PLD6_HUMAN
ID PLD6_HUMAN Reviewed; 252 AA.
AC Q8N2A8; Q8N5Y1;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Mitochondrial cardiolipin hydrolase;
DE EC=3.1.-.- {ECO:0000250|UniProtKB:Q5SWZ9};
DE AltName: Full=Choline phosphatase 6;
DE AltName: Full=Mitochondrial phospholipase {ECO:0000303|PubMed:17028579};
DE Short=MitoPLD {ECO:0000303|PubMed:17028579};
DE EC=3.1.4.- {ECO:0000269|PubMed:17028579, ECO:0000269|PubMed:24599962, ECO:0000269|PubMed:26711011};
DE AltName: Full=Phosphatidylcholine-hydrolyzing phospholipase D6;
DE AltName: Full=Phospholipase D6;
DE Short=PLD6 {ECO:0000303|PubMed:26678338};
DE AltName: Full=Protein zucchini homolog {ECO:0000250|UniProtKB:Q9VKD7};
GN Name=PLD6;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Amygdala;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS PRO-42 AND HIS-108.
RC TISSUE=Brain;
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT,
RP HOMODIMERIZATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF HIS-156.
RX PubMed=17028579; DOI=10.1038/ncb1487;
RA Choi S.Y., Huang P., Jenkins G.M., Chan D.C., Schiller J., Frohman M.A.;
RT "A common lipid links Mfn-mediated mitochondrial fusion and SNARE-regulated
RT exocytosis.";
RL Nat. Cell Biol. 8:1255-1262(2006).
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=21397847; DOI=10.1016/j.devcel.2011.01.005;
RA Watanabe T., Chuma S., Yamamoto Y., Kuramochi-Miyagawa S., Totoki Y.,
RA Toyoda A., Hoki Y., Fujiyama A., Shibata T., Sado T., Noce T., Nakano T.,
RA Nakatsuji N., Lin H., Sasaki H.;
RT "MITOPLD is a mitochondrial protein essential for nuage formation and piRNA
RT biogenesis in the mouse germline.";
RL Dev. Cell 20:364-375(2011).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF HIS-156.
RX PubMed=21397848; DOI=10.1016/j.devcel.2011.01.004;
RA Huang H., Gao Q., Peng X., Choi S.Y., Sarma K., Ren H., Morris A.J.,
RA Frohman M.A.;
RT "piRNA-associated germline nuage formation and spermatogenesis require
RT MitoPLD profusogenic mitochondrial-surface lipid signaling.";
RL Dev. Cell 20:376-387(2011).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=24599962; DOI=10.1074/jbc.m113.531921;
RA Baba T., Kashiwagi Y., Arimitsu N., Kogure T., Edo A., Maruyama T.,
RA Nakao K., Nakanishi H., Kinoshita M., Frohman M.A., Yamamoto A., Tani K.;
RT "Phosphatidic acid (PA)-preferring phospholipase A1 regulates mitochondrial
RT dynamics.";
RL J. Biol. Chem. 289:11497-11511(2014).
RN [8]
RP FUNCTION.
RX PubMed=26678338; DOI=10.1016/j.ccell.2015.10.013;
RA von Eyss B., Jaenicke L.A., Kortlever R.M., Royla N., Wiese K.E.,
RA Letschert S., McDuffus L.A., Sauer M., Rosenwald A., Evan G.I., Kempa S.,
RA Eilers M.;
RT "A MYC-Driven Change in Mitochondrial Dynamics Limits YAP/TAZ Function in
RT Mammary Epithelial Cells and Breast Cancer.";
RL Cancer Cell 28:743-757(2015).
RN [9]
RP FUNCTION, AND INTERACTION WITH MIGA1 AND MIGA2.
RX PubMed=26711011; DOI=10.1016/j.molcel.2015.11.017;
RA Zhang Y., Liu X., Bai J., Tian X., Zhao X., Liu W., Duan X., Shang W.,
RA Fan H.Y., Tong C.;
RT "Mitoguardin regulates mitochondrial fusion through MitoPLD and is required
RT for neuronal homeostasis.";
RL Mol. Cell 61:111-124(2016).
RN [10]
RP FUNCTION.
RX PubMed=28063496; DOI=10.1016/bs.mie.2016.09.041;
RA Philip F., Ha E.E., Seeliger M.A., Frohman M.A.;
RT "Measuring Phospholipase D Enzymatic Activity Through Biochemical and
RT Imaging Methods.";
RL Methods Enzymol. 583:309-325(2017).
RN [11]
RP INTERACTION WITH GK2.
