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Pheromone-processing carboxypeptidase KEX1 (EC 3.4.16.6) (Carboxypeptidase D) (Killer expression defective protein 1)

 KEX1_YEAST              Reviewed;         729 AA.
P09620; D6VTV1;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
23-MAY-2018, entry version 171.
RecName: Full=Pheromone-processing carboxypeptidase KEX1;
EC=3.4.16.6;
AltName: Full=Carboxypeptidase D;
AltName: Full=Killer expression defective protein 1;
Flags: Precursor;
Name=KEX1; OrderedLocusNames=YGL203C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND MUTAGENESIS OF
SER-198.
PubMed=3301004; DOI=10.1016/0092-8674(87)90030-4;
Dmochowska A., Dignard D., Henning D., Thomas D.Y., Bussey H.;
"Yeast KEX1 gene encodes a putative protease with a carboxypeptidase
B-like function involved in killer toxin and alpha-factor precursor
processing.";
Cell 50:573-584(1987).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169869;
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M.,
Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J.,
Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E.,
Clemente M.L., Coblenz A., Coglievina M., Coissac E., Defoor E.,
Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B.,
Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L.,
Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M.,
Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M.,
Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B.,
Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W.,
Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A.,
Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S.,
Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L.,
Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S.,
Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J.,
Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M.,
Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B.,
Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J.,
Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M.,
van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M.,
Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H.,
Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M.,
Zollner A., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
Nature 387:81-84(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
FUNCTION.
PubMed=4364866;
Wickner R.B.;
"Chromosomal and nonchromosomal mutations affecting the 'killer
character' of Saccharomyces cerevisiae.";
Genetics 76:423-432(1974).
[5]
FUNCTION.
PubMed=773743;
Wickner R.B., Leibowitz M.J.;
"Two chromosomal genes required for killing expression in killer
strains of Saccharomyces cerevisiae.";
Genetics 82:429-442(1976).
[6]
FUNCTION.
PubMed=3305079; DOI=10.1016/0014-5793(87)80967-5;
Wagner J.C., Wolf D.H.;
"Hormone (pheromone) processing enzymes in yeast. The carboxy-terminal
processing enzyme of the mating pheromone alpha-factor,
carboxypeptidase ysc alpha, is absent in alpha-factor maturation-
defective kex1 mutant cells.";
FEBS Lett. 221:423-426(1987).
[7]
FUNCTION.
PubMed=3301840;
Zhu H., Bussey H., Thomas D.Y., Gagnon J., Bell A.W.;
"Determination of the carboxyl termini of the alpha and beta subunits
of yeast K1 killer toxin. Requirement of a carboxypeptidase B-like
activity for maturation.";
J. Biol. Chem. 262:10728-10732(1987).
[8]
CHARACTERIZATION.
PubMed=2668738; DOI=10.1128/MCB.9.6.2706;
Cooper A., Bussey H.;
"Characterization of the yeast KEX1 gene product: a carboxypeptidase
involved in processing secreted precursor proteins.";
Mol. Cell. Biol. 9:2706-2714(1989).
[9]
GLYCOSYLATION, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=1469044; DOI=10.1083/jcb.119.6.1459;
Cooper A., Bussey H.;
"Yeast Kex1p is a Golgi-associated membrane protein: deletions in a
cytoplasmic targeting domain result in mislocalization to the vacuolar
membrane.";
J. Cell Biol. 119:1459-1468(1992).
[10]
FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=8416959;
Latchinian-Sadek L., Thomas D.Y.;
"Expression, purification, and characterization of the yeast KEX1 gene
product, a polypeptide precursor processing carboxypeptidase.";
J. Biol. Chem. 268:534-540(1993).
[11]
FUNCTION.
PubMed=10972812; DOI=10.1046/j.1365-2958.2000.02063.x;
Eisfeld K., Riffer F., Mentges J., Schmitt M.J.;
"Endocytotic uptake and retrograde transport of a virally encoded
killer toxin in yeast.";
Mol. Microbiol. 37:926-940(2000).
[12]
FUNCTION.
PubMed=11988505;
Riffer F., Eisfeld K., Breinig F., Schmitt M.J.;
"Mutational analysis of K28 preprotoxin processing in the yeast
Saccharomyces cerevisiae.";
Microbiology 148:1317-1328(2002).
[13]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[14]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[15]
FUNCTION.
