{PDOC00122}
{PS00131; CARBOXYPEPT_SER_SER}
{PS00560; CARBOXYPEPT_SER_HIS}
{BEGIN}
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* Serine carboxypeptidases, active sites *
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All  known  carboxypeptidases  are either  metallo carboxypeptidases or serine
carboxypeptidases  (EC 3.4.16.5  and  EC 3.4.16.6).  The catalytic activity of
the serine   carboxypeptidases,   like  that  of  the  trypsin  family  serine
proteases, is  provided  by  a  charge relay system involving an aspartic acid
residue hydrogen-bonded to a histidine, which is itself  hydrogen-bonded  to a
serine [1]. Proteins known to be serine carboxypeptidases are:

 - Barley and wheat serine carboxypeptidases I, II, and III [2].
 - Yeast carboxypeptidase Y (YSCY) (gene PRC1), a  vacuolar  protease involved
   in degrading small peptides.
 - Yeast  KEX1  protease,  involved in killer toxin and alpha-factor precursor
   processing.
 - Fission  yeast  sxa2,  a probable carboxypeptidase involved in degrading or
   processing mating pheromones [3].
 - Penicillium janthinellum carboxypeptidase S1 [4].
 - Aspergullus niger carboxypeptidase pepF.
 - Aspergullus satoi carboxypeptidase cpdS.
 - Vertebrate protective protein / cathepsin A [5], a  lysosomal protein which
   is not only a carboxypeptidase but also  essential for the activity of both
   beta-galactosidase and neuraminidase.
 - Mosquito vitellogenic carboxypeptidase (VCP) [6].
 - Naegleria fowleri virulence-related protein Nf314 [7].
 - Yeast hypothetical protein YBR139w.
 - Caenorhabditis elegans hypothetical proteins C08H9.1, F13D12.6, F32A5.3,
   F41C3.5 and K10B2.2.

This family also includes:

 - Sorghum   (s)-hydroxymandelonitrile  lyase  (EC  4.1.2.11)  (hydroxynitrile
   lyase) (HNL) [8], an enzyme involved in plant cyanogenesis.

The sequences  surrounding  the  active site serine and histidine residues are
highly conserved in all these serine carboxypeptidases.

-Consensus pattern: [LIVM]-x-[GSTA]-E-S-Y-[AG]-[GS]
                    [S is the active site residue]
-Sequences known to belong to this class detected by the pattern: ALL,  except
 for HNL.
-Other sequence(s) detected in Swiss-Prot: 3.

-Consensus pattern: [LIVF]-x(2)-[LIVSTA]-x-[IVPST]-x-[GSDNQL]-[SAGV]-[SG]-H-x-
                    [IVAQ]-P-x(3)-[PSA]
                    [H is the active site residue]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Note: These proteins belong to family S10 in the classification of peptidases
 [9,E1].

-Last update: February 2003 / Patterns and text revised.

[ 1] Liao D.I., Remington S.J.
     "Structure of wheat serine carboxypeptidase II at 3.5-A resolution. A
     new class of serine proteinase."
     J. Biol. Chem. 265:6528-6531(1990).
     PubMed=2324088
[ 2] Sorensen S.B., Svendsen I., Breddam K.
     "Primary structure of carboxypeptidase III from malted barley."
     Carlsberg Res. Commun. 54:193-202(1989).
     PubMed=2639682
[ 3] Imai Y., Yamamoto M.
     "Schizosaccharomyces pombe sxa1+ and sxa2+ encode putative proteases
     involved in the mating response."
     Mol. Cell. Biol. 12:1827-1834(1992).
     PubMed=1549128
[ 4] Svendsen I., Hofmann T., Endrizzi J., Remington S.J., Breddam K.
     "The primary structure of carboxypeptidase S1 from Penicillium
     janthinellum."
     FEBS Lett. 333:39-43(1993).
     PubMed=8224168
[ 5] Galjart N.J., Morreau H., Willemsen R., Gillemans N., Bonten E.J.,
     d'Azzo A.
     "Human lysosomal protective protein has cathepsin A-like activity
     distinct from its protective function."
     J. Biol. Chem. 266:14754-14762(1991).
     PubMed=1907282
[ 6] Cho W.L., Deitsch K.W., Raikhel A.S.
     "An extraovarian protein accumulated in mosquito oocytes is a
     carboxypeptidase activated in embryos."
     Proc. Natl. Acad. Sci. U.S.A. 88:10821-10824(1991).
     PubMed=1961751
[ 7] Hu W.N., Kopachik W., Band R.N.
     "Cloning and characterization of transcripts showing virulence-related
     gene expression in Naegleria fowleri."
     Infect. Immun. 60:2418-2424(1992).
     PubMed=1587609
[ 8] Wajant H., Mundry K.W., Pfizenmaier K.
     "Molecular cloning of hydroxynitrile lyase from Sorghum bicolor (L.).
     Homologies to serine carboxypeptidases."
     Plant Mol. Biol. 26:735-746(1994).
     PubMed=7948927
[ 9] Rawlings N.D., Barrett A.J.
     "Families of serine peptidases."
     Methods Enzymol. 244:19-61(1994).
     PubMed=7845208
[E1] https://www.uniprot.org/docs/peptidas

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