Q9CQV6 (MLP3B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	Map1lc3b
Synonyms:	Map1alc3, Map1lc3

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	125 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subunit structure	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. Ref.9
Subcellular location	Cytoplasm › cytoskeleton. Endomembrane system; Lipid-anchor. Cytoplasmic vesicle › autophagosome membrane; Lipid-anchor. Note: LC3-II binds to the autophagic membranes By similarity. Localizes also to discrete punctae along the ciliary axoneme. Ref.5 Ref.6 Ref.7 Ref.10
Post-translational modification	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. Ref.6 Ref.7 Phosphorylation at Ser-12 by PKA inhibits conjugation to phosphatidylethanolamine (PE) By similarity. Interaction with MAPK15 reduces the inhibitory phosphorylation and increases autophagy activity By similarity.
Sequence similarities	Belongs to the ATG8 family.

Ontologies

Keywords
Biological process	Autophagy Ubl conjugation pathway
Cellular component	Cytoplasm Cytoplasmic vesicle Cytoskeleton Membrane Microtubule
PTM	Lipoprotein Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	autophagy Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	autophagic vacuole Inferred from direct assay PubMed 22783020. Source: MGI autophagic vacuole membrane Inferred from electronic annotation. Source: UniProtKB-SubCell axoneme Inferred from direct assay Ref.10. Source: UniProtKB cytoplasmic vesicle Inferred from electronic annotation. Source: UniProtKB-KW endomembrane system Inferred from electronic annotation. Source: UniProtKB-SubCell microtubule Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	protein binding Inferred from physical interaction Ref.9. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 120	119	Microtubule-associated proteins 1A/1B light chain 3B		PRO_0000017200
	Propeptide	121 – 125	5	Removed in mature form		PRO_0000017201
Sites
	Site	120 – 121	2	Cleavage; by ATG4B
Amino acid modifications
	Modified residue	12	1	Phosphoserine; by PKA By similarity
	Lipidation	120	1	Phosphatidylethanolamine amidated glycine By similarity
Experimental info
	Sequence conflict	89	1	V → L in BAB22641. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9CQV6 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 520E29028163FA8D	FASTA	125	14,617
	10 20 30 40 50 60 MPSEKTFKQR RSFEQRVEDV RLIREQHPTK IPVIIERYKG EKQLPVLDKT KFLVPDHVNM 70 80 90 100 110 120 SELIKIIRRR LQLNANQAFF LLVNGHSMVS VSTPISEVYE SERDEDGFLY MVYASQETFG TAMAV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"LC3 conjugation system in mammalian autophagy." Tanida I., Ueno T., Kominami E. Int. J. Biochem. Cell Biol. 36:2503-2518(2004) [PubMed] [Europe PMC] [Abstract] 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]	"Functional interaction between autophagy and ciliogenesis." Pampliega O., Orhon I., Patel B., Sridhar S., Diaz-Carretero A., Beau I., Codogno P., Satir B.H., Satir P., Cuervo A.M. Nature 502:194-200(2013) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
CCDS	CCDS22726.1.
RefSeq	NP_080436.1. NM_026160.4.
UniGene	Mm.28357.
3D structure databases
ProteinModelPortal	Q9CQV6.
SMR	Q9CQV6. Positions 5-122.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
BioGrid	212190. 5 interactions.
IntAct	Q9CQV6. 3 interactions.
STRING	10090.ENSMUSP00000034270.
PTM databases
PhosphoSite	Q9CQV6.
Proteomic databases
MaxQB	Q9CQV6.
PaxDb	Q9CQV6.
PRIDE	Q9CQV6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000034270; ENSMUSP00000034270; ENSMUSG00000031812.
GeneID	67443.
KEGG	mmu:67443.
UCSC	uc009nrw.1. mouse.
Organism-specific databases
CTD	81631.
MGI	MGI:1914693. Map1lc3b.
Phylogenomic databases
eggNOG	NOG283348.
GeneTree	ENSGT00390000012937.
HOGENOM	HOG000232034.
HOVERGEN	HBG051706.
InParanoid	Q9CQV6.
KO	K10435.
OrthoDB	EOG7XH6RV.
PhylomeDB	Q9CQV6.
TreeFam	TF312964.
Gene expression databases
ArrayExpress	Q9CQV6.
Bgee	Q9CQV6.
Genevestigator	Q9CQV6.
Family and domain databases
InterPro	IPR004241. Atg8_like. IPR029071. Ubiquitin-rel_dom. [Graphical view]
PANTHER	PTHR10969. PTHR10969. 1 hit.
Pfam	PF02991. Atg8. 1 hit. [Graphical view]
SUPFAM	SSF54236. SSF54236. 1 hit.
ProtoNet	Search...
Other
NextBio	324582.
PRO	Q9CQV6.
SOURCE	Search...

Entry information

Entry name

MLP3B_MOUSE

Accession

Primary (citable) accession number: Q9CQV6
Secondary accession number(s): Q3U9W5, Q9D1R0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2002
Last sequence update:	January 23, 2007
Last modified:	July 9, 2014
This is version 110 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program