GBRL1_HUMAN
ID GBRL1_HUMAN Reviewed; 117 AA.
AC Q9H0R8; B4E0Y7; Q6FIE6;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Gamma-aminobutyric acid receptor-associated protein-like 1;
DE AltName: Full=Early estrogen-regulated protein;
DE AltName: Full=GABA(A) receptor-associated protein-like 1;
DE AltName: Full=Glandular epithelial cell protein 1;
DE Short=GEC-1;
DE Flags: Precursor;
GN Name=GABARAPL1; Synonyms=GEC1;
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] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Placenta;
RX PubMed=11374880; DOI=10.1006/bbrc.2001.4908;
RA Vernier-Magnin S., Muller S., Sallot M., Radom J., Musard J.-F., Adami P.,
RA Dulieu P., Remy-Martin J.-P., Jouvenot M., Fraichard A.;
RT "A novel early estrogen-regulated gene gec1 encodes a protein related to
RT GABARAP.";
RL Biochem. Biophys. Res. Commun. 284:118-125(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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] (ISOFORM 2).
RA Liu C., Yu L.;
RT "Alternative splicing pattern analysis of human Atg8 family proteins.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Thymus;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [8]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Colon;
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 [10]
RP FUNCTION, AND INTERACTION WITH OPRK1.
RX PubMed=16431922; DOI=10.1074/jbc.m509805200;
RA Chen C., Li J.-G., Chen Y., Huang P., Wang Y., Liu-Chen L.-Y.;
RT "GEC1 interacts with the kappa opioid receptor and enhances expression of
RT the receptor.";
RL J. Biol. Chem. 281:7983-7993(2006).
RN [11]
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 [12]
RP FUNCTION, SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE, LIPIDATION AT
RP GLY-116, AND MUTAGENESIS OF GLY-116.
RX PubMed=20404487; DOI=10.4161/auto.6.4.11819;
RA Chakrama F.Z., Seguin-Py S., Le Grand J.N., Fraichard A.,
RA Delage-Mourroux R., Despouy G., Perez V., Jouvenot M., Boyer-Guittaut M.;
RT "GABARAPL1 (GEC1) associates with autophagic vesicles.";
RL Autophagy 6:495-505(2010).
RN [13]
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 [14]
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 [15]
RP INTERACTION WITH MAPK15.
RX PubMed=22948227; DOI=10.4161/auto.21857;
RA Colecchia D., Strambi A., Sanzone S., Iavarone C., Rossi M., Dall'Armi C.,
RA Piccioni F., Verrotti di Pianella A., Chiariello M.;
RT "MAPK15/ERK8 stimulates autophagy by interacting with LC3 and GABARAP
RT proteins.";
RL Autophagy 8:1724-1740(2012).
RN [16]
RP INTERACTION WITH ATG13; RB1CC1 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 [17]
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 [18]
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 [19]
RP DECONJUGATION BY LEGIONELLA RAVZ (MICROBIAL INFECTION).
RX PubMed=23112293; DOI=10.1126/science.1227026;
RA Choy A., Dancourt J., Mugo B., O'Connor T.J., Isberg R.R., Melia T.J.,
RA Roy C.R.;
RT "The Legionella effector RavZ inhibits host autophagy through irreversible
RT Atg8 deconjugation.";
RL Science 338:1072-1076(2012).
RN [20]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=23690988; DOI=10.1371/journal.pone.0063133;
RA Le Grand J.N., Bon K., Fraichard A., Zhang J., Jouvenot M., Risold P.Y.,
RA Boyer-Guittaut M., Delage-Mourroux R.;
RT "Specific distribution of the autophagic protein GABARAPL1/GEC1 in the
RT developing and adult mouse brain and identification of neuronal populations
RT expressing GABARAPL1/GEC1.";
RL PLoS ONE 8:E63133-E63133(2013).
RN [21]
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 [22]
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 [23]
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 [24]
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 [25]
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 [26]
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 [27]
RP PROTEOLYTIC CLEAVAGE, AND SUBCELLULAR LOCATION.
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 [28]
RP INTERACTION WITH TEX264; FUNCTION.