RX PubMed=28852571; DOI=10.1038/celldisc.2017.30;
RA Chen Y., Liang P., Huang Y., Li M., Zhang X., Ding C., Feng J., Zhang Z.,
RA Zhang X., Gao Y., Zhang Q., Cao S., Zheng H., Liu D., Songyang Z.,
RA Huang J.;
RT "Glycerol kinase-like proteins cooperate with Pld6 in regulating sperm
RT mitochondrial sheath formation and male fertility.";
RL Cell Discov. 3:17030-17030(2017).
CC -!- FUNCTION: Presents phospholipase and nuclease activities, depending on
CC the different physiological conditions (PubMed:17028579,
CC PubMed:24599962, PubMed:21397847, PubMed:28063496). Interaction with
CC Mitoguardin (MIGA1 or MIGA2) affects the dimer conformation,
CC facilitating the lipase activity over the nuclease activity
CC (PubMed:26711011). Plays a key role in mitochondrial fusion and fission
CC via its phospholipase activity (PubMed:17028579, PubMed:24599962,
CC PubMed:26678338). In its phospholipase role, it uses the mitochondrial
CC lipid cardiolipin as substrate to generate phosphatidate (PA or 1,2-
CC diacyl-sn-glycero-3-phosphate), a second messenger signaling lipid
CC (PubMed:17028579, PubMed:24599962, PubMed:26711011). Production of PA
CC facilitates Mitofusin-mediated fusion, whereas the cleavage of PA by
CC the Lipin family of phosphatases produces diacylgycerol (DAG) which
CC promotes mitochondrial fission (PubMed:24599962). Both Lipin and DAG
CC regulate mitochondrial dynamics and membrane fusion/fission, important
CC processes for adapting mitochondrial metabolism to changes in cell
CC physiology. Mitochondrial fusion enables cells to cope with the
CC increased nucleotide demand during DNA synthesis (PubMed:26678338).
CC Mitochondrial function and dynamics are closely associated with
CC biological processes such as cell growth, proliferation, and
CC differentiation (PubMed:21397848). Mediator of MYC activity, promotes
CC mitochondrial fusion and activates AMPK which in turn inhibits YAP/TAZ,
CC thereby inducing cell growth and proliferation (PubMed:26678338). The
CC endonuclease activity plays a critical role in PIWI-interacting RNA
CC (piRNA) biogenesis during spermatogenesis (PubMed:21397847,
CC PubMed:21397848). Implicated in spermatogenesis and sperm fertility in
CC testicular germ cells, its single strand-specific nuclease activity is
CC critical for the biogenesis/maturation of PIWI-interacting RNA (piRNA).
CC MOV10L1 selectively binds to piRNA precursors and funnels them to the
CC endonuclease that catalyzes the first cleavage step of piRNA processing
CC to generate piRNA intermediate fragments that are subsequently loaded
CC to Piwi proteins. Cleaves either DNA or RNA substrates with similar
CC affinity, producing a 5' phosphate end, in this way it participates in
CC the processing of primary piRNA transcripts. piRNAs provide essential
CC protection against the activity of mobile genetic elements. piRNA-
CC mediated transposon silencing is thus critical for maintaining genome
CC stability, in particular in germline cells when transposons are
CC mobilized as a consequence of wide-spread genomic demethylation (By
CC similarity). PA may act as signaling molecule in the
CC recognition/transport of the precursor RNAs of primary piRNAs
CC (PubMed:21397847). Interacts with tesmin in testes, suggesting a role
CC in spermatogenesis via association with its interacting partner (By
CC similarity). {ECO:0000250|UniProtKB:Q5SWZ9,
CC ECO:0000269|PubMed:17028579, ECO:0000269|PubMed:21397847,
CC ECO:0000269|PubMed:21397848, ECO:0000269|PubMed:24599962,
CC ECO:0000269|PubMed:26678338, ECO:0000269|PubMed:26711011,
CC ECO:0000269|PubMed:28063496}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a cardiolipin + H2O = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-
CC glycerol) + a 1,2-diacyl-sn-glycero-3-phosphate + H(+);
CC Xref=Rhea:RHEA:44884, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58608, ChEBI:CHEBI:62237, ChEBI:CHEBI:64716;
CC Evidence={ECO:0000269|PubMed:17028579, ECO:0000269|PubMed:24599962,
CC ECO:0000269|PubMed:26711011};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44885;
CC Evidence={ECO:0000269|PubMed:17028579, ECO:0000269|PubMed:24599962,
CC ECO:0000269|PubMed:26711011};
CC -!- ACTIVITY REGULATION: MYC stimulates its phospholipase activity
CC (PubMed:26678338). MIGA1 and MIGA2 increase PLD6 self-association
CC affinity and affects the homodimer conformation facilitating its
CC phospholipase activity over the nuclease activity (PubMed:26711011).
