ATG2B_MOUSE
ID ATG2B_MOUSE Reviewed; 2075 AA.
AC Q80XK6; A0PJL7; Q8BIQ4; Q8BIV0; Q8R1H5; Q9CWK6;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 3.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Autophagy-related protein 2 homolog B;
GN Name=Atg2b {ECO:0000312|MGI:MGI:1923809};
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 [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-797 (ISOFORM 1).
RC STRAIN=C57BL/6J;
RC TISSUE=Embryonic stem cell, Heart, Hippocampus, and Wolffian duct;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Colon, Limb, and Liver;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-379, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-379; SER-839; SER-1007;
RP TYR-1011; SER-1015; SER-1017 AND THR-1021, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and 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).
CC -!- FUNCTION: Lipid transfer protein required for both autophagosome
CC formation and regulation of lipid droplet morphology and dispersion.
CC Tethers the edge of the isolation membrane (IM) to the endoplasmic
CC reticulum (ER) and mediates direct lipid transfer from ER to IM for IM
CC expansion (By similarity). Binds to the ER exit site (ERES), which is
CC the membrane source for autophagosome formation, and extracts
CC phospholipids from the membrane source and transfers them to ATG9
CC (ATG9A or ATG9B) to the IM for membrane expansion (By similarity).
CC Lipid transfer activity is enhanced by WDR45/WIPI4, which promotes
CC ATG2B-association with phosphatidylinositol 3-monophosphate (PI3P)-
CC containing membranes (By similarity). {ECO:0000250|UniProtKB:Q2TAZ0,
CC ECO:0000250|UniProtKB:Q96BY7}.
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:0000250|UniProtKB:Q2TAZ0};
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:0000250|UniProtKB:Q2TAZ0};
CC -!- SUBUNIT: Interacts with WDR45/WIPI4. {ECO:0000250|UniProtKB:Q96BY7}.
CC -!- INTERACTION:
CC Q80XK6; O07177: mak; Xeno; NbExp=3; IntAct=EBI-11566520, EBI-25767633;
CC Q80XK6; O07422: Rv0178; Xeno; NbExp=3; IntAct=EBI-11566520, EBI-25767563;
CC Q80XK6; I6Y946: Rv0925c; Xeno; NbExp=3; IntAct=EBI-11566520, EBI-25767727;
CC Q80XK6; P9WIT1: Rv2280; Xeno; NbExp=3; IntAct=EBI-11566520, EBI-25767539;
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC {ECO:0000250|UniProtKB:Q96BY7}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q96BY7}. Lipid droplet
CC {ECO:0000250|UniProtKB:Q96BY7}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P53855}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P53855}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q80XK6-2; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80XK6-4; Sequence=VSP_035038;
CC Name=3;
CC IsoId=Q80XK6-5; Sequence=VSP_035039;
CC -!- DOMAIN: The chorein N-terminal domain mediates lipid transfer activity.
CC {ECO:0000250|UniProtKB:Q2TAZ0}.
CC -!- SIMILARITY: Belongs to the ATG2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH46427.3; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AK085790; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC28052.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK010577; BAB27040.1; -; mRNA.
DR EMBL; AK032840; BAC28052.1; ALT_INIT; mRNA.
DR EMBL; AK083213; BAC38812.1; -; mRNA.
DR EMBL; AK085790; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC024533; AAH24533.1; -; mRNA.
DR EMBL; BC046427; AAH46427.3; ALT_INIT; mRNA.
DR EMBL; BC062182; AAH62182.1; -; mRNA.
DR CCDS; CCDS36550.1; -. [Q80XK6-2]
DR RefSeq; NP_083930.5; NM_029654.4. [Q80XK6-2]
DR AlphaFoldDB; Q80XK6; -.
DR BioGRID; 218175; 2.
DR IntAct; Q80XK6; 11.
DR MINT; Q80XK6; -.
DR STRING; 10090.ENSMUSP00000037441; -.
DR iPTMnet; Q80XK6; -.
DR PhosphoSitePlus; Q80XK6; -.
DR EPD; Q80XK6; -.
DR jPOST; Q80XK6; -.
DR MaxQB; Q80XK6; -.
DR PaxDb; Q80XK6; -.
DR PeptideAtlas; Q80XK6; -.
DR PRIDE; Q80XK6; -.
