ID   KEX1_ASPOR              Reviewed;         625 AA.
AC   Q2UPI1;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   22-FEB-2023, entry version 87.
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=AO090005001632;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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; AP007151; BAE56534.1; -; Genomic_DNA.
DR   RefSeq; XP_001818536.1; XM_001818484.2.
DR   AlphaFoldDB; Q2UPI1; -.
DR   SMR; Q2UPI1; -.
DR   STRING; 510516.Q2UPI1; -.
DR   ESTHER; aspor-q2upi1; Carboxypeptidase_S10.
DR   MEROPS; S10.007; -.
DR   GlyCosmos; Q2UPI1; 4 sites, No reported glycans.
DR   EnsemblFungi; BAE56534; BAE56534; AO090005001632.
DR   GeneID; 5990481; -.
DR   KEGG; aor:AO090005001632; -.
DR   VEuPathDB; FungiDB:AO090005001632; -.
DR   HOGENOM; CLU_008523_11_0_1; -.
DR   OMA; EMADQFV; -.
DR   OrthoDB; 1647009at2759; -.
DR   Proteomes; UP000006564; Chromosome 1.
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; IDA:AspGD.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0030448; P:hyphal growth; IMP:AspGD.
DR   GO; GO:0075307; P:positive regulation of conidium formation; IMP:AspGD.
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; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..41
FT                   /evidence="ECO:0000255"
FT   CHAIN           42..625
FT                   /note="Pheromone-processing carboxypeptidase kex1"
FT                   /id="PRO_0000411905"
FT   TOPO_DOM        42..523
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        524..544
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        545..625
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          480..511
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          574..625
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        591..617
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        193
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        390
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        452
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   CARBOHYD        122
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        441
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        449
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        501
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   625 AA;  70272 MW;  721A55B7A7097E83 CRC64;
     MFSSISRGFA KSETGDTFSF SFKSSWLLSL LVLWGPPLTT AKSAADYYVR SLPGAPDGPL
     LKMHAGHIEV DPQNNGNLFF WHYQNRHIAN RQRTVIWLNG GPGCSSMDGA LMEVGPYRLK
     DNLTLEYNEG SWDEFANLLF VDQPVGTGFS YVNTDSYLHE LDEMSAHFII FLDKFFELFP
     EYEGDDIYLA GESYAGQHIP YIAKAILDRN KNAVSPWNLR GLLIGNGWIS PADQYPSYLT
     FAYEEGLIKE DSRTAKSLEV LQSVCQSKLE TGGKDRIHIG DCETVLQELL SKTLDSDNKC
     YNMYDIRLRD TVPSCGMNWP QDLKDVKPYL RRADVVKALN INPEKKSGWE ECSGAVSSSF
     LPQKSVPAVQ LLPSLLESGI SVLLFSGDKD LICNHVGTEQ LINNMKWGGG VGFETSPGVW
     APRHDWTFEG EPAGIYQHAR NLTYVLLYNS SHMAPYDLPR QTRDMLDRFM KVDIASIGGS
     PADSRIDGEK LPQTSVGGHP NSTAAEEQEK ERMKQAEWKA YAKSGEAVLV VVIIGVSVWG
     FFIWRSRQRH RRYQGLYHED VSGASVLERF HNKRSGQDVE AGDFDESELD DLHSPDMARE
     HYTVGEDSDE DDVNRQHQRT TINPS
//