KEX1_PODAN
ID KEX1_PODAN Reviewed; 585 AA.
AC B2B762; A0A090D5M0;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, 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; OrderedLocusNames=Pa_2_10030; ORFNames=PODANS_2_10030;
OS Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS (Pleurage anserina).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC Podospora anserina.
OX NCBI_TaxID=515849;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL Genome Biol. 9:R77.1-R77.22(2008).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Genetics 197:421-432(2014).
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; CU640366; CAP73640.1; -; Genomic_DNA.
DR EMBL; FO904937; CDP26043.1; -; Genomic_DNA.
DR RefSeq; XP_001911812.1; XM_001911777.1.
DR AlphaFoldDB; B2B762; -.
DR SMR; B2B762; -.
DR STRING; 5145.XP_001911812.1; -.
DR MEROPS; S10.007; -.
DR EnsemblFungi; CAP73640; CAP73640; PODANS_2_10030.
DR GeneID; 6195504; -.
DR KEGG; pan:PODANSg8857; -.
DR VEuPathDB; FungiDB:PODANS_2_10030; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_11_0_1; -.
DR OrthoDB; 607679at2759; -.
DR Proteomes; UP000001197; Chromosome 2.
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..18
FT /evidence="ECO:0000255"
FT CHAIN 19..585
FT /note="Pheromone-processing carboxypeptidase KEX1"
FT /id="PRO_0000411941"
FT TOPO_DOM 19..469
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 470..490
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 491..585
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 526..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..585
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 135
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 335
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 397
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT CARBOHYD 386
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 447
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 585 AA; 65374 MW; 84EDD573F229D2BB CRC64;
MCLLARVRHI EITPDVNGNM FFWHFQNKHI ANKQRTVIWL NGGPGCSSED GALMEIGPYR
LKDKDTLVYN EGAWNEFANV LFVDNPVGTG FSYVDTNAYV RELDVMADQF VTFLEKWFKL
FPEYEHDDIF IAGESYAGQY IPYIAKAILE RNKKGGESSY KWNLAGLLIG NGWISPPEQY
EAYLQFAYEK GIVKKGSDAA SKLEVQQRIC SKQLAVGPAL VDNTDCEKIL QDLLQLTATS
KGGEQRCVNM YDVRLTDTYP SCGMNWPPDL DAVTPYLRRN DVIQALHVNP NKVTGWVECN
GQVGANFKPS SKPSVELLPD LLKEVPIILF SGSEDLICNH LGTEALISNL QWNGGKGFEI
TPGTWAPRRD WTFEGEAAGF WQEARNLTYV VFYNSSHMVP FDYPRRTRDM LDRFMGVDIS
SIGGKPTDSR LDGEKVPETT VGGVAGNGTD AQQAEKEKLD TARWEAYRKS GEIVLVIVAF
SAAGWGWWVW RERKKRRGYM GVSGGENISP SGEARGREGF RDKRSAADLE AGDFDENELD
DLHMRTPTTV MGGEGNDPRY SVGAASEDSE DEEDVKGKGK EKMSG
