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[1]
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NUCLEOTIDE SEQUENCE [MRNA].
Laser M.,
Li Y.,
Xu L.,
Darden A.,
Wu B.X.,
Hazard E.S. III,
Crosson C.,
Ma J.X.;
"Identification and characterization of a novel gene induced by ischemic preconditioning in the retina.";
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
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[2]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
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).
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- FUNCTION: GABARAPL1 (GABARAPL2 or GABARAP or MAP1LC3)-modifier protein conjugating enzyme involved in its E2-like covalent binding to PE. ATG7 (E1-like enzyme) facilitates this reaction by forming an E1-E2 complex with ATG3 (E2-like enzyme). Preferred substrate is MAP1LC3A. Formation of the GABARAPL1-PE conjugate is essential for autophagy (By similarity).
- SUBUNIT: Interacts with ATG7 and ATG12. The complex, composed of ATG3 and ATG7, plays a role in the conjugation of ATG12 to ATG5 (By similarity).
- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
- SIMILARITY: Belongs to the ATG3 family.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 314 AA [This is the length of the unprocessed precursor] |
Molecular weight: 35822 Da [This is the MW of the unprocessed precursor] |
CRC64: 4C78AB0F628C9BDF [This is a checksum on the sequence] |
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10 20 30 40 50 60
MQNVINTVKG KALEVAEYLT PVLKESKFKE TGVITPEEFV AAGDHLVHHC PTWQWATGEE
70 80 90 100 110 120
LKVKAYLPTG KQFLVTKNVP CYKRCKQMEY SDELEAIIEE DDGDGGWVDT YHNTGITGIT
130 140 150 160 170 180
EAVKEITLES KDSIKLQDCS VLCDEEEEEE EGEAADMEEY EESGLLETDE ATLDTRRIVE
190 200 210 220 230 240
ACKAKADAGG EDAILQTRTY DLYITYDKYY QTPRLWLFGY DEQRQPLTVE HMYEDISQDH
250 260 270 280 290 300
VKKTVTIENH PHLPPPPMCS VHPCRHAEVM KKIIETVAEG GGELGVHMYL LIFLKFVQAV
310
IPTIEYDYTR HFTM
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Q6AZ50 in FASTA format |
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