KEX1_ASPOR
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 03-AUG-2022, entry version 85.
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 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 Proteomes; UP000006564; Chromosome 1.
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; 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; -; 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..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