RX PubMed=31006538; DOI=10.1016/j.molcel.2019.03.033;
RA Chino H., Hatta T., Natsume T., Mizushima N.;
RT "Intrinsically disordered protein TEX264 mediates ER-phagy.";
RL Mol. Cell 0:0-0(2019).
RN [29]
RP INTERACTION WITH TEX264; FUNCTION.
RX PubMed=31006537; DOI=10.1016/j.molcel.2019.03.034;
RA An H., Ordureau A., Paulo J.A., Shoemaker C.J., Denic V., Harper J.W.;
RT "TEX264 is an endoplasmic reticulum-resident ATG8-interacting protein
RT critical for ER remodeling during nutrient stress.";
RL Mol. Cell 0:0-0(2019).
RN [30]
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 [31]
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 [32]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 3-111.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human gamma-aminobutyric acid receptor-associated
RT protein-like 1 (GABARAP1).";
RL Submitted (SEP-2007) to the PDB data bank.
RN [33] {ECO:0007744|PDB:5LXH, ECO:0007744|PDB:5LXI}
RP X-RAY CRYSTALLOGRAPHY (1.44 ANGSTROMS) IN COMPLEX WITH ATG4B, PROTEOLYTIC
RP CLEAVAGE, AND MUTAGENESIS OF HIS-9; ARG-28; ARG-47 AND ARG-67.
RX PubMed=28287329; DOI=10.1080/15548627.2017.1287651;
RA Skytte Rasmussen M., Mouilleron S., Kumar Shrestha B., Wirth M., Lee R.,
RA Bowitz Larsen K., Abudu Princely Y., O'Reilly N., Sjottem E., Tooze S.A.,
RA Lamark T., Johansen T.;
RT "ATG4B contains a C-terminal LIR motif important for binding and efficient
RT cleavage of mammalian orthologs of yeast Atg8.";
RL Autophagy 13:834-853(2017).
CC -!- FUNCTION: Ubiquitin-like modifier that increases cell-surface
CC expression of kappa-type opioid receptor through facilitating
CC anterograde intracellular trafficking of the receptor
CC (PubMed:16431922). Involved in formation of autophagosomal vacuoles
CC (PubMed:20404487). While 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:20404487). Through its
CC interaction with the reticulophagy receptor TEX264, participates in the
CC remodeling of subdomains of the endoplasmic reticulum into
CC autophagosomes upon nutrient stress, which then fuse with lysosomes for
CC endoplasmic reticulum turnover (PubMed:31006538, PubMed:31006537).
CC {ECO:0000269|PubMed:16431922, ECO:0000269|PubMed:20404487,
CC ECO:0000269|PubMed:31006537, ECO:0000269|PubMed:31006538}.
CC -!- SUBUNIT: Interacts with ATG13, OPRK1, RB1CC1 and ULK1 (PubMed:16431922,
CC PubMed:23043107). Interacts with TP53INP1 and TP53INP2
CC (PubMed:22470510). Directly interacts with SQSTM1 (PubMed:17580304).
CC Interacts with ATG3, ATG7 and MAP15. Interacts with TECPR2
CC (PubMed:20562859). Interacts with TBC1D5 (PubMed:22354992). Interacts
CC with MAPK15 (PubMed:22948227). Interacts with TRIM5 (PubMed:25127057).
CC Interacts with MEFV and TRIM21 (PubMed:26347139). Interacts with WDFY3
CC (PubMed:24668264). Interacts with the reticulophagy receptor TEX264
CC (PubMed:31006538, PubMed:31006537). Interacts with UBA5
CC (PubMed:26929408). Interacts with KBTBD6 AND KBTBD7; the interaction is
CC direct (PubMed:25684205). {ECO:0000269|PubMed:16431922,
CC ECO:0000269|PubMed:17580304, ECO:0000269|PubMed:20562859,
CC ECO:0000269|PubMed:22354992, ECO:0000269|PubMed:22470510,
CC ECO:0000269|PubMed:22948227, ECO:0000269|PubMed:23043107,
CC ECO:0000269|PubMed:24668264, ECO:0000269|PubMed:25127057,
CC ECO:0000269|PubMed:25684205, ECO:0000269|PubMed:26347139,
CC ECO:0000269|PubMed:26929408, ECO:0000269|PubMed:31006537,
CC ECO:0000269|PubMed:31006538}.
