KEX1_FUSV7
ID KEX1_FUSV7 Reviewed; 613 AA.
AC C7YRS6;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 1.
DT 03-AUG-2022, entry version 50.
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=NECHADRAFT_69476;
OS Fusarium vanettenii (strain ATCC MYA-4622 / CBS 123669 / FGSC 9596 / NRRL
OS 45880 / 77-13-4) (Fusarium solani subsp. pisi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium solani species complex; Fusarium vanettenii.
OX NCBI_TaxID=660122;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4622 / CBS 123669 / FGSC 9596 / NRRL 45880 / 77-13-4;
RX PubMed=19714214; DOI=10.1371/journal.pgen.1000618;
RA Coleman J.J., Rounsley S.D., Rodriguez-Carres M., Kuo A., Wasmann C.C.,
RA Grimwood J., Schmutz J., Taga M., White G.J., Zhou S., Schwartz D.C.,
RA Freitag M., Ma L.-J., Danchin E.G.J., Henrissat B., Coutinho P.M.,
RA Nelson D.R., Straney D., Napoli C.A., Barker B.M., Gribskov M., Rep M.,
RA Kroken S., Molnar I., Rensing C., Kennell J.C., Zamora J., Farman M.L.,
RA Selker E.U., Salamov A., Shapiro H., Pangilinan J., Lindquist E.,
RA Lamers C., Grigoriev I.V., Geiser D.M., Covert S.F., Temporini E.,
RA VanEtten H.D.;
RT "The genome of Nectria haematococca: contribution of supernumerary
RT chromosomes to gene expansion.";
RL PLoS Genet. 5:E1000618-E1000618(2009).
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; GG698899; EEU45125.1; -; Genomic_DNA.
DR RefSeq; XP_003050838.1; XM_003050792.1.
DR AlphaFoldDB; C7YRS6; -.
DR SMR; C7YRS6; -.
DR STRING; 140110.NechaP69476; -.
DR ESTHER; nech7-kex1; Carboxypeptidase_S10.
DR MEROPS; S10.007; -.
DR EnsemblFungi; NechaT69476; NechaP69476; NechaG69476.
DR GeneID; 9667997; -.
DR KEGG; nhe:NECHADRAFT_69476; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_11_0_1; -.
DR InParanoid; C7YRS6; -.
DR OMA; EMADQFV; -.
DR OrthoDB; 607679at2759; -.
DR Proteomes; UP000005206; 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; 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..27
FT /evidence="ECO:0000255"
FT CHAIN 28..613
FT /note="Pheromone-processing carboxypeptidase KEX1"
FT /id="PRO_0000411928"
FT TOPO_DOM 28..513
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 514..534
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 535..613
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 466..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 184
FT /evidence="ECO:0000250"
FT ACT_SITE 379
FT /evidence="ECO:0000250"
FT ACT_SITE 441
FT /evidence="ECO:0000250"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 438
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 490
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 613 AA; 68205 MW; C8B75F63C38D4CB5 CRC64;
MAFLSIPSPR RWAALLSLSL GPILGAADAT SNSAADYYVR DLPGLPKDGP NIKMHAGHIE
VTPESHGNLF FWHFENQHIA DKQRTVIWIN GGPGCSSEDG AMMEIGPYRL KDKENLYYNN
GSWGEFANLL FVDNPVGTGY SLVDTNAYVK ELDEMADQFI QFLEKWFALF PQYDRDDIYI
AGESYAGQHI PYIAKAILDR NKKNPSKAWN LQGLLIGNGW ISPVDQYPAY ISFAHEKGII
EKGSDNDKKL QSALRGCERV IASSPGRVDY GECEEILKNI LELTRDGNKC INMYDVRLTD
TYPSCGMNWP PDLEYLTPYL GRKDVVDALH VTSMKSTGWK ECSGAVGGAF TARNSKPAVE
LLPDLLKEVP VLLFSGAEDF ICNHLGTEEL ISKLEWNGGK GFEVTPGNWA PRRDWTFEGE
TAGFWQEARN LTYVLIYNSS HMVPFDLPRR SRDMLDRFMG VDISNIGGDP TDSRIDGEKG
PETTVGGASN KTQSAAQDHQ KQLDEAKWAA YQKSGEVVLV IVIIAAIAWG YFVWRERRKG
AAYHALANHD NNSHSNGFRA KSQPGDLESA AFDESELDDL HGSTPATATS ARFPVNRNDT
REKFVTKYAE PSS
