KEX1_USTMA
ID KEX1_USTMA Reviewed; 657 AA.
AC Q4P8U8; A0A0D1DXN4;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=UMAG_03465;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) 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; CM003148; KIS68371.1; -; Genomic_DNA.
DR RefSeq; XP_011389921.1; XM_011391619.1.
DR AlphaFoldDB; Q4P8U8; -.
DR SMR; Q4P8U8; -.
DR STRING; 5270.UM03465P0; -.
DR ESTHER; ustma-q4p8u8; Carboxypeptidase_S10.
DR MEROPS; S10.007; -.
DR PRIDE; Q4P8U8; -.
DR EnsemblFungi; KIS68371; KIS68371; UMAG_03465.
DR GeneID; 23563908; -.
DR KEGG; uma:UMAG_03465; -.
DR VEuPathDB; FungiDB:UMAG_03465; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_11_0_1; -.
DR InParanoid; Q4P8U8; -.
DR OMA; EMADQFV; -.
DR OrthoDB; 607679at2759; -.
DR Proteomes; UP000000561; Chromosome 9.
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 PANTHER; PTHR11802; PTHR11802; 1.
DR Pfam; PF00450; Peptidase_S10; 1.
DR PRINTS; PR00724; CRBOXYPTASEC.
DR SUPFAM; SSF53474; SSF53474; 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..?
FT /evidence="ECO:0000255"
FT CHAIN ?..657
FT /note="Pheromone-processing carboxypeptidase KEX1"
FT /id="PRO_0000411950"
FT TOPO_DOM ?..539
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 540..560
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 561..657
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 584..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..622
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 198
FT /evidence="ECO:0000250"
FT ACT_SITE 397
FT /evidence="ECO:0000250"
FT ACT_SITE 455
FT /evidence="ECO:0000250"
FT CARBOHYD 432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 657 AA; 71455 MW; 700D1FEB7CCC422C CRC64;
MPLLDPREVL LRRGIPIPAA ASFHVPGLPD LHAESSSSTA LAHPLQMSAG YLPARPIEAD
GQPKDNAHLF FLLLRARHVP AKRKLIIWFN GGPGCSSFDG AMMEVGAWRM DGKGGLVWVK
DGASWNEYAD ILFLDQPAGT GFSYVNTNAY TKSLPQAADE VVHFLEQFVQ VYPEYSRDVE
LEYGSQGSGV DVYLAGESFA GQYIPYTAKA IVKSPKPPVS LKGIAIGNGF IDPKSQYGTE
LETMVQKNIW TTSSGEYKHV AGLVKACHEE LDKSNQREIG KCELILQTII ASTTTKTQGA
SGYTCINVYD VRLSDSSPAC GMNWPTTLPA MYDYLRRPDV RKALHVDEHH KPEAWVECNA
NVGSAMRTDT TSPPSVQLLP ELLDSGVKVL LFAGEEDLIC NAIGVQRAAE NLEWGGAKGF
DDKQPAQDWY VNGTHAGTWR TARNLTYVGI KGASHMVGVD KPIESHDMIV RFMGIDYMKV
AGPNALIPSR VGNEPDRVLI TGGGGGIAQI GKDGSRVIPG SGKTEEEVAE EARWRAYYDA
GSFALMVLLI AVGIGTWLLL RARKQRRLNR NRIGRGGALR LATTTELGAS RSTTGNGDTD
ETSNNHELER LVGGKHVEDD DDDVEEHIFN VGDEDLSDSN GENGPPVVKA RHTGSQR
