ADT4_MOUSE
ID ADT4_MOUSE Reviewed; 320 AA.
AC Q3V132; Q80W28;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=ADP/ATP translocase 4 {ECO:0000305};
DE AltName: Full=ADP,ATP carrier protein 4 {ECO:0000303|PubMed:17137571};
DE AltName: Full=Adenine nucleotide translocator 4 {ECO:0000303|PubMed:17681941};
DE Short=ANT 4 {ECO:0000303|PubMed:17681941};
DE AltName: Full=Solute carrier family 25 member 31 {ECO:0000305};
DE AltName: Full=Sperm flagellar energy carrier protein {ECO:0000303|PubMed:17137571};
GN Name=Slc25a31 {ECO:0000303|PubMed:18667754, ECO:0000312|MGI:MGI:1920583};
GN Synonyms=Aac4 {ECO:0000303|PubMed:17137571},
GN Ant4 {ECO:0000303|PubMed:17681941}, Sfec {ECO:0000303|PubMed:17137571};
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 [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17137571; DOI=10.1016/j.ydbio.2006.10.004;
RA Kim Y.-H., Haidl G., Schaefer M., Egner U., Mandal A., Herr J.C.;
RT "Compartmentalization of a unique ADP/ATP carrier protein SFEC (sperm
RT flagellar energy carrier, AAC4) with glycolytic enzymes in the fibrous
RT sheath of the human sperm flagellar principal piece.";
RL Dev. Biol. 302:463-476(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 TISSUE SPECIFICITY.
RX PubMed=16051982; DOI=10.1634/stemcells.2005-0119;
RA Rodic N., Oka M., Hamazaki T., Murawski M.R., Jorgensen M., Maatouk D.M.,
RA Resnick J.L., Li E., Terada N.;
RT "DNA methylation is required for silencing of ant4, an adenine nucleotide
RT translocase selectively expressed in mouse embryonic stem cells and germ
RT cells.";
RL Stem Cells 23:1314-1323(2005).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=17681941; DOI=10.1074/jbc.m704386200;
RA Brower J.V., Rodic N., Seki T., Jorgensen M., Fliess N., Yachnis A.T.,
RA McCarrey J.R., Oh S.P., Terada N.;
RT "Evolutionarily conserved mammalian adenine nucleotide translocase 4 is
RT essential for spermatogenesis.";
RL J. Biol. Chem. 282:29658-29666(2007).
RN [6]
RP INDUCTION.
RX PubMed=18667754; DOI=10.1095/biolreprod.108.067645;
RA Kehoe S.M., Oka M., Hankowski K.E., Reichert N., Garcia S., McCarrey J.R.,
RA Gaubatz S., Terada N.;
RT "A conserved E2F6-binding element in murine meiosis-specific gene
RT promoters.";
RL Biol. Reprod. 79:921-930(2008).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19556438; DOI=10.1530/rep-09-0201;
RA Brower J.V., Lim C.H., Jorgensen M., Oh S.P., Terada N.;
RT "Adenine nucleotide translocase 4 deficiency leads to early meiotic arrest
RT of murine male germ cells.";
RL Reproduction 138:463-470(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=31489369; DOI=10.1126/sciadv.aaw4597;
RA Karch J., Bround M.J., Khalil H., Sargent M.A., Latchman N., Terada N.,
RA Peixoto P.M., Molkentin J.D.;
RT "Inhibition of mitochondrial permeability transition by deletion of the ANT
RT family and CypD.";
RL Sci. Adv. 5:eaaw4597-eaaw4597(2019).
CC -!- FUNCTION: ADP:ATP antiporter that mediates import of ADP into the
CC mitochondrial matrix for ATP synthesis, and export of ATP out to fuel
CC the cell (By similarity). Cycles between the cytoplasmic-open state (c-
CC state) and the matrix-open state (m-state): operates by the alternating
CC access mechanism with a single substrate-binding site intermittently
CC exposed to either the cytosolic (c-state) or matrix (m-state) side of
CC the inner mitochondrial membrane (By similarity). Specifically required
CC during spermatogenesis, probably to mediate ADP:ATP exchange in
CC spermatocytes (PubMed:17137571, PubMed:17681941, PubMed:19556438).