CC -!- INTERACTION:
CC Q9H0R8; Q8IVF2-2: AHNAK2; NbExp=3; IntAct=EBI-746969, EBI-10217765;
CC Q9H0R8; Q8IVF2-3: AHNAK2; NbExp=8; IntAct=EBI-746969, EBI-12078468;
CC Q9H0R8; O75143: ATG13; NbExp=2; IntAct=EBI-746969, EBI-2798775;
CC Q9H0R8; Q2TAZ0: ATG2A; NbExp=3; IntAct=EBI-746969, EBI-2514077;
CC Q9H0R8; Q9NT62: ATG3; NbExp=3; IntAct=EBI-746969, EBI-988094;
CC Q9H0R8; Q8WYN0: ATG4A; NbExp=6; IntAct=EBI-746969, EBI-3044060;
CC Q9H0R8; Q9Y4P1: ATG4B; NbExp=10; IntAct=EBI-746969, EBI-712014;
CC Q9H0R8; O95352: ATG7; NbExp=6; IntAct=EBI-746969, EBI-987834;
CC Q9H0R8; O60238: BNIP3L; NbExp=3; IntAct=EBI-746969, EBI-849893;
CC Q9H0R8; J3KQ12: BSCL2; NbExp=3; IntAct=EBI-746969, EBI-11532900;
CC Q9H0R8; Q9NW68: BSDC1; NbExp=3; IntAct=EBI-746969, EBI-721848;
CC Q9H0R8; Q9P1Z2: CALCOCO1; NbExp=3; IntAct=EBI-746969, EBI-749920;
CC Q9H0R8; Q13137: CALCOCO2; NbExp=7; IntAct=EBI-746969, EBI-739580;
CC Q9H0R8; Q14677: CLINT1; NbExp=2; IntAct=EBI-746969, EBI-1171113;
CC Q9H0R8; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-746969, EBI-11988027;
CC Q9H0R8; Q8WXU2: DNAAF4; NbExp=2; IntAct=EBI-746969, EBI-2946907;
CC Q9H0R8; P63167: DYNLL1; NbExp=3; IntAct=EBI-746969, EBI-349105;
CC Q9H0R8; Q8TF40: FNIP1; NbExp=2; IntAct=EBI-746969, EBI-2946919;
CC Q9H0R8; Q9BQS8: FYCO1; NbExp=2; IntAct=EBI-746969, EBI-2869338;
CC Q9H0R8; P40939: HADHA; NbExp=4; IntAct=EBI-746969, EBI-356720;
CC Q9H0R8; P55084: HADHB; NbExp=4; IntAct=EBI-746969, EBI-356635;
CC Q9H0R8; O00410: IPO5; NbExp=4; IntAct=EBI-746969, EBI-356424;
CC Q9H0R8; Q86V97: KBTBD6; NbExp=4; IntAct=EBI-746969, EBI-2514778;
CC Q9H0R8; Q8WVZ9: KBTBD7; NbExp=6; IntAct=EBI-746969, EBI-473695;
CC Q9H0R8; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-746969, EBI-10172290;
CC Q9H0R8; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-746969, EBI-10172052;
CC Q9H0R8; Q9BQD3: KXD1; NbExp=4; IntAct=EBI-746969, EBI-739657;
CC Q9H0R8; Q9UH92-3: MLX; NbExp=3; IntAct=EBI-746969, EBI-8852072;
CC Q9H0R8; Q14596: NBR1; NbExp=4; IntAct=EBI-746969, EBI-742698;
CC Q9H0R8; Q8NI08: NCOA7; NbExp=2; IntAct=EBI-746969, EBI-80799;
CC Q9H0R8; P46934: NEDD4; NbExp=6; IntAct=EBI-746969, EBI-726944;
CC Q9H0R8; P46934-3: NEDD4; NbExp=3; IntAct=EBI-746969, EBI-11980721;
CC Q9H0R8; Q8TD19: NEK9; NbExp=6; IntAct=EBI-746969, EBI-1044009;
CC Q9H0R8; Q12857-2: NFIA; NbExp=3; IntAct=EBI-746969, EBI-12119652;
CC Q9H0R8; O75323: NIPSNAP2; NbExp=6; IntAct=EBI-746969, EBI-307133;
CC Q9H0R8; Q92636: NSMAF; NbExp=7; IntAct=EBI-746969, EBI-2947053;
CC Q9H0R8; P41145: OPRK1; NbExp=5; IntAct=EBI-746969, EBI-925028;
CC Q9H0R8; Q9H4L5: OSBPL3; NbExp=3; IntAct=EBI-746969, EBI-1051317;
