ID GBRAP_HUMAN Reviewed; 117 AA. AC O95166; DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 27-MAR-2024, entry version 195. DE RecName: Full=Gamma-aminobutyric acid receptor-associated protein {ECO:0000305}; DE AltName: Full=GABA(A) receptor-associated protein; DE AltName: Full=MM46; DE Flags: Precursor; GN Name=GABARAP {ECO:0000312|HGNC:HGNC:4067}; Synonyms=FLC3B; GN ORFNames=HT004; 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], FUNCTION, TISSUE SPECIFICITY, AND INTERACTION RP WITH GABRG2 AND BETA-TUBULIN. RC TISSUE=Brain; RX PubMed=9892355; DOI=10.1038/16264; RA Wang H., Bedford F.K., Brandon N.J., Moss S.J., Olsen R.W.; RT "GABA(A)-receptor-associated protein links GABA(A) receptors and the RT cytoskeleton."; RL Nature 397:69-72(1999). RN [2] 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 [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Iijima M., Mitsui Y.; RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Ye M., Fu G., Wu J., Zhou J., Zhang Q., Shen Y., Kan L., He K., Gu B., RA Chen S., Mao M., Chen Z.; RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Hypothalamus; RX PubMed=10931946; DOI=10.1073/pnas.160270997; RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J., RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., RA Chen M.-D., Chen J.-L.; RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis RT and full-length cDNA cloning."; RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000). RN [6] 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 [7] 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 [8] 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 [9] RP FUNCTION, 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 [10] RP FUNCTION, AND INTERACTION WITH DDX47. RX PubMed=15977068; DOI=10.1007/s10529-005-3628-2; RA Lee J.H., Rho S.B., Chun T.; RT "GABAA receptor-associated protein (GABARAP) induces apoptosis by RT interacting with DEAD (Asp-Glu-Ala-Asp/His) box polypeptide 47 (DDX 47)."; RL Biotechnol. Lett. 27:623-628(2005). 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 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 [13] 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 [14] RP FUNCTION, INTERACTION WITH TECPR2, AND MUTAGENESIS OF 49-TYR-LEU-50 AND RP ARG-67. 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 [15] 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 [16] 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 [17] RP FUNCTION, AND 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 [18] 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 [19] 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 [20] 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 [21] 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 [22] 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 [23] RP INTERACTION WITH FLCN. RX PubMed=25126726; DOI=10.4161/auto.29640; RA Dunlop E.A., Seifan S., Claessens T., Behrends C., Kamps M.A., Rozycka E., RA Kemp A.J., Nookala R.K., Blenis J., Coull B.J., Murray J.T., RA van Steensel M.A., Wilkinson S., Tee A.R.; RT "FLCN, a novel autophagy component, interacts with GABARAP and is regulated RT by ULK1 phosphorylation."; RL Autophagy 10:1749-1760(2014). RN [24] 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 [25] 