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Reviewed, UniProtKB/Swiss-Prot Q9H492 (MLP3A_HUMAN)

Last modified June 16, 2009. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Microtubule-associated proteins 1A/1B light chain 3A
Alternative name(s):
    Microtubule-associated protein 1 light chain 3 alpha
    MAP1A/1B light chain 3 A
    MAP1A/MAP1B LC3 A
    MAP1 light chain 3-like protein 1
    Autophagy-related protein LC3 A
    Autophagy-related ubiquitin-like modifier LC3 A
Gene names
Name: MAP1LC3A
OrganismHomo sapiens (Human)
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

Probably involved in formation of autophagosomal vacuoles (autophagosomes).

Subunit structure

3 different light chains, LC1, LC2 and LC3, can associate with MAP1A and MAP1B proteins By similarity.

Subcellular location

Cytoplasm. Endomembrane system; Lipid-anchor. Cytoplasmic vesicleautophagosome membrane; Lipid-anchor. Note: LC3-II binds to the autophagic membranes.

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 APG4B/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.6

Sequence similarities

Belongs to the MAP1 LC3 family.

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

Amino acid modifications

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

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.

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: 12740394] [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., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed: 17974005] [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: 11780052] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS 1 AND 2).
[5]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Uterus.
[6]"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: 15187094] [Abstract]
Cited for: LIPIDATION, CLEAVAGE BY APG4B.
+Additional computationally mapped references.

Cross-references

Sequence databases

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.
BC015810 mRNA. Translation: AAH15810.1.
IPIIPI00015423.
IPI00415014.
RefSeqNP_115903.1.
NP_852610.1.
UniGeneHs.632273

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
3ECIX-ray2.65A/B1-121[»]
SMRQ9H492. Positions 1-120.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9H492. 1 interaction.

Proteomic databases

PRIDEQ9H492.

Genome annotation databases

EnsemblENSG00000101460. Homo sapiens. [Contig view]
GeneID84557.
KEGGhsa:84557.

Organism-specific databases

GeneCardsGC20P032598.
H-InvDBHIX0015748.
HGNCHGNC:6838. MAP1LC3A.
HPAHPA007649.
MIM601242. gene.
PharmGKBPA30582.
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ9H492.
OMAQ9H492. TPISEIY.

Gene expression databases

BgeeQ9H492.
CleanExHS_MAP1LC3A.
GermOnlineENSG00000101460. Homo sapiens.

Family and domain databases

InterProIPR004241. MAP1_LC3.
[Graphical view]
PANTHERPTHR10969. MAP1_LC3. 1 hit.
PfamPF02991. MAP1_LC3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio74441.
PMAP-CutDBQ9H492.
SOURCESearch...

Entry information

Entry nameMLP3A_HUMAN
AccessionPrimary (citable) accession number: Q9H492
Secondary accession number(s): Q9BXW5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: May 10, 2005
Last modified: June 16, 2009
This is version 58 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 20

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

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents