ID   MLP3B_RAT               Reviewed;         142 AA.
AC   Q62625; Q6XVN7;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   13-OCT-2009, entry version 75.
DE   RecName: Full=Microtubule-associated proteins 1A/1B light chain 3B;
DE   AltName: Full=Microtubule-associated protein 1 light chain 3 beta;
DE   AltName: Full=MAP1A/1B light chain 3 B;
DE   AltName: Full=MAP1A/MAP1B LC3 B;
DE   AltName: Full=MAP1 light chain 3-like protein 2;
DE   AltName: Full=Autophagy-related protein LC3 B;
DE   AltName: Full=Autophagy-related ubiquitin-like modifier LC3 B;
DE   Flags: Precursor;
GN   Name=Map1lc3b; Synonyms=Map1alc3, Map1lc3;
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] (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=94209331; PubMed=7908909;
RA   Mann S.S., Hammarback J.A.;
RT   "Molecular characterization of light chain 3. A microtubule binding
RT   subunit of MAP1A and MAP1B.";
RL   J. Biol. Chem. 269:11492-11497(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=Sprague-Dawley; 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   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=Sprague-Dawley;
RA   Zhou G., Dai F., Yu L.;
RT   "Rattus norvegicus microtubule-associated protein 1 light chain 3
RT   (Map1lc3).";
RL   Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Heart, and Pituitary;
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   [5]
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.
RN   [6]
RP   SUBCELLULAR LOCATION, CLEAVAGE, AND MUTAGENESIS OF GLY-120.
RX   PubMed=11060023; DOI=10.1093/emboj/19.21.5720;
RA   Kabeya Y., Mizushima N., Ueno T., Yamamoto A., Kirisako T., Noda T.,
RA   Kominami E., Ohsumi Y., Yoshimori T.;
RT   "LC3, a mammalian homologue of yeast Apg8p, is localized in
RT   autophagosome membranes after processing.";
RL   EMBO J. 19:5720-5728(2000).
RN   [7]
RP   REVIEW.
RX   PubMed=15325588; DOI=10.1016/j.biocel.2004.05.009;
RA   Tanida I., Ueno T., Kominami E.;
RT   "LC3 conjugation system in mammalian autophagy.";
RL   Int. J. Biochem. Cell Biol. 36:2503-2518(2004).
RN   [8]
RP   INTERACTION WITH CABP1.
RX   PubMed=15095872; DOI=10.1016/j.jmb.2003.12.054;
RA   Seidenbecher C.I., Landwehr M., Smalla K.H., Kreutz M.,
RA   Dieterich D.C., Zuschratter W., Reissner C., Hammarback J.A.,
RA   Bockers T.M., Gundelfinger E.D., Kreutz M.R.;
RT   "Caldendrin but not calmodulin binds to light chain 3 of MAP1A/B: an
RT   association with the microtubule cytoskeleton highlighting exclusive
RT   binding partners for neuronal Ca(2+)-sensor proteins.";
RL   J. Mol. Biol. 336:957-970(2004).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 1-120.
RX   PubMed=15265004; DOI=10.1111/j.1356-9597.2004.00750.x;
RA   Sugawara K., Suzuki N.N., Fujioka Y., Mizushima N., Ohsumi Y.,
RA   Inagaki F.;
RT   "The crystal structure of microtubule-associated protein light chain
RT   3, a mammalian homologue of Saccharomyces cerevisiae Atg8.";
RL   Genes Cells 9:611-618(2004).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-124 IN COMPLEX WITH ATG4B.
RX   PubMed=19322194; DOI=10.1038/emboj.2009.80;
RA   Satoo K., Noda N.N., Kumeta H., Fujioka Y., Mizushima N., Ohsumi Y.,
RA   Inagaki F.;
RT   "The structure of Atg4B-LC3 complex reveals the mechanism of LC3
RT   processing and delipidation during autophagy.";
RL   EMBO J. 28:1341-1350(2009).
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. Interacts at microtubules with
CC       CABP1 (via EF-hands 1 and 2) but not with calmodulin. A calcium-
CC       dependent binding site is located at the C-terminus while a
CC       calcium-independent binding site is located at the N-terminus.
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=Q62625-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q62625-2; Sequence=VSP_012092;
CC   -!- TISSUE SPECIFICITY: Abundant only in neurons. Detected in testes.