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 [26] 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 [27] RP INTERACTION WITH IRGM AND STX17. RX PubMed=29420192; DOI=10.1083/jcb.201708039; RA Kumar S., Jain A., Farzam F., Jia J., Gu Y., Choi S.W., Mudd M.H., RA Claude-Taupin A., Wester M.J., Lidke K.A., Rusten T.E., Deretic V.; RT "Mechanism of Stx17 recruitment to autophagosomes via IRGM and mammalian RT Atg8 proteins."; RL J. Cell Biol. 217:997-1013(2018). RN [28] 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 [29] 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 [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 INTERACTION WITH DNM2. RX PubMed=32315611; DOI=10.1016/j.devcel.2020.03.018; RA Puri C., Manni M.M., Vicinanza M., Hilcenko C., Zhu Y., Runwal G., RA Stamatakou E., Menzies F.M., Mamchaoui K., Bitoun M., Rubinsztein D.C.; RT "A DNM2 Centronuclear Myopathy Mutation Reveals a Link between Recycling RT Endosome Scission and Autophagy."; RL Dev. Cell 53:154.e6-168.e6(2020). RN [32] RP INTERACTION WITH RETREG1; RETREG2 AND RETREG3. RX PubMed=34338405; DOI=10.15252/embr.202052289; RA Reggio A., Buonomo V., Berkane R., Bhaskara R.M., Tellechea M., Peluso I., RA Polishchuk E., Di Lorenzo G., Cirillo C., Esposito M., Hussain A., RA Huebner A.K., Huebner C.A., Settembre C., Hummer G., Grumati P., Stolz A.; RT "Role of FAM134 paralogues in endoplasmic reticulum remodeling, ER-phagy, RT and Collagen quality control."; RL EMBO Rep. 22:e52289-e52289(2021). RN [33] 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 [34] RP INTERACTION WITH CT55. RX PubMed=36481789; DOI=10.1038/s41418-022-01098-6; RA Zhang G., Jiang C., Yang Y., Wang Y., Zhou H., Dai S., Liu M., Yang Y., RA Yang L., Shen Q., Zhang T., Zhang X., Yang Y., Shen Y.; RT "Deficiency of cancer/testis antigen gene CT55 causes male infertility in RT humans and mice."; RL Cell Death Differ. 30:500-514(2023). RN [35] RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS), AND INTERACTION WITH GABRG2; RP ALPHA-TUBULIN AND BETA-TUBULIN. RX PubMed=11729197; DOI=10.1074/jbc.m109753200; RA Knight D., Harris R., McAlister M.S.B., Phelan J.P., Geddes S., Moss S.J., RA Driscoll P.C., Keep N.H.; RT "The X-ray crystal structure and putative ligand-derived peptide binding RT properties of gamma-aminobutyric acid receptor type A receptor-associated RT protein."; RL J. Biol. Chem. 277:5556-5561(2002). RN [36] RP STRUCTURE BY NMR. RX PubMed=11875056; DOI=10.1074/jbc.c200050200; RA Stangler T., Mayr L.M., Willbold D.; RT "Solution structure of human GABA(A) receptor-associated protein GABARAP: RT implications for biological function and its regulation."; RL J. Biol. Chem. 277:13363-13366(2002). RN [37] RP STRUCTURE BY NMR. RX PubMed=11885988; DOI=10.1023/a:1013884402033; RA Kouno T., Miura K., Kanematsu T., Shirakawa M., Hirata M., Kawano K.; RT "1H, 13C and '5N resonance assignments of GABARAP, GABAA receptor RT associated protein."; RL J. Biomol. NMR 22:97-98(2002). RN [38] RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS). RX PubMed=18638487; DOI=10.1016/j.jmb.2008.06.086; RA Weiergraber O.H., Stangler T., Thielmann Y., Mohrluder J., Wiesehan K., RA Willbold D.; RT "Ligand binding mode of GABAA receptor-associated protein."; RL J. Mol. Biol. 381:1320-1331(2008). RN [39] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH