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Q8C0J2 (A16L1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Autophagy-related protein 16-1
Alternative name(s):
APG16-like 1
Gene names
Name:Atg16l1
Synonyms:Apg16l
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length607 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays an essential role in autophagy: interacts with ATG12-ATG5 to mediate the conjugation of phosphatidylethanolamine (PE) to LC3 (MAP1LC3A, MAP1LC3B or MAP1LC3C), to produce a membrane-bound activated form of LC3 named LC3-II. Thereby, controls the elongation of the nascent autophagosomal membrane. Ref.1 Ref.7

Subunit structure

Interacts with TMEM59, TLR2 and NOD2 By similarity. Homooligomer. Interacts with ATG5. Part of either the minor and major complexes respectively composed of 4 sets of ATG12-ATG5 and ATG16L1 (400 kDa) or 8 sets of ATG12-ATG5 and ATG16L1 (800 kDa). Interacts with RAB33B. Ref.1 Ref.5

Subcellular location

Cytoplasm. Preautophagosomal structure membrane; Peripheral membrane protein. Note: Localized to preautophagosomal structure (PAS) where it is involved in the membrane targeting of ATG5. Localizes also to discrete punctae along the ciliary axoneme. Ref.1 Ref.6

Tissue specificity

Widely expressed. In the liver, isoform 2 is highly expressed and isoform 1 is weakly expressed. Isoform 3 is expressed in the brain. Ref.1

Post-translational modification

Proteolytic cleavage by activated CASP3 leads to degradation and may regulate autophagy upon cellular stress and apoptotic stimuli.

Sequence similarities

Belongs to the WD repeat ATG16 family.

Contains 7 WD repeats.

Sequence caution

The sequence BAD21370.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Rb1cc1Q9ESK93EBI-769195,EBI-647302

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8C0J2-1)

Also known as: Apg16Lbeta;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8C0J2-2)

Also known as: Apg16Lalpha;

The sequence of this isoform differs from the canonical sequence as follows:
     266-284: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q8C0J2-3)

Also known as: Apg16Lgamma;

The sequence of this isoform differs from the canonical sequence as follows:
     284-284: G → GLSESPLLGHHSSDAAR
Isoform 4 (identifier: Q8C0J2-4)

The sequence of this isoform differs from the canonical sequence as follows:
     284-284: G → GLSESPLLGHHSSDAAR
     443-452: IKTVFAGSSC → EEMQSLCVFM
     453-607: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: Q8C0J2-5)

The sequence of this isoform differs from the canonical sequence as follows:
     266-284: Missing.
     442-442: C → CEEMQSLCVLMVFGFLSG
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 607607Autophagy-related protein 16-1
PRO_0000050849

Regions

Repeat320 – 35940WD 1
Repeat364 – 40340WD 2
Repeat406 – 44540WD 3
Repeat447 – 48438WD 4
Repeat486 – 52540WD 5
Repeat532 – 57342WD 6
Repeat575 – 60733WD 7
Coiled coil79 – 230152 Potential
Motif296 – 2994Caspase cleavage

Amino acid modifications

Modified residue2691Phosphoserine By similarity
Modified residue2871Phosphoserine By similarity

Natural variations

Alternative sequence266 – 28419Missing in isoform 2 and isoform 5.
VSP_013391
Alternative sequence2841G → GLSESPLLGHHSSDAAR in isoform 3 and isoform 4.
VSP_013392
Alternative sequence4421C → CEEMQSLCVLMVFGFLSG in isoform 5.
VSP_013393
Alternative sequence443 – 45210IKTVFAGSSC → EEMQSLCVFM in isoform 4.
VSP_013394
Alternative sequence453 – 607155Missing in isoform 4.
VSP_013395

