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Overview

Uniprot IDQ8NEL9
Protein NamePhospholipase DDHD1
Gene NameDDHD1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
375 IARTVTQKLGFSKAS
380 TQKLGFSKASSSGTR

Function

Phospholipase A1 (PLA1) that hydrolyzes ester bonds at the sn-1 position of glycerophospholipids producing a free fatty acid and a lysophospholipid (Probable) (PubMed:20359546, PubMed:22922100). Prefers phosphatidate (1,2-diacyl-sn-glycero-3-phosphate, PA) as substrate in vitro, but can efficiently hydrolyze phosphatidylinositol (1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol), PI), as well as a range of other glycerophospholipid substrates such as phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine, PC), phosphatidylethanolamine (1,2-diacyl-sn-glycero-3-phosphoethanolamine, PE), phosphatidylserine (1,2-diacyl-sn-glycero-3-phospho-L-serine, PS) and phosphatidylglycerol (1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol), PG) (Probable) (PubMed:20359546). Involved in the regulation of the endogenous content of polyunsaturated PI and PS lipids in the nervous system. Changes in these lipids extend to downstream metabolic products like PI phosphates PIP and PIP2, which play fundamental roles in cell biology (By similarity). Regulates mitochondrial morphology (PubMed:24599962). These dynamic changes may be due to PA hydrolysis at the mitochondrial surface (PubMed:24599962). May play a regulatory role in spermatogenesis or sperm function (PubMed:24599962)

Protein Sequence

10 MNYPGRGSPR 20 SPEHNGRGGG 30 GGAWELGSDA 40 RPAFGGGVCC 50 FEHLPGGDPD 60 DGDVPLALLR 70 GEPGLHLAPG 80 TDDHNHHLAL 90 DPCLSDENYD 100 FSSAESGSSL 110 RYYSEGESGG 120 GGSSLSLHPP 130 QQPPLVPTNS 140 GGGGATGGSP 150 GERKRTRLGG 160 PAARHRYEVV 170 TELGPEEVRW 180 FYKEDKKTWK 190 PFIGYDSLRI 200 ELAFRTLLQT 210 TGARPQGGDR 220 DGDHVCSPTG 230 PASSSGEDDD 240 EDRACGFCQS 250 TTGHEPEMVE 260 LVNIEPVCVR 270 GGLYEVDVTQ 280 GECYPVYWNQ 290 ADKIPVMRGQ 300 WFIDGTWQPL 310 EEEESNLIEQ 320 EHLNCFRGQQ 330 MQENFDIEVS 340 KSIDGKDAVH 350 SFKLSRNHVD 360 WHSVDEVYLY 370 SDATTSKIAR 380 TVTQKLGFSK 390 ASSSGTRLHR 400 GYVEEATLED 410 KPSQTTHIVF 420 VVHGIGQKMD 430 QGRIIKNTAM 440 MREAARKIEE 450 RHFSNHATHV 460 EFLPVEWRSK 470 LTLDGDTVDS 480 ITPDKVRGLR 490 DMLNSSAMDI 500 MYYTSPLYRD 510 ELVKGLQQEL 520 NRLYSLFCSR 530 NPDFEEKGGK 540 VSIVSHSLGC 550 VITYDIMTGW 560 NPVRLYEQLL 570 QKEEELPDER 580 WMSYEERHLL 590 DELYITKRRL 600 KEIEERLHGL 610 KASSMTQTPA 620 LKFKVENFFC 630 MGSPLAVFLA 640 LRGIRPGNTG 650 SQDHILPREI 660 CNRLLNIFHP 670 TDPVAYRLEP 680 LILKHYSNIS 690 PVQIHWYNTS 700 NPLPYEHMKP 710 SFLNPAKEPT 720 SVSENEGIST 730 IPSPVTSPVL 740 SRRHYGESIT 750 NIGKASILGA 760 ASIGKGLGGM 770 LFSRFGRSST 780 TQSSETSKDS 790 MEDEKKPVAS 800 PSATTVGTQT 810 LPHSSSGFLD 820 SAYFRLQESF 830 FNLPQLLFPE 840 NVMQNKDNAL 850 VELDHRIDFE 860 LREGLVESRY 870 WSAVTSHTAY 880 WSSLDVALFL 890 LTFMYKHEHD 900 DDAKPNLDPI

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Biological Process GO:0046488 phosphatidylinositol metabolic process
Biological Process GO:0090141 positive regulation of mitochondrial fission
Cellular Component GO:0005829 cytosol
Molecular Function GO:0004620 glycerophospholipase activity
Molecular Function GO:0008970 glycerophospholipid phospholipase A1 activity
Molecular Function GO:0046872 metal ion binding

Reference

PMID: N/A