CALR, AND INTERACTION RP WITH CALR. RX PubMed=19154346; DOI=10.1111/j.1742-4658.2008.06857.x; RA Thielmann Y., Weiergraber O.H., Mohrluder J., Willbold D.; RT "Structural framework of the GABARAP-calreticulin interface -- implications RT for substrate binding to endoplasmic reticulum chaperones."; RL FEBS J. 276:1140-1152(2009). RN [40] {ECO:0007744|PDB:3WIM} RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH WDFY3, INTERACTION RP WITH SQSTM1, AND MUTAGENESIS OF LYS-24; TYR-25 AND ASP-54. 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 [41] {ECO:0007744|PDB:4XC2} RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 3-116 IN COMPLEX WITH KBTBD6 AIM RP MOTIF, FUNCTION, AND 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 [42] {ECO:0007744|PDB:7BRQ, ECO:0007744|PDB:7BRT, ECO:0007744|PDB:7BRU} RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 1-116 IN CHIMERIC CONSTRUCTS WITH RP RETREG1; RTN3 AND SEC62. RX PubMed=32620754; DOI=10.1038/s41467-020-17163-y; RA Mochida K., Yamasaki A., Matoba K., Kirisako H., Noda N.N., Nakatogawa H.; RT "Super-assembly of ER-phagy receptor Atg40 induces local ER remodeling at RT contacts with forming autophagosomal membranes."; RL Nat. Commun. 11:3306-3306(2020). RN [43] {ECO:0007744|PDB:8AFI} RP X-RAY CRYSTALLOGRAPHY (2.66 ANGSTROMS) OF 2-116 IN COMPLEX WITH ATG3, RP INTERACTION WITH ATG3, REGION, AND SITE. RX PubMed=37252361; DOI=10.1021/acscentsci.3c00009; RA Farnung J., Muhar M., Liang J.R., Tolmachova K.A., Benoit R.M., Corn J.E., RA Bode J.W.; RT "Semisynthetic LC3 Probes for Autophagy Pathways Reveal a Noncanonical LC3 RT Interacting Region Motif Crucial for the Enzymatic Activity of Human RT ATG3."; RL ACS Cent. Sci. 9:1025-1034(2023). CC -!- FUNCTION: Ubiquitin-like modifier that plays a role in intracellular CC transport of GABA(A) receptors and its interaction with the CC cytoskeleton (PubMed:9892355). Involved in autophagy: while LC3s are CC involved in elongation of the phagophore membrane, the GABARAP/GATE-16 CC subfamily is essential for a later stage in autophagosome maturation CC (PubMed:15169837, PubMed:20562859, PubMed:22948227). 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). Also required for the CC local activation of the CUL3(KBTBD6/7) E3 ubiquitin ligase complex, CC regulating ubiquitination and degradation of TIAM1, a guanyl-nucleotide CC exchange factor (GEF) that activates RAC1 and downstream signal CC transduction (PubMed:25684205). Thereby, regulates different biological CC processes including the organization of the cytoskeleton, cell CC migration and proliferation (PubMed:25684205). Involved in apoptosis CC (PubMed:15977068). {ECO:0000269|PubMed:15169837, CC ECO:0000269|PubMed:15977068, ECO:0000269|PubMed:20562859, CC ECO:0000269|PubMed:22948227, ECO:0000269|PubMed:25684205, CC ECO:0000269|PubMed:31006538, ECO:0000269|PubMed:9892355}. CC -!- SUBUNIT: Interacts with GPHN and NSF (By similarity). Interacts with CC ATG7, ATG13 (PubMed:11096062, PubMed:12507496, PubMed:23043107). CC Interacts with ATG3 (PubMed:37252361, PubMed:11825910, CC PubMed:12507496). Interacts with alpha- and beta-tubulin CC (PubMed:9892355, PubMed:11729197). Interacts with GABRG2 CC (PubMed:9892355, PubMed:11729197). Interacts with RB1CC1 CC (PubMed:23043107). Interacts with ULK1 (PubMed:11146101, CC PubMed:23043107). Interacts with CALR (PubMed:19154346). Interacts with CC DDX47 (PubMed:15977068). Interacts with TP53INP1 and TP53INP2 CC (PubMed:19056683, PubMed:22421968, PubMed:22470510). Interacts with CC TBC1D5 and TBC1D25 (PubMed:21383079, PubMed:22354992). Directly CC interacts with SQSTM1 (PubMed:17580304, PubMed:24668264). Interacts CC with MAPK15 (PubMed:22948227). Interacts with TECPR2 (PubMed:20562859). CC Interacts with PCM1 (PubMed:24089205). Interacts with TRIM5 and TRIM21 CC (PubMed:25127057, PubMed:26347139). Interacts with MEFV CC (PubMed:26347139). Interacts with KIF21B (By similarity). Interacts CC with WDFY3; this interaction is required for WDFY3 recruitment to CC MAP1LC3B-positive p62/SQSTM1 bodies (PubMed:24668264). Interacts with CC the reticulophagy receptor TEX264 (PubMed:31006538). Interacts with CC UBA5 (PubMed:26929408). Interacts with FLCN; interaction regulates CC autophagy (PubMed:25126726). Interacts with KBTBD6 and KBTBD7; the CC interaction is direct and required for the ubiquitination of TIAM1 CC (PubMed:25684205). Interacts with reticulophagy regulators RETREG1, CC RETREG2 and RETREG3 (PubMed:34338405). Interacts with IRGM CC (PubMed:29420192). Interacts with STX17 (PubMed:29420192). Interacts CC with CT55; this interaction may be important for GABARAP protein CC stability (PubMed:36481789). Interacts with DNM2 (PubMed:32315611). CC {ECO:0000250|UniProtKB:P60517, ECO:0000269|PubMed:11096062, CC ECO:0000269|PubMed:11146101, ECO:0000269|PubMed:11729197, CC ECO:0000269|PubMed:11825910, ECO:0000269|PubMed:12507496, CC ECO:0000269|PubMed:15977068, ECO:0000269|PubMed:17580304, CC ECO:0000269|PubMed:19056683, ECO:0000269|PubMed:19154346, CC ECO:0000269|PubMed:20562859, ECO:0000269|PubMed:21383079, CC ECO:0000269|PubMed:22354992, ECO:0000269|PubMed:22421968, CC ECO:0000269|PubMed:22470510, ECO:0000269|PubMed:22948227, CC ECO:0000269|PubMed:23043107, ECO:0000269|PubMed:24089205, CC ECO:0000269|PubMed:24668264, ECO:0000269|PubMed:25126726, CC ECO:0000269|PubMed:25127057, ECO:0000269|PubMed:25684205, CC ECO:0000269|PubMed:26347139, ECO:0000269|PubMed:26929408, CC ECO:0000269|PubMed:29420192, ECO:0000269|PubMed:31006538, CC ECO:0000269|PubMed:32315611, ECO:0000269|PubMed:34338405, CC ECO:0000269|PubMed:36481789, ECO:0000269|PubMed:9892355}. CC -!- INTERACTION: CC O95166; O75143: ATG13; NbExp=3; IntAct=EBI-712001, EBI-2798775; CC O95166; Q2TAZ0: ATG2A; NbExp=2; IntAct=EBI-712001, EBI-2514077; CC O95166; Q9NT62: ATG3; NbExp=5; IntAct=EBI-712001, EBI-988094; CC O95166; Q9Y4P1: ATG4B; NbExp=8; IntAct=EBI-712001, EBI-712014; CC O95166; Q9H1Y0: ATG5; NbExp=2; IntAct=EBI-712001, EBI-1047414; CC O95166; O95352: ATG7; NbExp=8; IntAct=EBI-712001, EBI-987834; CC O95166; P27797: CALR; NbExp=4; IntAct=EBI-712001, EBI-1049597; CC O95166; Q9H0S4: DDX47; NbExp=3; IntAct=EBI-712001, EBI-2515241; CC O95166; Q8WXU2: DNAAF4; NbExp=4; IntAct=EBI-712001, EBI-2946907; CC O95166; Q96RU3: FNBP1; NbExp=2; IntAct=EBI-712001, EBI-1111248; CC O95166; Q8TF40: FNIP1; NbExp=5; IntAct=EBI-712001, EBI-2946919; CC O95166; Q9BQS8: FYCO1; NbExp=2; IntAct=EBI-712001, EBI-2869338; CC O95166; P18507-2: GABRG2; NbExp=3; IntAct=EBI-712001, EBI-15096952; CC O95166; P40939: HADHA; NbExp=5; IntAct=EBI-712001, EBI-356720; CC O95166; O00410: IPO5; NbExp=6; IntAct=EBI-712001, EBI-356424; CC O95166; Q86V97: KBTBD6; NbExp=3; IntAct=EBI-712001, EBI-2514778; CC O95166; Q8WVZ9: KBTBD7; NbExp=2; IntAct=EBI-712001, EBI-473695; CC O95166; Q86YT6: MIB1; NbExp=3; IntAct=EBI-712001, EBI-2129148; CC O95166; Q14596: NBR1; NbExp=6; IntAct=EBI-712001, EBI-742698; CC O95166; Q8NI08: NCOA7; NbExp=4; IntAct=EBI-712001, EBI-80799; CC O95166; P46934: NEDD4; NbExp=6; IntAct=EBI-712001, EBI-726944; CC O95166; Q8TD19: NEK9; NbExp=5; IntAct=EBI-712001, EBI-1044009; CC O95166; O75323: NIPSNAP2; NbExp=5; IntAct=EBI-712001, EBI-307133; CC O95166; Q92636: NSMAF; NbExp=2; IntAct=EBI-712001, EBI-2947053; CC O95166; Q15154: PCM1; NbExp=8; IntAct=EBI-712001, EBI-741421; CC O95166; Q9Y4G2: PLEKHM1; NbExp=2; IntAct=EBI-712001, EBI-473814; CC O95166; Q9NS23: RASSF1; NbExp=2; IntAct=EBI-712001, EBI-367363; CC O95166; Q8WWW0: RASSF5; NbExp=2; IntAct=EBI-712001, EBI-367390; CC O95166; Q13501: SQSTM1; NbExp=17; IntAct=EBI-712001, EBI-307104; CC O95166; O95210: STBD1; NbExp=6; IntAct=EBI-712001, EBI-2947137; CC O95166; Q13188: STK3; NbExp=2; IntAct=EBI-712001, EBI-992580; CC O95166; Q13043: STK4; NbExp=2; IntAct=EBI-712001, EBI-367376; CC O95166; Q8TC07: TBC1D15; NbExp=5; IntAct=EBI-712001, EBI-1048247; CC O95166; Q9UPU7: TBC1D2B; NbExp=2; IntAct=EBI-712001, EBI-2947180; CC O95166; O15040: TECPR2; NbExp=2; IntAct=EBI-712001, EBI-2946991; CC O95166; Q96A56: TP53INP1; NbExp=3; IntAct=EBI-712001, EBI-9986117; CC O95166; Q969E8: TSR2; NbExp=5; IntAct=EBI-712001, EBI-746981; CC O95166; Q9GZZ9: UBA5; NbExp=2; IntAct=EBI-712001, EBI-747805; CC O95166; Q9Z2F7: Bnip3l; Xeno; NbExp=2; IntAct=EBI-712001, EBI-1774669; CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane CC {ECO:0000269|PubMed:12507496, ECO:0000269|PubMed:15169837, CC ECO:0000269|PubMed:17580304, ECO:0000269|PubMed:19056683}. Endomembrane CC system {ECO:0000250|UniProtKB:P60517}. Cytoplasm, cytoskeleton CC {ECO:0000250|UniProtKB:P60517}. Golgi apparatus membrane CC {ECO:0000250|UniProtKB:P60517}. Cytoplasmic vesicle CC {ECO:0000250|UniProtKB:P60517}. Note=Largely associated with CC intracellular membrane structures including the Golgi apparatus and CC postsynaptic cisternae. Colocalizes with microtubules (By similarity). CC Localizes also to discrete punctae along the ciliary axoneme (By CC similarity). {ECO:0000250|UniProtKB:P60517, CC ECO:0000250|UniProtKB:Q9DCD6}. CC -!- TISSUE SPECIFICITY: Heart, brain, placenta, liver, skeletal muscle, CC kidney and pancreas. {ECO:0000269|PubMed:11146101, CC ECO:0000269|PubMed:9892355}. 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, GABARAP-I (PubMed:15169837, PubMed:20818167, PubMed:30661429). CC The processed form is then activated by APG7L/ATG7, transferred to ATG3 CC and conjugated to phosphatidylethanolamine (PE) phospholipid to form CC the membrane-bound form, GABARAP-II (PubMed:15169837). During non- CC canonical autophagy, the processed form is conjugated to CC phosphatidylserine (PS) phospholipid (PubMed:33909989). ATG4 proteins CC also mediate the delipidation of PE-conjugated forms (PubMed:33909989). CC In addition, ATG4B and ATG4D mediate delipidation of ATG8 proteins CC conjugated to PS during non-canonical autophagy (PubMed:33909989). CC ATG4B constitutes the major protein for proteolytic activation CC (PubMed:30661429). ATG4D is the main enzyme for delipidation activity CC (By similarity). {ECO:0000250|UniProtKB:Q9DCD6, CC ECO:0000269|PubMed:15169837, ECO:0000269|PubMed:20818167, CC ECO:0000269|PubMed:30661429, 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 -!