PubMed=17210951; DOI=10.1083/jcb.200609182;
Heiman M.G., Engel A., Walter P.;
"The Golgi-resident protease Kex2 acts in conjunction with Prm1 to
facilitate cell fusion during yeast mating.";
J. Cell Biol. 176:209-222(2007).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-660, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=17287358; DOI=10.1073/pnas.0607084104;
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
"Analysis of phosphorylation sites on proteins from Saccharomyces
cerevisiae by electron transfer dissociation (ETD) mass
spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[17]
FUNCTION.
PubMed=18474590; DOI=10.1074/jbc.M801303200;
Hauptmann P., Lehle L.;
"Kex1 protease is involved in yeast cell death induced by defective N-
glycosylation, acetic acid, and chronological aging.";
J. Biol. Chem. 283:19151-19163(2008).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[19]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
PubMed=8745419;
Shilton B.H., Li Y., Tessier D., Thomas D.Y., Cygler M.;
"Crystallization of a soluble form of the Kex1p serine
carboxypeptidase from Saccharomyces cerevisiae.";
Protein Sci. 5:395-397(1996).
[20]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 23-505.
PubMed=9220988; DOI=10.1021/bi970433n;
Shilton B.H., Thomas D.Y., Cygler M.;
"Crystal structure of Kex1deltap, a prohormone-processing
carboxypeptidase from Saccharomyces cerevisiae.";
Biochemistry 36:9002-9012(1997).
-!- FUNCTION: Protease with a carboxypeptidase B-like function
involved in the C-terminal processing of the lysine and arginine
residues from the precursors of K1, K2 and K28 killer toxins and
a-factor (mating pheromone). Involved in the programmed cell death
caused by defective N-glycosylation and contributes also to the
active cell death program induced by acetic acid stress or during
chronological aging. Promotes cell fusion by proteolytically
processing substrates that act in parallel to PRM1 as an
alternative fusion machine, as cell wall components, or both.
{ECO:0000269|PubMed:10972812, ECO:0000269|PubMed:11988505,
ECO:0000269|PubMed:1469044, ECO:0000269|PubMed:17210951,
ECO:0000269|PubMed:18474590, ECO:0000269|PubMed:3301004,
ECO:0000269|PubMed:3301840, ECO:0000269|PubMed:3305079,
ECO:0000269|PubMed:4364866, ECO:0000269|PubMed:773743,
ECO:0000269|PubMed:8416959}.
-!- CATALYTIC ACTIVITY: Preferential release of a C-terminal arginine
or lysine residue.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=284 uM for benzoyl-Phe-Ala-Arg {ECO:0000269|PubMed:8416959};
KM=516 uM for furylacryloyl-Ala-Arg
{ECO:0000269|PubMed:8416959};
KM=962 uM for furylacryloyl-Ala-Lys
{ECO:0000269|PubMed:8416959};
Vmax=64.25 umol/min/mg enzyme toward benzoyl-Phe-Ala-Arg
{ECO:0000269|PubMed:8416959};
Vmax=22.35 umol/min/mg enzyme toward furylacryloyl-Ala-Arg
{ECO:0000269|PubMed:8416959};
Vmax=11.55 umol/min/mg enzyme toward furylacryloyl-Ala-Lys
{ECO:0000269|PubMed:8416959};
-!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
membrane {ECO:0000269|PubMed:14562095,
ECO:0000269|PubMed:1469044}; Single-pass type I membrane protein
{ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:1469044}.
-!- MISCELLANEOUS: Present with 8550 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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EMBL; M17231; AAA34717.1; -; Genomic_DNA.
EMBL; Z72725; CAA96915.1; -; Genomic_DNA.
EMBL; BK006941; DAA07912.1; -; Genomic_DNA.
PIR; A29651; A29651.
RefSeq; NP_011312.1; NM_001181068.1.
PDB; 1AC5; X-ray; 2.40 A; A=23-505.
PDBsum; 1AC5; -.
ProteinModelPortal; P09620; -.
SMR; P09620; -.
BioGrid; 33053; 185.
IntAct; P09620; 58.
MINT; P09620; -.
STRING; 4932.YGL203C; -.
ESTHER; yeast-kex01; Carboxypeptidase_S10.
MEROPS; S10.007; -.
iPTMnet; P09620; -.
MaxQB; P09620; -.
PaxDb; P09620; -.
PRIDE; P09620; -.
EnsemblFungi; YGL203C; YGL203C; YGL203C.
