GKNKIHLDDC EKVLSEMLTK TMDVSKNECI
     NSYDIRLRDE APACGMNWPP ELTHMNYYLR QPELISALNI NPEKKSGWME CSNAVSSTFR
     TQKSVPSVQL LPGLIESGIP ILLFSGDKDL ICNHVGTEEL INNMKWNGGT GFETSPGVWA
     PRHDWTFEGE PAGIYQYARN LTYVLFYNAS HMVPYDLPRQ SRDMLDRFMQ VDIASIGGSP
     ADSRIDGEKL PQTSVGGHPN STAAEEQEKK KMKEAEWKAY AKSGEAVLVV VIIGVIVWGF
     FIWRSRRHHR GYRSVYNKNM SGSSVLERFH SKRSGADMEA GDFDEAELDD LHSPGLDREH
     YAVGDDSDDE QQHQRQGSRP EGGQS
//