ID   MLP3A_HUMAN             Reviewed;         121 AA.
AC   Q9H492; Q9BXW5;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 2.
DT   09-FEB-2010, entry version 68.
DE   RecName: Full=Microtubule-associated proteins 1A/1B light chain 3A;
DE   AltName: Full=Microtubule-associated protein 1 light chain 3 alpha;
DE   AltName: Full=MAP1A/MAP1B light chain 3 A;
DE            Short=MAP1A/MAP1B LC3 A;
DE   AltName: Full=MAP1 light chain 3-like protein 1;
DE   AltName: Full=Autophagy-related protein LC3 A;
DE   AltName: Full=Autophagy-related ubiquitin-like modifier LC3 A;
DE   Flags: Precursor;
GN   Name=MAP1LC3A;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND MUTAGENESIS OF GLY-120.
RX   MEDLINE=22765575; PubMed=12740394; DOI=10.1074/jbc.M303800200;
RA   He H., Dang Y., Dai F., Guo Z., Wu J., She X., Pei Y., Chen Y.,
RA   Ling W., Wu C., Zhao S., Liu J.O., Yu L.;
RT   "Post-translational modifications of three members of the human
RT   MAP1LC3 family and detection of a novel type of modification for
RT   MAP1LC3B.";
RL   J. Biol. Chem. 278:29278-29287(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT   vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Amygdala;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS 1 AND 2).
RX   MEDLINE=21638749; PubMed=11780052; DOI=10.1038/414865a;
RA   Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA   Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA   Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA   Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA   Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA   Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA   Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA   Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA   Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA   Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA   Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA   Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA   Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA   Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA   Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA   Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA   Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA   Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA   Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA   Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA   Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA   Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA   Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 20.";
RL   Nature 414:865-871(2001).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Uterus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   LIPIDATION, AND CLEAVAGE BY APG4B.
RX   PubMed=15187094; DOI=10.1074/jbc.M401461200;
RA   Tanida I., Sou Y.-S., Ezaki J., Minematsu-Ikeguchi N., Ueno T.,
RA   Kominami E.;
RT   "HsAtg4B/HsApg4B/autophagin-1 cleaves the carboxyl termini of three
RT   human Atg8 homologues and delipidates microtubule-associated protein
RT   light chain 3- and GABAA receptor-associated protein-phospholipid
RT   conjugates.";
RL   J. Biol. Chem. 279:36268-36276(2004).
CC   -!- FUNCTION: Probably involved in formation of autophagosomal
CC       vacuoles (autophagosomes).
CC   -!- SUBUNIT: 3 different light chains, LC1, LC2 and LC3, can associate
CC       with MAP1A and MAP1B proteins (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Endomembrane system; Lipid-
CC       anchor. Cytoplasmic vesicle, autophagosome membrane; Lipid-anchor.
CC       Note=LC3-II binds to the autophagic membranes.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9H492-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9H492-2; Sequence=VSP_013660;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Most abundant in heart, brain, liver, skeletal
CC       muscle and testis but absent in thymus and peripheral blood
CC       leukocytes.
CC   -!- PTM: The precursor molecule is cleaved by APG4B/ATG4B to form the
CC       cytosolic form, LC3-I. This is activated by APG7L/ATG7,
CC       transferred to ATG3 and conjugated to phospholipid to form the
CC       membrane-bound form, LC3-II.
CC   -!- SIMILARITY: Belongs to the MAP1 LC3 family.
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DR   EMBL; AF276658; AAK35151.1; -; mRNA.
DR   EMBL; BT007452; AAP36120.1; -; mRNA.
DR   EMBL; AL833855; CAD38714.1; -; mRNA.
DR   EMBL; AL118520; CAC14078.1; -; Genomic_DNA.
DR   EMBL; AL118520; CAI40290.1; -; Genomic_DNA.
DR   EMBL; BC015810; AAH15810.1; -; mRNA.
DR   IPI; IPI00015423; -.
DR   IPI; IPI00415014; -.