GeneID; 852670; -.
KEGG; sce:YGL203C; -.
EuPathDB; FungiDB:YGL203C; -.
SGD; S000003171; KEX1.
GeneTree; ENSGT00880000137977; -.
HOGENOM; HOG000113220; -.
InParanoid; P09620; -.
KO; K01288; -.
OMA; NEIYFAG; -.
OrthoDB; EOG092C255X; -.
BioCyc; MetaCyc:YGL203C-MONOMER; -.
BioCyc; YEAST:YGL203C-MONOMER; -.
BRENDA; 3.4.16.6; 984.
EvolutionaryTrace; P09620; -.
PRO; PR:P09620; -.
Proteomes; UP000002311; Chromosome VII.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005802; C:trans-Golgi network; IDA:SGD.
GO; GO:0004185; F:serine-type carboxypeptidase activity; IDA:SGD.
GO; GO:0006915; P:apoptotic process; IMP:SGD.
GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IBA:GO_Central.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR001563; Peptidase_S10.
InterPro; IPR033124; Ser_caboxypep_his_AS.
InterPro; IPR018202; Ser_caboxypep_ser_AS.
PANTHER; PTHR11802; PTHR11802; 1.
Pfam; PF00450; Peptidase_S10; 1.
PRINTS; PR00724; CRBOXYPTASEC.
SUPFAM; SSF53474; SSF53474; 1.
PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1.
PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
1: Evidence at protein level;
3D-structure; Apoptosis; Carboxypeptidase; Complete proteome;
Glycoprotein; Golgi apparatus; Hydrolase; Membrane; Phosphoprotein;
Protease; Reference proteome; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 22
CHAIN 23 729 Pheromone-processing carboxypeptidase
KEX1.
/FTId=PRO_0000004287.
TOPO_DOM 23 616 Lumenal. {ECO:0000255}.
TRANSMEM 617 637 Helical. {ECO:0000255}.
TOPO_DOM 638 729 Cytoplasmic. {ECO:0000255}.
COMPBIAS 526 531 Poly-Glu.
COMPBIAS 545 561 Poly-Asp.
COMPBIAS 567 578 Poly-Asp.
COMPBIAS 597 607 Poly-Glu.
COMPBIAS 703 711 Poly-Lys.
ACT_SITE 198 198
ACT_SITE 405 405 {ECO:0000250}.
ACT_SITE 470 470 {ECO:0000250}.
MOD_RES 660 660 Phosphoserine.
{ECO:0000244|PubMed:17287358}.
CARBOHYD 81 81 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 459 459 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:1469044}.
CARBOHYD 467 467 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:1469044}.
MUTAGEN 198 198 S->A: Inactivates enzyme.
{ECO:0000269|PubMed:3301004}.
HELIX 26 28 {ECO:0000244|PDB:1AC5}.
HELIX 33 35 {ECO:0000244|PDB:1AC5}.
HELIX 39 41 {ECO:0000244|PDB:1AC5}.
STRAND 50 57 {ECO:0000244|PDB:1AC5}.
STRAND 61 63 {ECO:0000244|PDB:1AC5}.
STRAND 72 79 {ECO:0000244|PDB:1AC5}.
HELIX 84 86 {ECO:0000244|PDB:1AC5}.
STRAND 91 95 {ECO:0000244|PDB:1AC5}.
TURN 98 100 {ECO:0000244|PDB:1AC5}.
HELIX 104 109 {ECO:0000244|PDB:1AC5}.
STRAND 110 116 {ECO:0000244|PDB:1AC5}.
STRAND 122 124 {ECO:0000244|PDB:1AC5}.
HELIX 129 131 {ECO:0000244|PDB:1AC5}.
STRAND 133 138 {ECO:0000244|PDB:1AC5}.
HELIX 154 156 {ECO:0000244|PDB:1AC5}.
HELIX 166 183 {ECO:0000244|PDB:1AC5}.
HELIX 187 189 {ECO:0000244|PDB:1AC5}.
STRAND 190 198 {ECO:0000244|PDB:1AC5}.
HELIX 200 217 {ECO:0000244|PDB:1AC5}.
STRAND 226 235 {ECO:0000244|PDB:1AC5}.
HELIX 239 243 {ECO:0000244|PDB:1AC5}.
HELIX 246 252 {ECO:0000244|PDB:1AC5}.
