ID   SCPL1_DICDI             Reviewed;         416 AA.
AC   Q54DY7;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Serine carboxypeptidase S10 family member 1;
DE            EC=3.4.16.-;
DE   Flags: Precursor;
GN   ORFNames=DDB_G0291912;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Probable carboxypeptidase. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR   EMBL; AAFI02000186; EAL61486.1; -; Genomic_DNA.
DR   RefSeq; XP_629909.1; XM_629907.1.
DR   AlphaFoldDB; Q54DY7; -.
DR   SMR; Q54DY7; -.
DR   STRING; 44689.DDB0266717; -.
DR   ESTHER; dicdi-q54dy7; Carboxypeptidase_S10.
DR   MEROPS; S10.009; -.
DR   PaxDb; Q54DY7; -.
DR   EnsemblProtists; EAL61486; EAL61486; DDB_G0291912.
DR   GeneID; 8628410; -.
DR   KEGG; ddi:DDB_G0291912; -.
DR   dictyBase; DDB_G0291912; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_10_1_1; -.
DR   InParanoid; Q54DY7; -.
DR   OMA; PDAFCDP; -.
DR   PhylomeDB; Q54DY7; -.
DR   PRO; PR:Q54DY7; -.
DR   Proteomes; UP000002195; Chromosome 6.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IBA:GO_Central.
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; 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; PS00131; CARBOXYPEPT_SER_SER; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW   Secreted; Signal; Zymogen.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..?
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000331588"
FT   CHAIN           ?..416
FT                   /note="Serine carboxypeptidase S10 family member 1"
FT                   /id="PRO_0000331589"
FT   ACT_SITE        156
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        338
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        396
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   CARBOHYD        33
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        84
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        235
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        273
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        295
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        385
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   416 AA;  46858 MW;  77D8B34233296557 CRC64;
     MMKLLFIIIS IIFVINVSNS TPTLQLSGYF NVNETTNANL FYLFYESQNS PSTDPLILWL
     TGGPGCSSLM AAFYENGPYF VNDNLTLSEN PNSWNMVANV LYVDSPLGAG FSYVVDSDGY
     STTETEISEN LYSFLTQFLS KYPKYSKLPL YIFGESYAGH YVPSFSYYIY QKNLGLATIN
     LKGLAIGNGM VDPYIQYGSL GPFAYAHGML DINALKETEG LYESCQQAID SGDYNMTTQI
     CNNIMDIVQE YAGNFNVYDV SKTCYPNEPL CYNFTAIIDY LNLASTKQSF GVLPNSTWNV
     CSTQPYSAII RDWFNTPINY IPTLLENYKV LVYNGNYDWI CNFLGSTEWT SQLKWKYNQE
     FNNSPRKILY INGNTISGYS QSYDNLTMQV LLGASHMAPR EAPVAALAMV ESFIQN