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Q9BXW4 (MLP3C_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 96. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Microtubule-associated proteins 1A/1B light chain 3C
Alternative name(s):
Autophagy-related protein LC3 C
Autophagy-related ubiquitin-like modifier LC3 C
MAP1 light chain 3-like protein 3
MAP1A/MAP1B light chain 3 C
Short name=MAP1A/MAP1B LC3 C
Microtubule-associated protein 1 light chain 3 gamma
Gene names
Name:MAP1LC3C
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length147 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 that plays a crucial role in antibacterial autophagy (xenophagy) through the selective binding of CALCOCO2. Recruites all ATG8 family members to infecting bacteria such as S.Typhimurium. Ref.8

Subunit structure

3 different light chains, LC1, LC2 and LC3, can associate with MAP1A and MAP1B proteins By similarity. Interacts with TP53INP1 and TP53INP2. Interacts with CALCOCO2. Interacts with TECPR2. Ref.5 Ref.6 Ref.8

Subcellular location

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

Tissue specificity

Most abundant in placenta, lung and ovary. 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.4). Ref.4

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.

Sequence similarities

Belongs to the ATG8 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 126126Microtubule-associated proteins 1A/1B light chain 3C
PRO_0000017204
Propeptide127 – 14721Removed in mature form
PRO_0000017205

Sites

Site126 – 1272Cleavage; by ATG4B By similarity

Amino acid modifications

Lipidation1261Phosphatidylethanolamine amidated glycine Probable

Experimental info

Mutagenesis1261G → A: No processing of precursor. Ref.1

Secondary structure

......................... 147
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9BXW4 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: D3DFA8EE5985C3AA

FASTA14716,852
        10         20         30         40         50         60 
MPPPQKIPSV RPFKQRKSLA IRQEEVAGIR AKFPNKIPVV VERYPRETFL PPLDKTKFLV 

        70         80         90        100        110        120 
PQELTMTQFL SIIRSRMVLR ATEAFYLLVN NKSLVSMSAT MAEIYRDYKD EDGFVYMTYA 

       130        140 
SQETFGCLES AAPRDGSSLE DRPCNPL 

« Hide

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], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF GLY-126.
[2]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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].
[4]"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, CLEAVAGE BY APG4B.
[5]"Network organization of the human autophagy system."
Behrends C., Sowa M.E., Gygi S.P., Harper J.W.
Nature 466:68-76(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TECPR2.
[6]"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.
[7]"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.
[8]"LC3C, bound selectively by a noncanonical LIR motif in NDP52, is required for antibacterial autophagy."
von Muhlinen N., Akutsu M., Ravenhill B.J., Foeglein A., Bloor S., Rutherford T.J., Freund S.M., Komander D., Randow F.
Mol. Cell 48:329-342(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-126 IN COMPLEX WITH CALCOCO2, INTERACTION WITH CALCOCO2, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF276659 mRNA. Translation: AAK35152.1.
BX571673 Genomic DNA. Translation: CAH72477.1.
BC127722 mRNA. Translation: AAI27723.1.
BC132986 mRNA. Translation: AAI32987.1.
BC132988 mRNA. Translation: AAI32989.1.
RefSeqNP_001004343.1. NM_001004343.2.
XP_005273196.1. XM_005273139.1.
UniGeneHs.534971.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3VVWX-ray2.50B1-126[»]
3WAMX-ray1.75A8-125[»]
3WAPX-ray3.10A8-125[»]
ProteinModelPortalQ9BXW4.
SMRQ9BXW4. Positions 13-126.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid136855. 17 interactions.
IntActQ9BXW4. 51 interactions.
STRING9606.ENSP00000349785.

Polymorphism databases

DMDM84028113.

Proteomic databases

PaxDbQ9BXW4.
PRIDEQ9BXW4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000357246; ENSP00000349785; ENSG00000197769.
GeneID440738.
KEGGhsa:440738.
UCSCuc001hzk.2. human.

Organism-specific databases

CTD440738.
GeneCardsGC01M242158.
HGNCHGNC:13353. MAP1LC3C.
MIM609605. gene.
neXtProtNX_Q9BXW4.
PharmGKBPA142671482.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG245878.
HOGENOMHOG000232034.
HOVERGENHBG051706.
InParanoidQ9BXW4.
KOK10435.
OMATQFVTII.
OrthoDBEOG7XH6RV.
PhylomeDBQ9BXW4.
TreeFamTF312964.

Gene expression databases

BgeeQ9BXW4.
CleanExHS_MAP1LC3C.
GenevestigatorQ9BXW4.

Family and domain databases

InterProIPR004241. Atg8_like.
IPR027731. MAP1A/MAP1B_LC3C.
[Graphical view]
PANTHERPTHR10969. PTHR10969. 1 hit.
PTHR10969:SF17. PTHR10969:SF17. 1 hit.
PfamPF02991. Atg8. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi440738.
NextBio109492.
PROQ9BXW4.
SOURCESearch...

Entry information

Entry nameMLP3C_HUMAN
AccessionPrimary (citable) accession number: Q9BXW4
Secondary accession number(s): A0PJY8, A2RUP0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 96 of the entry and version 1 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 1

Human chromosome 1: entries, gene names and cross-references to MIM