Experimental info

Mutagenesis2991D → E: Prevents cleavage by activated CASP3. Ref.7
Mutagenesis3001T → A: No effect on the stability of the protein. Enhances cleavage and degradation mediated by activated CASP3. Results in reduced autophagy and defective clearance of intestinal pathogens. Ref.7
Sequence conflict831Q → H in BAC55090. Ref.1
Sequence conflict831Q → H in BAC55091. Ref.1
Sequence conflict831Q → H in BAC55092. Ref.1
Sequence conflict831Q → H in BAB23866. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Apg16Lbeta) [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 63920320883A69DF

FASTA60768,172
        10         20         30         40         50         60 
MSSGLRAADF PRWKRHIAEE LRRRDRLQRQ AFEEIILQYT KLLEKSDLHS VLTQKLQAEK 

        70         80         90        100        110        120 
HDMPNRHEIS PGHDGAWNDS QLQEMAQLRI KHQEELTELH KKRGELAQLV IDLNNQMQQK 

       130        140        150        160        170        180 
DKEIQMNEAK ISEYLQTISD LETNCLDLRT KLQDLEVANQ TLKDEYDALQ ITFTALEEKL 

       190        200        210        220        230        240 
RKTTEENQEL VTRWMAEKAQ EANRLNAENE KDSRRRQARL QKELAEAAKE PLPVEQDDDI 

       250        260        270        280        290        300 
EVIVDETSDH TEETSPVRAV SRAATKRLSQ PAGGLLDSIT NIFGRRSVSS IPVPQDIMDT 

       310        320        330        340        350        360 
HPASGKDVRV PTTASYVFDA HDGEVNAVQF SPGSRLLATG GMDRRVKLWE AFGDKCEFKG 

       370        380        390        400        410        420 
SLSGSNAGIT SIEFDSAGAY LLAASNDFAS RIWTVDDYRL RHTLTGHSGK VLSAKFLLDN 

       430        440        450        460        470        480 
ARIVSGSHDR TLKLWDLRSK VCIKTVFAGS SCNDIVCTEQ CVMSGHFDKK IRFWDIRSES 

       490        500        510        520        530        540 
VVREMELLGK ITALDLNPER TELLSCSRDD LLKVIDLRTN AVKQTFSAPG FKCGSDWTRV 

       550        560        570        580        590        600 
VFSPDGSYVA AGSAEGSLYV WSVLTGKVEK VLSKQHSSSI NAVAWAPSGL HVVSVDKGSR 


AVLWAQP 

« Hide

Isoform 2 (Apg16Lalpha) [UniParc].

Checksum: CE2AB829A7911274
Show »

FASTA58866,203
Isoform 3 (Apg16Lgamma) [UniParc].

Checksum: 823453BB5D7DE6FE
Show »

FASTA62369,831
Isoform 4 [UniParc].

Checksum: FFB7AC4AE34DF8F7
Show »

FASTA46853,024
Isoform 5 [UniParc].

Checksum: B0BB8DE0748401B6
Show »

