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Database: UniProt
Entry: C5MB07_CANTT
LinkDB: C5MB07_CANTT
Original site: C5MB07_CANTT 
ID   C5MB07_CANTT            Unreviewed;       928 AA.
AC   C5MB07;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 64.
DE   SubName: Full=Kexin {ECO:0000313|EMBL:EER32824.1};
GN   ORFNames=CTRG_03249 {ECO:0000313|EMBL:EER32824.1};
OS   Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=294747 {ECO:0000313|EMBL:EER32824.1, ECO:0000313|Proteomes:UP000002037};
RN   [1] {ECO:0000313|EMBL:EER32824.1, ECO:0000313|Proteomes:UP000002037}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-3404 / T1 {ECO:0000313|Proteomes:UP000002037};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
CC       {ECO:0000256|ARBA:ARBA00005325}.
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DR   EMBL; GG692398; EER32824.1; -; Genomic_DNA.
DR   RefSeq; XP_002548952.1; XM_002548906.1.
DR   AlphaFoldDB; C5MB07; -.
DR   STRING; 294747.C5MB07; -.
DR   MEROPS; S08.070; -.
DR   EnsemblFungi; CTRG_03249-t43_1; CTRG_03249-t43_1-p1; CTRG_03249.
DR   GeneID; 8295971; -.
DR   KEGG; ctp:CTRG_03249; -.
DR   VEuPathDB; FungiDB:CTRG_03249; -.
DR   eggNOG; KOG3525; Eukaryota.
DR   HOGENOM; CLU_002976_2_1_1; -.
DR   OrthoDB; 5474719at2759; -.
DR   Proteomes; UP000002037; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005802; C:trans-Golgi network; IEA:EnsemblFungi.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0007323; P:peptide pheromone maturation; IEA:EnsemblFungi.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04059; Peptidases_S8_Protein_convertases_Kexins_Furin-like; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR034182; Kexin/furin.
DR   InterPro; IPR002884; P_dom.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   PANTHER; PTHR42884:SF14; NEUROENDOCRINE CONVERTASE 1; 1.
DR   PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 1.
DR   Pfam; PF01483; P_proprotein; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51829; P_HOMO_B; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000002037};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..928
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005668335"
FT   TRANSMEM        779..799
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          503..643
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000259|PROSITE:PS51829"
FT   REGION          663..778
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          802..928
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        663..679
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        680..732
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        733..749
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        750..765
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        820..836
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        851..885
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        912..928
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        218
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        256
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        427
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   928 AA;  103853 MW;  757883D2DF6DBD1B CRC64;
     MLPIKLLILI LGYLLSPTIQ NEIIPTRDYE SKNYFLVELN TTNSQKPLID FINKYQNHYT
     FEHQLPSLDN YYVFSIDKNH PHNSFLGNHN SNGYNLMKRE VGYEEHYDDL ISSVQAIHML
     PPKKLSKRIP VPIYEEDLED FTSINQNDDL IARDENNEAT DKAHQKLAQI SSELDIHDPE
     FAAQWHLINL KYPGHDVNAT GLWLEDILGQ GIVTALVDDG VDAESEDIKD NFNADGSWDF
     NNNGKSPLPR LFDDYHGTRC AGEIAAVKND VCGIGVAWKS QVSGIRILSG PITSADEASA
     MIYGLDHNDI YSCSWGPTDN GRVLSEPEVI VKKAMIKGIQ EGRDKKGALY VFASGNGGRF
     GDSCNFDGYT NSIYSITVGA IDHKGLHPEY SEACSAVMVV TYSSGSNEHI HTTDIKKKCS
     ATHGGTSAAA PLASGIYSLV LSANPDLTWR DVQYISVLSA TPVNEDDGNY QVTALNRKYS
     HKYGYGKTDA YQMVHFAKNW KNVKPQAWYY SDVTEVNDSI KTQEDSSKVI KSSITVTEKD
     LKVMNVERVE HITVKVNIEA NYRGRVGMRI ISPTGVISDL AAFRRSDASG KGFQNWTFMS
     VAHWGESGLG EWKVEVFADD SHGDNVVINF KDWQFRIFGE SIDADKAELY DLEKDYAAVR
     RELLEKGDDK PEDKQTTSSS ETTKVETTEG QVGEETSIAN GETTTSQDNS TTSTDKSNET
     GTPATSSNVK PSETDSDSEE QNKEGDNKQQ EEEGEEEDET DDGEESDDKT KVKSSDHTGI
     YFMSIAVVGF VAVLLLMKFH KTPGSGRRRR RREEYEFDII PGEDYSDSDE EDDQDHDSFD
     LGNRNDQRLQ GQGQREYDRR DDEARDRLFD EFNAESLPDH ESDMFKIGDD EEEELNPSSG
     EQSSGKGPVD KSQTKVDQKH DSDIDSNK
//
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