DDHD1_MOUSE
ID DDHD1_MOUSE Reviewed; 547 AA.
AC Q80YA3; Q8VEF2;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Phospholipase DDHD1 {ECO:0000305};
DE EC=3.1.1.-;
DE AltName: Full=DDHD domain-containing protein 1;
DE AltName: Full=Phosphatidic acid-preferring phospholipase A1 homolog;
DE Short=PA-PLA1;
GN Name=Ddhd1 {ECO:0000312|MGI:MGI:2150302};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 271-547 (ISOFORM 2).
RC TISSUE=Eye, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Liver, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Phospholipase that hydrolyzes phosphatidic acid, including
CC 1,2-dioleoyl-sn-phosphatidic acid. The different isoforms may change
CC the substrate specificity (By similarity). Required for the
CC organization of the endoplasmic reticulum exit sites (ERES), also known
CC as transitional endoplasmic reticulum (tER) (By similarity).
CC {ECO:0000250|UniProtKB:Q8NEL9}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = (9Z)-
CC octadecenoate + 2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H(+);
CC Xref=Rhea:RHEA:45128, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:74546, ChEBI:CHEBI:77593;
CC Evidence={ECO:0000250|UniProtKB:Q8NEL9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45129;
CC Evidence={ECO:0000250|UniProtKB:Q8NEL9};
CC -!- SUBUNIT: Forms homooligomers and, to a much smaller extent,
CC heterooligomers with DDHD2. Interacts with SEC23A and SEC24C.
CC {ECO:0000250|UniProtKB:Q8NEL9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8NEL9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q80YA3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80YA3-2; Sequence=VSP_008630;
CC -!- SIMILARITY: Belongs to the PA-PLA1 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; BC018552; AAH18552.1; -; mRNA.
DR EMBL; BC043475; AAH43475.1; -; mRNA.
DR RefSeq; NP_001034195.2; NM_001039106.3.
DR RefSeq; NP_001036184.1; NM_001042719.2.
DR RefSeq; NP_001271328.1; NM_001284399.1. [Q80YA3-1]
DR RefSeq; NP_789815.3; NM_176845.5.
DR AlphaFoldDB; Q80YA3; -.
DR BioGRID; 227895; 2.
DR IntAct; Q80YA3; 1.
DR MINT; Q80YA3; -.
DR STRING; 10090.ENSMUSP00000084577; -.
DR ChEMBL; CHEMBL3259505; -.
DR iPTMnet; Q80YA3; -.
DR PhosphoSitePlus; Q80YA3; -.
DR MaxQB; Q80YA3; -.
DR PaxDb; Q80YA3; -.
DR PRIDE; Q80YA3; -.
DR ProteomicsDB; 279844; -. [Q80YA3-1]
DR ProteomicsDB; 279845; -. [Q80YA3-2]
DR DNASU; 114874; -.
DR GeneID; 114874; -.
DR KEGG; mmu:114874; -.
DR UCSC; uc007tgu.2; mouse. [Q80YA3-1]
DR UCSC; uc007tgv.2; mouse. [Q80YA3-2]
DR CTD; 80821; -.
DR MGI; MGI:2150302; Ddhd1.
DR eggNOG; KOG2308; Eukaryota.
DR InParanoid; Q80YA3; -.
DR OrthoDB; 777968at2759; -.
DR BRENDA; 3.1.1.118; 3474.
DR Reactome; R-MMU-1483166; Synthesis of PA.
DR BioGRID-ORCS; 114874; 6 hits in 73 CRISPR screens.
DR ChiTaRS; Ddhd1; mouse.
DR PRO; PR:Q80YA3; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q80YA3; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004620; F:phospholipase activity; IBA:GO_Central.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0090141; P:positive regulation of mitochondrial fission; ISO:MGI.
DR GO; GO:0030382; P:sperm mitochondrion organization; IMP:MGI.
DR InterPro; IPR004177; DDHD_dom.
DR Pfam; PF02862; DDHD; 1.
DR SMART; SM01127; DDHD; 1.
DR PROSITE; PS51043; DDHD; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Hydrolase; Lipid degradation;
KW Lipid metabolism; Phosphoprotein; Reference proteome.
FT CHAIN 1..547
FT /note="Phospholipase DDHD1"
FT /id="PRO_0000079846"
FT DOMAIN 258..533
FT /note="DDHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00378"
FT REGION 414..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 184
FT /evidence="ECO:0000250"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 460..488
FT /note="YFRLQESFFYLPQLLFPENVMQSKDDSLV -> L (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_008630"
SQ SEQUENCE 547 AA; 61823 MW; 56341B29192471D0 CRC64;
MDEVYLYSDA TTSKIARTVT QKLGFSKASS SGTRLHRGYV EEATLEDKPS QTSHIVFVVH
GIGQKMDQGR IIKNTAMMRE AARKMEEKHF SNHATHVEFL PVEWRSKLTL DGDTVDSITP
DKVRGLRDML NSSAMDIMYY TSPLYRDELV KGLQQELNRL YSLFCSRNPD FEEKGGKVSI
VSHSLGCVIT YDIMMGWNPG GLYEQLLQKE EELPDERWMS YEERHLLDEL YITKRRLREI
EDRLHGLKAP SISQTPALKF KVENFFCMGS PLAVFLALRG IRPGNSGSQD HILPREICNR
LLNIFHPTDP VAYRLEPLIL KHYSNISPVQ IHWYNTSNPL PYEHMKPNFL NPAKEPTSVS
DSENIAAIPS PVTSPVLSRR HYGESITNIG KASILGAASI GKGLGGMLFS RFGRSSASQP
SEPSKDSLED DKKPSASPST TTVATQTLPH SGSGFLDSAY FRLQESFFYL PQLLFPENVM
QSKDDSLVEL EHRIDFELRE GLVESRYWSA VTSHTAYWSS LDVALFLLTF MYKHEHDTEA
KPSLGSL