CC Large ATP supplies from mitochondria may be critical for normal
CC progression of spermatogenesis during early stages of meiotic prophase
CC I, including DNA double-strand break repair and chromosomal synapsis
CC (PubMed:19556438). In addition to its ADP:ATP antiporter activity, also
CC involved in mitochondrial uncoupling and mitochondrial permeability
CC transition pore (mPTP) activity (PubMed:31489369). Plays a role in
CC mitochondrial uncoupling by acting as a proton transporter: proton
CC transport uncouples the proton flows via the electron transport chain
CC and ATP synthase to reduce the efficiency of ATP production and cause
CC mitochondrial thermogenesis (By similarity). Proton transporter
CC activity is inhibited by ADP:ATP antiporter activity, suggesting that
CC SLC25A31/ANT4 acts as a master regulator of mitochondrial energy output
CC by maintaining a delicate balance between ATP production (ADP:ATP
CC antiporter activity) and thermogenesis (proton transporter activity)
CC (By similarity). Proton transporter activity requires free fatty acids
CC as cofactor, but does not transport it (By similarity). Also plays a
CC key role in mPTP opening, a non-specific pore that enables free passage
CC of the mitochondrial membranes to solutes of up to 1.5 kDa, and which
CC contributes to cell death (PubMed:31489369). It is however unclear if
CC SLC25A31/ANT4 constitutes a pore-forming component of mPTP or regulates
CC it (PubMed:31489369). {ECO:0000250|UniProtKB:G2QNH0,
CC ECO:0000250|UniProtKB:P48962, ECO:0000269|PubMed:17137571,
CC ECO:0000269|PubMed:17681941, ECO:0000269|PubMed:19556438,
CC ECO:0000269|PubMed:31489369}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP(in) + ATP(out) = ADP(out) + ATP(in); Xref=Rhea:RHEA:34999,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:P48962};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) = H(+)(out); Xref=Rhea:RHEA:34979, ChEBI:CHEBI:15378;
CC Evidence={ECO:0000250|UniProtKB:P48962};
CC -!- ACTIVITY REGULATION: The matrix-open state (m-state) is inhibited by
CC the membrane-permeable bongkrekic acid (BKA). The cytoplasmic-open
CC state (c-state) is inhibited by the membrane-impermeable toxic
CC inhibitor carboxyatractyloside (CATR) (By similarity). Proton
CC transporter activity is inhibited by ADP:ATP antiporter activity (By
CC similarity). {ECO:0000250|UniProtKB:G2QNH0,
CC ECO:0000250|UniProtKB:P48962}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:G2QNH0,
CC ECO:0000250|UniProtKB:P02722}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P02722}; Multi-pass membrane protein
CC {ECO:0000255}. Membrane {ECO:0000250|UniProtKB:Q9H0C2}; Multi-pass
CC membrane protein {ECO:0000255}. Cell projection, cilium, flagellum
CC membrane {ECO:0000269|PubMed:17137571}; Multi-pass membrane protein
CC {ECO:0000255}. Note=In sperm flagellum this protein is located in the
CC fibrous sheath, a non-mitochondrial region (By similarity). May
CC localize to non-mitochondrial membranes (By similarity).
CC {ECO:0000250|UniProtKB:Q9H0C2}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in undifferentiated
CC embryonic stem cells and germ cells (PubMed:16051982, PubMed:31489369).
