KEX1_LACTC
ID KEX1_LACTC Reviewed; 745 AA.
AC C5DLM9;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 56.
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=KLTH0G01980g;
OS Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS (Yeast) (Kluyveromyces thermotolerans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=559295;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284;
RX PubMed=19525356; DOI=10.1101/gr.091546.109;
RG The Genolevures Consortium;
RA Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT "Comparative genomics of protoploid Saccharomycetaceae.";
RL Genome Res. 19:1696-1709(2009).
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; CU928171; CAR24690.1; -; Genomic_DNA.
DR RefSeq; XP_002555127.1; XM_002555081.1.
DR AlphaFoldDB; C5DLM9; -.
DR SMR; C5DLM9; -.
DR STRING; 559295.C5DLM9; -.
DR MEROPS; S10.007; -.
DR EnsemblFungi; CAR24690; CAR24690; KLTH0G01980g.
DR GeneID; 8293386; -.
DR KEGG; lth:KLTH0G01980g; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_11_2_1; -.
DR InParanoid; C5DLM9; -.
DR OMA; NGWIDPD; -.
DR OrthoDB; 607679at2759; -.
DR Proteomes; UP000002036; Chromosome G.
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 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..47
FT /evidence="ECO:0000255"
FT CHAIN 48..745
FT /note="Pheromone-processing carboxypeptidase KEX1"
FT /id="PRO_0000411922"
FT TOPO_DOM 48..655
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 656..676
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 677..745
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 515..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..549
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..581
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..630
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..651
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 214
FT /evidence="ECO:0000250"
FT ACT_SITE 418
FT /evidence="ECO:0000250"
FT ACT_SITE 482
FT /evidence="ECO:0000250"
FT CARBOHYD 471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 479
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 552
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 745 AA; 82855 MW; ECAC755742FE5B2E CRC64;
MSHFKYRNQT TDICNAAALD AFAMYSNYSV PLALLFALLL SFQTARALKA ADEYAVSPDL
IPGLSQAEDR ALVPTMHAGH IPLDENNDEH TKNYFFWKFH DESGSASGPA RDTLIFWLNG
GPGCSSMDGA LMESGALRID SDGKAYLNRG GWHTRGDIVF VDQPAGTGFS TVASDNDYDN
DLKVVSEHFV AFLRNYFQVF PDDAGKQVVF AGESYAGQFI PYFARAVLDQ DEVQVNLQAL
LIGNGWIDPN QQSLYYIPFA VEKGLITQDD PSFSYLLKQQ ENCQNKINSK ENDRFSFKEC
ENILNNLLEV TRKIKDSEGK KVPSDQQCIN MYDLRLKDSY PSCGMNWPQD LPNLGKFFGT
EGVLEALHLD PEHVSQWHEC DDKVSNYLKN PDSRASAAIL PGLLEAGLEV MLFNGDQDII
CNNMGVEAVI SQMSWGGETG FSENVQLYDW VYRSPENSEI TPAGFVKYDR NLTFMSVYNA
SHMVPFDNAL VSRGVVDLFL NDVDLVQIDG RDTLITDDVN KGKDGDASET DDTTELDCEG
KDKLSEECKQ LNASKGQNGE SDKDEGEKGN EEDDNDDTED GKKDAGDEKD DGEKDDDEKD
GDEKDGDEKD EEDDDDKDEN EKDEEDDDKD GDKPEGKNND GAEDEDDDHN SGSHLAVTMI
CLLVSGTIIG GLYFTFRDRF RPRLRAILVD PTNRSEASKK TVSWAADLEQ DAADLSNPEN
GAKKKGPYTS VPTQESRDSF ELDNL
