KEX1_YARLI
ID KEX1_YARLI Reviewed; 614 AA.
AC Q6CFP3;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=YALI0B05170g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382128; CAG82750.1; -; Genomic_DNA.
DR RefSeq; XP_500519.1; XM_500519.1.
DR AlphaFoldDB; Q6CFP3; -.
DR SMR; Q6CFP3; -.
DR STRING; 4952.CAG82750; -.
DR ESTHER; yarli-q6cfp3; Carboxypeptidase_S10.
DR MEROPS; S10.007; -.
DR EnsemblFungi; CAG82750; CAG82750; YALI0_B05170g.
DR GeneID; 2906626; -.
DR KEGG; yli:YALI0B05170g; -.
DR VEuPathDB; FungiDB:YALI0_B05170g; -.
DR HOGENOM; CLU_008523_11_0_1; -.
DR InParanoid; Q6CFP3; -.
DR OMA; EMADQFV; -.
DR Proteomes; UP000001300; Chromosome B.
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 InterPro; IPR033124; Ser_caboxypep_his_AS.
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; PS00560; CARBOXYPEPT_SER_HIS; 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..17
FT /evidence="ECO:0000255"
FT CHAIN 18..614
FT /note="Pheromone-processing carboxypeptidase KEX1"
FT /id="PRO_0000411953"
FT TOPO_DOM 18..518
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 519..539
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 540..614
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 465..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..490
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 177
FT /evidence="ECO:0000250"
FT ACT_SITE 379
FT /evidence="ECO:0000250"
FT ACT_SITE 437
FT /evidence="ECO:0000250"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 426
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 614 AA; 69331 MW; 1E9B44FB4EA02442 CRC64;
MKLSWSLFCG LASLALSQFD EAPPSQSDYF VRHIPGLDSV DNYTMHSGNI LTDAAHNGNL
FFWLVEAQYK ITERPKTIVW FNGGPGCSSM DGALLEVGPF RIVDDKLRVD PNKGSWHKYA
NVLFVDQPYG TGYSYSDTDS YLTGLGQVGD EMDSFMTQFL KLFPERAHDD FYLAGESYAG
QYIPYIATKL QQTRTVDLKG LLIGNGWMDP ANQYYQYVPY ALDYGVIEKT EEHVKDLKEL
TDTCERAINI AKDKNNGRLP VHIRACEDIM NGIVELSRNE RSAPESEGIC VNYYDVSKED
KWPSCGMNWP EILPYVTDWL RQDATVQALN VNNDKQESWQ ECNGAVGSRM RQGNDDAAVY
LLPDLLESME ILFFNGDRDL ICNHYGNERM IEQLEWNGKK GWTEGLELDD WVVDGVSKGK
KQSDRNLTYV RIYNASHMVP YDEPEACLTM LNDFIGVSKA LSDLSGNKPG RGSENPSDLD
DQKSGDQKSD DDSSSDDDDD AEHDKKIASD AMWKAYYQAG FTALIVVLII LGLAGFLFWR
KNRGHIYQEE TSLLGSCFGG ISRWRNSSGG PLSNQQGTFD SRQRLMEPGE YYDLGEIAEE
DEDAEELVIR RPEV
