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Protein

Microtubule-associated proteins 1A/1B light chain 3B

Gene

Map1lc3b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Ubiquitin-like modifier involved in formation of autophagosomal vacuoles (autophagosomes). Plays a role in mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Whereas LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei120 – 1212Cleavage; by ATG4B

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Autophagy, Ubl conjugation pathway

Names & Taxonomyi

Protein namesi
Recommended name:
Microtubule-associated proteins 1A/1B light chain 3B
Alternative name(s):
Autophagy-related protein LC3 B
Autophagy-related ubiquitin-like modifier LC3 B
MAP1 light chain 3-like protein 2
MAP1A/MAP1B light chain 3 B
Short name:
MAP1A/MAP1B LC3 B
Microtubule-associated protein 1 light chain 3 beta
Gene namesi
Name:Map1lc3b
Synonyms:Map1alc3, Map1lc3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1914693. Map1lc3b.

Subcellular locationi

GO - Cellular componenti

  • autophagic vacuole Source: MGI
  • autophagic vacuole membrane Source: GO_Central
  • axoneme Source: UniProtKB
  • cytoplasmic vesicle Source: UniProtKB-KW
  • cytosol Source: GO_Central
  • endomembrane system Source: UniProtKB-SubCell
  • extrinsic component of membrane Source: GO_Central
  • intracellular Source: MGI
  • membrane Source: MGI
  • microtubule Source: UniProtKB-KW
  • mitochondrion Source: MGI
  • pre-autophagosomal structure Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Membrane, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 120119Microtubule-associated proteins 1A/1B light chain 3BPRO_0000017200Add
BLAST
Propeptidei121 – 1255Removed in mature formPRO_0000017201

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei12 – 121Phosphoserine; by PKABy similarity
Lipidationi120 – 1201Phosphatidylethanolamine amidated glycineBy similarity

Post-translational modificationi

The precursor molecule is cleaved by APG4B/ATG4B to form LC3-I. This is activated by APG7L/ATG7, transferred to ATG3 and conjugated to phospholipid to form LC3-II (By similarity).By similarity
Phosphorylation at Ser-12 by PKA inhibits conjugation to phosphatidylethanolamine (PE). Interaction with MAPK15 reduces the inhibitory phosphorylation and increases autophagy activity.By similarity

Keywords - PTMi

Lipoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ9CQV6.
PaxDbiQ9CQV6.
PRIDEiQ9CQV6.

PTM databases

PhosphoSiteiQ9CQV6.

Expressioni

Gene expression databases

BgeeiQ9CQV6.
ExpressionAtlasiQ9CQV6. baseline and differential.
GenevisibleiQ9CQV6. MM.

Interactioni

Subunit structurei

3 different light chains, LC1, LC2 and LC3, can associate with MAP1A and MAP1B proteins (By similarity). Interacts with CABP1 (By similarity). Interacts with FYCO1 (via C-terminus) (By similarity). Interacts with TP53INP1 and TP53INP2 (By similarity). Interacts with TBC1D25. Directly interacts with SQSTM1; this interaction leads to MAP1LC3B recruitment to inclusion bodies containing polyubiquitinated protein aggregates and to inclusion body degradation by autophagy (By similarity). Interacts with ATG4B, MAPK15 and BNIP3 (By similarity). Interacts with MAPB1, KEAP1, PCM1, OFD1, CEP131, and TECPR2 (By similarity). Interacts with TBC1D5 (By similarity). Found in a complex with UBQLN1 and UBQLN2 (By similarity). Interacts with UBQLN4 (via STI1 1 and 2 domains) (By similarity). Interacts with UBQLN1 in the presence of UBQLN4 (By similarity).By similarity1 Publication

Protein-protein interaction databases

BioGridi212190. 5 interactions.
IntActiQ9CQV6. 4 interactions.
STRINGi10090.ENSMUSP00000034270.

Structurei

3D structure databases

ProteinModelPortaliQ9CQV6.
SMRiQ9CQV6. Positions 5-122.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATG8 family.Curated

Phylogenomic databases

eggNOGiNOG283348.
GeneTreeiENSGT00390000012937.
HOGENOMiHOG000232034.
HOVERGENiHBG051706.
InParanoidiQ9CQV6.
KOiK10435.
OrthoDBiEOG7XH6RV.
PhylomeDBiQ9CQV6.
TreeFamiTF312964.