DR   RefSeq; NP_115903.1; -.
DR   RefSeq; NP_852610.1; -.
DR   UniGene; Hs.632273; -.
DR   PDB; 3ECI; X-ray; 2.65 A; A/B=1-121.
DR   PDBsum; 3ECI; -.
DR   IntAct; Q9H492; 3.
DR   STRING; Q9H492; -.
DR   PRIDE; Q9H492; -.
DR   Ensembl; ENST00000360668; ENSP00000353886; ENSG00000101460; Homo sapiens.
DR   Ensembl; ENST00000397709; ENSP00000380821; ENSG00000101460; Homo sapiens.
DR   GeneID; 84557; -.
DR   KEGG; hsa:84557; -.
DR   UCSC; uc002xap.1; human.
DR   UCSC; uc002xaq.1; human.
DR   CTD; 84557; -.
DR   GeneCards; GC20P032598; -.
DR   H-InvDB; HIX0015748; -.
DR   HGNC; HGNC:6838; MAP1LC3A.
DR   HPA; HPA007649; -.
DR   MIM; 601242; gene.
DR   PharmGKB; PA30582; -.
DR   eggNOG; prNOG20683; -.
DR   HOVERGEN; Q9H492; -.
DR   OMA; TPISEIY; -.
DR   OrthoDB; EOG9WM7DJ; -.
DR   PhylomeDB; Q9H492; -.
DR   NextBio; 74441; -.
DR   PMAP-CutDB; Q9H492; -.
DR   ArrayExpress; Q9H492; -.
DR   Bgee; Q9H492; -.
DR   CleanEx; HS_MAP1LC3A; -.
DR   Genevestigator; Q9H492; -.
DR   GermOnline; ENSG00000101460; Homo sapiens.
DR   GO; GO:0031225; C:anchored to membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005776; C:autophagic vacuole; IDA:UniProtKB.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0031090; C:organelle membrane; IDA:UniProtKB.
DR   GO; GO:0008429; F:phosphatidylethanolamine binding; IDA:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0000045; P:autophagic vacuole assembly; ISS:UniProtKB.
DR   GO; GO:0019941; P:modification-dependent protein catabolic pr...; IEA:UniProtKB-KW.
DR   InterPro; IPR004241; MAP1_LC3.
DR   PANTHER; PTHR10969; MAP1_LC3; 1.
DR   Pfam; PF02991; MAP1_LC3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Autophagy; Complete proteome;
KW   Cytoplasm; Cytoplasmic vesicle; Lipoprotein; Membrane; Microtubule;
KW   Ubl conjugation pathway.
FT   CHAIN         1    120       Microtubule-associated proteins 1A/1B
FT                                light chain 3A.
FT                                /FTId=PRO_0000017192.
FT   PROPEP      121    121       Removed in mature form.
FT                                /FTId=PRO_0000017193.
FT   LIPID       120    120       Phosphatidylethanolamine amidated glycine
FT                                (Probable).
FT   VAR_SEQ       1     13       MPSDRPFKQRRSF -> MKMRFFSSPCGKAAVDP (in
FT                                isoform 2).
FT                                /FTId=VSP_013660.
FT   MUTAGEN     120    120       G->A: No processing of precursor.
FT   HELIX         7     10
FT   HELIX        13     26
FT   STRAND       30     37
FT   STRAND       51     55
FT   HELIX        60     71
FT   STRAND       79     83
FT   TURN         84     86
FT   HELIX        95    102
FT   STRAND      109    115
SQ   SEQUENCE   121 AA;  14272 MW;  48C1FBE8F7892AF3 CRC64;
     MPSDRPFKQR RSFADRCKEV QQIRDQHPSK IPVIIERYKG EKQLPVLDKT KFLVPDHVNM
     SELVKIIRRR LQLNPTQAFF LLVNQHSMVS VSTPIADIYE QEKDEDGFLY MVYASQETFG
     F
//