GBRL2_HUMAN
ID GBRL2_HUMAN Reviewed; 117 AA.
AC P60520; O08765; Q6FG91; Q9DCP8; Q9UQF7;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Gamma-aminobutyric acid receptor-associated protein-like 2;
DE AltName: Full=GABA(A) receptor-associated protein-like 2;
DE AltName: Full=Ganglioside expression factor 2;
DE Short=GEF-2;
DE AltName: Full=General protein transport factor p16;
DE AltName: Full=Golgi-associated ATPase enhancer of 16 kDa;
DE Short=GATE-16;
DE AltName: Full=MAP1 light chain 3-related protein;
DE Flags: Precursor;
GN Name=GABARAPL2; Synonyms=FLC3A, GEF2;
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 [MRNA], TISSUE SPECIFICITY, AND INTERACTION WITH ULK1.
RC TISSUE=Frontal cortex;
RX PubMed=11146101; DOI=10.1016/s0169-328x(00)00218-7;
RA Okazaki N., Yan J., Yuasa S., Ueno T., Kominami E., Masuho Y., Koga H.,
RA Muramatsu M.-A.;
RT "Interaction of the Unc-51-like kinase and microtubule-associated protein
RT light chain 3 related proteins in the brain: possible role of vesicular
RT transport in axonal elongation.";
RL Brain Res. Mol. Brain Res. 85:1-12(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=11414770; DOI=10.1006/geno.2001.6555;
RA Xin Y., Yu L., Chen Z., Zheng L., Fu Q., Jiang J., Zhang P., Gong R.,
RA Zhao S.;
RT "Cloning, expression patterns, and chromosome localization of three human
RT and two mouse homologues of GABA(A) receptor-associated protein.";
RL Genomics 74:408-413(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Storch S., Braulke T.;
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pituitary;
RA Song H., Peng Y., Yu Y., Fu G., Mao M., Zhang Q., Zhu H., Li G., Luo M.,
RA Chen J., Hu R.;
RT "Human GEF2 homolog gene.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and 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 [9]
RP INTERACTION WITH ATG7.
RX PubMed=11096062; DOI=10.1074/jbc.c000752200;
RA Tanida I., Tanida-Miyake E., Ueno T., Kominami E.;
RT "The human homolog of Saccharomyces cerevisiae Apg7p is a Protein-
RT activating enzyme for multiple substrates including human Apg12p, GATE-16,
RT GABARAP, and MAP-LC3.";
RL J. Biol. Chem. 276:1701-1706(2001).
RN [10]
RP INTERACTION WITH ATG3.
RX PubMed=11825910; DOI=10.1074/jbc.m200385200;
RA Tanida I., Tanida-Miyake E., Komatsu M., Ueno T., Kominami E.;
RT "Human Apg3p/Aut1p homologue is an authentic E2 enzyme for multiple
RT substrates, GATE-16, GABARAP, and MAP-LC3, and facilitates the conjugation
RT of hApg12p to hApg5p.";
RL J. Biol. Chem. 277:13739-13744(2002).
RN [11]
RP LIPIDATION AT GLY-116, INTERACTION WITH ATG3 AND ATG7, AND SUBCELLULAR
RP LOCATION.
RX PubMed=12507496; DOI=10.1016/s0006-291x(02)02907-8;
RA Tanida I., Komatsu M., Ueno T., Kominami E.;
RT "GATE-16 and GABARAP are authentic modifiers mediated by Apg7 and Apg3.";
RL Biochem. Biophys. Res. Commun. 300:637-644(2003).
RN [12]
RP CLEAVAGE, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-116.
RX PubMed=15169837; DOI=10.1242/jcs.01131;
RA Kabeya Y., Mizushima N., Yamamoto A., Oshitani-Okamoto S., Ohsumi Y.,
RA Yoshimori T.;
RT "LC3, GABARAP and GATE16 localize to autophagosomal membrane depending on
RT form-II formation.";
RL J. Cell Sci. 117:2805-2812(2004).
RN [13]
RP INTERACTION WITH SQSTM1, AND SUBCELLULAR LOCATION.
RX PubMed=17580304; DOI=10.1074/jbc.m702824200;
RA Pankiv S., Clausen T.H., Lamark T., Brech A., Bruun J.A., Outzen H.,
RA Overvatn A., Bjorkoy G., Johansen T.;
RT "p62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of
RT ubiquitinated protein aggregates by autophagy.";
RL J. Biol. Chem. 282:24131-24145(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [15]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH TP53INP2.
RX PubMed=19056683; DOI=10.1091/mbc.e08-07-0671;
RA Nowak J., Archange C., Tardivel-Lacombe J., Pontarotti P., Pebusque M.J.,
RA Vaccaro M.I., Velasco G., Dagorn J.C., Iovanna J.L.;
RT "The TP53INP2 protein is required for autophagy in mammalian cells.";
RL Mol. Biol. Cell 20:870-881(2009).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-24, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [17]
RP CLEAVAGE BY ATG4B.