Family and domain databases

InterProiIPR004241. Atg8_like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PANTHERiPTHR10969. PTHR10969. 1 hit.
PfamiPF02991. Atg8. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9CQV6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSEKTFKQR RSFEQRVEDV RLIREQHPTK IPVIIERYKG EKQLPVLDKT
60 70 80 90 100
KFLVPDHVNM SELIKIIRRR LQLNANQAFF LLVNGHSMVS VSTPISEVYE
110 120
SERDEDGFLY MVYASQETFG TAMAV
Length:125
Mass (Da):14,617
Last modified:January 23, 2007 - v3
Checksum:i520E29028163FA8D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti89 – 891V → L in BAB22641 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF255953 mRNA. Translation: AAL83723.1.
AK002795 mRNA. Translation: BAB22364.1.
AK003106 mRNA. Translation: BAB22569.1.
AK003205 mRNA. Translation: BAB22641.1.
AK003558 mRNA. Translation: BAB22855.1.
AK012604 mRNA. Translation: BAB28350.1.
AK132329 mRNA. Translation: BAE21108.1.
AK151614 mRNA. Translation: BAE30551.1.
BC068180 mRNA. Translation: AAH68180.1.
CCDSiCCDS22726.1.
RefSeqiNP_080436.1. NM_026160.4.
UniGeneiMm.28357.

Genome annotation databases

EnsembliENSMUST00000034270; ENSMUSP00000034270; ENSMUSG00000031812.
GeneIDi67443.
KEGGimmu:67443.
UCSCiuc009nrw.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF255953 mRNA. Translation: AAL83723.1.
AK002795 mRNA. Translation: BAB22364.1.
AK003106 mRNA. Translation: BAB22569.1.
AK003205 mRNA. Translation: BAB22641.1.
AK003558 mRNA. Translation: BAB22855.1.
AK012604 mRNA. Translation: BAB28350.1.
AK132329 mRNA. Translation: BAE21108.1.
AK151614 mRNA. Translation: BAE30551.1.
BC068180 mRNA. Translation: AAH68180.1.
CCDSiCCDS22726.1.
RefSeqiNP_080436.1. NM_026160.4.
UniGeneiMm.28357.

3D structure databases

ProteinModelPortaliQ9CQV6.
SMRiQ9CQV6. Positions 5-122.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212190. 5 interactions.
IntActiQ9CQV6. 4 interactions.
STRINGi10090.ENSMUSP00000034270.

PTM databases

PhosphoSiteiQ9CQV6.

Proteomic databases

MaxQBiQ9CQV6.
PaxDbiQ9CQV6.
PRIDEiQ9CQV6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034270; ENSMUSP00000034270; ENSMUSG00000031812.
GeneIDi67443.
KEGGimmu:67443.
UCSCiuc009nrw.1. mouse.

Organism-specific databases

CTDi81631.
MGIiMGI:1914693. Map1lc3b.

Phylogenomic databases

eggNOGiNOG283348.
GeneTreeiENSGT00390000012937.
HOGENOMiHOG000232034.
HOVERGENiHBG051706.
InParanoidiQ9CQV6.
KOiK10435.
OrthoDBiEOG7XH6RV.
PhylomeDBiQ9CQV6.
TreeFamiTF312964.

Miscellaneous databases

NextBioi324582.
PROiQ9CQV6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CQV6.
ExpressionAtlasiQ9CQV6. baseline and differential.
GenevisibleiQ9CQV6. MM.

Family and domain databases

InterProiIPR004241. Atg8_like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PANTHERiPTHR10969. PTHR10969. 1 hit.
PfamiPF02991. Atg8. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Yu L.
    Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Bone marrow, Embryo, Head, Heart and Kidney.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6.
    Tissue: Brain.
  4. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 31-37 AND 52-65, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain.
  5. "Dissection of autophagosome formation using Apg5-deficient mouse embryonic stem cells."
    Mizushima N., Yamamoto A., Hatano M., Kobayashi Y., Kabeya Y., Suzuki K., Tokuhisa T., Ohsumi Y., Yoshimori T.
    J. Cell Biol. 152:657-668(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  6. "Mammalian Apg12p, but not the Apg12p.Apg5p conjugate, facilitates LC3 processing."
    Tanida I., Nishitani T., Nemoto T., Ueno T., Kominami E.
    Biochem. Biophys. Res. Commun. 296:1164-1170(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE.
  7. "A single protease, Apg4B, is specific for the autophagy-related ubiquitin-like proteins GATE-16, MAP1-LC3, GABARAP, and Apg8L."
    Hemelaar J., Lelyveld V.S., Kessler B.M., Ploegh H.L.
    J. Biol. Chem. 278:51841-51850(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE BY ATG4B, SUBCELLULAR LOCATION.
  8. Cited for: REVIEW.
  9. "OATL1, a novel autophagosome-resident Rab33B-GAP, regulates autophagosomal maturation."
    Itoh T., Kanno E., Uemura T., Waguri S., Fukuda M.
    J. Cell Biol. 192:839-853(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TBC1D25.
  10. Cited for: SUBCELLULAR LOCATION.

Entry informationi

Entry nameiMLP3B_MOUSE
AccessioniPrimary (citable) accession number: Q9CQV6
Secondary accession number(s): Q3U9W5, Q9D1R0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 119 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.