- SIMILARITY: Belongs to the ATG8 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF161586; AAD47641.1; -; mRNA. DR EMBL; AB030711; BAB21549.1; -; mRNA. DR EMBL; AF044671; AAD02337.1; -; mRNA. DR EMBL; AF067171; AAD32455.1; -; mRNA. DR EMBL; AF183425; AAG09694.1; -; mRNA. DR CCDS; CCDS11092.1; -. DR RefSeq; NP_009209.1; NM_007278.1. DR PDB; 1GNU; X-ray; 1.75 A; A=1-117. DR PDB; 1KLV; NMR; -; A=1-117. DR PDB; 1KM7; NMR; -; A=1-117. DR PDB; 1KOT; NMR; -; A=1-117. DR PDB; 3D32; X-ray; 1.30 A; A/B=1-117. DR PDB; 3DOW; X-ray; 2.30 A; A=1-117. DR PDB; 3WIM; X-ray; 2.60 A; A=1-117. DR PDB; 4XC2; X-ray; 1.90 A; A/B/C/D=3-116. DR PDB; 5DPS; X-ray; 2.00 A; A/B/C=2-117. DR PDB; 6HB9; X-ray; 1.30 A; A=3-116. DR PDB; 6HOG; X-ray; 1.26 A; A=2-112. DR PDB; 6HOH; X-ray; 2.25 A; A/B/C/D=2-112. DR PDB; 6HOJ; X-ray; 1.51 A; A/B/C=1-112. DR PDB; 6HOK; X-ray; 1.61 A; A=1-112. DR PDB; 6HYL; X-ray; 1.56 A; A/B=1-117. DR PDB; 6HYM; X-ray; 1.86 A; A/B=1-117. DR PDB; 6HYN; X-ray; 1.14 A; A=1-117. DR PDB; 6HYO; X-ray; 1.07 A; A=1-117. DR PDB; 6YOP; X-ray; 1.10 A; A=1-117. DR PDB; 7AA8; X-ray; 1.25 A; C=1-117. DR PDB; 7BRQ; X-ray; 1.40 A; A=1-116. DR PDB; 7BRT; X-ray; 2.00 A; A/B=1-116. DR PDB; 7BRU; X-ray; 2.15 A; A/B/C=1-116. DR PDB; 7BV4; X-ray; 2.00 A; A/B/E/G=1-117. DR PDB; 7EA7; X-ray; 2.69 A; A/B=1-117. DR PDB; 7LSW; X-ray; 3.05 A; A/B/C/D/E/F=1-117. DR PDB; 7LT6; X-ray; 1.80 A; A/B/C=1-117. DR PDB; 7VEC; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J/K/L=1-116. DR PDB; 7VED; X-ray; 2.02 A; A/B=1-116. DR PDB; 7YO9; X-ray; 1.75 A; A=1-116. DR PDB; 7ZKR; X-ray; 1.10 A; A=1-117. DR PDB; 7ZL7; X-ray; 1.55 A; A/C=1-117. DR PDB; 8AFI; X-ray; 2.66 A; A/C/E/G/I/K/M/O=2-116. DR PDBsum; 1GNU; -. DR PDBsum; 1KLV; -. DR PDBsum; 1KM7; -. DR PDBsum; 1KOT; -. DR PDBsum; 3D32; -. DR PDBsum; 3DOW; -. DR PDBsum; 3WIM; -. DR PDBsum; 4XC2; -. DR PDBsum; 5DPS; -. DR PDBsum; 6HB9; -. DR PDBsum; 6HOG; -. DR PDBsum; 6HOH; -. DR PDBsum; 6HOJ; -. DR PDBsum; 6HOK; -. DR PDBsum; 6HYL; -. DR PDBsum; 6HYM; -. DR PDBsum; 6HYN; -. DR PDBsum; 6HYO; -. DR PDBsum; 6YOP; -. DR PDBsum; 7AA8; -. DR PDBsum; 7BRQ; -. DR PDBsum; 7BRT; -. DR PDBsum; 7BRU; -. DR PDBsum; 7BV4; -. DR PDBsum; 7EA7; -. DR PDBsum; 7LSW; -. DR PDBsum; 7LT6; -. DR PDBsum; 7VEC; -. DR PDBsum; 7VED; -. DR PDBsum; 7YO9; -. DR PDBsum; 7ZKR; -. DR PDBsum; 7ZL7; -. DR PDBsum; 8AFI; -. DR AlphaFoldDB; O95166; -. DR BMRB; O95166; -. DR SMR; O95166; -. DR BioGRID; 116465; 112. DR DIP; DIP-35050N; -. DR ELM; O95166; -. DR IntAct; O95166; 502. DR MINT; O95166; -. DR STRING; 9606.ENSP00000306866; -. DR ChEMBL; CHEMBL4879423; -. DR MoonDB; O95166; Predicted. DR TCDB; 1.A.9.5.2; the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family. DR iPTMnet; O95166; -. DR PhosphoSitePlus; O95166; -. DR BioMuta; GABARAP; -. DR EPD; O95166; -. DR jPOST; O95166; -. DR MassIVE; O95166; -. DR PaxDb; 9606-ENSP00000306866; -. DR PeptideAtlas; O95166; -. DR ProteomicsDB; 50679; -. DR Pumba; O95166; -. DR Antibodypedia; 11841; 760 antibodies from 37 providers. DR DNASU; 11337; -. DR