MLP3B_MOUSE
ID MLP3B_MOUSE Reviewed; 125 AA.
AC Q9CQV6; Q3U9W5; Q9D1R0;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Microtubule-associated proteins 1A/1B light chain 3B {ECO:0000305};
DE AltName: Full=Autophagy-related protein LC3 B;
DE AltName: Full=Autophagy-related ubiquitin-like modifier LC3 B;
DE AltName: Full=MAP1 light chain 3-like protein 2;
DE AltName: Full=MAP1A/MAP1B light chain 3 B;
DE Short=MAP1A/MAP1B LC3 B;
DE AltName: Full=Microtubule-associated protein 1 light chain 3 beta;
DE Flags: Precursor;
GN Name=Map1lc3b {ECO:0000312|MGI:MGI:1914693}; Synonyms=Map1alc3, Map1lc3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Yu L.;
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Embryo, Head, Heart, and Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [4]
RP PROTEIN SEQUENCE OF 31-37 AND 52-65, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=11266458; DOI=10.1083/jcb.152.4.657;
RA Mizushima N., Yamamoto A., Hatano M., Kobayashi Y., Kabeya Y., Suzuki K.,
RA Tokuhisa T., Ohsumi Y., Yoshimori T.;
RT "Dissection of autophagosome formation using Apg5-deficient mouse embryonic
RT stem cells.";
RL J. Cell Biol. 152:657-668(2001).
RN [6]
RP SUBCELLULAR LOCATION, AND PROTEOLYTIC CLEAVAGE.
RX PubMed=12207896; DOI=10.1016/s0006-291x(02)02057-0;
RA Tanida I., Nishitani T., Nemoto T., Ueno T., Kominami E.;
RT "Mammalian Apg12p, but not the Apg12p.Apg5p conjugate, facilitates LC3
RT processing.";
RL Biochem. Biophys. Res. Commun. 296:1164-1170(2002).
RN [7]
RP CLEAVAGE BY ATG4B, AND SUBCELLULAR LOCATION.
RX PubMed=14530254; DOI=10.1074/jbc.m308762200;
RA Hemelaar J., Lelyveld V.S., Kessler B.M., Ploegh H.L.;
RT "A single protease, Apg4B, is specific for the autophagy-related ubiquitin-
RT like proteins GATE-16, MAP1-LC3, GABARAP, and Apg8L.";
RL J. Biol. Chem. 278:51841-51850(2003).
RN [8]
RP REVIEW.
RX PubMed=15325588; DOI=10.1016/j.biocel.2004.05.009;
RA Tanida I., Ueno T., Kominami E.;
RT "LC3 conjugation system in mammalian autophagy.";
RL Int. J. Biochem. Cell Biol. 36:2503-2518(2004).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [10]
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 [11]
RP INTERACTION WITH PLCL1.
RX PubMed=23399561; DOI=10.1016/j.bbrc.2013.01.119;
RA Umebayashi H., Mizokami A., Matsuda M., Harada K., Takeuchi H., Tanida I.,
RA Hirata M., Kanematsu T.;
RT "Phospholipase C-related catalytically inactive protein, a novel
RT microtubule-associated protein 1 light chain 3-binding protein, negatively
RT regulates autophagosome formation.";
RL Biochem. Biophys. Res. Commun. 432:268-274(2013).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=24089209; DOI=10.1038/nature12639;
RA Pampliega O., Orhon I., Patel B., Sridhar S., Diaz-Carretero A., Beau I.,
RA Codogno P., Satir B.H., Satir P., Cuervo A.M.;
RT "Functional interaction between autophagy and ciliogenesis.";
RL Nature 502:194-200(2013).
RN [13]
RP INTERACTION WITH CRY1 AND PER2.
RX PubMed=29937374; DOI=10.1016/j.cmet.2018.05.023;
RA Toledo M., Batista-Gonzalez A., Merheb E., Aoun M.L., Tarabra E., Feng D.,
RA Sarparanta J., Merlo P., Botre F., Schwartz G.J., Pessin J.E., Singh R.;
RT "Autophagy regulates the liver clock and glucose metabolism by degrading
RT CRY1.";
RL Cell Metab. 28:268-281(2018).
RN [14]
RP INTERACTION WITH PJVK.