CC Single stranded DNA (ssDNA) hydrolase activity does not depend upon,
CC but is stimulated by the presence of Ca(2+) and Mn(2+) (By similarity).
CC {ECO:0000250|UniProtKB:Q5SWZ9, ECO:0000269|PubMed:26678338,
CC ECO:0000269|PubMed:26711011}.
CC -!- SUBUNIT: Homodimer (PubMed:17028579). Interacts with MOV10L1 (By
CC similarity). Interacts with MIGA1 and MIGA2; possibly facilitating
CC homodimer formation (PubMed:26711011). Interacts with GK2
CC (PubMed:28852571). {ECO:0000250|UniProtKB:Q5SWZ9,
CC ECO:0000269|PubMed:17028579, ECO:0000269|PubMed:26711011,
CC ECO:0000269|PubMed:28852571}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:17028579}; Single-pass membrane protein
CC {ECO:0000269|PubMed:17028579}. Golgi apparatus
CC {ECO:0000250|UniProtKB:Q5SWZ9}. Note=Localization in the mitochondrial
CC outer membrane is found in different cell types where phospholipase is
CC the predominant activity, however, in pachytene spermatocytes and
CC spermatids of mouse testes where nuclease activity is predominant,
CC localization is restricted to the Golgi, suggesting this enzyme is
CC localized in different subcellular compartments depending on the role
CC (phospholipase or nuclease) it needs to play in each cell type and
CC developmental stage. {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in testis and ovary, but
CC not limited to gonads (at protein level) (PubMed:17028579,
CC PubMed:21397847). It is also found in brain, heart, pituitary gland,
CC prostate, pancreas, thyroid, bone marrow, lung and muscle
CC (PubMed:21397847). {ECO:0000269|PubMed:17028579,
CC ECO:0000269|PubMed:21397847}.
CC -!- DOMAIN: In contrast to other members of the phospholipase D family,
CC contains only one PLD phosphodiesterase domain, suggesting that it has
CC a single half-catalytic and requires homodimerization to form a
CC complete active site. {ECO:0000269|PubMed:17028579}.
CC -!- SIMILARITY: Belongs to the phospholipase D family. MitoPLD/Zucchini
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: Evidence for subcellular location in the Golgi was determined
CC in pachytene spermatocytes and spermatids in mouse testes. They observe
CC that the ectopically expressed PLD6 protein was localized to the
CC mitochondria in PLD6-transfected cells. Authors claim a possible
CC explanation for the contradictory results is that previous studies have
CC reported the localization of exogenous PLD6, but not endogenous PLD6,
CC in cultured cells. The reason for differences observed in subcellular
CC localization of exogenous and endogenous PLD6 is not clear but one
CC attributable reason may be that different types of anti-PLD6 antibodies
CC have been used in previous studies. {ECO:0000250|UniProtKB:Q5SWZ9}.
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DR EMBL; AK090899; BAC03541.1; -; mRNA.
DR EMBL; AC055811; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC031263; AAH31263.1; -; mRNA.
DR CCDS; CCDS11182.1; -.
DR RefSeq; NP_849158.2; NM_178836.3.
DR AlphaFoldDB; Q8N2A8; -.
DR SMR; Q8N2A8; -.
DR BioGRID; 128367; 49.
DR IntAct; Q8N2A8; 12.
DR STRING; 9606.ENSP00000317177; -.
DR SwissLipids; SLP:000001047; -.
DR iPTMnet; Q8N2A8; -.
DR PhosphoSitePlus; Q8N2A8; -.
DR SwissPalm; Q8N2A8; -.
DR BioMuta; PLD6; -.
DR DMDM; 74728697; -.
DR EPD; Q8N2A8; -.
DR MassIVE; Q8N2A8; -.
DR MaxQB; Q8N2A8; -.
DR PaxDb; Q8N2A8; -.
DR PeptideAtlas; Q8N2A8; -.
DR PRIDE; Q8N2A8; -.
DR ProteomicsDB; 71671; -.
DR Antibodypedia; 63312; 92 antibodies from 21 providers.
DR DNASU; 201164; -.
DR Ensembl; ENST00000321560.4; ENSP00000317177.3; ENSG00000179598.6.
DR GeneID; 201164; -.
DR KEGG; hsa:201164; -.
DR MANE-Select; ENST00000321560.4; ENSP00000317177.3; NM_178836.4; NP_849158.2.
DR UCSC; uc002gqz.4; human.