RX PubMed=20818167; DOI=10.4161/auto.6.7.13075;
RA Shu C.W., Drag M., Bekes M., Zhai D., Salvesen G.S., Reed J.C.;
RT "Synthetic substrates for measuring activity of autophagy proteases:
RT autophagins (Atg4).";
RL Autophagy 6:936-947(2010).
RN [18]
RP FUNCTION.
RX PubMed=20418806; DOI=10.1038/emboj.2010.74;
RA Weidberg H., Shvets E., Shpilka T., Shimron F., Shinder V., Elazar Z.;
RT "LC3 and GATE-16/GABARAP subfamilies are both essential yet act differently
RT in autophagosome biogenesis.";
RL EMBO J. 29:1792-1802(2010).
RN [19]
RP INTERACTION WITH TECPR2.
RX PubMed=20562859; DOI=10.1038/nature09204;
RA Behrends C., Sowa M.E., Gygi S.P., Harper J.W.;
RT "Network organization of the human autophagy system.";
RL Nature 466:68-76(2010).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [21]
RP INTERACTION WITH TBC1D25.
RX PubMed=21383079; DOI=10.1083/jcb.201008107;
RA Itoh T., Kanno E., Uemura T., Waguri S., Fukuda M.;
RT "OATL1, a novel autophagosome-resident Rab33B-GAP, regulates autophagosomal
RT maturation.";
RL J. Cell Biol. 192:839-853(2011).
RN [22]
RP INTERACTION WITH TP53INP1.
RX PubMed=22421968; DOI=10.1038/cdd.2012.30;
RA Seillier M., Peuget S., Gayet O., Gauthier C., N'guessan P., Monte M.,
RA Carrier A., Iovanna J.L., Dusetti N.J.;
RT "TP53INP1, a tumor suppressor, interacts with LC3 and ATG8-family proteins
RT through the LC3-interacting region (LIR) and promotes autophagy-dependent
RT cell death.";
RL Cell Death Differ. 19:1525-1535(2012).
RN [23]
RP INTERACTION WITH ATG13 AND ULK1.
RX PubMed=23043107; DOI=10.1074/jbc.m112.378109;
RA Alemu E.A., Lamark T., Torgersen K.M., Birgisdottir A.B., Larsen K.B.,
RA Jain A., Olsvik H., Overvatn A., Kirkin V., Johansen T.;
RT "ATG8 family proteins act as scaffolds for assembly of the ULK complex:
RT sequence requirements for LC3-interacting region (LIR) motifs.";
RL J. Biol. Chem. 287:39275-39290(2012).
RN [24]
RP INTERACTION WITH TBC1D5.
RX PubMed=22354992; DOI=10.1128/mcb.06717-11;
RA Popovic D., Akutsu M., Novak I., Harper J.W., Behrends C., Dikic I.;
RT "Rab GTPase-activating proteins in autophagy: regulation of endocytic and
RT autophagy pathways by direct binding to human ATG8 modifiers.";
RL Mol. Cell. Biol. 32:1733-1744(2012).
RN [25]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=22311637; DOI=10.1074/mcp.m111.014035;
RA Dengjel J., Hoyer-Hansen M., Nielsen M.O., Eisenberg T., Harder L.M.,
RA Schandorff S., Farkas T., Kirkegaard T., Becker A.C., Schroeder S.,
RA Vanselow K., Lundberg E., Nielsen M.M., Kristensen A.R., Akimov V.,
RA Bunkenborg J., Madeo F., Jaattela M., Andersen J.S.;
RT "Identification of autophagosome-associated proteins and regulators by
RT quantitative proteomic analysis and genetic screens.";
RL Mol. Cell. Proteomics 11:M111.014035.1-M111.014035.17(2012).
RN [26]
RP INTERACTION WITH TP53INP1 AND TP53INP2.
RX PubMed=22470510; DOI=10.1371/journal.pone.0034034;
RA Sancho A., Duran J., Garcia-Espana A., Mauvezin C., Alemu E.A., Lamark T.,
RA Macias M.J., Desalle R., Royo M., Sala D., Chicote J.U., Palacin M.,
RA Johansen T., Zorzano A.;
RT "DOR/Tp53inp2 and Tp53inp1 constitute a metazoan gene family encoding dual
RT regulators of autophagy and transcription.";
RL PLoS ONE 7:E34034-E34034(2012).
RN [27]
RP INTERACTION WITH BNIP3, AND FUNCTION.
RX PubMed=23209295; DOI=10.1074/jbc.m112.399345;
RA Zhu Y., Massen S., Terenzio M., Lang V., Chen-Lindner S., Eils R.,
RA Novak I., Dikic I., Hamacher-Brady A., Brady N.R.;
RT "Modulation of serines 17 and 24 in the LC3-interacting region of Bnip3
RT determines pro-survival mitophagy versus apoptosis.";
RL J. Biol. Chem. 288:1099-1113(2013).
RN [28]
RP INTERACTION WITH PCM1.
