ID   MLP3A_MOUSE             Reviewed;         121 AA.
AC   Q91VR7; Q9DC74;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-NOV-2008, entry version 46.
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Heart;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NMRI; TISSUE=Mammary tumor;
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).
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; AK003122; BAB22582.1; -; mRNA.
DR   EMBL; BC010596; AAH10596.1; -; mRNA.
DR   RefSeq; NP_080011.1; -.
DR   UniGene; Mm.196239; -.
DR   HSSP; P60519; 1EO6.
DR   SMR; Q91VR7; 1-120.
DR   Ensembl; ENSMUSG00000027602; Mus musculus.
DR   GeneID; 66734; -.
DR   KEGG; mmu:66734; -.
DR   MGI; MGI:1915661; Map1lc3a.
DR   HOGENOM; Q91VR7; -.
DR   HOVERGEN; Q91VR7; -.
DR   NextBio; 322507; -.
DR   ArrayExpress; Q91VR7; -.
DR   GermOnline; ENSMUSG00000027602; Mus musculus.
DR   GO; GO:0005776; C:autophagic vacuole; ISS: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; ISS:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0000045; P:autophagosome formation; ISS: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   2: Evidence at transcript level;
KW   Autophagy; Cytoplasm; Cytoplasmic vesicle; Lipoprotein; Membrane;
KW   Microtubule; Ubl conjugation pathway.
FT   CHAIN         1    120       Microtubule-associated proteins 1A/1B
FT                                light chain 3A.
FT                                /FTId=PRO_0000017194.
FT   PROPEP      121    121       Removed in mature form (Probable).
FT                                /FTId=PRO_0000017195.
FT   LIPID       120    120       Phosphatidylethanolamine amidated glycine
FT                                (Probable).
FT   CONFLICT     12     12       S -> T (in Ref. 1; BAB22582).
SQ   SEQUENCE   121 AA;  14272 MW;  48C1FBE8F7892AF3 CRC64;
     MPSDRPFKQR RSFADRCKEV QQIRDQHPSK IPVIIERYKG EKQLPVLDKT KFLVPDHVNM
     SELVKIIRRR LQLNPTQAFF LLVNQHSMVS VSTPIADIYE QEKDEDGFLY MVYASQETFG
     F
//