KEX1_CANAL
ID KEX1_CANAL Reviewed; 702 AA.
AC Q5AFP8; A0A1D8PQP4; Q3MPN8;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 100.
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=CAALFM_C700940WA;
GN ORFNames=CaJ7.0112, CaO19.7020;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15937140; DOI=10.1534/genetics.104.034652;
RA Chibana H., Oka N., Nakayama H., Aoyama T., Magee B.B., Magee P.T.,
RA Mikami Y.;
RT "Sequence finishing and gene mapping for Candida albicans chromosome 7 and
RT syntenic analysis against the Saccharomyces cerevisiae genome.";
RL Genetics 170:1525-1537(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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; AP006852; BAE44622.1; -; Genomic_DNA.
DR EMBL; CP017629; AOW30469.1; -; Genomic_DNA.
DR RefSeq; XP_720314.1; XM_715221.1.
DR AlphaFoldDB; Q5AFP8; -.
DR SMR; Q5AFP8; -.
DR STRING; 237561.Q5AFP8; -.
DR ESTHER; canal-q5afp8; Carboxypeptidase_S10.
DR MEROPS; S10.007; -.
DR PRIDE; Q5AFP8; -.
DR GeneID; 3637955; -.
DR KEGG; cal:CAALFM_C700940WA; -.
DR CGD; CAL0000182553; KEX1.
DR VEuPathDB; FungiDB:C7_00940W_A; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_11_2_1; -.
DR InParanoid; Q5AFP8; -.
DR OMA; EMADQFV; -.
DR OrthoDB; 607679at2759; -.
DR Proteomes; UP000000559; Chromosome 7.
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:0001897; P:cytolysis by symbiont of host cells; IMP:CGD.
DR GO; GO:0016485; P:protein processing; IMP:CGD.
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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..702
FT /note="Pheromone-processing carboxypeptidase KEX1"
FT /id="PRO_0000411907"
FT TOPO_DOM 20..555
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 556..576
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 577..702
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 491..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..702
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 184
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT ACT_SITE 394
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT ACT_SITE 452
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 702 AA; 78712 MW; C17ACDB9E7F89718 CRC64;
MKLILSTLIV FIHTLLVSAL PTKEGSDPNS AKKYLVSDLP GLHENITPDN SIPLMFAGQL
EIYPETDTHY FFWKFSDSNP ETVTNRTIFW LNGGPGCSSM DGALLETGPF RINSQQQVIS
NNGSWHKMGD IIYVDQPAGT GFSYSDTYIT DLDQVAEYFL KFMEKYYELF PEEIGYEIYF
AGESYAGQYI PYIADAILQR NKKLVDGEHK YDLRGVLIGN GWVSPNEQSL SYLPFFKDHG
LIDVHHPKWA TLLAKHEQCQ KIVNKIDSTF DDGVVHYYEV SSSTCEAILT DLLEYTQDTA
SEKDQRCVNM YDYTLRDSYP SCGMNWPYEL VNVGPFLRQE KVMHQLNLIN LKKWNECNGR
VGRTFQARHS IPAVHLLPEL AKEIPVMLFN GANDIICNSQ GVLSYLQKLQ WNGETGFTNK
DNQISWIYDN KEVGYIIWER NISFINIYNS SHMVPYDLPD VSRALIDLIT GKYDEKDVDG
KKSFVTYPLG SRKESDASAD GEENAGSDKV PGDSPSQTID PMISSSTASS SSVESSLSSS
TASADSDSTS SKFTRLIQLA VILVIFWGVY VLYASYKSRP SSIIKKPTNN TSNVTRSSAG
KKKNVQWADQ LNQFEDDERT QEPNQGIIAK AIGKITGSKD TRGRYAPVQR GNGNEYIDDI
ELGEGLSDPN VDEFIIGSDD DEEQGQAHSG AATHNQKQKP MN
