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UniProtKB/Swiss-Prot entry Q9CQV6


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MLP3B_MOUSE
Primary accession number Q9CQV6
Secondary accession numbers Q3U9W5 Q9D1R0
Integrated into Swiss-Prot on November 8, 2002
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    June 16, 2009 (Entry version 63)
Name and origin of the protein
Protein name Microtubule-associated proteins 1A/1B light chain 3B [Precursor]
Synonyms Microtubule-associated protein 1 light chain 3 beta
MAP1A/1B light chain 3 B
MAP1A/MAP1B LC3 B
MAP1 light chain 3-like protein 2
Autophagy-related protein LC3 B
Autophagy-related ubiquitin-like modifier LC3 B
Gene name
Name: Map1lc3b
Synonyms: Map1alc3, Map1lc3
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Yu L.;
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Bone marrow, Embryo, Head, Heart, and Kidney;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6;
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 31-37 AND 52-65, AND MASS SPECTROMETRY.
STRAIN=C57BL/6;
TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[5]
REVIEW.
DOI=10.1016/j.biocel.2004.05.009; PubMed=15325588 [NCBI, ExPASy, EBI, Israel, Japan]
Tanida I., Ueno T., Kominami E.;
"LC3 conjugation system in mammalian autophagy.";
Int. J. Biochem. Cell Biol. 36:2503-2518(2004).
Comments
  • FUNCTION: Probably involved in formation of autophagosomal vacuoles (autophagosomes).
  • SUBUNIT: 3 different light chains, LC1, LC2 and LC3, can associate with MAP1A and MAP1B proteins (By similarity).
  • SUBCELLULAR LOCATION: Cytoplasm. Endomembrane system; Lipid-anchor. Cytoplasmic vesicle, autophagosome membrane; Lipid-anchor (By similarity). Note=LC3-II binds to the autophagic membranes (By similarity).
  • PTM: The precursor molecule is cleaved by APG4B/ATG4B to form LC3-I. This is activated by APG7L/ATG7, transferred to ATG3 and conjugated to phospholipid to form LC3-II (By similarity).
  • SIMILARITY: Belongs to the MAP1 LC3 family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF255953; AAL83723.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK002795; BAB22364.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK003106; BAB22569.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK003205; BAB22641.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK003558; BAB22855.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK012604; BAB28350.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK132329; BAE21108.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK151614; BAE30551.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC068180; AAH68180.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00230349; -.
RefSeq NP_080436.1; -.
UniGene Mm.28357
3D structure databases
HSSP O08765; 1EO6. [HSSP ENTRY / PDB]
SMR Q9CQV6; 1-120.
ModBase Q9CQV6.
Organism-specific databases
MGI MGI:1914693; Map1lc3b.
Gene expression databases
Bgee Q9CQV6; -.
GermOnline ENSMUSG00000031812; Mus musculus.
Ontologies
GO
GO:0000421; Cellular component: autophagic vacuole membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0031410; Cellular component: cytoplasmic vesicle (inferred from electronic annotation from UniProtKB-SubCell).
GO:0012505; Cellular component: endomembrane system (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005874; Cellular component: microtubule (inferred from electronic annotation from UniProtKB-KW).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from MGI).
GO:0006914; Biological process: autophagy (inferred from electronic annotation from UniProtKB-KW).
GO:0019941; Biological process: modification-dependent protein catabolic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR004241; MAP1_LC3.
Graphical view of domain structure.
PANTHER PTHR10969; MAP1_LC3; 1.
Pfam PF02991; MAP1_LC3; 1.
Pfam graphical view of domain structure.
Proteomic databases
PRIDE Q9CQV6; -.
Genome annotation databases
Ensembl ENSMUSG00000031812; Mus musculus. [Contig view]
GeneID 67443; -.
KEGG mmu:67443; -.
Phylogenomic databases
HOGENOM Q9CQV6; -.
HOVERGEN Q9CQV6; -.
OMA Q9CQV6; FKERRPF.
Other
NextBio 324582; -.
SOURCE Map1lc3b; Mus musculus.
ProtoNet Q9CQV6.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Autophagy; Cytoplasm; Cytoplasmic vesicle; Direct protein sequencing; Lipoprotein; Membrane; Microtubule; Ubl conjugation pathway.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   120  119     Microtubule-associated proteins 1A/1B light chain 3B. PRO_0000017200
PROPEP   121   125  5     Removed in mature form (By similarity). PRO_0000017201
LIPID   120   120        Phosphatidylethanolamine amidated glycine (By similarity). 
CONFLICT   89    89        V -> L (in Ref. 2; BAB22641). 
Sequence information
Length: 125 AA [This is the length of the unprocessed precursor] Molecular weight: 14617 Da [This is the MW of the unprocessed precursor] CRC64: 520E29028163FA8D [This is a checksum on the sequence]
        10         20         30         40         50         60 
MPSEKTFKQR RSFEQRVEDV RLIREQHPTK IPVIIERYKG EKQLPVLDKT KFLVPDHVNM 

        70         80         90        100        110        120 
SELIKIIRRR LQLNANQAFF LLVNGHSMVS VSTPISEVYE SERDEDGFLY MVYASQETFG 


TAMAV 

Q9CQV6 in FASTA format

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