HELIX 263 279 {ECO:0000244|PDB:1AC5}.
HELIX 283 286 {ECO:0000244|PDB:1AC5}.
STRAND 287 289 {ECO:0000244|PDB:1AC5}.
HELIX 291 294 {ECO:0000244|PDB:1AC5}.
HELIX 296 303 {ECO:0000244|PDB:1AC5}.
STRAND 314 317 {ECO:0000244|PDB:1AC5}.
STRAND 320 325 {ECO:0000244|PDB:1AC5}.
TURN 327 333 {ECO:0000244|PDB:1AC5}.
HELIX 337 345 {ECO:0000244|PDB:1AC5}.
HELIX 350 353 {ECO:0000244|PDB:1AC5}.
TURN 358 360 {ECO:0000244|PDB:1AC5}.
HELIX 369 374 {ECO:0000244|PDB:1AC5}.
HELIX 383 386 {ECO:0000244|PDB:1AC5}.
HELIX 387 392 {ECO:0000244|PDB:1AC5}.
STRAND 396 402 {ECO:0000244|PDB:1AC5}.
HELIX 410 419 {ECO:0000244|PDB:1AC5}.
STRAND 425 428 {ECO:0000244|PDB:1AC5}.
STRAND 433 439 {ECO:0000244|PDB:1AC5}.
STRAND 452 457 {ECO:0000244|PDB:1AC5}.
STRAND 460 465 {ECO:0000244|PDB:1AC5}.
HELIX 472 475 {ECO:0000244|PDB:1AC5}.
HELIX 477 487 {ECO:0000244|PDB:1AC5}.
STRAND 492 496 {ECO:0000244|PDB:1AC5}.
STRAND 499 504 {ECO:0000244|PDB:1AC5}.
SEQUENCE 729 AA; 82245 MW; 70583F279AC02A41 CRC64;
MFYNRWLGTW LAMSALIRIS VSLPSSEEYK VAYELLPGLS EVPDPSNIPQ MHAGHIPLRS
EDADEQDSSD LEYFFWKFTN NDSNGNVDRP LIIWLNGGPG CSSMDGALVE SGPFRVNSDG
KLYLNEGSWI SKGDLLFIDQ PTGTGFSVEQ NKDEGKIDKN KFDEDLEDVT KHFMDFLENY
FKIFPEDLTR KIILSGESYA GQYIPFFANA ILNHNKFSKI DGDTYDLKAL LIGNGWIDPN
TQSLSYLPFA MEKKLIDESN PNFKHLTNAH ENCQNLINSA STDEAAHFSY QECENILNLL
LSYTRESSQK GTADCLNMYN FNLKDSYPSC GMNWPKDISF VSKFFSTPGV IDSLHLDSDK
IDHWKECTNS VGTKLSNPIS KPSIHLLPGL LESGIEIVLF NGDKDLICNN KGVLDTIDNL
KWGGIKGFSD DAVSFDWIHK SKSTDDSEEF SGYVKYDRNL TFVSVYNASH MVPFDKSLVS
RGIVDIYSND VMIIDNNGKN VMITTDDDSD QDATTESGDK PKENLEEEEQ EAQNEEGKEK
EGNKDKDGDD DNDNDDDDED DHNSEGDDDD DDDDDEDDNN EKQSNQGLED SRHKSSEYEQ
EEEEVEEFAE EISMYKHKAV VVTIVTFLIV VLGVYAYDRR VRRKARHTIL VDPNNRQHDS
PNKTVSWADD LESGLGAEDD LEQDEQLEGG APISSTSNKA GSKLKTKKKK KYTSLPNTEI
DESFEMTDF


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U0615r CLIA Carboxypeptidase B2,Carboxypeptidase R,Carboxypeptidase U,Cpb2,CPR,CPU,Rat,Rattus norvegicus,TAFI,Thrombin-activable fibrinolysis inhibitor 96T
E0615r ELISA Carboxypeptidase B2,Carboxypeptidase R,Carboxypeptidase U,Cpb2,CPR,CPU,Rat,Rattus norvegicus,TAFI,Thrombin-activable fibrinolysis inhibitor 96T
E0615b ELISA Bos taurus,Bovine,Carboxypeptidase B2,Carboxypeptidase U,CPB2,CPU,pCPB,Plasma carboxypeptidase B,TAFI,Thrombin-activable fibrinolysis inhibitor 96T


 

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