RX PubMed=30936319; DOI=10.1073/pnas.1821844116;
RA Defourny J., Aghaie A., Perfettini I., Avan P., Delmaghani S., Petit C.;
RT "Pejvakin-mediated pexophagy protects auditory hair cells against noise-
RT induced damage.";
RL Proc. Natl. Acad. Sci. U.S.A. 116:8010-8017(2019).
RN [15]
RP LIPIDATION, AND DELIPIDATION.
RX PubMed=33795848; DOI=10.1038/s41418-021-00776-1;
RA Tamargo-Gomez I., Martinez-Garcia G.G., Suarez M.F., Rey V., Fueyo A.,
RA Codina-Martinez H., Bretones G., Caravia X.M., Morel E., Dupont N.,
RA Cabo R., Tomas-Zapico C., Souquere S., Pierron G., Codogno P.,
RA Lopez-Otin C., Fernandez A.F., Marino G.;
RT "ATG4D is the main ATG8 delipidating enzyme in mammalian cells and protects
RT against cerebellar neurodegeneration.";
RL Cell Death Differ. 28:2651-2672(2021).
CC -!- FUNCTION: Ubiquitin-like modifier involved in formation of
CC autophagosomal vacuoles (autophagosomes). Plays a role in mitophagy
CC which contributes to regulate mitochondrial quantity and quality by
CC eliminating the mitochondria to a basal level to fulfill cellular
CC energy requirements and preventing excess ROS production. In response
CC to cellular stress and upon mitochondria fission, binds C-18 ceramides
CC and anchors autophagolysosomes to outer mitochondrial membranes to
CC eliminate damaged mitochondria. While LC3s are involved in elongation
CC of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential
CC for a later stage in autophagosome maturation. Promotes primary
CC ciliogenesis by removing OFD1 from centriolar satellites via the
CC autophagic pathway. Through its interaction with the reticulophagy
CC receptor TEX264, participates in the remodeling of subdomains of the
CC endoplasmic reticulum into autophagosomes upon nutrient stress, which
CC then fuse with lysosomes for endoplasmic reticulum turnover. Upon
CC nutrient stress, directly recruits cofactor JMY to the phagophore
CC membrane surfaces and promotes JMY's actin nucleation activity and
CC autophagosome biogenesis during autophagy.
CC {ECO:0000250|UniProtKB:Q9GZQ8}.
CC -!- SUBUNIT: 3 different light chains, LC1, LC2 and LC3, can associate with
CC MAP1A and MAP1B proteins (By similarity). Interacts at microtubules
CC with CABP1 (via EF-hands 1 and 2) but not with calmodulin. Interacts
CC with FYCO1 (via C-terminus). Interacts with TP53INP1 and TP53INP2 (By
CC similarity). Interacts with TBC1D25 (PubMed:21383079). Directly
CC interacts with SQSTM1; this interaction leads to MAP1LC3B recruitment
CC to inclusion bodies containing polyubiquitinated protein aggregates and
CC to inclusion body degradation by autophagy. Interacts with ATG4B,
CC MAPK15 and BNIP3. Interacts with MAPB1, KEAP1, PCM1, OFD1, CEP131, and
CC TECPR2. Interacts with TBC1D5. Found in a complex with UBQLN1 and
CC UBQLN2. Interacts with UBQLN4 (via STI1 1 and 2 domains). Interacts
CC with UBQLN1 in the presence of UBQLN4. Interacts with ATG13. Interacts
CC with RETREG1, RETREG2 and RETREG3 (By similarity). Interacts with
CC PLCL1; the interaction inhibits autophagosome formation
CC (PubMed:23399561). Interacts with TRIM16. Interacts with CRY1 and PER2
CC (PubMed:29937374). Interacts with the reticulophagy receptor TEX264 (By
CC similarity). Membrane-bound form LC3-II interacts with PHB1 and PHB2;
CC the interaction takes place upon Parkin-mediated mitochondrial damage
CC (By similarity). Interacts with PJVK; the interaction is direct
CC (PubMed:30936319). Interacts with KBTBD6 and KBTBD7; the interaction is
CC direct (By similarity). Interacts with AMBRA1 (via LIR motif) (By
CC similarity). Interacts with JMY; the interaction results in the
CC activation of JYM's nucleation activity in the cytoplasm (By
CC similarity). Interacts with MOAP1 (via LIR motif) (By similarity).
