KEX1_COPC7
ID KEX1_COPC7 Reviewed; 618 AA.
AC A8NYP0;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 61.
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=CC1G_01392;
OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=240176;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003;
RX PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA Burns C., Canbaeck B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA Kuees U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.-J.,
RA Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA Zolan M.E., Pukkila P.J.;
RT "Insights into evolution of multicellular fungi from the assembled
RT chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
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; AACS02000005; EAU84396.1; -; Genomic_DNA.
DR RefSeq; XP_001837480.1; XM_001837428.2.
DR AlphaFoldDB; A8NYP0; -.
DR SMR; A8NYP0; -.
DR STRING; 5346.XP_001837480.1; -.
DR ESTHER; copc7-kex1; Carboxypeptidase_S10.
DR MEROPS; S10.007; -.
DR EnsemblFungi; EAU84396; EAU84396; CC1G_01392.
DR GeneID; 6014036; -.
DR KEGG; cci:CC1G_01392; -.
DR VEuPathDB; FungiDB:CC1G_01392; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_11_1_1; -.
DR InParanoid; A8NYP0; -.
DR OMA; EMADQFV; -.
DR OrthoDB; 607679at2759; -.
DR Proteomes; UP000001861; 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 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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..618
FT /note="Pheromone-processing carboxypeptidase KEX1"
FT /id="PRO_0000411917"
FT TOPO_DOM 24..520
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 521..541
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 542..618
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 551..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..618
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT ACT_SITE 388
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT ACT_SITE 445
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 442
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 466
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 618 AA; 68888 MW; A6B18F31D04065E2 CRC64;
MLSAIWTGFV TLFLCSFVQG APADNVLPSA ASFYVPSIPG IIPNPDYRLQ IYAGHLPAES
NKTLLASNDV TAHLYFVMVK NRRVADKERV VFWFNGGPGC SSFDGLMMEV GPWRWDGQPE
GKESFIVKEG GWEEYTTMVF VDQPPGTGFS FTSTDQYAKT MKDAQWHILE FLRNFYQVFP
EVLTMDTYLA GESFAGQWIP YFADAILESS LQIPLRGIAI GNGWMDARRQ YLSYLDYSLK
MGLIKDNSED WKEVKAAHDR CEAHLEKLEG DPIHIRECGS IIMKVINQKR PDNEKGEKMC
LNMYDVRFTD TSPACGLNWP PEMHAITHFL GRKDVVRALH AERHPGSWVE CRRPVHRAFK
DGEEESSITV LPRVLSKIPV LIFAGDQDLI CNYVGLENMI KSLTWNGETG LGTVETQSWS
VNSTATGTWV ESRNLTYVKI FNASHMAPFD LPHVTHDMML RFMGVNFSSI VGGSAMIPSS
LGDAAKPVFV GGHLPQPSTP ALPAGKTPEQ DKAMWEAYYN AGSAALVLVL IMLVIGLFIW
YRRRKSRLQL PSNQSGELAE ESIPLRSEME DRGGNGVSNG GAWKGKARAS EPVFEVGDSD
EDEPSPYRKP DGGGDRNV