CC Q9H0R8; Q96AQ6: PBXIP1; NbExp=3; IntAct=EBI-746969, EBI-740845;
CC Q9H0R8; P10644: PRKAR1A; NbExp=2; IntAct=EBI-746969, EBI-476431;
CC Q9H0R8; P28070: PSMB4; NbExp=3; IntAct=EBI-746969, EBI-603350;
CC Q9H0R8; Q15256-5: PTPRR; NbExp=3; IntAct=EBI-746969, EBI-18347359;
CC Q9H0R8; Q9Y3P9: RABGAP1; NbExp=2; IntAct=EBI-746969, EBI-1057545;
CC Q9H0R8; Q8WWW0: RASSF5; NbExp=2; IntAct=EBI-746969, EBI-367390;
CC Q9H0R8; Q14257: RCN2; NbExp=4; IntAct=EBI-746969, EBI-356710;
CC Q9H0R8; Q86VR2: RETREG3; NbExp=8; IntAct=EBI-746969, EBI-10192441;
CC Q9H0R8; Q14151: SAFB2; NbExp=2; IntAct=EBI-746969, EBI-352869;
CC Q9H0R8; Q8IZE3: SCYL3; NbExp=3; IntAct=EBI-746969, EBI-1380680;
CC Q9H0R8; Q8IZE3-2: SCYL3; NbExp=3; IntAct=EBI-746969, EBI-11959369;
CC Q9H0R8; Q13501: SQSTM1; NbExp=15; IntAct=EBI-746969, EBI-307104;
CC Q9H0R8; O95210: STBD1; NbExp=8; IntAct=EBI-746969, EBI-2947137;
CC Q9H0R8; Q13188: STK3; NbExp=2; IntAct=EBI-746969, EBI-992580;
CC Q9H0R8; Q13043: STK4; NbExp=2; IntAct=EBI-746969, EBI-367376;
CC Q9H0R8; Q13033-2: STRN3; NbExp=3; IntAct=EBI-746969, EBI-1053876;
CC Q9H0R8; Q86VP1: TAX1BP1; NbExp=3; IntAct=EBI-746969, EBI-529518;
CC Q9H0R8; Q8TC07: TBC1D15; NbExp=2; IntAct=EBI-746969, EBI-1048247;
CC Q9H0R8; Q3MII6: TBC1D25; NbExp=4; IntAct=EBI-746969, EBI-11899977;
CC Q9H0R8; Q9UPU7: TBC1D2B; NbExp=5; IntAct=EBI-746969, EBI-2947180;
CC Q9H0R8; B9A6K1: TBC1D5; NbExp=3; IntAct=EBI-746969, EBI-10217641;
CC Q9H0R8; Q92609: TBC1D5; NbExp=5; IntAct=EBI-746969, EBI-742381;
CC Q9H0R8; O15040: TECPR2; NbExp=2; IntAct=EBI-746969, EBI-2946991;
CC Q9H0R8; Q9BT49: THAP7; NbExp=3; IntAct=EBI-746969, EBI-741350;
CC Q9H0R8; Q0P631: TMEM131; NbExp=5; IntAct=EBI-746969, EBI-12946715;
CC Q9H0R8; Q15025: TNIP1; NbExp=7; IntAct=EBI-746969, EBI-357849;
CC Q9H0R8; Q96A56: TP53INP1; NbExp=9; IntAct=EBI-746969, EBI-9986117;
CC Q9H0R8; Q9GZZ9: UBA5; NbExp=2; IntAct=EBI-746969, EBI-747805;
CC Q9H0R8; O75385: ULK1; NbExp=2; IntAct=EBI-746969, EBI-908831;
CC Q9H0R8; C9J7I0: UMAD1; NbExp=3; IntAct=EBI-746969, EBI-10989060;
CC Q9H0R8; Q8IZQ1: WDFY3; NbExp=3; IntAct=EBI-746969, EBI-1569256;
CC Q9H0R8; O15209: ZBTB22; NbExp=4; IntAct=EBI-746969, EBI-723574;
CC Q9H0R8; Q9Z2F7: Bnip3l; Xeno; NbExp=4; IntAct=EBI-746969, EBI-1774669;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome
CC {ECO:0000269|PubMed:17580304, ECO:0000269|PubMed:20404487,
CC ECO:0000269|PubMed:30661429, ECO:0000305|PubMed:23690988}. Cytoplasmic
CC vesicle membrane {ECO:0000269|PubMed:20404487}; Lipid-anchor
CC {ECO:0000269|PubMed:20404487}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q0VGK0}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q0VGK0}. Golgi apparatus