CC {ECO:0000250|UniProtKB:Q62625, ECO:0000250|UniProtKB:Q9GZQ8,
CC ECO:0000269|PubMed:21383079, ECO:0000269|PubMed:23399561,
CC ECO:0000269|PubMed:29937374, ECO:0000269|PubMed:30936319}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane
CC {ECO:0000269|PubMed:11266458, ECO:0000269|PubMed:12207896}; Lipid-
CC anchor {ECO:0000250|UniProtKB:Q9GZQ8}. Endomembrane system
CC {ECO:0000269|PubMed:12207896}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q9GZQ8}. Mitochondrion membrane
CC {ECO:0000250|UniProtKB:Q9GZQ8}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q9GZQ8}. Cytoplasm, cytoskeleton
CC {ECO:0000305|PubMed:12207896}. Cytoplasmic vesicle
CC {ECO:0000250|UniProtKB:Q9GZQ8}. Note=LC3-II binds to the autophagic
CC membranes. LC3-II localizes with the mitochondrial inner membrane
CC during Parkin-mediated mitophagy (By similarity). Localizes also to
CC discrete punctae along the ciliary axoneme (By similarity).
CC {ECO:0000250|UniProtKB:Q9GZQ8}.
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, LC3-I (PubMed:12207896, PubMed:14530254). The processed form is
CC then activated by APG7L/ATG7, transferred to ATG3 and conjugated to
CC phosphatidylethanolamine (PE) phospholipid to form the membrane-bound
CC form, LC3-II (By similarity). During non-canonical autophagy, the
CC processed form is conjugated to phosphatidylserine (PS) phospholipid
CC (By similarity). ATG4 proteins also mediate the delipidation of PE-
CC conjugated forms (PubMed:33795848). In addition, ATG4B and ATG4D
CC mediate delipidation of ATG8 proteins conjugated to PS during non-
CC canonical autophagy (By similarity). ATG4B constitutes the major
CC protein for proteolytic activation (By similarity). ATG4D is the main
CC enzyme for delipidation activity (PubMed:33795848).
CC {ECO:0000250|UniProtKB:Q9GZQ8, ECO:0000269|PubMed:12207896,
CC ECO:0000269|PubMed:14530254, ECO:0000269|PubMed:33795848}.
CC -!- PTM: Phosphorylation by PKA inhibits conjugation of
CC phosphatidylethanolamine (PE). Interaction with MAPK15 reduces the
CC inhibitory phosphorylation and increases autophagy activity.
CC {ECO:0000250|UniProtKB:Q9GZQ8}.
CC -!- SIMILARITY: Belongs to the ATG8 family. {ECO:0000305}.
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DR EMBL; AF255953; AAL83723.1; -; mRNA.
DR EMBL; AK002795; BAB22364.1; -; mRNA.
DR EMBL; AK003106; BAB22569.1; -; mRNA.
DR EMBL; AK003205; BAB22641.1; -; mRNA.
DR EMBL; AK003558; BAB22855.1; -; mRNA.
DR EMBL; AK012604; BAB28350.1; -; mRNA.
DR EMBL; AK132329; BAE21108.1; -; mRNA.
DR EMBL; AK151614; BAE30551.1; -; mRNA.
DR EMBL; BC068180; AAH68180.1; -; mRNA.
DR CCDS; CCDS22726.1; -.
DR RefSeq; NP_080436.1; NM_026160.4.
DR PDB; 5WRD; X-ray; 1.90 A; A/B=1-125.
DR PDB; 5YIQ; X-ray; 2.60 A; A=1-125.
DR PDB; 5YIS; X-ray; 2.20 A; A/B=1-125.
DR PDBsum; 5WRD; -.
DR PDBsum; 5YIQ; -.
DR PDBsum; 5YIS; -.
DR AlphaFoldDB; Q9CQV6; -.
DR BMRB; Q9CQV6; -.
DR SMR; Q9CQV6; -.
DR BioGRID; 212190; 29.
DR DIP; DIP-61580N; -.
DR ELM; Q9CQV6; -.
DR IntAct; Q9CQV6; 7.
DR MINT; Q9CQV6; -.
DR STRING; 10090.ENSMUSP00000034270; -.
DR iPTMnet; Q9CQV6; -.
DR PhosphoSitePlus; Q9CQV6; -.
DR SwissPalm; Q9CQV6; -.
DR MaxQB; Q9CQV6; -.
DR PaxDb; Q9CQV6; -.
DR PRIDE; Q9CQV6; -.
DR ProteomicsDB; 290260; -.
DR DNASU; 67443; -.
DR Ensembl; ENSMUST00000034270; ENSMUSP00000034270; ENSMUSG00000031812.