CC Expression is down-regulated after embryonic stem cells differentiation
CC (PubMed:16051982). In adults, only expressed in developing gametes in
CC testis (PubMed:16051982). In testis, expressed at higher level in
CC spermatocytes. Expression is probably associated with entry of the male
CC germ cells into meiosis (PubMed:17681941). Expressed at very low level
CC in Sertoli cells (PubMed:17681941). {ECO:0000269|PubMed:16051982,
CC ECO:0000269|PubMed:17681941, ECO:0000269|PubMed:31489369}.
CC -!- DEVELOPMENTAL STAGE: In testis, expression increases upon transition of
CC premeiotic type B spermatogonia into the early stages of meiosis as
CC represented by preleptotene spermatocytes (PubMed:17681941). Continues
CC to increase through the leptotene and zygotene spermatocyte stages,
CC peaking in early pachytene spermatocytes (PubMed:17681941). Expression
CC decreases in late pachytene spermatocytes and in later round spermatids
CC (PubMed:17681941). {ECO:0000269|PubMed:17681941}.
CC -!- INDUCTION: Expression is repressed by E2F6.
CC {ECO:0000269|PubMed:18667754}.
CC -!- DOMAIN: The transmembrane helices are not perpendicular to the plane of
CC the membrane, but cross the membrane at an angle. Odd-numbered
CC transmembrane helices exhibit a sharp kink, due to the presence of a
CC conserved proline residue. {ECO:0000250|UniProtKB:P02722}.
CC -!- DISRUPTION PHENOTYPE: Male mice display a significant reduction in
CC testicular size and are sterile, due to impaired spermatogenesis
CC (PubMed:17681941). Males show increased levels of apoptosis within the
CC spermatocyte layer of the seminiferous epithelium, accompanied by the
CC absence of spermatids and spermatozoa within the seminiferous
CC epithelium and lumen respectively (PubMed:17681941). Early meiotic
CC arrest: an accumulation of leptotene spermatocytes, a decrease in
CC pachytene spermatocytes and an absence of diplotene spermatocytes are
CC observed in spermatocytes (PubMed:19556438). Deletion of Slc25a4/Ant1,
CC Slc25a5/Ant2 and Slc25a31/Ant4 in liver completely inhibits
CC mitochondrial permeability transition pore (mPTP) (PubMed:31489369).
CC Mice lacking Slc25a4/Ant1, Slc25a5/Ant2, Slc25a31/Ant4 and Ppif lack
CC Ca(2+)-induced mPTP formation (PubMed:31489369).
CC {ECO:0000269|PubMed:17681941, ECO:0000269|PubMed:19556438,
CC ECO:0000269|PubMed:31489369}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; AY550241; AAT42264.1; -; mRNA.
DR EMBL; AK132722; BAE21321.1; -; mRNA.
DR EMBL; BC050810; AAH50810.1; -; mRNA.
DR CCDS; CCDS17326.1; -.
DR RefSeq; NP_848473.2; NM_178386.3.
DR AlphaFoldDB; Q3V132; -.
DR SMR; Q3V132; -.
DR BioGRID; 215933; 6.
DR IntAct; Q3V132; 3.
DR MINT; Q3V132; -.
DR STRING; 10090.ENSMUSP00000088723; -.
DR iPTMnet; Q3V132; -.
DR PhosphoSitePlus; Q3V132; -.
DR jPOST; Q3V132; -.
DR MaxQB; Q3V132; -.
DR PaxDb; Q3V132; -.
DR PRIDE; Q3V132; -.
DR ProteomicsDB; 296191; -.
DR Antibodypedia; 3024; 154 antibodies from 24 providers.
DR DNASU; 73333; -.
DR Ensembl; ENSMUST00000091184; ENSMUSP00000088723; ENSMUSG00000069041.
DR GeneID; 73333; -.
DR KEGG; mmu:73333; -.
DR UCSC; uc008pbi.2; mouse.
DR CTD; 83447; -.
DR MGI; MGI:1920583; Slc25a31.
DR VEuPathDB; HostDB:ENSMUSG00000069041; -.
DR eggNOG; KOG0749; Eukaryota.
DR GeneTree; ENSGT00940000160648; -.