CC {ECO:0000250|UniProtKB:Q0VGK0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H0R8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H0R8-2; Sequence=VSP_044422;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Expressed at very high levels in the
CC brain, heart, peripheral blood leukocytes, liver, kidney, placenta and
CC skeletal muscle. Expressed at very low levels in thymus and small
CC intestine. In the brain, expression is particularly intense in
CC motoneurons in the embryo and in neurons involved in somatomotor and
CC neuroendocrine functions in the adult, particularly in the substantia
CC nigra pars compacta. {ECO:0000269|PubMed:11374880,
CC ECO:0000269|PubMed:11414770, ECO:0000269|PubMed:23690988}.
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, GABARAPL1-I (PubMed:20404487, PubMed:29458288, PubMed:30661429,
CC PubMed:28287329). 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, GABARAPL1-II
CC (PubMed:20404487, PubMed:29458288). 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 GABARAPL1 recycling when autophagosomes
CC fuse with lysosomes (PubMed:20404487, PubMed:29458288,
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:Q8R3R8,
CC ECO:0000269|PubMed:20404487, ECO:0000269|PubMed:28287329,
CC ECO:0000269|PubMed:29458288, ECO:0000269|PubMed:30661429,
CC 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:23112293,
CC PubMed:31722778). RavZ is also able to mediate delipidation of ATG8
CC proteins conjugated to phosphatidylserine (PS) (PubMed:33909989).
CC {ECO:0000269|PubMed:23112293, ECO:0000269|PubMed:31722778,
CC ECO:0000269|PubMed:33909989}.
CC -!- SIMILARITY: Belongs to the ATG8 family. {ECO:0000305}.
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DR EMBL; AF287012; AAK55962.1; -; mRNA.
DR EMBL; AF087847; AAK20399.1; -; mRNA.
DR EMBL; JN663881; AEZ06294.1; -; mRNA.
DR EMBL; AL136676; CAB66611.1; -; mRNA.
DR EMBL; AK303581; BAG64599.1; -; mRNA.
DR EMBL; CR533480; CAG38511.1; -; mRNA.
DR EMBL; AC115676; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471094; EAW96164.1; -; Genomic_DNA.
DR EMBL; BC009309; AAH09309.1; -; mRNA.
DR EMBL; BC028315; AAH28315.1; -; mRNA.
DR CCDS; CCDS8620.1; -. [Q9H0R8-1]
DR CCDS; CCDS86280.1; -. [Q9H0R8-2]
DR RefSeq; NP_113600.1; NM_031412.2. [Q9H0R8-1]
DR RefSeq; XP_005253401.1; XM_005253344.4.
DR PDB; 2L8J; NMR; -; A=2-115.
DR PDB; 2R2Q; X-ray; 1.65 A; A/B=3-111.
DR PDB; 5DPT; X-ray; 2.90 A; A/B=2-117.
DR PDB; 5LXH; X-ray; 1.58 A; A/B/C=1-117.
DR PDB; 5LXI; X-ray; 1.44 A; B/D=1-117.
DR PDB; 6HOI; X-ray; 1.14 A; A/B=1-117.
DR PDB; 6HOL; X-ray; 1.40 A; A/B=1-117.
DR PDB; 6YOO; X-ray; 1.06 A; A=1-117.
