ID   A9UGY9_HUMAN            Unreviewed;       275 AA.
AC   A9UGY9;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 132.
DE   RecName: Full=Autophagy protein 5 {ECO:0000256|RuleBase:RU361202};
GN   Name=ATG5 {ECO:0000313|EMBL:ABX79918.1};
GN   ORFNames=hCG_32959 {ECO:0000313|EMBL:EAW48415.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:ABX79918.1};
RN   [1] {ECO:0000313|EMBL:EAW48415.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=11181995; DOI=10.1126/science.1058040;
RA   Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G.,
RA   Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D., Amanatides P.,
RA   Ballew R.M., Huson D.H., Wortman J.R., Zhang Q., Kodira C.D., Zheng X.H.,
RA   Chen L., Skupski M., Subramanian G., Thomas P.D., Zhang J.,
RA   Gabor Miklos G.L., Nelson C., Broder S., Clark A.G., Nadeau J.,
RA   McKusick V.A., Zinder N., Levine A.J., Roberts R.J., Simon M., Slayman C.,
RA   Hunkapiller M., Bolanos R., Delcher A., Dew I., Fasulo D., Flanigan M.,
RA   Florea L., Halpern A., Hannenhalli S., Kravitz S., Levy S., Mobarry C.,
RA   Reinert K., Remington K., Abu-Threideh J., Beasley E., Biddick K.,
RA   Bonazzi V., Brandon R., Cargill M., Chandramouliswaran I., Charlab R.,
RA   Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K.,
RA   Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z., Guan P.,
RA   Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A., Lai Z., Lei Y.,
RA   Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V., Milshina N.,
RA   Moore H.M., Naik A.K., Narayan V.A., Neelam B., Nusskern D., Rusch D.B.,
RA   Salzberg S., Shao W., Shue B., Sun J., Wang Z., Wang A., Wang X., Wang J.,
RA   Wei M., Wides R., Xiao C., Yan C., Yao A., Ye J., Zhan M., Zhang W.,
RA   Zhang H., Zhao Q., Zheng L., Zhong F., Zhong W., Zhu S., Zhao S.,
RA   Gilbert D., Baumhueter S., Spier G., Carter C., Cravchik A., Woodage T.,
RA   Ali F., An H., Awe A., Baldwin D., Baden H., Barnstead M., Barrow I.,
RA   Beeson K., Busam D., Carver A., Center A., Cheng M.L., Curry L.,
RA   Danaher S., Davenport L., Desilets R., Dietz S., Dodson K., Doup L.,
RA   Ferriera S., Garg N., Gluecksmann A., Hart B., Haynes J., Haynes C.,
RA   Heiner C., Hladun S., Hostin D., Houck J., Howland T., Ibegwam C.,
RA   Johnson J., Kalush F., Kline L., Koduru S., Love A., Mann F., May D.,
RA   McCawley S., McIntosh T., McMullen I., Moy M., Moy L., Murphy B.,
RA   Nelson K., Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M.,
RA   Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C.,
RA   Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N., Tse S.,
RA   Vech C., Wang G., Wetter J., Williams S., Williams M., Windsor S.,
RA   Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F., Guigo R.,
RA   Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A., Mi H., Lazareva B.,
RA   Hatton T., Narechania A., Diemer K., Muruganujan A., Guo N., Sato S.,
RA   Bafna V., Istrail S., Lippert R., Schwartz R., Walenz B., Yooseph S.,
RA   Allen D., Basu A., Baxendale J., Blick L., Caminha M., Carnes-Stine J.,
RA   Caulk P., Chiang Y.H., Coyne M., Dahlke C., Mays A., Dombroski M.,
RA   Donnelly M., Ely D., Esparham S., Fosler C., Gire H., Glanowski S.,
RA   Glasser K., Glodek A., Gorokhov M., Graham K., Gropman B., Harris M.,
RA   Heil J., Henderson S., Hoover J., Jennings D., Jordan C., Jordan J.,
RA   Kasha J., Kagan L., Kraft C., Levitsky A., Lewis M., Liu X., Lopez J.,
RA   Ma D., Majoros W., McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N.,
RA   Nodell M., Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J.,
RA   Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E.,
RA   Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.;
RT   "The sequence of the human genome.";
RL   Science 291:1304-1351(2001).
