KEX1_ARTBC
ID KEX1_ARTBC Reviewed; 596 AA.
AC D4B5L8;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 45.
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=ARB_03758;
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371;
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
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; ABSU01000043; EFE29379.1; -; Genomic_DNA.
DR RefSeq; XP_003010019.1; XM_003009973.1.
DR AlphaFoldDB; D4B5L8; -.
DR SMR; D4B5L8; -.
DR STRING; 663331.D4B5L8; -.
DR MEROPS; S10.007; -.
DR EnsemblFungi; EFE29379; EFE29379; ARB_03758.
DR GeneID; 9525614; -.
DR KEGG; abe:ARB_03758; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_11_0_1; -.
DR OMA; PWYTQGE; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
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..17
FT /evidence="ECO:0000255"
FT CHAIN 18..596
FT /note="Pheromone-processing carboxypeptidase KEX1"
FT /id="PRO_0000411899"
FT TOPO_DOM 18..486
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 487..507
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 508..596
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 447..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..554
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..596
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 154
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 404
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 412
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 596 AA; 66677 MW; 3BD06AC1853CA859 CRC64;
MLGLATTVTL ESSGCSSKMC FRLLCSVSSR PARGTFVEDA CWVYIISHTF FPFNMTWRVV
NIFISLSMDG ALMEIGPYRL QDDHTLIYNN GSWDEFANLL FVDQPVGTGF SYVSTDSYVR
ELGPMADQFV TFLERWFNVF PEYERDDIYI AGESYAGQYI PYIADAIVRR NEKLSANGTS
WNVQGLLIGN GWISPLEQYR SYLPFSYKEG VLDKNSDGAK AAESQLSKCM SKLKEVGKFG
VHVDECERVL ELILDTTKVD GKCINMYDVR LEDTPDACGM NWPPDISLVT SYLRRPDVVK
ALNINEDKTT GWRECSPGVG RNLQATESVP SVQLLPGLLE RGMPIVLFSG DKDLICNHIG
TEDLIHNMTW LNATGFELSP DVWAPRHNWE FEGSAAGIYQ QARNLTYVKF YNASHMVPFD
FPRRSRDMLD RFLGIDITSI GGDPADSRID GLKGAPTSVG AHPNSTTAEE KEKEKIKIAA
WEAYYKSGEV ALVVVAIAAS LWGFFIWRSK RREKGLEYKG IYPNLESFSS ASLATFRGKR
RGRMDVESAP RPDEAELETL YNAAEGSDPQ DGEENFSDGK GDNEKAQSHA GMGKSR