DR CTD; 201164; -.
DR DisGeNET; 201164; -.
DR GeneCards; PLD6; -.
DR HGNC; HGNC:30447; PLD6.
DR HPA; ENSG00000179598; Tissue enhanced (testis).
DR MIM; 614960; gene.
DR neXtProt; NX_Q8N2A8; -.
DR OpenTargets; ENSG00000179598; -.
DR PharmGKB; PA164724625; -.
DR VEuPathDB; HostDB:ENSG00000179598; -.
DR eggNOG; ENOG502RXG9; Eukaryota.
DR GeneTree; ENSGT00390000004368; -.
DR HOGENOM; CLU_080814_0_1_1; -.
DR InParanoid; Q8N2A8; -.
DR OMA; QPFIKEF; -.
DR OrthoDB; 1489926at2759; -.
DR PhylomeDB; Q8N2A8; -.
DR TreeFam; TF332817; -.
DR PathwayCommons; Q8N2A8; -.
DR Reactome; R-HSA-1483148; Synthesis of PG.
DR Reactome; R-HSA-1483166; Synthesis of PA.
DR Reactome; R-HSA-5601884; PIWI-interacting RNA (piRNA) biogenesis.
DR SignaLink; Q8N2A8; -.
DR BioGRID-ORCS; 201164; 8 hits in 1085 CRISPR screens.
DR ChiTaRS; PLD6; human.
DR GenomeRNAi; 201164; -.
DR Pharos; Q8N2A8; Tbio.
DR PRO; PR:Q8N2A8; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q8N2A8; protein.
DR Bgee; ENSG00000179598; Expressed in oviduct epithelium and 146 other tissues.
DR Genevisible; Q8N2A8; HS.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0035755; F:cardiolipin hydrolase activity; IDA:UniProtKB.
DR GO; GO:0016891; F:endoribonuclease activity, producing 5'-phosphomonoesters; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0043046; P:DNA methylation involved in gamete generation; ISS:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; ISS:UniProtKB.
DR GO; GO:0008053; P:mitochondrial fusion; IMP:UniProtKB.
DR GO; GO:0030719; P:P granule organization; ISS:UniProtKB.
DR GO; GO:0034587; P:piRNA metabolic process; ISS:UniProtKB.
DR GO; GO:0010636; P:positive regulation of mitochondrial fusion; IDA:MGI.
DR GO; GO:0007286; P:spermatid development; ISS:UniProtKB.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR Pfam; PF13091; PLDc_2; 1.
DR SMART; SM00155; PLDc; 1.
DR PROSITE; PS50035; PLD; 1.
PE 1: Evidence at protein level;
KW Differentiation; Endonuclease; Golgi apparatus; Hydrolase;
KW Lipid degradation; Lipid metabolism; Meiosis; Membrane; Metal-binding;
KW Mitochondrion; Mitochondrion outer membrane; Nuclease; Reference proteome;
KW Spermatogenesis; Transmembrane; Transmembrane helix; Zinc; Zinc-finger.
FT CHAIN 1..252
FT /note="Mitochondrial cardiolipin hydrolase"
FT /id="PRO_0000325910"
FT TOPO_DOM 1..4
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 5..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..252
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 151..178
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ZN_FING 45..78
FT /note="C3H1-type; atypical"
FT REGION 1..39
FT /note="Required for mitochondrial localization"
FT ACT_SITE 156
FT /evidence="ECO:0000305"
FT ACT_SITE 158
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 163
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT VARIANT 42
FT /note="L -> P (in dbSNP:rs17856924)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_039951"
FT VARIANT 108
FT /note="R -> H (in dbSNP:rs11551966)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_039952"
FT MUTAGEN 156
FT /note="H->N: Mitochondrial fragmentation. No apoptosis, no
FT alterations of cell homeostasis."
FT /evidence="ECO:0000269|PubMed:17028579,
FT ECO:0000269|PubMed:21397848"
SQ SEQUENCE 252 AA; 28273 MW; CE3A205C1D42B497 CRC64;
MGRLSWQVAA AAAVGLALTL EALPWVLRWL RSRRRRPRRE ALFFPSQVTC TEALLRAPGA
ELAELPEGCP CGLPHGESAL SRLLRALLAA RASLDLCLFA FSSPQLGRAV QLLHQRGVRV
RVVTDCDYMA LNGSQIGLLR KAGIQVRHDQ DPGYMHHKFA IVDKRVLITG SLNWTTQAIQ
NNRENVLITE DDEYVRLFLE EFERIWEQFN PTKYTFFPPK KSHGSCAPPV SRAGGRLLSW
HRTCGTSSES QT
