KEX1_OGAPD
ID KEX1_OGAPD Reviewed; 610 AA.
AC E7R7R2; A1IMC1; W1QIR9;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 46.
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=HPODL_04558;
OS Ogataea parapolymorpha (strain ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL
OS Y-7560 / DL-1) (Yeast) (Hansenula polymorpha).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Ogataea.
OX NCBI_TaxID=871575;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1;
RA Bae J.-H., Sohn J.-H., Kang H.-A., Choi E.-S., Rhee S.-K.;
RT "Cloning of the KEX1 gene encoding carboxypeptidase B-like protease from
RT Hansenula polymorpha.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1;
RX PubMed=24279325; DOI=10.1186/1471-2164-14-837;
RA Ravin N.V., Eldarov M.A., Kadnikov V.V., Beletsky A.V., Schneider J.,
RA Mardanova E.S., Smekalova E.M., Zvereva M.I., Dontsova O.A., Mardanov A.V.,
RA Skryabin K.G.;
RT "Genome sequence and analysis of methylotrophic yeast Hansenula polymorpha
RT DL1.";
RL BMC Genomics 14:837-837(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; AF090325; AAQ13482.1; -; Genomic_DNA.
DR EMBL; AEOI02000004; ESX01783.1; -; Genomic_DNA.
DR RefSeq; XP_013936369.1; XM_014080894.1.
DR AlphaFoldDB; E7R7R2; -.
DR SMR; E7R7R2; -.
DR STRING; 1005962.E7R7R2; -.
DR MEROPS; S10.007; -.
DR EnsemblFungi; ESX01783; ESX01783; HPODL_04558.
DR GeneID; 25773986; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_11_2_1; -.
DR OMA; NGWIDPD; -.
DR OrthoDB; 607679at2759; -.
DR Proteomes; UP000008673; Chromosome II.
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..18
FT /evidence="ECO:0000255"
FT CHAIN 19..610
FT /note="Pheromone-processing carboxypeptidase KEX1"
FT /id="PRO_0000411937"
FT TOPO_DOM 19..494
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 495..515
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 516..610
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 469..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 176
FT /evidence="ECO:0000250"
FT ACT_SITE 371
FT /evidence="ECO:0000250"
FT ACT_SITE 429
FT /evidence="ECO:0000250"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 418
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 426
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 610 AA; 69724 MW; B31CC03D8132DA5F CRC64;
MSRYFLLACT LALQCVAASQ EDYIVKDLPG LSNIPAVVRP VMHAGHLEID EEHNTELFFW
RFQNPKNNGT HQTLHRNELI VWLNGGPGCS SMDGAMMETG PLRVSDKLEV ELNPGSWTQV
ADILFVDQPA GTGFSYTDSY DTELKQAAQH FWQFLKTYYQ LFPEDRTKKL YLAGESYAGQ
YIPYFAKEII ENNSLNISLE GLLIGNGWID PDIQSLSYVP FSLEAGFLDR QSPSMAQVLK
QHEKCQQAID DPSNHDFEKV ECVKIFHSIL AASRDETKPA KEQCVNMYDY RKHDYFPACG
SNWPEGLPTV TKFLNLDAVQ KALNLKSAKR WHECDGKVEF FFQPEHSVKS FDLLPKLLEK
MKIALFAGDK DIICNHKSIE MVIEKLQITP GQFGFTNSRK SGWIYDGQEV GEVETQSNLT
YIKVFNSSHM VPYDLPEVSR GLFDIITNSI EKRSTDIVTP VYDSRGNYKF VEEKQDTDQN
EEEEKEKPPK HHHSLTFYVA EVAILAVLAY LLYSFYKSFA KSRKSAFLSL SSKKKKKQVH
WFDESDIGMD QEAGEADHKP KSMLESVFNK LGYGGQYDTV QDGRDIEMAP VEEHEDQFII
QSDEEEFGHR