RX PubMed=24089205; DOI=10.1038/nature12606;
RA Tang Z., Lin M.G., Stowe T.R., Chen S., Zhu M., Stearns T., Franco B.,
RA Zhong Q.;
RT "Autophagy promotes primary ciliogenesis by removing OFD1 from centriolar
RT satellites.";
RL Nature 502:254-257(2013).
RN [29]
RP INTERACTION WITH TRIM5.
RX PubMed=25127057; DOI=10.1016/j.devcel.2014.06.013;
RA Mandell M.A., Jain A., Arko-Mensah J., Chauhan S., Kimura T., Dinkins C.,
RA Silvestri G., Munch J., Kirchhoff F., Simonsen A., Wei Y., Levine B.,
RA Johansen T., Deretic V.;
RT "TRIM proteins regulate autophagy and can target autophagic substrates by
RT direct recognition.";
RL Dev. Cell 30:394-409(2014).
RN [30]
RP INTERACTION WITH WDFY3.
RX PubMed=24668264; DOI=10.1002/embr.201338003;
RA Lystad A.H., Ichimura Y., Takagi K., Yang Y., Pankiv S., Kanegae Y.,
RA Kageyama S., Suzuki M., Saito I., Mizushima T., Komatsu M., Simonsen A.;
RT "Structural determinants in GABARAP required for the selective binding and
RT recruitment of ALFY to LC3B-positive structures.";
RL EMBO Rep. 15:557-565(2014).
RN [31]
RP INTERACTION WITH MEFV AND TRIM21.
RX PubMed=26347139; DOI=10.1083/jcb.201503023;
RA Kimura T., Jain A., Choi S.W., Mandell M.A., Schroder K., Johansen T.,
RA Deretic V.;
RT "TRIM-mediated precision autophagy targets cytoplasmic regulators of innate
RT immunity.";
RL J. Cell Biol. 210:973-989(2015).
RN [32]
RP INTERACTION WITH KBTBD6 AND KBTBD7.
RX PubMed=25684205; DOI=10.1016/j.molcel.2014.12.040;
RA Genau H.M., Huber J., Baschieri F., Akutsu M., Doetsch V., Farhan H.,
RA Rogov V., Behrends C.;
RT "CUL3-KBTBD6/KBTBD7 ubiquitin ligase cooperates with GABARAP proteins to
RT spatially restrict TIAM1-RAC1 signaling.";
RL Mol. Cell 57:995-1010(2015).
RN [33]
RP INTERACTION WITH UBA5.
RX PubMed=26929408; DOI=10.1074/jbc.m116.715474;
RA Habisov S., Huber J., Ichimura Y., Akutsu M., Rogova N., Loehr F.,
RA McEwan D.G., Johansen T., Dikic I., Doetsch V., Komatsu M., Rogov V.V.,
RA Kirkin V.;
RT "Structural and functional analysis of a novel interaction motif within
RT UFM1-activating enzyme 5 (UBA5) required for binding to ubiquitin-like
RT proteins and ufmylation.";
RL J. Biol. Chem. 291:9025-9041(2016).
RN [34]
RP PROTEOLYTIC CLEAVAGE, DELIPIDATION, AND LIPIDATION AT GLY-116.
RX PubMed=29458288; DOI=10.1080/15548627.2018.1437341;
RA Kauffman K.J., Yu S., Jin J., Mugo B., Nguyen N., O'Brien A., Nag S.,
RA Lystad A.H., Melia T.J.;
RT "Delipidation of mammalian Atg8-family proteins by each of the four ATG4
RT proteases.";
RL Autophagy 14:992-1010(2018).
RN [35]
RP PROTEOLYTIC CLEAVAGE.
RX PubMed=30661429; DOI=10.1080/15548627.2019.1569925;
RA Agrotis A., Pengo N., Burden J.J., Ketteler R.;
RT "Redundancy of human ATG4 protease isoforms in autophagy and LC3/GABARAP
RT processing revealed in cells.";
RL Autophagy 15:976-997(2019).
RN [36]
RP DECONJUGATION BY LEGIONELLA RAVZ (MICROBIAL INFECTION).
RX PubMed=31722778; DOI=10.5483/bmbrep.2019.52.12.211;
RA Park S.W., Jun Y.W., Jeon P., Lee Y.K., Park J.H., Lee S.H., Lee J.A.,
RA Jang D.J.;
RT "LIR motifs and the membrane-targeting domain are complementary in the
RT function of RavZ.";
RL BMB Rep. 52:700-705(2019).
RN [37]
RP PHOSPHORYLATION AT SER-87 AND SER-88, LIPIDATION AT GLY-116, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF 87-SER-SER-88 AND SER-88.
RX PubMed=31709703; DOI=10.15252/embr.201948317;
RA Herhaus L., Bhaskara R.M., Lystad A.H., Gestal-Mato U.,
RA Covarrubias-Pinto A., Bonn F., Simonsen A., Hummer G., Dikic I.;
RT "TBK1-mediated phosphorylation of LC3C and GABARAP-L2 controls
RT autophagosome shedding by ATG4 protease.";
RL EMBO Rep. 21:e48317-e48317(2020).
RN [38]
RP LIPIDATION AT GLY-116.