DR PDB; 7AA7; X-ray; 1.45 A; A/B=1-117.
DR PDB; 7AA9; X-ray; 1.72 A; A/C/E/G/I/K=1-117.
DR PDB; 7JHX; X-ray; 1.91 A; A/B=1-117.
DR PDBsum; 2L8J; -.
DR PDBsum; 2R2Q; -.
DR PDBsum; 5DPT; -.
DR PDBsum; 5LXH; -.
DR PDBsum; 5LXI; -.
DR PDBsum; 6HOI; -.
DR PDBsum; 6HOL; -.
DR PDBsum; 6YOO; -.
DR PDBsum; 7AA7; -.
DR PDBsum; 7AA9; -.
DR PDBsum; 7JHX; -.
DR AlphaFoldDB; Q9H0R8; -.
DR SMR; Q9H0R8; -.
DR BioGRID; 117223; 137.
DR DIP; DIP-35597N; -.
DR ELM; Q9H0R8; -.
DR IntAct; Q9H0R8; 536.
DR MINT; Q9H0R8; -.
DR STRING; 9606.ENSP00000266458; -.
DR GlyGen; Q9H0R8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H0R8; -.
DR PhosphoSitePlus; Q9H0R8; -.
DR BioMuta; GABARAPL1; -.
DR DMDM; 44887973; -.
DR EPD; Q9H0R8; -.
DR jPOST; Q9H0R8; -.
DR MassIVE; Q9H0R8; -.
DR MaxQB; Q9H0R8; -.
DR PaxDb; Q9H0R8; -.
DR PeptideAtlas; Q9H0R8; -.
DR PRIDE; Q9H0R8; -.
DR ProteomicsDB; 5710; -.
DR ProteomicsDB; 80321; -. [Q9H0R8-1]
DR Antibodypedia; 42119; 437 antibodies from 30 providers.
DR DNASU; 23710; -.
DR Ensembl; ENST00000266458.10; ENSP00000266458.5; ENSG00000139112.11. [Q9H0R8-1]
DR Ensembl; ENST00000421801.6; ENSP00000411256.2; ENSG00000139112.11. [Q9H0R8-2]
DR Ensembl; ENST00000543602.5; ENSP00000445857.1; ENSG00000139112.11. [Q9H0R8-2]
DR Ensembl; ENST00000545887.1; ENSP00000444186.1; ENSG00000139112.11. [Q9H0R8-1]
DR GeneID; 23710; -.
DR KEGG; hsa:23710; -.
DR MANE-Select; ENST00000266458.10; ENSP00000266458.5; NM_031412.4; NP_113600.1.
DR UCSC; uc001qxs.4; human. [Q9H0R8-1]
DR CTD; 23710; -.
DR DisGeNET; 23710; -.
DR GeneCards; GABARAPL1; -.
DR HGNC; HGNC:4068; GABARAPL1.
DR HPA; ENSG00000139112; Low tissue specificity.
DR MIM; 607420; gene.
DR neXtProt; NX_Q9H0R8; -.
DR OpenTargets; ENSG00000139112; -.
DR PharmGKB; PA28481; -.
DR VEuPathDB; HostDB:ENSG00000139112; -.
DR eggNOG; KOG1654; Eukaryota.
DR GeneTree; ENSGT00940000156876; -.
DR HOGENOM; CLU_146808_0_0_1; -.
DR InParanoid; Q9H0R8; -.
DR OMA; AHDQDIS; -.
DR OrthoDB; 1508198at2759; -.
DR PhylomeDB; Q9H0R8; -.
DR TreeFam; TF314556; -.
DR PathwayCommons; Q9H0R8; -.
DR Reactome; R-HSA-1632852; Macroautophagy.
DR SABIO-RK; Q9H0R8; -.
DR SignaLink; Q9H0R8; -.
DR SIGNOR; Q9H0R8; -.
DR BioGRID-ORCS; 23710; 9 hits in 1075 CRISPR screens.
DR ChiTaRS; GABARAPL1; human.
DR EvolutionaryTrace; Q9H0R8; -.
DR GenomeRNAi; 23710; -.
DR Pharos; Q9H0R8; Tbio.
