ID MP3B2_HUMAN Reviewed; 125 AA.
AC A6NCE7;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 128.
DE RecName: Full=Microtubule-associated proteins 1A/1B light chain 3 beta 2;
DE AltName: Full=Microtubule-associated proteins 1A/1B light chain 3B-like;
DE Flags: Precursor;
GN Name=MAP1LC3B2;
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 [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Birkett C., Cho J., Gau Y., Hamer R., Kelly S., Kovacs K., Liu L., Liu X.,
RA Porter J., Sachs A., Shu Y., Sun Z., Wong J., Wu M., Zhang X., Jay G.,
RA He W.;
RT "High-throughput cloning of full-length human cDNAs directly from cDNA
RT libraries optimized for large and rare transcripts.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
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).
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.
CC {ECO:0000250|UniProtKB:Q9GZQ8}.
CC -!- SUBUNIT: 3 different light chains, LC1, LC2 and LC3, can associate with
CC MAP1A and MAP1B proteins. {ECO:0000250|UniProtKB:Q9GZQ8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane
CC {ECO:0000250|UniProtKB:Q9GZQ8}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q9GZQ8}. Endomembrane system
CC {ECO:0000250|UniProtKB:Q9GZQ8}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q9GZQ8}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q9CQV6}.
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:30661429). The processed form is then activated by
CC 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 (By similarity). In addition, ATG4B and ATG4D mediate
CC delipidation of ATG8 proteins conjugated to PS during non-canonical
CC autophagy (By similarity). {ECO:0000250|UniProtKB:Q9GZQ8,
CC ECO:0000269|PubMed:30661429}.
CC -!- SIMILARITY: Belongs to the ATG8 family. {ECO:0000305}.
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DR EMBL; DN994744; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC125603; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW98085.1; -; Genomic_DNA.
DR CCDS; CCDS41841.1; -.
DR RefSeq; NP_001078950.1; NM_001085481.1.
DR AlphaFoldDB; A6NCE7; -.
DR BMRB; A6NCE7; -.
DR SMR; A6NCE7; -.
DR BioGRID; 568619; 20.
DR IntAct; A6NCE7; 11.
DR STRING; 9606.ENSP00000450524; -.
DR iPTMnet; A6NCE7; -.
DR PhosphoSitePlus; A6NCE7; -.
DR SwissPalm; A6NCE7; -.
DR BioMuta; MAP1LC3B2; -.
DR EPD; A6NCE7; -.
DR jPOST; A6NCE7; -.
DR MassIVE; A6NCE7; -.
DR MaxQB; A6NCE7; -.
DR PaxDb; 9606-ENSP00000450524; -.
DR PeptideAtlas; A6NCE7; -.
DR ProteomicsDB; 828; -.
DR Pumba; A6NCE7; -.
DR TopDownProteomics; A6NCE7; -.
DR Antibodypedia; 75194; 32 antibodies from 7 providers.
DR DNASU; 643246; -.
DR Ensembl; ENST00000556529.4; ENSP00000450524.1; ENSG00000258102.5.
DR GeneID; 643246; -.
DR KEGG; hsa:643246; -.
DR MANE-Select; ENST00000556529.4; ENSP00000450524.1; NM_001085481.3; NP_001078950.1.
DR UCSC; uc009zwk.2; human.
DR AGR; HGNC:34390; -.
DR CTD; 643246; -.
DR DisGeNET; 643246; -.
DR GeneCards; MAP1LC3B2; -.
DR HGNC; HGNC:34390; MAP1LC3B2.
DR HPA; ENSG00000258102; Tissue enhanced (brain).
DR neXtProt; NX_A6NCE7; -.
DR OpenTargets; ENSG00000258102; -.
DR PharmGKB; PA162394969; -.
DR VEuPathDB; HostDB:ENSG00000258102; -.
DR eggNOG; KOG1654; Eukaryota.
DR GeneTree; ENSGT00940000154158; -.
DR HOGENOM; CLU_119276_1_0_1; -.
DR InParanoid; A6NCE7; -.
DR OMA; DHIPLVC; -.
DR OrthoDB; 652940at2759; -.
DR PhylomeDB; A6NCE7; -.
DR TreeFam; TF312964; -.
DR PathwayCommons; A6NCE7; -.
DR SignaLink; A6NCE7; -.
DR BioGRID-ORCS; 643246; 11 hits in 730 CRISPR screens.
DR ChiTaRS; MAP1LC3B2; human.
DR GenomeRNAi; 643246; -.
DR Pharos; A6NCE7; Tdark.
DR PRO; PR:A6NCE7; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; A6NCE7; Protein.
DR Bgee; ENSG00000258102; Expressed in cerebellar hemisphere and 97 other cell types or tissues.
DR Genevisible; A6NCE7; HS.
DR GO; GO:0005776; C:autophagosome; IBA:GO_Central.
DR GO; GO:0000421; C:autophagosome membrane; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR GO; GO:0097352; P:autophagosome maturation; IBA:GO_Central.
DR GO; GO:0006995; P:cellular response to nitrogen starvation; IBA:GO_Central.
DR GO; GO:0016236; P:macroautophagy; IBA:GO_Central.
DR CDD; cd17235; Ubl_ATG8_MAP1LC3B; 1.
DR InterPro; IPR004241; Atg8-like.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10969; MICROTUBULE-ASSOCIATED PROTEINS 1A/1B LIGHT CHAIN 3-RELATED; 1.
DR PANTHER; PTHR10969:SF15; MICROTUBULE-ASSOCIATED PROTEINS 1A_1B LIGHT CHAIN 3 BETA 2-RELATED; 1.
DR Pfam; PF02991; ATG8; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
PE 1: Evidence at protein level;
KW Autophagy; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Lipoprotein;
KW Membrane; Microtubule; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..120
FT /note="Microtubule-associated proteins 1A/1B light chain 3
FT beta 2"
FT /id="PRO_0000343732"
FT PROPEP 121..125
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:Q9GZQ8"
FT /id="PRO_0000343733"
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"
SQ SEQUENCE 125 AA; 14628 MW; BB141DEC6AA1E83F CRC64;
MPSEKTFKQR RTFEQRVEDV RLIREQHPTK IPVIIERYKG EKQLPVLDKT KFLVPDHVNM
SELIKIIRRR LQLNANQAFF LLVNGHSMVS VSTPISEVYE SEKDEDGFLY MVCASQETFG
MKLSV
//