DR ProteomicsDB; 265177; -. [Q80XK6-2]
DR ProteomicsDB; 265178; -. [Q80XK6-4]
DR ProteomicsDB; 265179; -. [Q80XK6-5]
DR Antibodypedia; 94; 150 antibodies from 28 providers.
DR DNASU; 76559; -.
DR Ensembl; ENSMUST00000041055; ENSMUSP00000037441; ENSMUSG00000041341. [Q80XK6-2]
DR GeneID; 76559; -.
DR KEGG; mmu:76559; -.
DR UCSC; uc007oyp.2; mouse. [Q80XK6-2]
DR UCSC; uc007oyq.1; mouse. [Q80XK6-5]
DR UCSC; uc029rxu.1; mouse. [Q80XK6-4]
DR CTD; 55102; -.
DR MGI; MGI:1923809; Atg2b.
DR VEuPathDB; HostDB:ENSMUSG00000041341; -.
DR eggNOG; KOG2993; Eukaryota.
DR GeneTree; ENSGT00620000087966; -.
DR HOGENOM; CLU_001781_0_0_1; -.
DR InParanoid; Q80XK6; -.
DR OMA; PFKSAVH; -.
DR OrthoDB; 196897at2759; -.
DR PhylomeDB; Q80XK6; -.
DR TreeFam; TF313482; -.
DR BioGRID-ORCS; 76559; 7 hits in 71 CRISPR screens.
DR ChiTaRS; Atg2b; mouse.
DR PRO; PR:Q80XK6; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q80XK6; protein.
DR Bgee; ENSMUSG00000041341; Expressed in saccule of membranous labyrinth and 235 other tissues.
DR ExpressionAtlas; Q80XK6; baseline and differential.
DR Genevisible; Q80XK6; MM.
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:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0000407; C:phagophore assembly site; IBA:GO_Central.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0120013; F:lipid transfer activity; ISO:MGI.
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:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0044805; P:late nucleophagy; IBA:GO_Central.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IBA:GO_Central.
DR GO; GO:0061709; P:reticulophagy; IBA:GO_Central.
DR InterPro; IPR026849; ATG2.
DR InterPro; IPR015412; Autophagy-rel_C.
DR InterPro; IPR026854; VPS13-like_N.
DR PANTHER; PTHR13190; PTHR13190; 1.
DR Pfam; PF09333; ATG_C; 1.
DR Pfam; PF12624; Chorein_N; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Autophagy; Endoplasmic reticulum; Lipid droplet;
KW Lipid transport; Membrane; Phosphoprotein; Reference proteome; Transport.
FT CHAIN 1..2075
FT /note="Autophagy-related protein 2 homolog B"
FT /id="PRO_0000089910"
FT DOMAIN 13..107
FT /note="Chorein N-terminal"
FT /evidence="ECO:0000255"
FT REGION 1373..1403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1570..1593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1759..1792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2055..2075
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1573..1590
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2059..2075
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96BY7"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96BY7"
FT MOD_RES 839
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 885
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96BY7"
FT MOD_RES 898
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96BY7"
FT MOD_RES 1007
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1011
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1015
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1017
