ID S9YA82_CAMFR Unreviewed; 931 AA.
AC S9YA82;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN ORFNames=CB1_000479003 {ECO:0000313|EMBL:EPY84371.1};
OS Camelus ferus (Wild bactrian camel) (Camelus bactrianus ferus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Tylopoda; Camelidae; Camelus.
OX NCBI_TaxID=419612 {ECO:0000313|EMBL:EPY84371.1, ECO:0000313|Proteomes:UP000030684};
RN [1] {ECO:0000313|EMBL:EPY84371.1, ECO:0000313|Proteomes:UP000030684}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=bactrian camel {ECO:0000313|Proteomes:UP000030684};
RX PubMed=23149746;
RG Bactrian Camels Genome Sequencing and Analysis Consortium;
RA Jirimutu, Wang Z., Ding G., Chen G., Sun Y., Sun Z., Zhang H., Wang L.,
RA Hasi S., Zhang Y., Li J., Shi Y., Xu Z., He C., Yu S., Li S., Zhang W.,
RA Batmunkh M., Ts B., Narenbatu, Unierhu, Bat-Ireedui S., Gao H.,
RA Baysgalan B., Li Q., Jia Z., Turigenbayila, Subudenggerile, Narenmanduhu,
RA Wang Z., Wang J., Pan L., Chen Y., Ganerdene Y., Dabxilt, Erdemt, Altansha,
RA Altansukh, Liu T., Cao M., Aruuntsever, Bayart, Hosblig, He F., Zha-ti A.,
RA Zheng G., Qiu F., Sun Z., Zhao L., Zhao W., Liu B., Li C., Chen Y.,
RA Tang X., Guo C., Liu W., Ming L., Temuulen, Cui A., Li Y., Gao J., Li J.,
RA Wurentaodi, Niu S., Sun T., Zhai Z., Zhang M., Chen C., Baldan T.,
RA Bayaer T., Li Y., Meng H.;
RT "Genome sequences of wild and domestic bactrian camels.";
RL Nat. Commun. 3:1202-1202(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-
CC sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:14445,
CC ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58608; EC=3.1.4.4;
CC Evidence={ECO:0000256|PIRNR:PIRNR009376};
CC -!- SIMILARITY: Belongs to the phospholipase D family.
CC {ECO:0000256|ARBA:ARBA00008664, ECO:0000256|PIRNR:PIRNR009376}.
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DR EMBL; KB016763; EPY84371.1; -; Genomic_DNA.
DR AlphaFoldDB; S9YA82; -.
DR Proteomes; UP000030684; Unassembled WGS sequence.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-UniRule.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-UniRule.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IEA:InterPro.
DR CDD; cd01254; PH_PLD; 1.
DR CDD; cd09843; PLDc_vPLD2_1; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR InterPro; IPR016555; PLipase_D_euk.
DR InterPro; IPR015679; PLipase_D_fam.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR PANTHER; PTHR18896:SF121; PHOSPHOLIPASE D2; 1.
DR Pfam; PF00614; PLDc; 1.
DR Pfam; PF13091; PLDc_2; 1.
DR Pfam; PF00787; PX; 1.
DR PIRSF; PIRSF009376; Phospholipase_D_euk; 1.
DR SMART; SM00155; PLDc; 2.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR SUPFAM; SSF64268; PX domain; 1.
DR PROSITE; PS50035; PLD; 2.
DR PROSITE; PS50195; PX; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR009376};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|PIRNR:PIRNR009376};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|PIRNR:PIRNR009376};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Reference proteome {ECO:0000313|Proteomes:UP000030684}.
FT DOMAIN 74..204
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 446..473
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 760..787
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 931 AA; 105168 MW; 6AFE0DC622508C43 CRC64;
MAATPESLFP TGGDLDSSQL HMEPDEVDTL KEGEDPADRM HPFLAIYNLQ PLKMHPLVFA
PGVPVIAQVV GTERYTSGSK VAGLASGRRV GTCTLYSVRL THGDFTWTTK KKFRHFQELH
RDLLRHKVLM SLLPLARFAV AYAPAQEAAN REMPSLPRAG PEGSARHASS KQKYLENYLN
RLLTMSFYRN YHAMTEFLEV SQLSFIPDLG CKGLEGVIRK RSGGHRVPGL TCCGRDQVCY
RWSKRWLVVK DSFLMYMCLE TGAISFVQLF DPGFEVQVGK RSTEARYGVR IDTSHRSLIL
KCSSYRQARW WAQEITELAQ GPGKDFIQLH RHDSYAPPRP GTLARWFVNG AGYFAAVADA
ILQAQEEIFI TDWWLSPEVY LKRPAHSDDW RLDIMLKRKA EEGVRVSILL FKEVELALGI
NSGYSKRALM LLHPNIKVMR HPDQVTLWAH HEKLLVVDQV VAFLGGLDLA YGRWDDLHYR
LTDLGNSSES ATPQPPTLCS DSLDTPDLSH NQLFWLGKDY SNLITKDWVH LDRPFEDFID
RETTPRMPWR DIGVVIHGLP ARDLARHFIQ RWNFTKTTKA KYKIPLYPYL LPKSNSTANQ
LPFVLPGGQC ATVQVLRSVD RWSAGTSENS ILNAYLHTIR ESQHFLYIEN QFFISCSDGR
TVLNKVGDEI VDRILKAHKQ GQCFRVYVLL PLLPGFEGDI STGGGNAIQA ILHFTYRTLC
RGEYSILHRL KAAMGTAWRN YMSICGLRTH GELGGHPVSE LIYIHSKMLI ADDRTVIIGS
ANINDRSLLG KRDSELAVLI EDTETEPSLM GGVEYQAGSV ILGADARPNL DLQDPICDDF
FQLWQDTAES NANIYEQIFR CLPSNAIRSL RALREYVAVE PLATVSPPLA QSELTQVQGH
LVHFPLKFLE DESLLPPLGS KEGVMPLEVW T
//