DR PRO; PR:Q9H0R8; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9H0R8; protein.
DR Bgee; ENSG00000139112; Expressed in Brodmann (1909) area 23 and 212 other tissues.
DR ExpressionAtlas; Q9H0R8; baseline and differential.
DR Genevisible; Q9H0R8; HS.
DR GO; GO:0005776; C:autophagosome; IDA:MGI.
DR GO; GO:0000421; C:autophagosome membrane; IBA:GO_Central.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0048487; F:beta-tubulin binding; ISS:UniProtKB.
DR GO; GO:0050811; F:GABA receptor binding; ISS:UniProtKB.
DR GO; GO:0030957; F:Tat protein binding; IPI: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:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0006995; P:cellular response to nitrogen starvation; IBA:GO_Central.
DR GO; GO:0061723; P:glycophagy; IEA:Ensembl.
DR GO; GO:0016236; P:macroautophagy; IBA:GO_Central.
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; Alternative splicing; Autophagy; Cytoplasm;
KW Cytoplasmic vesicle; Cytoskeleton; Endoplasmic reticulum; Golgi apparatus;
KW Lipoprotein; Membrane; Microtubule; Reference proteome.
FT CHAIN 1..116
FT /note="Gamma-aminobutyric acid receptor-associated protein-
FT like 1"
FT /id="PRO_0000212369"
FT PROPEP 117
FT /note="Removed in mature form"
FT /evidence="ECO:0000305|PubMed:20404487"
FT /id="PRO_0000420208"
FT SITE 115..116
FT /note="(Microbial infection) Cleavage; by RavZ"
FT /evidence="ECO:0000269|PubMed:23112293"
FT SITE 116..117
FT /note="Cleavage; by ATG4B"
FT /evidence="ECO:0000269|PubMed:20404487"
FT LIPID 116
FT /note="Phosphatidylethanolamine amidated glycine;
FT alternate"
FT /evidence="ECO:0000269|PubMed:33909989,
FT ECO:0000305|PubMed:20404487, ECO:0000305|PubMed:29458288"
FT LIPID 116
FT /note="Phosphatidylserine amidated glycine; alternate"
FT /evidence="ECO:0000269|PubMed:33909989"
FT VAR_SEQ 97..117
FT /note="DNHEEDYFLYVAYSDESVYGK -> VMVLVAQYWMPSSAVWHPLALVLDALI
FT THLRSGAEGVIYPDPLTYGSVRL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.3"
FT /id="VSP_044422"
FT MUTAGEN 9
FT /note="H->A: Abolished interaction with ATG4B."
FT /evidence="ECO:0000269|PubMed:28287329"
FT MUTAGEN 28
FT /note="R->A: Does not affect interaction with ATG4B."
FT /evidence="ECO:0000269|PubMed:28287329"
FT MUTAGEN 47
FT /note="R->A: Abolished interaction with ATG4B."
FT /evidence="ECO:0000269|PubMed:28287329"
FT MUTAGEN 67
FT /note="R->A: Abolished interaction with ATG4B."
FT /evidence="ECO:0000269|PubMed:28287329"
FT MUTAGEN 116
FT /note="G->A: No processing of precursor."
FT /evidence="ECO:0000269|PubMed:20404487"
FT HELIX 4..8
FT /evidence="ECO:0007829|PDB:6YOO"
FT HELIX 11..24
FT /evidence="ECO:0007829|PDB:6YOO"
FT STRAND 28..35
FT /evidence="ECO:0007829|PDB:6YOO"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:6YOO"
FT HELIX 57..67
FT /evidence="ECO:0007829|PDB:6YOO"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:6YOO"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:7AA9"
FT HELIX 91..98
FT /evidence="ECO:0007829|PDB:6YOO"
FT STRAND 105..115
FT /evidence="ECO:0007829|PDB:6YOO"
SQ SEQUENCE 117 AA; 14044 MW; 7F56E345255F564B CRC64;
MKFQYKEDHP FEYRKKEGEK IRKKYPDRVP VIVEKAPKAR VPDLDKRKYL VPSDLTVGQF
YFLIRKRIHL RPEDALFFFV NNTIPPTSAT MGQLYEDNHE EDYFLYVAYS DESVYGK