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1021
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1525
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96BY7"
FT VAR_SEQ 1..1890
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_035038"
FT VAR_SEQ 577..2075
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_035039"
FT CONFLICT 128
FT /note="A -> T (in Ref. 2; BAC28052)"
FT /evidence="ECO:0000305"
FT CONFLICT 356
FT /note="R -> Q (in Ref. 2; BAC38812)"
FT /evidence="ECO:0000305"
FT CONFLICT 1577
FT /note="I -> IS (in Ref. 1; AAH46427)"
FT /evidence="ECO:0000305"
FT CONFLICT 1914
FT /note="K -> R (in Ref. 1; AAH62182)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2075 AA; 231399 MW; CF44446E4810C1EF CRC64;
MPWPFSESIK KRACRYLLQR YLGHFLQEKL SLEQLSLDLY QGTGSLAQVP LDKWCLNEIL
ESADAPLEVT EGFIQSISLS VPWGSLLQDN CALEVRGLEM VFRPRPRVAT GSEPMYWSSF
MTSSMQLAKE CLSQKLTDEQ GEASQPFEGL EKFAETIETV LRRVKVTFID TVLRIEHVPE
NSKTGAALEI RVDRTVYCDE TADESSGVNV HQPTAFAHKL LQLSGVSLFW DEFSASAKSS
PVCSTAPVET EPKLSPSWNP KIVYEPHPQL TRTLPEIAPS DPVQIGRLLG RLELSLTLKQ
NEVLPGAKLD VDGQIDSFHL FLSPRQVHLL LDMLAAIAGP ENSSKIGLAN KDRKNRPMQQ
EDEYRIQMEL NRYYLRKDSL SMGVSSEKSF YETETARTPS SREEEVFFSM ADMDMSHSLS
SLPPLGDPPH MDLELSLTST YTNTPAGSPL SATVLQPTWG EFADHKEQPV RGPAFQSDVV
HPASLQKAAL SSRSASVDES RPEFICRLAL GIFSVSVLHI DPLSPAETSL NVNPLTRMAT
DFFSCVEKMD PAIFSTGDFK SFRAVFAEAC SHDHLRFIGT GIKVSYEQRQ RSASRHFSTD
MSVGQMEFLE CLFPTDCHSV PSHYTELLTF HSKEGTDAHL PVCLQLHYKH SETRGPQGNQ
ARLSSVPQKA ELQIKLNPVC CELDISIVDR LNSLLQPQKL TTVEMMASHM YASYNKHISL
HKAFTEVFLD DSHSPANRRV SVQVATPALH LSVRFPIPDL RSDQERGPWF KKSLQKETLH
LEFTDLESKT EFVGGSTPEQ TKLELTFREL SGSFQEEKGG PSVKFFHVSG GVDGDTASSD
DFDWPRMVLK INPPAMHSIL ERIAAEEEEE NDGHYQEEED GGAHSLKDVC DLRRPAPSPF
SSRRVMFENE QMVMPGDPVE MTEFQDKAIS NSHYVLELLL PNIHLTLPNK GFYEKLYNRI
FNDLLLWEPT APSPVETLEN VSYGIGLSVA SQLINTFSKD SFSPFKSAVH YDEDSGSEEE
TLQYFSAVDP NYRSRRKKKL DSQNKNSQSF LSVLLSINHG LMAVFTDVKQ ENGDPMESKH
GEFWLEFNSG SFFCVTKYEG FEDKHYICLH SSSLRLYHKG IVDGAILPTE TRLPCSTRPH
WLEPTIYSSE EDGLSRTASD GVGGDNLNML SVAVKILSDK SESNTKEFLV AVGLKGATLQ
HRVLPAGLSW HEQILNFLNI ADEPVLGYNP PTSFTTFHVH LWSCALDYRP LHLPLRSLLT
VETFSISSSV ALDKSSSTLR IIMDEAALHL SDKCNTVTVN LNRDYVRVMD MGLLELTITA
VKSDSDGEQT APRFELHCSS DVVHIRTCSD SCAALMNLIQ YVASYGDLHG PHKAEMKPGV
PQRKPKVDSS ARSSSHGPVL PEADQQILRD LMSDAMEEID LQQASAPVGP QANGVLDEKS
HTQEPCCSDL FLFPDESGNV SQESSPAYPS LTHHLISDAV TGVTAENDDF CILFAPKTVV
QEKEEEPVIK IMVDDAIVIK DDYFSLPITR TDSSKAPLHF PIPAVRYVVK EVSLVWHLYG
GKDFATAPPT SPAKSYIPHS SPSQTPTRHG RHTVCGGKGR NHDFLMEIQL SKVKFQHEVY
PPCKPECESS LLEHPVSRQV FIVQDLEIRD RLATSQMNKF LYLYCSKDMP RKAHSNMLTI
KALHVRPESG RSPQECCLRV SLMPLRLNID QDALFFLKDF FTSLSTEVEL LLTPDPEVTK
SPGADVTCSL PRHLSTSKEP NLVVSFPGPK QASPNHRANS AEGGNGLEED VSAEETSFSD
QPVFFREFRF TAEVPIRLDY HGKHVSMDQG TLAGILIGLA QLNCSELKLK RLFYRHGLLG
IDKLFSYAIS EWLSDIKKNQ LPGILGGVGP MHSLVQLVQG LKDLVWLPIE QYRKDGRIVR
GFQRGAASFG TSTAMAALEL TNRMVQTIQA AAETAYDMVS PSTLSIEPKK AKRFPHHRLA
HQPVDLREGV AKAYSVVKEG ITDTAQTIYE TAAREHESRG VTGAVGEVLR QIPPAVVRPL
IVATEATSNV LGGMRNQIRP DVRQDESQKW RHGED
