ID   MLP3A_RAT               Reviewed;         121 AA.
AC   Q6XVN8;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-NOV-2008, entry version 37.
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/1B light chain 3 A;
DE   AltName: Full=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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RA   Dang Y., Yu L., Wu J., Pei Y.;
RT   "Cloning and characterization of rat lc3 orthologs.";
RL   Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
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   [3]
RP   PROTEIN SEQUENCE OF 31-37, AND MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (JUL-2007) to UniProtKB.
CC   -!- FUNCTION: Probably involved in formation of autophagosomal
CC       vacuoles (autophagosomes) (By similarity).
CC   -!- SUBUNIT: 3 different light chains, LC1, LC2 and LC3, can associate
CC       with MAP1A and MAP1B proteins (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Intracytoplasmic membrane; Lipid-
CC       anchor. Cytoplasmic vesicle, autophagosome membrane; Lipid-anchor
CC       (By similarity). Note=LC3-II binds to the autophagic membranes (By
CC       similarity).
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 (By similarity).
CC   -!- SIMILARITY: Belongs to the MAP1 LC3 family.
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DR   EMBL; AY206668; AAP42560.1; -; mRNA.
DR   EMBL; BC086389; AAH86389.1; -; mRNA.
DR   RefSeq; NP_955794.1; -.
DR   UniGene; Rn.3135; -.
DR   HSSP; P60517; 1KJT.
DR   SMR; Q6XVN8; 1-120.
DR   Ensembl; ENSRNOG00000025443; Rattus norvegicus.
DR   GeneID; 362245; -.
DR   KEGG; rno:362245; -.
DR   RGD; 735183; Map1lc3a.
DR   HOVERGEN; Q6XVN8; -.
DR   NextBio; 679168; -.
DR   ArrayExpress; Q6XVN8; -.
DR   GermOnline; ENSRNOG00000025443; Rattus norvegicus.
DR   GO; GO:0005776; C:autophagic vacuole; IDA:UniProtKB.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0031090; C:organelle membrane; IDA:UniProtKB.
DR   GO; GO:0000045; P:autophagosome formation; IDA:UniProtKB.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; 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   Autophagy; Cytoplasm; Cytoplasmic vesicle; Direct protein sequencing;
KW   Lipoprotein; Membrane; Microtubule; Ubl conjugation pathway.
FT   CHAIN         1    120       Microtubule-associated proteins 1A/1B
FT                                light chain 3A.
FT                                /FTId=PRO_0000017196.
FT   PROPEP      121    121       Removed in mature form (Probable).
FT                                /FTId=PRO_0000017197.
FT   LIPID       120    120       Phosphatidylethanolamine amidated glycine
FT                                (Probable).
SQ   SEQUENCE   121 AA;  14272 MW;  48C1FBE8F7892AF3 CRC64;
     MPSDRPFKQR RSFADRCKEV QQIRDQHPSK IPVIIERYKG EKQLPVLDKT KFLVPDHVNM
     SELVKIIRRR LQLNPTQAFF LLVNQHSMVS VSTPIADIYE QEKDEDGFLY MVYASQETFG
     F
//