DR GeneID; 67443; -.
DR KEGG; mmu:67443; -.
DR UCSC; uc009nrw.1; mouse.
DR CTD; 81631; -.
DR MGI; MGI:1914693; Map1lc3b.
DR VEuPathDB; HostDB:ENSMUSG00000031812; -.
DR eggNOG; KOG1654; Eukaryota.
DR HOGENOM; CLU_119276_1_0_1; -.
DR InParanoid; Q9CQV6; -.
DR OMA; EFSHDER; -.
DR OrthoDB; 1508198at2759; -.
DR PhylomeDB; Q9CQV6; -.
DR TreeFam; TF312964; -.
DR Reactome; R-MMU-1632852; Macroautophagy.
DR Reactome; R-MMU-5205685; PINK1-PRKN Mediated Mitophagy.
DR Reactome; R-MMU-8854214; TBC/RABGAPs.
DR Reactome; R-MMU-8934903; Receptor Mediated Mitophagy.
DR Reactome; R-MMU-9664873; Pexophagy.
DR Reactome; R-MMU-9755511; KEAP1-NFE2L2 pathway.
DR BioGRID-ORCS; 67443; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Map1lc3b; mouse.
DR PRO; PR:Q9CQV6; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9CQV6; protein.
DR Bgee; ENSMUSG00000031812; Expressed in external carotid artery and 256 other tissues.
DR ExpressionAtlas; Q9CQV6; baseline and differential.
DR Genevisible; Q9CQV6; MM.
DR GO; GO:0044754; C:autolysosome; IDA:MGI.
DR GO; GO:0005776; C:autophagosome; IDA:CAFA.
DR GO; GO:0000421; C:autophagosome membrane; ISO:MGI.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0005930; C:axoneme; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005875; C:microtubule associated complex; ISO:MGI.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0097001; F:ceramide binding; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0015631; F:tubulin binding; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR GO; GO:0097352; P:autophagosome maturation; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; IDA:CAFA.
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:0009267; P:cellular response to starvation; ISS:UniProtKB.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0016236; P:macroautophagy; IBA:GO_Central.
DR GO; GO:0000423; P:mitophagy; ISS:UniProtKB.
DR GO; GO:0070254; P:mucus secretion; IMP:MGI.
DR GO; GO:0070257; P:positive regulation of mucus secretion; IMP:MGI.
DR GO; GO:0032092; P:positive regulation of protein binding; ISO:MGI.
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; Autophagy; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW Direct protein sequencing; Lipoprotein; Membrane; Microtubule;
KW Mitochondrion; Phosphoprotein; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..120
FT /note="Microtubule-associated proteins 1A/1B light chain
FT 3B"
FT /id="PRO_0000017200"
FT PROPEP 121..125
FT /note="Removed in mature form"
FT /id="PRO_0000017201"
FT SITE 120..121
FT /note="Cleavage; by ATG4B"
FT /evidence="ECO:0000250|UniProtKB:Q9GZQ8"
FT LIPID 120
FT /note="Phosphatidylethanolamine amidated glycine;
FT alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9GZQ8"
FT LIPID 120
FT /note="Phosphatidylserine amidated glycine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9GZQ8"
FT CONFLICT 89
FT /note="V -> L (in Ref. 2; BAB22641)"
FT /evidence="ECO:0000305"
FT HELIX 7..10
FT /evidence="ECO:0007829|PDB:5WRD"
FT HELIX 13..26
FT /evidence="ECO:0007829|PDB:5WRD"
FT STRAND 30..37
FT /evidence="ECO:0007829|PDB:5WRD"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:5WRD"
FT HELIX 60..70
FT /evidence="ECO:0007829|PDB:5WRD"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:5WRD"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:5WRD"
FT HELIX 95..102
FT /evidence="ECO:0007829|PDB:5WRD"
FT STRAND 109..115
FT /evidence="ECO:0007829|PDB:5WRD"
FT HELIX 118..122
FT /evidence="ECO:0007829|PDB:5YIS"
SQ SEQUENCE 125 AA; 14617 MW; 520E29028163FA8D CRC64;
MPSEKTFKQR RSFEQRVEDV RLIREQHPTK IPVIIERYKG EKQLPVLDKT KFLVPDHVNM
SELIKIIRRR LQLNANQAFF LLVNGHSMVS VSTPISEVYE SERDEDGFLY MVYASQETFG
TAMAV