RN   [2] {ECO:0000313|EMBL:EAW48415.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ABX79918.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Mayo K., Miller K., Hakami R., Ulrich R., Elliott L.H.;
RT   "Expression of autophagy related genes in human CD14 cells infected with
RT   Streptococcus pyogenes.";
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:AGC52703.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Xu L.-H., Ouyang D.-Y., He X.-H.;
RT   "Cloning of cDNA of autophagy-related genes from human prostate cancer cell
RT   lines.";
RL   Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in autophagic vesicle formation. Conjugation with
CC       ATG12, through a ubiquitin-like conjugating system involving ATG7 as an
CC       E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme,
CC       is essential for its function. The ATG12-ATG5 conjugate acts as an E3-
CC       like enzyme which is required for lipidation of ATG8 family proteins
CC       and their association to the vesicle membranes. Involved in
CC       mitochondrial quality control after oxidative damage, and in subsequent
CC       cellular longevity. Plays a critical role in multiple aspects of
CC       lymphocyte development and is essential for both B and T lymphocyte
CC       survival and proliferation. Required for optimal processing and
CC       presentation of antigens for MHC II. Involved in the maintenance of
CC       axon morphology and membrane structures, as well as in normal adipocyte
CC       differentiation. Promotes primary ciliogenesis through removal of OFD1
CC       from centriolar satellites and degradation of IFT20 via the autophagic
CC       pathway. {ECO:0000256|ARBA:ARBA00003480}.
CC   -!- FUNCTION: May play an important role in the apoptotic process, possibly
CC       within the modified cytoskeleton. Its expression is a relatively late
CC       event in the apoptotic process, occurring downstream of caspase
CC       activity. Plays a crucial role in IFN-gamma-induced autophagic cell
CC       death by interacting with FADD. {ECO:0000256|ARBA:ARBA00025421}.
CC   -!- SUBUNIT: Conjugated with ATG12. {ECO:0000256|RuleBase:RU361202}.
CC   -!- INTERACTION:
CC       A9UGY9; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-10175276, EBI-10175300;
CC       A9UGY9; Q14145: KEAP1; NbExp=3; IntAct=EBI-10175276, EBI-751001;
CC       A9UGY9; P50222: MEOX2; NbExp=3; IntAct=EBI-10175276, EBI-748397;
CC       A9UGY9; Q8WW24: TEKT4; NbExp=3; IntAct=EBI-10175276, EBI-750487;
CC       A9UGY9; P55072: VCP; NbExp=3; IntAct=EBI-10175276, EBI-355164;
CC   -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC       {ECO:0000256|RuleBase:RU361202}; Peripheral membrane protein
CC       {ECO:0000256|RuleBase:RU361202}.
CC   -!- SIMILARITY: Belongs to the ATG5 family. {ECO:0000256|ARBA:ARBA00006910,
CC       ECO:0000256|RuleBase:RU361202}.
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DR   EMBL; EU283339; ABX79918.1; -; mRNA.
DR   EMBL; JQ924061; AGC52703.1; -; mRNA.
DR   EMBL; CH471051; EAW48415.1; -; Genomic_DNA.
DR   RefSeq; NP_001273035.1; NM_001286106.1.
DR   RefSeq; NP_004840.1; NM_004849.3.
DR   SMR; A9UGY9; -.
DR   IntAct; A9UGY9; 5.
DR   TCDB; 9.A.15.2.1; the autophagy-related phagophore-formation transporter (apt) family.
DR   Antibodypedia; 32129; 1231 antibodies from 43 providers.
DR   DNASU; 9474; -.
DR   GeneID; 9474; -.
DR   KEGG; hsa:9474; -.
DR   CTD; 9474; -.
DR   PharmGKB; PA24880; -.
DR   VEuPathDB; HostDB:ENSG00000057663; -.
DR   HOGENOM; CLU_051894_1_0_1; -.
DR   OMA; SIQKAVW; -.
DR   OrthoDB; 8084at2759; -.
DR   BioGRID-ORCS; 9474; 25 hits in 1168 CRISPR screens.
DR   ChiTaRS; ATG5; human.
DR   GenomeRNAi; 9474; -.
DR   ExpressionAtlas; A9UGY9; baseline and differential.
DR   GO; GO:0034274; C:Atg12-Atg5-Atg16 complex; IEA:Ensembl.
DR   GO; GO:0005776; C:autophagosome; IEA:Ensembl.
DR   GO; GO:0030424; C:axon; IEA:Ensembl.
DR   GO; GO:0005930; C:axoneme; IEA:Ensembl.
DR   GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; IEA:Ensembl.
DR   GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0035973; P:aggrephagy; IEA:Ensembl.
DR   GO; GO:0019883; P:antigen processing and presentation of endogenous antigen; IEA:Ensembl.
DR   GO; GO:0000045; P:autophagosome assembly; IEA:Ensembl.
DR   GO; GO:0001974; P:blood vessel remodeling; IEA:Ensembl.
DR   GO; GO:0010659; P:cardiac muscle cell apoptotic process; IEA:Ensembl.
DR   GO; GO:0071500; P:cellular response to nitrosative stress; IEA:Ensembl.
DR   GO; GO:0009267; P:cellular response to starvation; IEA:Ensembl.