DR HOGENOM; CLU_015166_12_0_1; -.
DR InParanoid; Q3V132; -.
DR OMA; AHCWLVI; -.
DR OrthoDB; 870903at2759; -.
DR PhylomeDB; Q3V132; -.
DR TreeFam; TF300743; -.
DR BioGRID-ORCS; 73333; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Slc25a31; mouse.
DR PRO; PR:Q3V132; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q3V132; protein.
DR Bgee; ENSMUSG00000069041; Expressed in spermatocyte and 26 other tissues.
DR ExpressionAtlas; Q3V132; baseline and differential.
DR Genevisible; Q3V132; MM.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005757; C:mitochondrial permeability transition pore complex; IMP:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005471; F:ATP:ADP antiporter activity; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007141; P:male meiosis I; IMP:UniProtKB.
DR GO; GO:0140021; P:mitochondrial ADP transmembrane transport; IEA:InterPro.
DR GO; GO:1990544; P:mitochondrial ATP transmembrane transport; IBA:GO_Central.
DR GO; GO:1901029; P:negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; IBA:GO_Central.
DR GO; GO:0046902; P:regulation of mitochondrial membrane permeability; IMP:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
DR Gene3D; 1.50.40.10; -; 1.
DR InterPro; IPR002113; ADT_euk_type.
DR InterPro; IPR002067; Mit_carrier.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR PANTHER; PTHR45635; PTHR45635; 1.
DR Pfam; PF00153; Mito_carr; 3.
DR PRINTS; PR00927; ADPTRNSLCASE.
DR PRINTS; PR00926; MITOCARRIER.
DR SUPFAM; SSF103506; SSF103506; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 1: Evidence at protein level;
KW Antiport; Cell membrane; Cell projection; Cilium; Differentiation;
KW Flagellum; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Repeat; Spermatogenesis; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..320
FT /note="ADP/ATP translocase 4"
FT /id="PRO_0000297626"
FT TOPO_DOM 1..20
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT TRANSMEM 21..50
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT TOPO_DOM 51..87
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305"
FT TRANSMEM 88..112
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT TOPO_DOM 113..122
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT TRANSMEM 123..143
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT TOPO_DOM 144..191
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305"
FT TRANSMEM 192..212
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT TOPO_DOM 213..223
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT TRANSMEM 224..244
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT TOPO_DOM 245..284
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305"
FT TRANSMEM 285..302
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT TOPO_DOM 303..320
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT REPEAT 19..111
FT /note="Solcar 1"
FT REPEAT 124..214
FT /note="Solcar 2"
FT REPEAT 221..308
FT /note="Solcar 3"
FT REGION 248..253
FT /note="Important for transport activity"
FT /evidence="ECO:0000250|UniProtKB:P12235"
FT MOTIF 248..253
FT /note="Nucleotide carrier signature motif"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT BINDING 93
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT BINDING 105
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT BINDING 248
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT CONFLICT 38
FT /note="A -> T (in Ref. 1; AAT42264 and 3; AAH50810)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 320 AA; 35258 MW; B718DB4AE6C6B2AA CRC64;
MSNESSKKQS SKKALFDPVS FSKDLLAGGV AAAVSKTAVA PIERVKLLLQ VQASSKQISP
EARYKGMLDC LVRIPREQGF LSYWRGNLAN VIRYFPTQAL NFAFKDKYKE LFMSGVNKEK
QFWRWFLANL ASGGAAGATS LCVVYPLDFA RTRLGVDIGK GPEQRQFTGL GDCIMKIAKS
DGLIGLYQGF GVSVQGIIVY RASYFGAYDT VKGLLPKPKE TPFLVSFIIA QIVTTCSGIL
SYPFDTVRRR MMMQSGESDR QYKGTIDCFL KIYRHEGVPA FFRGAFSNIL RGTGGALVLV
LYDKIKEFLN IDVGGSSSGD