FASTA60568,075

References

« Hide 'large scale' references
[1]"Mouse Apg16L, a novel WD-repeat protein, targets to the autophagic isolation membrane with the Apg12-Apg5 conjugate."
Mizushima N., Kuma A., Kobayashi Y., Yamamoto A., Matsubae M., Takao T., Natsume T., Ohsumi Y., Yoshimori T.
J. Cell Sci. 116:1679-1688(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH ATG5.
[2]"The transcriptional landscape of the mammalian genome."
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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
Strain: C57BL/6J.
Tissue: Cerebellum and Thymus.
[3]"Prediction of the coding sequences of mouse homologues of FLJ genes: the complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.
DNA Res. 11:127-135(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
Tissue: Fetal brain.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Strain: C57BL/6.
Tissue: Brain.
[5]"Golgi-resident small GTPase Rab33B interacts with Atg16L and modulates autophagosome formation."
Itoh T., Fujita N., Kanno E., Yamamoto A., Yoshimori T., Fukuda M.
Mol. Biol. Cell 19:2916-2925(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAB33B.
[6]"Functional interaction between autophagy and ciliogenesis."
Pampliega O., Orhon I., Patel B., Sridhar S., Diaz-Carretero A., Beau I., Codogno P., Satir B.H., Satir P., Cuervo A.M.
Nature 502:194-200(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[7]"A Crohn's disease variant in Atg16l1 enhances its degradation by caspase 3."
Murthy A., Li Y., Peng I., Reichelt M., Katakam A.K., Noubade R., Roose-Girma M., Devoss J., Diehl L., Graham R.R., van Lookeren Campagne M.
Nature 506:456-462(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN AUTOPHAGY, CLEAVAGE BY CASP3, MUTAGENESIS OF ASP-299 AND THR-300.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB087879 mRNA. Translation: BAC55090.1.
AB087880 mRNA. Translation: BAC55091.1.
AB087881 mRNA. Translation: BAC55092.1.
AK005181 mRNA. Translation: BAB23866.1.
AK030983 mRNA. Translation: BAC27201.1.
AK131120 Transcribed RNA. Translation: BAD21370.1. Different initiation.
BC049122 mRNA. Translation: AAH49122.1.
CCDSCCDS15136.1. [Q8C0J2-1]
CCDS56637.1. [Q8C0J2-3]
CCDS56638.1. [Q8C0J2-2]
RefSeqNP_001192320.1. NM_001205391.1. [Q8C0J2-3]
NP_084122.2. NM_029846.4. [Q8C0J2-1]
UniGeneMm.272972.
Mm.456099.

3D structure databases

ProteinModelPortalQ8C0J2.
SMRQ8C0J2. Positions 267-604.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid218476. 5 interactions.
DIPDIP-31966N.
IntActQ8C0J2. 4 interactions.
MINTMINT-136268.

PTM databases

PhosphoSiteQ8C0J2.

2D gel databases

REPRODUCTION-2DPAGEQ8C0J2.

Proteomic databases

MaxQBQ8C0J2.
PaxDbQ8C0J2.
PRIDEQ8C0J2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000027512; ENSMUSP00000027512; ENSMUSG00000026289. [Q8C0J2-1]
ENSMUST00000113186; ENSMUSP00000108811; ENSMUSG00000026289. [Q8C0J2-2]
ENSMUST00000113190; ENSMUSP00000108815; ENSMUSG00000026289. [Q8C0J2-3]
GeneID77040.
KEGGmmu:77040.
UCSCuc007bxl.2. mouse. [Q8C0J2-1]

Organism-specific databases

CTD55054.
MGIMGI:1924290. Atg16l1.

Phylogenomic databases

eggNOGCOG2319.
GeneTreeENSGT00740000115355.
HOVERGENHBG050534.
KOK17890.
OMALETECQE.
OrthoDBEOG70CR6M.
PhylomeDBQ8C0J2.
TreeFamTF315541.

Gene expression databases

ArrayExpressQ8C0J2.
BgeeQ8C0J2.
CleanExMM_ATG16L1.
GenevestigatorQ8C0J2.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
InterProIPR013923. Autophagy-rel_prot_16.
IPR020472. G-protein_beta_WD-40_rep.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamPF08614. ATG16. 1 hit.
PF00400. WD40. 5 hits.
[Graphical view]
PRINTSPR00320. GPROTEINBRPT.
SMARTSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMSSF50978. SSF50978. 1 hit.
PROSITEPS00678. WD_REPEATS_1. 3 hits.
PS50082. WD_REPEATS_2. 6 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio346354.
PROQ8C0J2.
SOURCESearch...

Entry information

Entry nameA16L1_MOUSE
AccessionPrimary (citable) accession number: Q8C0J2
Secondary accession number(s): Q6KAT7 expand/collapse secondary AC list , Q80U97, Q80U98, Q80U99, Q80Y53, Q9DB63
Entry history
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot