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Q9H492 (MLP3A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Microtubule-associated proteins 1A/1B light chain 3A
Alternative name(s):
Autophagy-related protein LC3 A
Autophagy-related ubiquitin-like modifier LC3 A
MAP1 light chain 3-like protein 1
MAP1A/MAP1B light chain 3 A
Short name=MAP1A/MAP1B LC3 A
Microtubule-associated protein 1 light chain 3 alpha
Gene names
Name:MAP1LC3A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length121 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Ubiquitin-like modifier involved in formation of autophagosomal vacuoles (autophagosomes). Whereas LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation. Ref.12

Subunit structure

3 different light chains, LC1, LC2 and LC3, can associate with MAP1A and MAP1B proteins By similarity. Interacts with SQSTM1 By similarity. Interacts with TP53INP1 and TP53INP2. Directly interacts with SQSTM1; this interaction leads to MAP1LC3A recruitment to inclusion bodies containing polyubiquitinated protein aggregates and to inclusion body degradation by autophagy. Interacts with ATG13 and ULK1. Ref.7 Ref.8 Ref.10 Ref.11 Ref.14 Ref.15

Subcellular location

Cytoplasmcytoskeleton. Endomembrane system; Lipid-anchor. Cytoplasmic vesicleautophagosome membrane; Lipid-anchor. Note: LC3-II binds to the autophagic membranes. Ref.1 Ref.10 Ref.11 Ref.13

Tissue specificity

Most abundant in heart, brain, liver, skeletal muscle and testis but absent in thymus and peripheral blood leukocytes. Ref.1

Post-translational modification

The precursor molecule is cleaved by ATG4B to form the cytosolic form, LC3-I. This is activated by APG7L/ATG7, transferred to ATG3 and conjugated to phospholipid to form the membrane-bound form, LC3-II (Ref.9). Ref.9

The Legionella effector RavZ is a deconjugating enzyme that produces an ATG8 product that would be resistant to reconjugation by the host machinery due to the cleavage of the reactive C-terminal glycine.

Phosphorylation at Ser-12 by PKA inhibits conjugation to phosphatidylethanolamine (PE). Interaction with MAPK15 reduces the inhibitory phosphorylation and increases autophagy activity.

Sequence similarities

Belongs to the ATG8 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Bnip3lQ9Z2F77EBI-720768,EBI-1774669From a different organism.
NBR1Q145965EBI-720768,EBI-742698
SQSTM1Q135017EBI-720768,EBI-307104
UBQLN4Q9NRR53EBI-720768,EBI-711226

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9H492-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9H492-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-13: MPSDRPFKQRRSF → MKMRFFSSPCGKAAVDP
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 120120Microtubule-associated proteins 1A/1B light chain 3A
PRO_0000017192
Propeptide1211Removed in mature form
PRO_0000017193

Sites

Site120 – 1212Cleavage; by ATG4B By similarity

Amino acid modifications

Modified residue121Phosphoserine; by PKA Ref.12
Lipidation1201Phosphatidylethanolamine amidated glycine Probable

Natural variations

Alternative sequence1 – 1313MPSDR…QRRSF → MKMRFFSSPCGKAAVDP in isoform 2.
VSP_013660

Experimental info

Mutagenesis1201G → A: No processing of precursor. Ref.1

Secondary structure

........................ 121
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 10, 2005. Version 2.
Checksum: 48C1FBE8F7892AF3

FASTA12114,272
        10         20         30         40         50         60 
MPSDRPFKQR RSFADRCKEV QQIRDQHPSK IPVIIERYKG EKQLPVLDKT KFLVPDHVNM 

        70         80         90        100        110        120 
SELVKIIRRR LQLNPTQAFF LLVNQHSMVS VSTPIADIYE QEKDEDGFLY MVYASQETFG 


F 

« Hide

Isoform 2 [UniParc].

Checksum: 097697B5424FC425
Show »

FASTA12514,493

References

« Hide 'large scale' references
[1]"Post-translational modifications of three members of the human MAP1LC3 family and detection of a novel type of modification for MAP1LC3B."
He H., Dang Y., Dai F., Guo Z., Wu J., She X., Pei Y., Chen Y., Ling W., Wu C., Zhao S., Liu J.O., Yu L.
J. Biol. Chem. 278:29278-29287(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF GLY-120.
[2]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Amygdala.
[4]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS 1 AND 2).
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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] (ISOFORM 1).
Tissue: Uterus.
[7]"The human homolog of Saccharomyces cerevisiae Apg7p is a Protein-activating enzyme for multiple substrates including human Apg12p, GATE-16, GABARAP, and MAP-LC3."
Tanida I., Tanida-Miyake E., Ueno T., Kominami E.
J. Biol. Chem. 276:1701-1706(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATG7.
[8]"Human Apg3p/Aut1p homologue is an authentic E2 enzyme for multiple substrates, GATE-16, GABARAP, and MAP-LC3, and facilitates the conjugation of hApg12p to hApg5p."
Tanida I., Tanida-Miyake E., Komatsu M., Ueno T., Kominami E.
J. Biol. Chem. 277:13739-13744(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATG3.
[9]"HsAtg4B/HsApg4B/autophagin-1 cleaves the carboxyl termini of three human Atg8 homologues and delipidates microtubule-associated protein light chain 3- and GABAA receptor-associated protein-phospholipid conjugates."
Tanida I., Sou Y.-S., Ezaki J., Minematsu-Ikeguchi N., Ueno T., Kominami E.
J. Biol. Chem. 279:36268-36276(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: LIPIDATION AT GLY-120, CLEAVAGE BY APG4B.
[10]"p62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of ubiquitinated protein aggregates by autophagy."
Pankiv S., Clausen T.H., Lamark T., Brech A., Bruun J.A., Outzen H., Overvatn A., Bjorkoy G., Johansen T.
J. Biol. Chem. 282:24131-24145(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SQSTM1, SUBCELLULAR LOCATION.
[11]"The TP53INP2 protein is required for autophagy in mammalian cells."
Nowak J., Archange C., Tardivel-Lacombe J., Pontarotti P., Pebusque M.J., Vaccaro M.I., Velasco G., Dagorn J.C., Iovanna J.L.
Mol. Biol. Cell 20:870-881(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH TP53INP2.
[12]"Regulation of the autophagy protein LC3 by phosphorylation."
Cherra S.J. III, Kulich S.M., Uechi G., Balasubramani M., Mountzouris J., Day B.W., Chu C.T.
J. Cell Biol. 190:533-539(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-12 BY PKA, FUNCTION.
[13]"TP53INP1, a tumor suppressor, interacts with LC3 and ATG8-family proteins through the LC3-interacting region (LIR) and promotes autophagy-dependent cell death."
Seillier M., Peuget S., Gayet O., Gauthier C., N'guessan P., Monte M., Carrier A., Iovanna J.L., Dusetti N.J.
Cell Death Differ. 19:1525-1535(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[14]"ATG8 family proteins act as scaffolds for assembly of the ULK complex: sequence requirements for LC3-interacting region (LIR) motifs."
Alemu E.A., Lamark T., Torgersen K.M., Birgisdottir A.B., Larsen K.B., Jain A., Olsvik H., Overvatn A., Kirkin V., Johansen T.
J. Biol. Chem. 287:39275-39290(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATG13 AND ULK1.
[15]"DOR/Tp53inp2 and Tp53inp1 constitute a metazoan gene family encoding dual regulators of autophagy and transcription."
Sancho A., Duran J., Garcia-Espana A., Mauvezin C., Alemu E.A., Lamark T., Macias M.J., Desalle R., Royo M., Sala D., Chicote J.U., Palacin M., Johansen T., Zorzano A.
PLoS ONE 7:E34034-E34034(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TP53INP1 AND TP53INP2.
[16]"The Legionella effector RavZ inhibits host autophagy through irreversible Atg8 deconjugation."
Choy A., Dancourt J., Mugo B., O'Connor T.J., Isberg R.R., Melia T.J., Roy C.R.
Science 338:1072-1076(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: DECONJUGATION BY LEGIONELLA RAVZ.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF276658 mRNA. Translation: AAK35151.1.
BT007452 mRNA. Translation: AAP36120.1.
AL833855 mRNA. Translation: CAD38714.1.
AL118520 Genomic DNA. Translation: CAC14078.1.
AL118520 Genomic DNA. Translation: CAI40290.1.
CH471077 Genomic DNA. Translation: EAW76263.1.
CH471077 Genomic DNA. Translation: EAW76264.1.
CH471077 Genomic DNA. Translation: EAW76265.1.
CH471077 Genomic DNA. Translation: EAW76266.1.
BC015810 mRNA. Translation: AAH15810.1.
CCDSCCDS13237.1. [Q9H492-2]
CCDS13238.1. [Q9H492-1]
RefSeqNP_115903.1. NM_032514.3. [Q9H492-1]
NP_852610.1. NM_181509.2. [Q9H492-2]
XP_005260634.1. XM_005260577.1. [Q9H492-1]
UniGeneHs.632273.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3ECIX-ray2.65A/B1-121[»]
3WALX-ray2.00A2-121[»]
3WANX-ray1.77A/B2-121[»]
ProteinModelPortalQ9H492.
SMRQ9H492. Positions 2-121.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124137. 99 interactions.
DIPDIP-49052N.
IntActQ9H492. 379 interactions.
MINTMINT-1420598.
STRING9606.ENSP00000363970.

PTM databases

PhosphoSiteQ9H492.

Polymorphism databases

DMDM85701362.

Proteomic databases

MaxQBQ9H492.
PaxDbQ9H492.
PRIDEQ9H492.

Protocols and materials databases

DNASU84557.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000360668; ENSP00000353886; ENSG00000101460. [Q9H492-1]
ENST00000374837; ENSP00000363970; ENSG00000101460. [Q9H492-2]
ENST00000397709; ENSP00000380821; ENSG00000101460. [Q9H492-1]
GeneID84557.
KEGGhsa:84557.
UCSCuc002xap.2. human. [Q9H492-2]
uc002xaq.2. human. [Q9H492-1]

Organism-specific databases

CTD84557.
GeneCardsGC20P033134.
HGNCHGNC:6838. MAP1LC3A.
HPAHPA007649.
MIM601242. gene.
neXtProtNX_Q9H492.
PharmGKBPA30582.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG264390.
HOGENOMHOG000232034.
HOVERGENHBG051706.
KOK10435.
OMAWAHADEV.
OrthoDBEOG7XH6RV.
PhylomeDBQ9H492.
TreeFamTF312964.

Gene expression databases

BgeeQ9H492.
CleanExHS_MAP1LC3A.
GenevestigatorQ9H492.

Family and domain databases

InterProIPR004241. Atg8_like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PANTHERPTHR10969. PTHR10969. 1 hit.
PfamPF02991. Atg8. 1 hit.
[Graphical view]
SUPFAMSSF54236. SSF54236. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9H492.
GeneWikiMAP1LC3A.
GenomeRNAi84557.
NextBio74441.
PMAP-CutDBQ9H492.
PROQ9H492.
SOURCESearch...

Entry information

Entry nameMLP3A_HUMAN
AccessionPrimary (citable) accession number: Q9H492
Secondary accession number(s): E1P5P4, E1P5P5, Q9BXW5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: May 10, 2005
Last modified: July 9, 2014
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM