PLBLA_DICDI
ID PLBLA_DICDI Reviewed; 574 AA.
AC Q550U9; Q8MWQ0;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Phospholipase B-like protein A;
DE EC=3.1.1.-;
DE Flags: Precursor;
GN Name=plbA; ORFNames=DDB_G0276767;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 231-239; 433-437; 464-473
RP AND 501-512, FUNCTION, AND ENZYME ACTIVITY.
RC STRAIN=AX3;
RX PubMed=15193148; DOI=10.1042/bj20040110;
RA Morgan C.P., Insall R., Haynes L., Cockcroft S.;
RT "Identification of phospholipase B from Dictyostelium discoideum reveals a
RT new lipase family present in mammals, flies and nematodes, but not yeast.";
RL Biochem. J. 382:441-449(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [3]
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: Phospholipase that removes both fatty-acid chains from
CC phosphatidylcholine and produces the water-soluble
CC glycerophosphorylcholine. In addition to phosphatidylcholine
CC deacylation, it also hydrolyzes phosphatidylinositol and
CC phosphatidylethanolamine. {ECO:0000269|PubMed:15193148}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the phospholipase B-like family. {ECO:0000305}.
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DR EMBL; AF411829; AAN03644.1; -; mRNA.
DR EMBL; AAFI02000019; EAL68885.1; -; Genomic_DNA.
DR RefSeq; XP_642833.1; XM_637741.1.
DR AlphaFoldDB; Q550U9; -.
DR SMR; Q550U9; -.
DR STRING; 44689.DDB0185225; -.
DR PaxDb; Q550U9; -.
DR EnsemblProtists; EAL68885; EAL68885; DDB_G0276767.
DR GeneID; 8620697; -.
DR KEGG; ddi:DDB_G0276767; -.
DR dictyBase; DDB_G0276767; plbA.
DR eggNOG; KOG3774; Eukaryota.
DR HOGENOM; CLU_027106_4_0_1; -.
DR InParanoid; Q550U9; -.
DR OMA; DELYHEC; -.
DR PhylomeDB; Q550U9; -.
DR PRO; PR:Q550U9; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005576; C:extracellular region; ISS:dictyBase.
DR GO; GO:0004620; F:phospholipase activity; IDA:dictyBase.
DR GO; GO:0046338; P:phosphatidylethanolamine catabolic process; IDA:dictyBase.
DR GO; GO:0031161; P:phosphatidylinositol catabolic process; IDA:dictyBase.
DR GO; GO:0009395; P:phospholipid catabolic process; IDA:dictyBase.
DR InterPro; IPR007000; PLipase_B-like.
DR PANTHER; PTHR12370; PTHR12370; 1.
DR Pfam; PF04916; Phospholip_B; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Hydrolase; Lipid degradation;
KW Lipid metabolism; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..574
FT /note="Phospholipase B-like protein A"
FT /id="PRO_0000286117"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 415
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 503
FT /note="S -> Y (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 505
FT /note="D -> E (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 512
FT /note="V -> R (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 574 AA; 64838 MW; B74CD789755B2952 CRC64;
MRVIRSLLLL TIAIIGSVLS QSSIDDGYTV FYSQPDNYYV KPGTFSNGVA QAIFSNEMMT
TGWSFMSISS SEGLYPNDII AAGAGYLEGY ISQEMIYQNW MNMYNNEYHN VIGSDVENWI
QENLQYLQTM IDSAPSNDLY WQNVETVLTQ ITYMQRGYNQ SVIDNGVDAS QSLGITEFFL
MNMDGDMIDL GPALNLTNGK QVTSPATATS PKQAFKEFMR RTGHCSALIK MTDDLSDLFS
GHTTWSSYYE MVRMFKVYNL KYLFNGQPPA SKVTMFSGYP GTLSSIDDFY LLDTKIVVIE
TTNGLMNNNL YHLITSESVL SWIRVIVANR LATGGESWCQ TFSLYNSGTY NNQWIIVDYN
KFIKGYGALD GTLYILEQVP DYVEYGDQTA ILRTGYWPSF NIPFYENIYG LTGFNETYAQ
FGNWFSYQAS PRSMIFKRDA NNIHSLTQFQ AMLRYNNWQN DPFSQGNAGN QISSRFDLVT
ADDPNNQYLD PDAFGGIDSK VVSADMVAAL LVNAQSGPSH DNETPFTWNS QWNQKYTYAG
QPTTWNFDWM TMSLQSMKPA SPSSDSSSDS TTFN