RX PubMed=33909989; DOI=10.1016/j.molcel.2021.03.020;
RA Durgan J., Lystad A.H., Sloan K., Carlsson S.R., Wilson M.I., Marcassa E.,
RA Ulferts R., Webster J., Lopez-Clavijo A.F., Wakelam M.J., Beale R.,
RA Simonsen A., Oxley D., Florey O.;
RT "Non-canonical autophagy drives alternative ATG8 conjugation to
RT phosphatidylserine.";
RL Mol. Cell 81:2031-2040(2021).
RN [39] {ECO:0007744|PDB:6H8C}
RP STRUCTURE BY NMR OF 1-116 IN COMPLEX WITH UBA5, INTERACTION WITH UBA5,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-47.
RX PubMed=30990354; DOI=10.1080/15548627.2019.1606637;
RA Huber J., Obata M., Gruber J., Akutsu M., Lohr F., Rogova N., Guntert P.,
RA Dikic I., Kirkin V., Komatsu M., Dotsch V., Rogov V.V.;
RT "An atypical LIR motif within UBA5 (ubiquitin like modifier activating
RT enzyme 5) interacts with GABARAP proteins and mediates membrane
RT localization of UBA5.";
RL Autophagy 16:256-270(2020).
CC -!- FUNCTION: Ubiquitin-like modifier involved in intra-Golgi traffic (By
CC similarity). Modulates intra-Golgi transport through coupling between
CC NSF activity and SNAREs activation (By similarity). It first stimulates
CC the ATPase activity of NSF which in turn stimulates the association
CC with GOSR1 (By similarity). Involved in autophagy (PubMed:20418806,
CC PubMed:23209295). Plays a role in mitophagy which contributes to
CC regulate mitochondrial quantity and quality by eliminating the
CC mitochondria to a basal level to fulfill cellular energy requirements
CC and preventing excess ROS production (PubMed:20418806,
CC PubMed:23209295). Whereas LC3s are involved in elongation of the
CC phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a
CC later stage in autophagosome maturation (PubMed:20418806,
CC PubMed:23209295). {ECO:0000250|UniProtKB:P60519,
CC ECO:0000269|PubMed:20418806, ECO:0000269|PubMed:23209295}.
CC -!- SUBUNIT: Monomer. Interacts with ATG3, ATG7, ATG13 and ULK1
CC (PubMed:11146101, PubMed:11825910, PubMed:11096062, PubMed:12507496,
CC PubMed:23043107). Interacts with TP53INP1 and TP53INP2
CC (PubMed:19056683, PubMed:22421968, PubMed:22470510). Interacts with
CC TBC1D25 (PubMed:21383079). Directly interacts with SQSTM1 and BNIP3
CC (PubMed:17580304, PubMed:23209295). Interacts with TECPR2 and PCM1
CC (PubMed:20562859, PubMed:24089205). Interacts with TBC1D5
CC (PubMed:22354992). Interacts with TRIM5 (PubMed:25127057). Interacts
CC with MEFV and TRIM21 (PubMed:26347139). Interacts with WDFY3
CC (PubMed:24668264). Interacts with UBA5; promoting recruitment of UBA5
CC to the endoplasmic reticulum membrane (PubMed:26929408,
CC PubMed:30990354). Interacts with GOSR1 (By similarity). Interacts with
CC KBTBD6 AND KBTBD7; the interaction is direct (PubMed:25684205).
CC {ECO:0000250|UniProtKB:P60519, ECO:0000269|PubMed:11096062,
CC ECO:0000269|PubMed:11146101, ECO:0000269|PubMed:11825910,
CC ECO:0000269|PubMed:12507496, ECO:0000269|PubMed:17580304,
CC ECO:0000269|PubMed:19056683, ECO:0000269|PubMed:20562859,
CC ECO:0000269|PubMed:21383079, ECO:0000269|PubMed:22354992,
CC ECO:0000269|PubMed:22421968, ECO:0000269|PubMed:22470510,
CC ECO:0000269|PubMed:23043107, ECO:0000269|PubMed:23209295,
CC ECO:0000269|PubMed:24089205, ECO:0000269|PubMed:24668264,
CC ECO:0000269|PubMed:25127057, ECO:0000269|PubMed:25684205,
CC ECO:0000269|PubMed:26347139, ECO:0000269|PubMed:26929408,
CC ECO:0000269|PubMed:30990354}.
