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 22-JUL-2008, entry version 65. 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). 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. CC -!- SUBCELLULAR LOCATION: Cytoplasm. Intracytoplasmic membrane; 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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- 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 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; 2Z0D; X-ray; 1.90 A; B=1-120. DR PDB; 2Z0E; X-ray; 1.90 A; B=1-124. DR PDBsum; 1UGM; -. DR PDBsum; 2Z0D; -. DR PDBsum; 2Z0E; -. DR Ensembl; ENSRNOG00000038106; Rattus norvegicus. DR GeneID; 64862; -. DR KEGG; rno:64862; -. DR RGD; 621315; Map1lc3b. DR HOVERGEN; Q62625; -. DR ArrayExpress; Q62625; -. DR GermOnline; ENSRNOG00000038106; Rattus norvegicus. DR GO; GO:0000421; C:autophagic vacuole membrane; IDA:UniProtKB. 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 //