Reviewed, UniProtKB/Swiss-Prot Q9H492 (MLP3A_HUMAN)

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	121 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	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 vesicle › autophagosome 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.

Ontologies

Keywords
Biological process	Autophagy Ubl conjugation pathway
Cellular component	Cytoplasm Cytoplasmic vesicle Membrane Microtubule
Coding sequence diversity	Alternative splicing
PTM	Lipoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	autophagic vacuole formation Inferred from sequence or structural similarity. Source: UniProtKB modification-dependent protein catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	autophagic vacuole membrane Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasmic vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Ref.6 Inferred from direct assay. Source: UniProtKB endomembrane system Inferred from electronic annotation. Source: UniProtKB-SubCell microtubule Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	phosphatidylethanolamine binding Inferred from direct assay. Source: UniProtKB protein binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 120	120	Microtubule-associated proteins 1A/1B light chain 3A		PRO_0000017192
	Propeptide	121	1	Removed in mature form		PRO_0000017193
Amino acid modifications
	Lipidation	120	1	Phosphatidylethanolamine amidated glycine Probable
Natural variations
	Alternative sequence	1 – 13	13	MPSDR…QRRSF → MKMRFFSSPCGKAAVDP in isoform 2.		VSP_013660
Experimental info
	Mutagenesis	120	1	G → A: No processing of precursor. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 10, 2005. Version 2. Checksum: 48C1FBE8F7892AF3	FASTA	121	14,272
	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
	Isoform 2. Checksum: 097697B5424FC425	FASTA	125	14,493
	10 20 30 40 50 60 MKMRFFSSPC GKAAVDPADR CKEVQQIRDQ HPSKIPVIIE RYKGEKQLPV LDKTKFLVPD 70 80 90 100 110 120 HVNMSELVKI IRRRLQLNPT QAFFLLVNQH SMVSVSTPIA DIYEQEKDED GFLYMVYASQ ETFGF

References

	« Hide 'large scale' referencesShow '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. , 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

EMBLGenBankDDBJ

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.

IPI

IPI00015423.
IPI00415014.

RefSeq

NP_115903.1.
NP_852610.1.

UniGene

Hs.632273

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3ECI	X-ray	2.65	A/B	1-121	[»]

SMR

Q9H492. Positions 1-120.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9H492. 1 interaction.

Proteomic databases

PRIDE

Q9H492.

Genome annotation databases

Ensembl

ENSG00000101460. Homo sapiens. [Contig view]

GeneID

84557.

KEGG

hsa:84557.

Organism-specific databases

GeneCards

GC20P032598.

H-InvDB

HIX0015748.

HGNC

HGNC:6838. MAP1LC3A.

HPA

HPA007649.

MIM

601242. gene.

PharmGKB

PA30582.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

Q9H492.

OMA

Q9H492. TPISEIY.

Gene expression databases

Bgee

Q9H492.

CleanEx

HS_MAP1LC3A.

GermOnline

ENSG00000101460. Homo sapiens.

Family and domain databases

InterPro

IPR004241. MAP1_LC3.
[Graphical view]

PANTHER

PTHR10969. MAP1_LC3. 1 hit.

Pfam

PF02991. MAP1_LC3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

74441.

PMAP-CutDB

Q9H492.

SOURCE

Search...

Entry information

Entry name

MLP3A_HUMAN

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)