CC -!- INTERACTION:
CC P60520; Q6RW13: AGTRAP; NbExp=3; IntAct=EBI-720116, EBI-741181;
CC P60520; Q8IVF2-2: AHNAK2; NbExp=3; IntAct=EBI-720116, EBI-10217765;
CC P60520; Q9P2R3: ANKFY1; NbExp=2; IntAct=EBI-720116, EBI-2513908;
CC P60520; Q8N6T3: ARFGAP1; NbExp=3; IntAct=EBI-720116, EBI-716933;
CC P60520; Q8N6T3-2: ARFGAP1; NbExp=3; IntAct=EBI-720116, EBI-6288865;
CC P60520; O75143: ATG13; NbExp=3; IntAct=EBI-720116, EBI-2798775;
CC P60520; Q676U5: ATG16L1; NbExp=2; IntAct=EBI-720116, EBI-535909;
CC P60520; Q2TAZ0: ATG2A; NbExp=2; IntAct=EBI-720116, EBI-2514077;
CC P60520; Q9NT62: ATG3; NbExp=5; IntAct=EBI-720116, EBI-988094;
CC P60520; Q9Y4P1: ATG4B; NbExp=10; IntAct=EBI-720116, EBI-712014;
CC P60520; O95352: ATG7; NbExp=7; IntAct=EBI-720116, EBI-987834;
CC P60520; Q9BXK5: BCL2L13; NbExp=4; IntAct=EBI-720116, EBI-747430;
CC P60520; O60238: BNIP3L; NbExp=3; IntAct=EBI-720116, EBI-849893;
CC P60520; Q9NW68: BSDC1; NbExp=3; IntAct=EBI-720116, EBI-721848;
CC P60520; Q9P1Z2: CALCOCO1; NbExp=3; IntAct=EBI-720116, EBI-749920;
CC P60520; Q13137: CALCOCO2; NbExp=7; IntAct=EBI-720116, EBI-739580;
CC P60520; Q8WXU2: DNAAF4; NbExp=2; IntAct=EBI-720116, EBI-2946907;
CC P60520; P63167: DYNLL1; NbExp=3; IntAct=EBI-720116, EBI-349105;
CC P60520; Q96FJ2: DYNLL2; NbExp=3; IntAct=EBI-720116, EBI-742371;
CC P60520; P00533: EGFR; NbExp=3; IntAct=EBI-720116, EBI-297353;
CC P60520; Q8IVP5: FUNDC1; NbExp=4; IntAct=EBI-720116, EBI-3059266;
CC P60520; Q9BQS8: FYCO1; NbExp=2; IntAct=EBI-720116, EBI-2869338;
CC P60520; P40939: HADHA; NbExp=4; IntAct=EBI-720116, EBI-356720;
CC P60520; P54257: HAP1; NbExp=3; IntAct=EBI-720116, EBI-712814;
CC P60520; Q2T9L4: INSYN1; NbExp=3; IntAct=EBI-720116, EBI-4311436;
CC P60520; O00410: IPO5; NbExp=5; IntAct=EBI-720116, EBI-356424;
CC P60520; Q8N6L0: KASH5; NbExp=3; IntAct=EBI-720116, EBI-749265;
CC P60520; Q86V97: KBTBD6; NbExp=2; IntAct=EBI-720116, EBI-2514778;
CC P60520; Q8WVZ9: KBTBD7; NbExp=3; IntAct=EBI-720116, EBI-473695;
CC P60520; Q8N8K9: KIAA1958; NbExp=7; IntAct=EBI-720116, EBI-10181113;
CC P60520; Q96L93-6: KIF16B; NbExp=3; IntAct=EBI-720116, EBI-10988217;
CC P60520; P60409: KRTAP10-7; NbExp=6; IntAct=EBI-720116, EBI-10172290;
CC P60520; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-720116, EBI-10172052;
CC P60520; Q8N653: LZTR1; NbExp=3; IntAct=EBI-720116, EBI-2350056;
CC P60520; Q9UH92: MLX; NbExp=5; IntAct=EBI-720116, EBI-741109;
CC P60520; Q9UH92-3: MLX; NbExp=3; IntAct=EBI-720116, EBI-8852072;
CC P60520; Q14596: NBR1; NbExp=11; IntAct=EBI-720116, EBI-742698;
CC P60520; P46934: NEDD4; NbExp=6; IntAct=EBI-720116, EBI-726944;
CC P60520; P46934-3: NEDD4; NbExp=3; IntAct=EBI-720116, EBI-11980721;
CC P60520; Q8TD19: NEK9; NbExp=7; IntAct=EBI-720116, EBI-1044009;
CC P60520; O75323: NIPSNAP2; NbExp=6; IntAct=EBI-720116, EBI-307133;
CC P60520; Q9NV35: NUDT15; NbExp=3; IntAct=EBI-720116, EBI-3924801;
CC P60520; Q9H4L5: OSBPL3; NbExp=3; IntAct=EBI-720116, EBI-1051317;
CC P60520; Q15154: PCM1; NbExp=2; IntAct=EBI-720116, EBI-741421;
CC P60520; Q9NS23: RASSF1; NbExp=2; IntAct=EBI-720116, EBI-367363;
CC P60520; Q8WWW0: RASSF5; NbExp=2; IntAct=EBI-720116, EBI-367390;
CC P60520; Q14257: RCN2; NbExp=6; IntAct=EBI-720116, EBI-356710;
CC P60520; Q9H6L5-1: RETREG1; NbExp=2; IntAct=EBI-720116, EBI-16159046;
CC P60520; Q9H6L5-2: RETREG1; NbExp=3; IntAct=EBI-720116, EBI-13382642;
CC P60520; Q86VR2: RETREG3; NbExp=3; IntAct=EBI-720116, EBI-10192441;
CC P60520; Q8IZE3-2: SCYL3; NbExp=3; IntAct=EBI-720116, EBI-11959369;
CC P60520; Q9H0K1: SIK2; NbExp=3; IntAct=EBI-720116, EBI-1181664;