DR   GO; GO:0061684; P:chaperone-mediated autophagy; IEA:Ensembl.
DR   GO; GO:0006325; P:chromatin organization; IEA:Ensembl.
DR   GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR   GO; GO:0060047; P:heart contraction; IEA:Ensembl.
DR   GO; GO:0000423; P:mitophagy; IEA:Ensembl.
DR   GO; GO:0070254; P:mucus secretion; IEA:Ensembl.
DR   GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; IEA:Ensembl.
DR   GO; GO:0050687; P:negative regulation of defense response to virus; IEA:Ensembl.
DR   GO; GO:0045824; P:negative regulation of innate immune response; IEA:Ensembl.
DR   GO; GO:0050765; P:negative regulation of phagocytosis; IEA:Ensembl.
DR   GO; GO:0031397; P:negative regulation of protein ubiquitination; IEA:Ensembl.
DR   GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IEA:Ensembl.
DR   GO; GO:0032480; P:negative regulation of type I interferon production; IEA:Ensembl.
DR   GO; GO:0039689; P:negative stranded viral RNA replication; IEA:Ensembl.
DR   GO; GO:0045060; P:negative thymic T cell selection; IEA:Ensembl.
DR   GO; GO:0048840; P:otolith development; IEA:Ensembl.
DR   GO; GO:0070257; P:positive regulation of mucus secretion; IEA:Ensembl.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:Ensembl.
DR   GO; GO:1902017; P:regulation of cilium assembly; IEA:Ensembl.
DR   GO; GO:0002718; P:regulation of cytokine production involved in immune response; IEA:Ensembl.
DR   GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; IEA:Ensembl.
DR   GO; GO:1902617; P:response to fluoride; IEA:Ensembl.
DR   GO; GO:0009620; P:response to fungus; IEA:Ensembl.
DR   GO; GO:0010040; P:response to iron(II) ion; IEA:Ensembl.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR   GO; GO:0042311; P:vasodilation; IEA:Ensembl.
DR   GO; GO:0055015; P:ventricular cardiac muscle cell development; IEA:Ensembl.
DR   Gene3D; 3.10.20.620; -; 1.
DR   Gene3D; 1.10.246.190; Autophagy protein Apg5, helix rich domain; 1.
DR   InterPro; IPR007239; Atg5.
DR   InterPro; IPR048940; ATG5_HBR.
DR   InterPro; IPR042526; Atg5_HR.
DR   InterPro; IPR048939; ATG5_UblA.
DR   InterPro; IPR042527; Atg5_UblA_dom_sf.
DR   InterPro; IPR048318; ATG5_UblB.
DR   PANTHER; PTHR13040; AUTOPHAGY PROTEIN 5; 1.
DR   PANTHER; PTHR13040:SF2; AUTOPHAGY PROTEIN 5; 1.
DR   Pfam; PF20637; ATG5_HBR; 1.
DR   Pfam; PF20638; ATG5_UblA; 1.
DR   Pfam; PF04106; ATG5_UblB; 1.
PE   1: Evidence at protein level;
KW   Autophagy {ECO:0000256|ARBA:ARBA00023006, ECO:0000256|RuleBase:RU361202};
KW   Isopeptide bond {ECO:0000256|ARBA:ARBA00022499,
KW   ECO:0000256|RuleBase:RU361202}; Membrane {ECO:0000256|RuleBase:RU361202};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843,
KW   ECO:0000256|RuleBase:RU361202}.
FT   DOMAIN          11..104
FT                   /note="Autophagy protein ATG5 UblA"
FT                   /evidence="ECO:0000259|Pfam:PF20638"
FT   DOMAIN          119..174
FT                   /note="Autophagy protein ATG5 alpha-helical bundle region"
FT                   /evidence="ECO:0000259|Pfam:PF20637"
FT   DOMAIN          184..269
FT                   /note="Autophagy protein ATG5 UblB"
FT                   /evidence="ECO:0000259|Pfam:PF04106"
SQ   SEQUENCE   275 AA;  32447 MW;  C33A1E0B3C1DBE5C CRC64;
     MTDDKDVLRD VWFGRIPTCF TLYQDEITER EAEPYYLLLP RVSYLTLVTD KVKKHFQKVM
     RQEDISEIWF EYEGTPLKWH YPIGLLFDLL ASSSALPWNI TVHFKSFPEK DLLHCPSKDA
     IEAHFMSCMK EADALKHKSQ VINEMQKKDH KQLWMGLQND RFDQFWAINR KLMEYPAEEN
     GFRYIPFRIY QTTTERPFIQ KLFRPVAADG QLHTLGDLLK EVCPSAIDPE DGEKKNQVMI
     HGIEPMLETP LQWLSEHLSY PDNFLHISII PQPTD
//