Ensembl; ENST00000302386.10; ENSP00000306866.5; ENSG00000170296.10. DR GeneID; 11337; -. DR KEGG; hsa:11337; -. DR MANE-Select; ENST00000302386.10; ENSP00000306866.5; NM_007278.2; NP_009209.1. DR AGR; HGNC:4067; -. DR CTD; 11337; -. DR DisGeNET; 11337; -. DR GeneCards; GABARAP; -. DR HGNC; HGNC:4067; GABARAP. DR HPA; ENSG00000170296; Low tissue specificity. DR MIM; 605125; gene. DR neXtProt; NX_O95166; -. DR OpenTargets; ENSG00000170296; -. DR PharmGKB; PA28480; -. DR VEuPathDB; HostDB:ENSG00000170296; -. DR eggNOG; KOG1654; Eukaryota. DR GeneTree; ENSGT00940000157496; -. DR HOGENOM; CLU_119276_0_0_1; -. DR InParanoid; O95166; -. DR OMA; AVYQEHK; -. DR OrthoDB; 652940at2759; -. DR PhylomeDB; O95166; -. DR TreeFam; TF314556; -. DR PathwayCommons; O95166; -. DR Reactome; R-HSA-1632852; Macroautophagy. DR Reactome; R-HSA-8854214; TBC/RABGAPs. DR SABIO-RK; O95166; -. DR SignaLink; O95166; -. DR SIGNOR; O95166; -. DR BioGRID-ORCS; 11337; 68 hits in 1158 CRISPR screens. DR ChiTaRS; GABARAP; human. DR EvolutionaryTrace; O95166; -. DR GeneWiki; GABARAP; -. DR GenomeRNAi; 11337; -. DR Pharos; O95166; Tbio. DR PRO; PR:O95166; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; O95166; Protein. DR Bgee; ENSG00000170296; Expressed in right testis and 97 other cell types or tissues. DR ExpressionAtlas; O95166; baseline and differential. DR GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl. DR GO; GO:0005776; C:autophagosome; IDA:UniProtKB. DR GO; GO:0000421; C:autophagosome membrane; IDA:UniProtKB. DR GO; GO:0005930; C:axoneme; ISS:UniProtKB. DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005764; C:lysosome; IEA:Ensembl. DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW. DR GO; GO:0005875; C:microtubule associated complex; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; TAS:ProtInc. DR GO; GO:0005790; C:smooth endoplasmic reticulum; IEA:Ensembl. DR GO; GO:0097225; C:sperm midpiece; IEA:Ensembl. DR GO; GO:0045202; C:synapse; IEA:GOC. DR GO; GO:0048487; F:beta-tubulin binding; IDA:UniProtKB. DR GO; GO:0050811; F:GABA receptor binding; IPI:UniProtKB. DR GO; GO:0008017; F:microtubule binding; IEA:Ensembl. DR GO; GO:0008429; F:phosphatidylethanolamine binding; IDA:UniProt. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB. DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central. DR GO; GO:0006995; P:cellular response to nitrogen starvation; IBA:GO_Central. DR GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc. DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IDA:UniProtKB. DR GO; GO:0016236; P:macroautophagy; IBA:GO_Central. DR GO; GO:0000226; P:microtubule cytoskeleton organization; IEA:Ensembl. DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB. DR GO; GO:1902524; P:positive regulation of protein K48-linked ubiquitination; IMP:UniProtKB. DR GO; GO:0006605; P:protein targeting; TAS:ProtInc. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0035020; P:regulation of Rac protein signal transduction; IMP:UniProtKB. DR CDD; cd17232; Ubl_ATG8_GABARAP; 1. DR InterPro; IPR004241; Atg8-like. DR InterPro; IPR029071; Ubiquitin-like_domsf. DR PANTHER; PTHR10969:SF20; GAMMA-AMINOBUTYRIC ACID RECEPTOR-ASSOCIATED PROTEIN; 1. DR PANTHER; PTHR10969; MICROTUBULE-ASSOCIATED PROTEINS 1A/1B LIGHT CHAIN 3-RELATED; 1. DR Pfam; PF02991; ATG8; 1. DR SUPFAM; SSF54236; Ubiquitin-like; 1. DR Genevisible; O95166; HS. PE 1: Evidence at protein level; KW 3D-structure; Apoptosis; Autophagy; Cytoplasm; Cytoplasmic vesicle; KW Cytoskeleton; Golgi apparatus; Lipoprotein; Membrane; Microtubule; KW Protein transport; Reference proteome; Transport. FT CHAIN 1..116 FT /note="Gamma-aminobutyric acid receptor-associated protein" FT /id="PRO_0000212363" FT PROPEP 117 FT /note="Removed in mature form" FT /evidence="ECO:0000269|PubMed:15169837" FT /id="PRO_0000423065" FT REGION 1..22 FT /note="Interaction with beta-tubulin" FT /evidence="ECO:0000269|PubMed:9892355" FT REGION 36..117 FT /note="Interaction with GPHN" FT /evidence="ECO:0000250|UniProtKB:Q9DCD6" FT REGION 36..68 FT /note="Interaction with GABRG2" FT /evidence="ECO:0000269|PubMed:9892355" FT REGION 48..50 FT /note="Interaction with LIR (LC3 nteracting Region) motif FT of ATG3" FT /evidence="ECO:0000269|PubMed:37252361, FT ECO:0007744|PDB:8AFI" FT SITE 17 FT /note="Interaction with LIR (LC3 nteracting Region) motif FT of ATG3" FT /evidence="ECO:0000269|PubMed:37252361, FT ECO:0007744|PDB:8AFI" FT SITE 28 FT /note="Interaction with LIR (LC3 nteracting Region) motif FT of ATG3" FT /evidence="ECO:0000269|PubMed:37252361, FT ECO:0007744|PDB:8AFI" FT SITE 116..117 FT /note="Cleavage; by ATG4B" FT /evidence="ECO:0000269|PubMed:15169837" FT LIPID 116 FT /note="Phosphatidylethanolamine amidated glycine; FT alternate" FT /evidence="ECO:0000269|PubMed:12507496, FT ECO:0000269|PubMed:33909989" FT LIPID 116 FT /note="Phosphatidylserine amidated glycine; alternate" FT /evidence="ECO:0000269|PubMed:33909989" FT MUTAGEN 24 FT /note="K->Q: No effect on WDFY3-binding. Impaired FT WDFY3-binding, but no effect on SQSTM1-binding; when FT associated with H-25 and H-54." FT /evidence="ECO:0000269|PubMed:24668264" FT MUTAGEN 25 FT /note="Y->H: No effect on WDFY3-binding. Impaired FT WDFY3-binding, but no effect on SQSTM1-binding; when FT associated with Q-24 and H-54." FT /evidence="ECO:0000269|PubMed:24668264" FT MUTAGEN 49..50 FT /note="YL->AA: Inhibits interaction with TECPR2." FT /evidence="ECO:0000269|PubMed:20562859" FT MUTAGEN 54 FT /note="D->H: No effect on WDFY3-binding. Impaired FT WDFY3-binding, but no effect on SQSTM1-binding; when FT associated with Q-24 and H-25." FT /evidence="ECO:0000269|PubMed:24668264" FT MUTAGEN 67 FT /note="R->A: No effect on interaction with TECPR2." FT /evidence="ECO:0000269|PubMed:20562859" FT MUTAGEN 116 FT /note="G->A: Impairs localization at the autophagosomal FT membrane." FT /evidence="ECO:0000269|PubMed:15169837" FT HELIX 4..8 FT /evidence="ECO:0007829|PDB:6HYO" FT HELIX 11..24 FT /evidence="ECO:0007829|PDB:6HYO" FT STRAND 28..35 FT /evidence="ECO:0007829|PDB:6HYO" FT STRAND 48..52 FT /evidence="ECO:0007829|PDB:6HYO" FT HELIX 57..67 FT /evidence="ECO:0007829|PDB:6HYO" FT STRAND 72..74 FT /evidence="ECO:0007829|PDB:8AFI" FT STRAND 77..80 FT /evidence="ECO:0007829|PDB:6HYO" FT STRAND 87..90 FT /evidence="ECO:0007829|PDB:7BV4" FT HELIX 91..98 FT /evidence="ECO:0007829|PDB:6HYO" FT STRAND 101..103 FT /evidence="ECO:0007829|PDB:1KM7" FT STRAND 105..114 FT /evidence="ECO:0007829|PDB:6HYO" SQ SEQUENCE 117 AA; 13918 MW; BC0B84B8A51C1E32 CRC64; MKFVYKEEHP FEKRRSEGEK IRKKYPDRVP VIVEKAPKAR IGDLDKKKYL VPSDLTVGQF YFLIRKRIHL RAEDALFFFV NNVIPPTSAT MGQLYQEHHE EDFFLYIAYS DESVYGL //