CC P60520; Q13501: SQSTM1; NbExp=21; IntAct=EBI-720116, EBI-307104;
CC P60520; O95210: STBD1; NbExp=5; IntAct=EBI-720116, EBI-2947137;
CC P60520; Q13188: STK3; NbExp=2; IntAct=EBI-720116, EBI-992580;
CC P60520; Q13043: STK4; NbExp=2; IntAct=EBI-720116, EBI-367376;
CC P60520; Q86VP1: TAX1BP1; NbExp=3; IntAct=EBI-720116, EBI-529518;
CC P60520; Q8TC07: TBC1D15; NbExp=2; IntAct=EBI-720116, EBI-1048247;
CC P60520; Q3MII6: TBC1D25; NbExp=4; IntAct=EBI-720116, EBI-11899977;
CC P60520; Q9UPU7: TBC1D2B; NbExp=3; IntAct=EBI-720116, EBI-2947180;
CC P60520; B9A6K1: TBC1D5; NbExp=3; IntAct=EBI-720116, EBI-10217641;
CC P60520; Q92609: TBC1D5; NbExp=5; IntAct=EBI-720116, EBI-742381;
CC P60520; Q66K14-2: TBC1D9B; NbExp=3; IntAct=EBI-720116, EBI-10217736;
CC P60520; O15040: TECPR2; NbExp=2; IntAct=EBI-720116, EBI-2946991;
CC P60520; Q9Y6I9: TEX264; NbExp=3; IntAct=EBI-720116, EBI-10329860;
CC P60520; Q15025: TNIP1; NbExp=6; IntAct=EBI-720116, EBI-357849;
CC P60520; Q96A56: TP53INP1; NbExp=6; IntAct=EBI-720116, EBI-9986117;
CC P60520; Q9H8W5-2: TRIM45; NbExp=3; IntAct=EBI-720116, EBI-11993364;
CC P60520; Q969E8: TSR2; NbExp=11; IntAct=EBI-720116, EBI-746981;
CC P60520; Q9GZZ9: UBA5; NbExp=17; IntAct=EBI-720116, EBI-747805;
CC P60520; O75385: ULK1; NbExp=3; IntAct=EBI-720116, EBI-908831;
CC P60520; Q8IZQ1: WDFY3; NbExp=3; IntAct=EBI-720116, EBI-1569256;
CC P60520; Q8N680: ZBTB2; NbExp=3; IntAct=EBI-720116, EBI-2515601;
CC P60520; Q6NX45: ZNF774; NbExp=3; IntAct=EBI-720116, EBI-10251462;
CC P60520; Q9Z2F7: Bnip3l; Xeno; NbExp=2; IntAct=EBI-720116, EBI-1774669;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome
CC {ECO:0000269|PubMed:12507496, ECO:0000269|PubMed:15169837,
CC ECO:0000269|PubMed:17580304, ECO:0000269|PubMed:19056683,
CC ECO:0000269|PubMed:22311637, ECO:0000269|PubMed:31709703}. Endoplasmic
CC reticulum membrane {ECO:0000269|PubMed:30990354}. Golgi apparatus
CC {ECO:0000250|UniProtKB:P60519}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Expressed at high levels in the brain,
CC heart, prostate, ovary, spleen and skeletal muscle. Expressed at very
CC low levels in lung, thymus and small intestine.
CC {ECO:0000269|PubMed:11146101, ECO:0000269|PubMed:11414770}.
CC -!- PTM: The precursor molecule is cleaved by ATG4 (ATG4A, ATG4B, ATG4C or
CC ATG4D) to expose the glycine at the C-terminus and form the cytosolic
CC form, GABARAPL2-I (PubMed:15169837, PubMed:20818167, PubMed:30661429,
CC PubMed:31709703). The processed form is then activated by APG7L/ATG7,
CC transferred to ATG3 and conjugated to phosphatidylethanolamine (PE)
CC phospholipid to form the membrane-bound form, GABARAPL2-II
CC (PubMed:15169837, PubMed:31709703). During non-canonical autophagy, the
CC processed form is conjugated to phosphatidylserine (PS) phospholipid
CC (PubMed:33909989). ATG4 proteins also mediate the delipidation of PE-
CC conjugated forms required for GABARAPL2 recycling when autophagosomes
CC fuse with lysosomes (PubMed:29458288, PubMed:31709703,
CC PubMed:33909989). In addition, ATG4B and ATG4D mediate delipidation of
CC ATG8 proteins conjugated to PS during non-canonical autophagy
CC (PubMed:33909989). ATG4B constitutes the major protein for proteolytic
CC activation (PubMed:30661429). ATG4D is the main enzyme for delipidation
CC activity (By similarity). {ECO:0000250|UniProtKB:P60521,
CC ECO:0000269|PubMed:15169837, ECO:0000269|PubMed:20818167,
CC ECO:0000269|PubMed:29458288, ECO:0000269|PubMed:30661429,
CC ECO:0000269|PubMed:31709703, ECO:0000269|PubMed:33909989}.
