ID A0A0C3PUB9_PISTI Unreviewed; 585 AA.
AC A0A0C3PUB9;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Pheromone-processing carboxypeptidase KEX1 {ECO:0000256|ARBA:ARBA00040628};
DE EC=3.4.16.6 {ECO:0000256|ARBA:ARBA00038895};
DE AltName: Full=Carboxypeptidase D {ECO:0000256|ARBA:ARBA00042717};
DE AltName: Full=Pheromone-processing carboxypeptidase kex1 {ECO:0000256|ARBA:ARBA00040403};
GN ORFNames=M404DRAFT_12665 {ECO:0000313|EMBL:KIO12379.1};
OS Pisolithus tinctorius Marx 270.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Sclerodermatineae; Pisolithaceae; Pisolithus.
OX NCBI_TaxID=870435 {ECO:0000313|EMBL:KIO12379.1, ECO:0000313|Proteomes:UP000054217};
RN [1] {ECO:0000313|EMBL:KIO12379.1, ECO:0000313|Proteomes:UP000054217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Marx 270 {ECO:0000313|EMBL:KIO12379.1,
RC ECO:0000313|Proteomes:UP000054217};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Costa M.D., Nagy L.G., Floudas D., Copeland A.,
RA Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Marx 270 {ECO:0000313|Proteomes:UP000054217};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential release of a C-terminal arginine or lysine
CC residue.; EC=3.4.16.6; Evidence={ECO:0000256|ARBA:ARBA00001003};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000256|ARBA:ARBA00004393}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004393}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the peptidase S10 family.
CC {ECO:0000256|ARBA:ARBA00009431}.
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DR EMBL; KN831947; KIO12379.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C3PUB9; -.
DR STRING; 870435.A0A0C3PUB9; -.
DR MEROPS; S10.007; -.
DR HOGENOM; CLU_008523_11_1_1; -.
DR InParanoid; A0A0C3PUB9; -.
DR OrthoDB; 1647009at2759; -.
DR Proteomes; UP000054217; Unassembled WGS sequence.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
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; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001563; Peptidase_S10.
DR InterPro; IPR033124; Ser_caboxypep_his_AS.
DR PANTHER; PTHR11802:SF190; PHEROMONE-PROCESSING CARBOXYPEPTIDASE KEX1; 1.
DR PANTHER; PTHR11802; SERINE PROTEASE FAMILY S10 SERINE CARBOXYPEPTIDASE; 1.
DR Pfam; PF00450; Peptidase_S10; 1.
DR PRINTS; PR00724; CRBOXYPTASEC.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1.
PE 3: Inferred from homology;
KW Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000054217};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 488..514
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 553..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..585
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 585 AA; 65634 MW; B14E145D2878B31C CRC64;
MSFPTPVPPA ASFYVPQLPG LQQDSEHPLH VYAGHIVSDP NVATASPNDV LAHLFFVMVK
ARRSADKERL MFWFNGGPGC SSFDGLMMEI GPWRMDDRGL PKTVDGGWEE YMTIVYVDQP
AGTGLSYTST EHYVHTLEEA TEQLIQFLRT FYQVFPEYRT TDTYLGGESF AGQYIPYFAS
GILDSNLNLP LKGVAIGNGW IDARNQYPAY IEYAVARGLV DLSSEHYRNS KKRTDECMVE
FNRITNLEPI NVDQCEGLLS YVLQPGRHAV NGVEKCTNVY DVRLEDDEPY CGMQWPPELA
NTTAYLGRQD VVRAFHATSK PESWVECGSQ AGRQFNAKLS TSAITLLPGL LERIPVLLFA
GDQDFICNYM GIESMIKSMT WNGEKGLGKV QTKLWTVDEQ PAGTWVSSRN LTYAKIFNAS
HMAPYDVPDV AHDMILRFVD MNFSAIVDGS ARIPSSVGDE SKPLFLEDTF PSSIPVKSPE
EIKAQWEAYY NAGSAVLILL LIAVAIGVCI WCRLRRRPIQ LLRQTSNRAS EENIPLTRTL
DPDSEEVLHR NFKGKERATE DEEVGTAIFD VGDDEDYHTD NSHHR
//
