KEX1_DEBHA
ID KEX1_DEBHA Reviewed; 684 AA.
AC B5RUL7;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 55.
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=DEHA2F22352g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382138; CAR66395.1; -; Genomic_DNA.
DR RefSeq; XP_002770877.1; XM_002770831.1.
DR AlphaFoldDB; B5RUL7; -.
DR SMR; B5RUL7; -.
DR STRING; 4959.XP_002770877.1; -.
DR MEROPS; S10.007; -.
DR EnsemblFungi; CAR66395; CAR66395; DEHA2F22352g.
DR GeneID; 8999041; -.
DR KEGG; dha:DEHA2F22352g; -.
DR VEuPathDB; FungiDB:DEHA2F22352g; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_11_2_1; -.
DR InParanoid; B5RUL7; -.
DR OMA; NGWIDPD; -.
DR OrthoDB; 607679at2759; -.
DR Proteomes; UP000000599; Chromosome F.
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; IPR033124; Ser_caboxypep_his_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.
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..684
FT /note="Pheromone-processing carboxypeptidase KEX1"
FT /id="PRO_0000411919"
FT TOPO_DOM 19..556
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 557..577
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 578..684
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 494..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 647..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..549
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..661
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT ACT_SITE 388
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT ACT_SITE 446
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 424
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 435
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 474
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 684 AA; 77336 MW; 8254AE19456BE382 CRC64;
MVIKYLLLIL VQSFVAFALP FTSRSDPKAE YLVTSLPGLY SNIRTDERPL MFAGQLELYP
ENQTHYFFWK YQDTNQIPEA KKRTIFWLNG GPGCSSMDGA LMEAGPFRIN KEGEVIYNEG
SWHKSGDMVF VDQPAGTGFS YSDDYDHDLD QITVEFVRFM EKFFELFPED ASNEIYFAGE
SYAGQYIPYI ADGILRRNKN LREGEKPFNL KGLMIGNGWI APNEQSLSYL PYSVQAGIIK
TNNPRWSSIL RQHQECQDIV SENDGPDGSD VSQVVSNTCE RVLNLILEAT RDQSAADNEQ
CVNMYDHTLR DSYPSCGMNW PPDLANVTPF LREQSVMNDL NLINHKKWSE CSGKVGNSFR
AKNSKPAIHL FPSILEEIPI MLFNGNRDII CNYIGIEGFI KKLTWNGQTG FSEDLDTLDW
VYDNKTAGYI QSERNLTVVN VFDASHMVPF DKPEISRSLI DIITGNFDEK EVDNKSDMKK
KSIVTYPLGV RMAKQKEESE SKTSPTSVTQ SKTSSISAVS GKSLATSTTL DQEHSATPSA
EAERAKNQQT SNRITRLIQL LVIVVLIWGV YILYSSYRSR PSSIIKTGPS GKKKNVQWAD
QLRQFEEEEI EQNEQGILSR ALNKLKGGDS RGTYAPTSGK TYEDIEMNEG ITEHTDNRVD
DFIIESDEED AHDENQTNKQ SVSK