CC -!- PTM: (Microbial infection) The Legionella effector RavZ is a
CC deconjugating enzyme that hydrolyzes the amide bond between the C-
CC terminal glycine residue and an adjacent aromatic residue in ATG8
CC proteins conjugated to phosphatidylethanolamine (PE), producing an ATG8
CC protein that is resistant to reconjugation by the host machinery due to
CC the cleavage of the reactive C-terminal glycine (PubMed:31722778). RavZ
CC is also able to mediate delipidation of ATG8 proteins conjugated to
CC phosphatidylserine (PS) (PubMed:33909989).
CC {ECO:0000269|PubMed:31722778, ECO:0000269|PubMed:33909989}.
CC -!- PTM: Phosphorylation at Ser-87 and Ser-88 by TBK1 prevents interaction
CC with ATG4 (ATG4A, ATG4B, ATG4C or ATG4D) (PubMed:31709703).
CC Phosphorylation by TBK1 on autophagosomes prevents their delipidation
CC by ATG4 and premature removal from nascent autophagosomes
CC (PubMed:31709703). {ECO:0000269|PubMed:31709703}.
CC -!- SIMILARITY: Belongs to the ATG8 family. {ECO:0000305}.
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DR EMBL; AB030710; BAB21548.1; -; mRNA.
DR EMBL; AF087848; AAK20400.1; -; mRNA.
DR EMBL; AJ010569; CAA09249.1; -; mRNA.
DR EMBL; AF077046; AAD27779.1; -; mRNA.
DR EMBL; CR542217; CAG47013.1; -; mRNA.
DR EMBL; AK289788; BAF82477.1; -; mRNA.
DR EMBL; CH471114; EAW95630.1; -; Genomic_DNA.
DR EMBL; BC005985; AAH05985.1; -; mRNA.
DR EMBL; BC014594; AAH14594.1; -; mRNA.
DR EMBL; BC029601; AAH29601.1; -; mRNA.
DR CCDS; CCDS10921.1; -.
DR RefSeq; NP_009216.1; NM_007285.6.
DR PDB; 4CO7; X-ray; 2.00 A; A/B=1-117.
DR PDB; 6H8C; NMR; -; A=1-116.
DR PDB; 7LK3; X-ray; 1.90 A; A/B=1-117.
DR PDBsum; 4CO7; -.
DR PDBsum; 6H8C; -.
DR PDBsum; 7LK3; -.
DR AlphaFoldDB; P60520; -.
DR SMR; P60520; -.
DR BioGRID; 116473; 138.
DR DIP; DIP-35051N; -.
DR ELM; P60520; -.
DR IntAct; P60520; 535.
DR MINT; P60520; -.
DR STRING; 9606.ENSP00000037243; -.
DR MoonDB; P60520; Predicted.
DR iPTMnet; P60520; -.
DR PhosphoSitePlus; P60520; -.
DR BioMuta; GABARAPL2; -.
DR DMDM; 44888808; -.
DR UCD-2DPAGE; P60520; -.
DR EPD; P60520; -.
DR jPOST; P60520; -.
DR MassIVE; P60520; -.
DR PaxDb; P60520; -.
DR PeptideAtlas; P60520; -.
DR PRIDE; P60520; -.
DR ProteomicsDB; 57214; -.
DR Antibodypedia; 30328; 587 antibodies from 35 providers.
DR DNASU; 11345; -.
DR Ensembl; ENST00000037243.7; ENSP00000037243.2; ENSG00000034713.8.
DR GeneID; 11345; -.
DR KEGG; hsa:11345; -.
DR MANE-Select; ENST00000037243.7; ENSP00000037243.2; NM_007285.7; NP_009216.1.
DR UCSC; uc002fen.3; human.
DR CTD; 11345; -.
DR DisGeNET; 11345; -.
DR GeneCards; GABARAPL2; -.
DR HGNC; HGNC:13291; GABARAPL2.
DR HPA; ENSG00000034713; Low tissue specificity.
DR MIM; 607452; gene.
DR neXtProt; NX_P60520; -.
DR OpenTargets; ENSG00000034713; -.
DR PharmGKB; PA28482; -.
DR VEuPathDB; HostDB:ENSG00000034713; -.
DR eggNOG; KOG1654; Eukaryota.
DR GeneTree; ENSGT00940000155010; -.
DR HOGENOM; CLU_119276_0_1_1; -.
DR InParanoid; P60520; -.
DR OMA; AKMKWMF; -.
DR OrthoDB; 1508198at2759; -.
DR PhylomeDB; P60520; -.
DR TreeFam; TF312964; -.
DR PathwayCommons; P60520; -.
DR Reactome; R-HSA-1632852; Macroautophagy.
DR Reactome; R-HSA-8854214; TBC/RABGAPs.
DR SABIO-RK; P60520; -.
