ATG2_SCHPO
ID ATG2_SCHPO Reviewed; 1646 AA.
AC O94649; O94434;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 4.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Autophagy-related protein 2;
DE AltName: Full=Meiotically up-regulated gene 36 protein;
GN Name=atg2; Synonyms=mug36; ORFNames=SPBC31E1.01c, SPBC660.18c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP FUNCTION IN SPORULATION.
RX PubMed=16303567; DOI=10.1016/j.cub.2005.10.038;
RA Martin-Castellanos C., Blanco M., Rozalen A.E., Perez-Hidalgo L.,
RA Garcia A.I., Conde F., Mata J., Ellermeier C., Davis L., San-Segundo P.,
RA Smith G.R., Moreno S.;
RT "A large-scale screen in S. pombe identifies seven novel genes required for
RT critical meiotic events.";
RL Curr. Biol. 15:2056-2062(2005).
RN [3]
RP DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=23950735; DOI=10.1371/journal.pgen.1003715;
RA Sun L.L., Li M., Suo F., Liu X.M., Shen E.Z., Yang B., Dong M.Q., He W.Z.,
RA Du L.L.;
RT "Global analysis of fission yeast mating genes reveals new autophagy
RT factors.";
RL PLoS Genet. 9:E1003715-E1003715(2013).
RN [4] {ECO:0007744|PDB:6A9E, ECO:0007744|PDB:6A9J}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 21-240, FUNCTION, CATALYTIC
RP ACTIVITY, AND DOMAIN.
RX PubMed=30911189; DOI=10.1038/s41594-019-0203-4;
RA Osawa T., Kotani T., Kawaoka T., Hirata E., Suzuki K., Nakatogawa H.,
RA Ohsumi Y., Noda N.N.;
RT "Atg2 mediates direct lipid transfer between membranes for autophagosome
RT formation.";
RL Nat. Struct. Mol. Biol. 26:281-288(2019).
CC -!- FUNCTION: Lipid transfer protein required for autophagosomes completion
CC and peroxisome degradation (PubMed:16303567, PubMed:30911189). Tethers
CC the edge of the isolation membrane (IM) to the endoplasmic reticulum
CC (ER) and mediates direct lipid transfer from ER to IM for IM expansion
CC (PubMed:30911189). Atg2 binds to the ER exit site (ERES), which is the
CC membrane source for autophagosome formation, using basic residues in
CC its N-terminal region (NR) and to the expanding edge of the IM through
CC its C-terminal region (PubMed:30911189). The latter binding is assisted
CC by an atg18-PtdIns3P interaction (PubMed:30911189). Atg2 then extracts
CC phospholipids from the membrane source using its NR and transfers them
CC to atg9 to the IM through its predicted beta-sheet-rich structure for
CC membrane expansion (PubMed:30911189). Atg2 is also involved in the
CC recruitment of lipids to a restricted region close to the vacuole,
CC termed the vacuole-isolation membrane contact site (VICS), which is
CC also essential for autophagosome formation (By similarity). May have a
CC role in sporulation (PubMed:16303567). {ECO:0000250|UniProtKB:P53855,
CC ECO:0000269|PubMed:16303567, ECO:0000269|PubMed:30911189}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-
CC sn-glycero-3-phosphocholine(out); Xref=Rhea:RHEA:38571,
CC ChEBI:CHEBI:57643; Evidence={ECO:0000269|PubMed:30911189};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) = a 1,2-diacyl-
CC sn-glycero-3-phospho-L-serine(out); Xref=Rhea:RHEA:38663,
CC ChEBI:CHEBI:57262; Evidence={ECO:0000269|PubMed:30911189};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) = a 1,2-
CC diacyl-sn-glycero-3-phosphoethanolamine(out); Xref=Rhea:RHEA:38895,
CC ChEBI:CHEBI:64612; Evidence={ECO:0000269|PubMed:30911189};
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC {ECO:0000269|PubMed:23950735}; Peripheral membrane protein
CC {ECO:0000269|PubMed:23950735}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P53855}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P53855}. Note=Localizes to the IM-ERES contact
CC site. {ECO:0000250|UniProtKB:P53855}.
CC -!- DOMAIN: The N-terminal region (NR) associates with the endoplasmic
CC reticulum (ER) and is responsible for the formation of the isolation
CC membrane at the PAS. {ECO:0000269|PubMed:30911189}.
CC -!- DOMAIN: The amphipathic helix in the C-terminal region binds to
CC membranes and facilitates atg18 binding to PtdIns3P to target the atg2-
CC atg18 complex to the PAS. {ECO:0000269|PubMed:30911189}.
CC -!- DISRUPTION PHENOTYPE: Impairs atg8-processing.
CC {ECO:0000269|PubMed:23950735}.
CC -!- SIMILARITY: Belongs to the ATG2 family. {ECO:0000305}.
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DR EMBL; CU329671; CAA22538.2; -; Genomic_DNA.
DR PIR; T40198; T40198.
DR RefSeq; XP_001713120.1; XM_001713068.2.
DR PDB; 6A9E; X-ray; 3.21 A; A/B=21-240.
DR PDB; 6A9J; X-ray; 2.70 A; A/B=21-240.
DR PDBsum; 6A9E; -.
DR PDBsum; 6A9J; -.
DR AlphaFoldDB; O94649; -.
DR SMR; O94649; -.
DR BioGRID; 280290; 2.
DR STRING; 4896.SPBC31E1.01c.1; -.
DR iPTMnet; O94649; -.
DR MaxQB; O94649; -.
DR PaxDb; O94649; -.
DR PRIDE; O94649; -.
DR EnsemblFungi; SPBC31E1.01c.1; SPBC31E1.01c.1:pep; SPBC31E1.01c.
DR PomBase; SPBC31E1.01c; atg2.
DR VEuPathDB; FungiDB:SPBC31E1.01c; -.
DR eggNOG; KOG2993; Eukaryota.
DR HOGENOM; CLU_244286_0_0_1; -.
DR InParanoid; O94649; -.
DR OMA; NSSSWLW; -.
DR PRO; PR:O94649; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
DR GO; GO:0000407; C:phagophore assembly site; IDA:PomBase.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0120013; F:lipid transfer activity; TAS:PomBase.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IBA:GO_Central.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; IMP:PomBase.
DR GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0030242; P:autophagy of peroxisome; IEA:InterPro.
DR GO; GO:0120009; P:intermembrane lipid transfer; TAS:PomBase.
DR GO; GO:0044805; P:late nucleophagy; IBA:GO_Central.
DR GO; GO:0016236; P:macroautophagy; IMP:PomBase.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IBA:GO_Central.
DR GO; GO:0061709; P:reticulophagy; IBA:GO_Central.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR InterPro; IPR026849; ATG2.
DR InterPro; IPR026885; ATG2_CAD_motif.
DR InterPro; IPR026886; ATG2_fungi/plants.
DR InterPro; IPR015412; Autophagy-rel_C.
DR InterPro; IPR026854; VPS13-like_N.
DR PANTHER; PTHR13190; PTHR13190; 2.
DR PANTHER; PTHR13190:SF1; PTHR13190:SF1; 2.
DR Pfam; PF13329; ATG2_CAD; 1.
DR Pfam; PF09333; ATG_C; 1.
DR Pfam; PF12624; Chorein_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autophagy; Endoplasmic reticulum; Lipid transport; Meiosis;
KW Membrane; Reference proteome; Sporulation; Transport.
