ID   PLBLC_DICDI             Reviewed;         565 AA.
AC   Q54M94;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Phospholipase B-like protein C;
DE            EC=3.1.1.-;
DE   Flags: Precursor;
GN   Name=plbC; ORFNames=DDB_G0286095;
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 phospholipase. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the phospholipase B-like family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AAFI02000085; EAL64426.1; -; Genomic_DNA.
DR   RefSeq; XP_637940.1; XM_632848.1.
DR   AlphaFoldDB; Q54M94; -.
DR   SMR; Q54M94; -.
DR   STRING; 44689.DDB0231378; -.
DR   PaxDb; Q54M94; -.
DR   EnsemblProtists; EAL64426; EAL64426; DDB_G0286095.
DR   GeneID; 8625451; -.
DR   KEGG; ddi:DDB_G0286095; -.
DR   dictyBase; DDB_G0286095; plbC.
DR   eggNOG; KOG3774; Eukaryota.
DR   HOGENOM; CLU_027106_4_0_1; -.
DR   InParanoid; Q54M94; -.
DR   OMA; ISQVTMS; -.
DR   PhylomeDB; Q54M94; -.
DR   PRO; PR:Q54M94; -.
DR   Proteomes; UP000002195; Chromosome 4.
DR   GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR   GO; GO:0004620; F:phospholipase activity; ISS:dictyBase.
DR   GO; GO:0046338; P:phosphatidylethanolamine catabolic process; ISS:dictyBase.
DR   GO; GO:0031161; P:phosphatidylinositol catabolic process; ISS:dictyBase.
DR   GO; GO:0009395; P:phospholipid catabolic process; ISS:dictyBase.
DR   InterPro; IPR007000; PLipase_B-like.
DR   PANTHER; PTHR12370; PTHR12370; 1.
DR   Pfam; PF04916; Phospholip_B; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..565
FT                   /note="Phospholipase B-like protein C"
FT                   /id="PRO_0000286119"
FT   CARBOHYD        53
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        118
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        200
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        201
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        211
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        266
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        302
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        406
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        485
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   565 AA;  64819 MW;  234F7DED23135E09 CRC64;
     MNKIIILISL FLNFLFGYVV CLNENNQKSQ NLIIPTYSIK LKSDGEYLVY SGNDTLSIAQ
     ASYTNEMMSI GWGYISITTN PKYNDSLQIE AAGYLEGYLS YEMIWQNWNN MMVNQNANNS
     FGNDIISWAK ENILYMNQQI QLNQNDPYWI NVNLVLQQLN GLTNGYSDAN QNPDRQLSLM
     DFILLNMNVE IYDIMNSLKN NSSSFYQQPN NNSFDNNQHC SALIKLTDDL TELYTGHTTW
     SDYYQMVRMI KSYNFRFSKL VAAKSNTTMF SGYPGVLMSV DDFYMLDSKL VVLETTNGIK
     DNDSELFKLI KPQSVLTWIR IIVTNRIAHS GKSWCEIFEK ENSGTYNNQW MIVDYNKFIK
     GVRVQDGTLY VFEQLPGYVE YADVTNILRT GYWPSFNVPY FETISNMSGF NYQSSSSDSS
     SSSGSIAYEQ YPRSQIFRRD SNKVYSISDF QAFMRYNDFQ NDPLAYGDPG NQISSRFDLI
     TPQNNASAAG GIDSKVTSLE LINQFLMIAQ SGPTHDQEPP FSWSSENWKN KYPTIGQPDT
     FDFEWVTFST TSFGSFPSAS NEKNY