DR SignaLink; P60520; -.
DR SIGNOR; P60520; -.
DR BioGRID-ORCS; 11345; 14 hits in 1086 CRISPR screens.
DR ChiTaRS; GABARAPL2; human.
DR GeneWiki; GABARAPL2; -.
DR GenomeRNAi; 11345; -.
DR Pharos; P60520; Tbio.
DR PRO; PR:P60520; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P60520; protein.
DR Bgee; ENSG00000034713; Expressed in pons and 205 other tissues.
DR ExpressionAtlas; P60520; baseline and differential.
DR Genevisible; P60520; HS.
DR GO; GO:0005776; C:autophagosome; IDA:UniProtKB.
DR GO; GO:0000421; C:autophagosome membrane; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IDA:BHF-UCL.
DR GO; GO:0051117; F:ATPase binding; ISS:UniProtKB.
DR GO; GO:0048487; F:beta-tubulin binding; ISS:UniProtKB.
DR GO; GO:0050811; F:GABA receptor binding; ISS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; NAS:UniProtKB.
DR GO; GO:0000149; F:SNARE binding; ISS:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; NAS:UniProtKB.
DR GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0006995; P:cellular response to nitrogen starvation; IBA:GO_Central.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; ISS:UniProtKB.
DR GO; GO:0016236; P:macroautophagy; IBA:GO_Central.
DR GO; GO:1901799; P:negative regulation of proteasomal protein catabolic process; IMP:BHF-UCL.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; ISS:UniProtKB.
DR GO; GO:0070972; P:protein localization to endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR004241; Atg8-like.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10969; PTHR10969; 1.
DR Pfam; PF02991; ATG8; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Autophagy; Cytoplasmic vesicle;
KW Endoplasmic reticulum; Golgi apparatus; Lipoprotein; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..116
FT /note="Gamma-aminobutyric acid receptor-associated protein-
FT like 2"
FT /id="PRO_0000212373"
FT PROPEP 117
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:15169837"
FT /id="PRO_0000423070"
FT SITE 116..117
FT /note="Cleavage; by ATG4"
FT /evidence="ECO:0000269|PubMed:15169837"
FT MOD_RES 24
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 87
FT /note="Phosphoserine; by TBK1"
FT /evidence="ECO:0000269|PubMed:31709703"
FT MOD_RES 88
FT /note="Phosphoserine; by TBK1"
FT /evidence="ECO:0000269|PubMed:31709703"
FT LIPID 116
FT /note="Phosphatidylethanolamine amidated glycine;
FT alternate"
FT /evidence="ECO:0000269|PubMed:12507496,
FT ECO:0000269|PubMed:33909989, ECO:0000305|PubMed:29458288"
FT LIPID 116
FT /note="Phosphatidylserine amidated glycine; alternate"
FT /evidence="ECO:0000269|PubMed:33909989"
FT VARIANT 51
FT /note="V -> A (in dbSNP:rs11556291)"
FT /id="VAR_049756"
FT MUTAGEN 47
FT /note="R->A: Strongly reduced interaction with UBA5."
FT /evidence="ECO:0000269|PubMed:30990354"
FT MUTAGEN 87..88
FT /note="SS->AA: Impaired phosphorylation by TBK1."
FT /evidence="ECO:0000269|PubMed:31709703"
FT MUTAGEN 87..88
FT /note="SS->DD: Phospho-mimetic mutant; impaired interaction
FT with ATG4 proteins, preventing cleavage at the C-terminus,
FT conjugation to phosphatidylethanolamine."
FT /evidence="ECO:0000269|PubMed:31709703"
FT MUTAGEN 88
FT /note="S->D: Phospho-mimetic mutant; abolished localization
FT to autophagosomes."
FT /evidence="ECO:0000269|PubMed:31709703"
FT MUTAGEN 116
FT /note="G->A: Impairs localization at the autophagosomal
FT membrane."
FT /evidence="ECO:0000269|PubMed:15169837"
FT CONFLICT 29
FT /note="V -> F (in Ref. 4; AAD27779)"
FT /evidence="ECO:0000305"
FT HELIX 4..8
FT /evidence="ECO:0007829|PDB:7LK3"
FT HELIX 11..24
FT /evidence="ECO:0007829|PDB:7LK3"
FT STRAND 28..35
FT /evidence="ECO:0007829|PDB:7LK3"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:6H8C"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:7LK3"
FT HELIX 57..67
FT /evidence="ECO:0007829|PDB:7LK3"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:7LK3"
FT HELIX 91..98
FT /evidence="ECO:0007829|PDB:7LK3"
FT STRAND 105..113
FT /evidence="ECO:0007829|PDB:7LK3"
SQ SEQUENCE 117 AA; 13667 MW; 17ACB540FD5B975B CRC64;
MKWMFKEDHS LEHRCVESAK IRAKYPDRVP VIVEKVSGSQ IVDIDKRKYL VPSDITVAQF
MWIIRKRIQL PSEKAIFLFV DKTVPQSSLT MGQLYEKEKD EDGFLYVAYS GENTFGF