CC   -!- PTM: The precursor molecule is cleaved by APG4B/ATG4B to form LC3-
CC       I. This is activated by APG7L/ATG7, transferred to ATG3 and
CC       conjugated to phospholipid to form LC3-II.
CC   -!- SIMILARITY: Belongs to the MAP1 LC3 family.
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DR   EMBL; U05784; AAA20645.1; -; mRNA.
DR   EMBL; AY206669; AAP42561.1; -; mRNA.
DR   EMBL; AY392036; AAQ94605.1; -; mRNA.
DR   EMBL; BC058144; AAH58144.1; -; mRNA.
DR   EMBL; BC083556; AAH83556.1; -; mRNA.
DR   IPI; IPI00231495; -.
DR   IPI; IPI00480725; -.
DR   PIR; A53624; A53624.
DR   RefSeq; NP_074058.2; -.
DR   UniGene; Rn.41412; -.
DR   PDB; 1UGM; X-ray; 2.05 A; A=1-120.
DR   PDB; 2K6Q; NMR; -; A=1-120.
DR   PDB; 2Z0D; X-ray; 1.90 A; B=1-120.
DR   PDB; 2Z0E; X-ray; 1.90 A; B=1-124.
DR   PDB; 2ZZP; X-ray; 2.05 A; B=1-124.
DR   PDBsum; 1UGM; -.
DR   PDBsum; 2K6Q; -.
DR   PDBsum; 2Z0D; -.
DR   PDBsum; 2Z0E; -.
DR   PDBsum; 2ZZP; -.
DR   STRING; Q62625; -.
DR   Ensembl; ENSRNOT00000019033; ENSRNOP00000019033; ENSRNOG00000038106; Rattus norvegicus.
DR   GeneID; 64862; -.
DR   KEGG; rno:64862; -.
DR   UCSC; NM_022867; rat.
DR   CTD; 64862; -.
DR   RGD; 621315; Map1lc3b.
DR   HOVERGEN; Q62625; -.
DR   NextBio; 613772; -.
DR   Genevestigator; Q62625; -.
DR   GermOnline; ENSRNOG00000038106; Rattus norvegicus.
DR   GO; GO:0031225; C:anchored to membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000421; C:autophagic vacuole membrane; IDA:UniProtKB.
DR   GO; GO:0030424; C:axon; IDA:RGD.
DR   GO; GO:0043025; C:cell soma; IDA:RGD.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0030425; C:dendrite; IDA:RGD.
DR   GO; GO:0005626; C:insoluble fraction; IDA:RGD.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005875; C:microtubule associated complex; IDA:RGD.
DR   GO; GO:0005625; C:soluble fraction; IDA:RGD.
DR   GO; GO:0008017; F:microtubule binding; IDA:RGD.
DR   GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0019941; P:modification-dependent protein catabolic pr...; IEA:UniProtKB-KW.
DR   GO; GO:0032092; P:positive regulation of protein binding; IDA:RGD.
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; Cytoplasm;
KW   Cytoplasmic vesicle; Direct protein sequencing; Lipoprotein; Membrane;
KW   Microtubule; Ubl conjugation pathway.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    120       Microtubule-associated proteins 1A/1B
FT                                light chain 3B.
FT                                /FTId=PRO_0000017202.
FT   PROPEP      121    142       Removed in mature form (Probable).
FT                                /FTId=PRO_0000017203.
FT   LIPID       120    120       Phosphatidylethanolamine amidated glycine
FT                                (By similarity).
FT   VAR_SEQ     126    142       Missing (in isoform 2).
FT                                /FTId=VSP_012092.
FT   MUTAGEN     120    120       G->A: No processing of precursor.
FT   HELIX         7     10
FT   HELIX        13     26
FT   STRAND       30     37
FT   STRAND       50     55
FT   HELIX        60     70
FT   STRAND       80     83
FT   STRAND       91     94
FT   HELIX        95    102
FT   STRAND      109    115
SQ   SEQUENCE   142 AA;  16394 MW;  D07E9D063C125E32 CRC64;
     MPSEKTFKQR RSFEQRVEDV RLIREQHPTK IPVIIERYKG EKQLPVLDKT KFLVPDHVNM
     SELIKIIRRR LQLNANQAFF LLVNGHSMVS VSTPISEVYE SERDEDGFLY MVYASQETFG
     TALAVTYMSA LKATATGREP CL
//