FT CHAIN 1..1646
FT /note="Autophagy-related protein 2"
FT /id="PRO_0000297691"
FT DOMAIN 26..121
FT /note="Chorein N-terminal"
FT /evidence="ECO:0000255"
FT REGION 16..35
FT /note="ER-targeting domain"
FT /evidence="ECO:0000305|PubMed:30911189"
FT REGION 1465..1490
FT /note="PAS-targeting domain"
FT /evidence="ECO:0000305|PubMed:30911189"
FT HELIX 21..39
FT /evidence="ECO:0007829|PDB:6A9J"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:6A9J"
FT HELIX 46..54
FT /evidence="ECO:0007829|PDB:6A9J"
FT STRAND 55..62
FT /evidence="ECO:0007829|PDB:6A9J"
FT HELIX 67..73
FT /evidence="ECO:0007829|PDB:6A9J"
FT STRAND 80..93
FT /evidence="ECO:0007829|PDB:6A9J"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:6A9J"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:6A9J"
FT STRAND 103..115
FT /evidence="ECO:0007829|PDB:6A9J"
FT HELIX 139..148
FT /evidence="ECO:0007829|PDB:6A9J"
FT HELIX 150..160
FT /evidence="ECO:0007829|PDB:6A9J"
FT HELIX 174..184
FT /evidence="ECO:0007829|PDB:6A9J"
FT STRAND 185..196
FT /evidence="ECO:0007829|PDB:6A9J"
FT STRAND 205..216
FT /evidence="ECO:0007829|PDB:6A9J"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:6A9J"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:6A9J"
SQ SEQUENCE 1646 AA; 184308 MW; EB02D98980EF1D5F CRC64;
MRLPSWLKNS SSWLWTAALS RTVQRRLLAF ALRKLIGSIL LENVQPEDID ILFSKGVLML
SNLQLNCSFL NAVVSLPMIN FTKGTLRRLI LRLNVTDIVN LNVELEVNGL SLEIELVPPD
ESLSSTTYED APSQLDILDN VVEYMNKTAS QDFEDEVINE GLESEIDGSS HNLLDSILQK
CLASTSVLMQ DALVYIGTAN MSTRLEAKLD FMSFSSVKSN STSRLLNING ITVSMVRPIS
KSNAGSSSPP RSEESFVSMD SSSSIVEGFE NDLSPSQVTL NESSIISSNR EEESFYSVHD
SVTQKKTRTS WLIFQCSGEF RLVFSIESSN LLVIESHVPS CVLNINSQVI AFLLYLYGYF
LPAPSTPGFS SNKPPLTMLQ LDIHISSVQI LTHCKLPESQ DFSMHNDVDE LLHTIPSNGA
VFEMKINQIQ IFNDNNDIDE LTMTFSDLDI FMDSVTLVSF GKSLQSPCSL IFKKLERIVS
LFIHIPGGEI SLPLGKALLL QESFVEFTND ISNLQNFLSN SDPFKRSIQE TFEAPKPFEV
EMNQPSFEII ALFDELQLQI LNELSTQSLY KLTLRVSHLQ FTRKSTGSLS SVLIFVKKIG
CQSELFNCEN SDWTKVSSST AFHLSNSLFE THDTTGTSNF AVSIQQEKHY YPVFQPAPTE
FSYPEKHFYF AVDNFNVFIS KEVVRLFKTL YETIASSLVT PVTPNKLVTS DYKNVLKIRT
RTFSLSLLND DGSSFALKCI RIKHYMCWAG AQLISLSLRL YNVSAEYLSE SLEILPVVSF
IRNLRNDEKY LLNADFSYAL KRSSGSNDNT IFVKITDLGY EHYPTCPWIS DLLKTYFPQD
PEVPFLAFPD FPFNIKLDLR ESIIGLNPRT LEAKLLLYLK SLDVEIDALV ASNPLNIRIM
AAETVVYIID KLNQSVLEGK TSVLKREILN SSLHFPGLSI KDTIEFVVKS LGYVEISQLK
NLTLSLVVNA EEGVFSTLIT VDNLDAQVQS CADSTELLIK VLSDLGSTED EEISDCYLAL
PIEDYAKSLT EVDYNFFENR GIDYKSNPTE QSTVLVSSDN DISSQEIKIV DDYYISSNEH
STHASDLASV SSEEFVIDDG SSSIIDISDE LQDESSSRDS LKKGIELIED YYLSQSTSKL
ESSVEGKNYL LKVKFKDINV NWDLHDGYDW EATRATISSA IEKLCDSSSQ NDKISPEAKT
LLFQSIVIKS FSKVGRLNIN HVSEPIDSDE FADYLSKSIS YHLRLGKSKS KKIGIEIKDL
QGSFTVYADS NEPNAVLNDL DIGLKDLIIY DHLSTSTWNK FFGRDSRSPS SKNRNQHMNA
QIVTVRPLPE LNNRELRLEF SVLPCKMYID QDTLDFLIRF LTFQTPSSSE TLNTEPDLPF
FQSICINATH VTIDFKFKSA DKVGLRSGKL PDLGSLIVMQ GSEVFLRQLQ IYGLSGAEEF
LNALLNVWLQ DIRNNQLSKV LNGVVPIRTM FTVGRGIKDI FVSPVRGLQG NHSVGSFRHG
IIKFTEKYVN DFLSLNAQGA TGTHSLLRQA ESYLERGSNA SASASRARSY YAEQPETIEQ
GLRQGYSGLK QGLLGAKSTL MGLPRETRSH KSLGGVAQTV GRKVPLIVLQ PMIGATEAVS
KTLLGLSNSL QPQRRQDMRE KYKRPG
