DDHD1_BOVIN
ID DDHD1_BOVIN Reviewed; 875 AA.
AC O46606;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 88.
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;
DE Short=PA-PLA1;
GN Name=DDHD1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), MASS SPECTROMETRY, FUNCTION,
RP AND MUTAGENESIS OF SER-540 AND SER-730.
RC TISSUE=Testis;
RX PubMed=9488669; DOI=10.1074/jbc.273.10.5468;
RA Higgs H.N., Han M.H., Johnson G.E., Glomset J.A.;
RT "Cloning of a phosphatidic acid-preferring phospholipase A1 from bovine
RT testis.";
RL J. Biol. Chem. 273:5468-5477(1998).
CC -!- FUNCTION: Phospholipase that hydrolyzes phosphatidic acid, including
CC 1,2-dioleoyl-sn-phosphatidic acid (PubMed:9488669). 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, ECO:0000269|PubMed:9488669}.
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=O46606-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O46606-2; Sequence=VSP_008627;
CC -!- MASS SPECTROMETRY: [Isoform 2]: Mass=97637; Mass_error=890;
CC Method=MALDI; Note=The measured range is 1-835.;
CC Evidence={ECO:0000269|PubMed:9488669};
CC -!- SIMILARITY: Belongs to the PA-PLA1 family. {ECO:0000305}.
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DR EMBL; AF045022; AAC03019.1; -; mRNA.
DR RefSeq; NP_788816.1; NM_176643.2. [O46606-1]
DR AlphaFoldDB; O46606; -.
DR STRING; 9913.ENSBTAP00000026549; -.
DR iPTMnet; O46606; -.
DR PaxDb; O46606; -.
DR PRIDE; O46606; -.
DR GeneID; 338047; -.
DR KEGG; bta:338047; -.
DR CTD; 80821; -.
DR eggNOG; KOG2308; Eukaryota.
DR InParanoid; O46606; -.
DR OrthoDB; 777968at2759; -.
DR BRENDA; 3.1.1.118; 908.
DR Proteomes; UP000009136; Unplaced.
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 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..875
FT /note="Phospholipase DDHD1"
FT /id="PRO_0000079844"
FT DOMAIN 614..861
FT /note="DDHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00378"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 101..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 770..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 540
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEL9"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEL9"
FT MOD_RES 726
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80YA3"
FT VAR_SEQ 343..382
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9488669"
FT /id="VSP_008627"
FT MUTAGEN 540
FT /note="S->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:9488669"
FT MUTAGEN 730
FT /note="S->A: No effect."
FT /evidence="ECO:0000269|PubMed:9488669"
SQ SEQUENCE 875 AA; 97576 MW; E1DF4FFD7DC75EB1 CRC64;
MNYPGHGSPR SSERNGGRGG DGAAWELGSD TEPAFGGSVC RFDHLPVGEP GDDEVPLALL
RGEPGLHLAP GAEDHNHHLA LDPCLSDDNY DFSSAESGSS LRYYSEGESG GGGSSSSLHP
PQQPLVPSNS GGGGAAGGGP GERKRTRPGG AAARHRYEVV TELGPEEVRW FYKEDKKTWK
PFIGYDSLRI ELAFRTLLQA TGARARAQDP DGDHVCGPAS PAGPASSSVE DEDEDRVCGF
CPRIAGHGRE MEELVNIERV CVRGGLYEVD VTQGECYPVY WNQSDKIPVM RGQWFIDGTW
QPLEEEESNL IEQEHLSRFR GQQMQESFDI EVSKPIDGKD AIHSFKLSRN HVDWHSVDEV
YLYSDATTSK IARTVTQKLG FSKASSSGTR LHRGYVEEAT LEDKPSQTTH IVFVVHGIGQ
KMDQGRIIKN TAMMREAARK IEERHFSNHA THVEFLPVEW RSKLTLDGDT VDSITPDKVR
GLRDMLNSSA MDIMYYTSPL YRDELVKGLQ QELNRLYSLF CSRNPNFEEK GGKVSIVSHS
LGCVITYDIM TGWNPVRLYE QLLQKEEELP DERWMSYEER HLLDELYITK RRLREIEERL
HGLKASSMTQ TPALKFKVEN FFCMGSPLAV FLALRGIRPG NTGSQDHILP REICNRLLNI
FHPTDPVAYR LEPLILKHYS NISPVQIHWY NTSNPLPYEY MKPSFLHPAK DPTSISENEG
ISTIPSPVTS PVLSRRHYGE SITNIGKASI LGAASIGKGL GGMLFSRFGR SSASQPSETS
RDSIEDEKKP VASPPMTTVA TQTLPHSSSG FLDSALELDH RIDFELREGL VESRYWSAVT
SHTAYWSSLD VALFLLTFMY KHEHDNNVKP SLDPV
