CACO2_HUMAN
ID CACO2_HUMAN Reviewed; 446 AA.
AC Q13137; B2RBT0; B4DDC4; B4DDT4; B4DP36; B4E0C0; E7ENK0; E7ETP5; E9PBE5;
AC Q53FQ5; Q53HB5; Q6IBN9; Q9BTF7;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Calcium-binding and coiled-coil domain-containing protein 2;
DE AltName: Full=Antigen nuclear dot 52 kDa protein;
DE AltName: Full=Nuclear domain 10 protein NDP52 {ECO:0000305};
DE Short=Nuclear domain 10 protein 52 {ECO:0000303|PubMed:7540613};
DE AltName: Full=Nuclear dot protein 52 {ECO:0000303|PubMed:9230084};
GN Name=CALCOCO2; Synonyms=NDP52 {ECO:0000303|PubMed:7540613};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INDUCTION.
RX PubMed=7540613; DOI=10.1083/jcb.130.1.1;
RA Korioth F., Gieffers C., Maul G.G., Frey J.;
RT "Molecular characterization of NDP52, a novel protein of the nuclear domain
RT 10, which is redistributed upon virus infection and interferon treatment.";
RL J. Cell Biol. 130:1-13(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3; 4 AND 5), AND
RP VARIANTS GLU-140; ALA-248 AND ALA-389.
RC TISSUE=Mammary gland, Neuroblastoma, Teratocarcinoma, and Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-248.
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-389.
RC TISSUE=Brain, and Gastric mucosa;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-389.
RA Mural R.J., Istrail S., Sutton G.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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-273.
RC TISSUE=Kidney, and Skin;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=9230084; DOI=10.1083/jcb.138.2.435;
RA Sternsdorf T., Jensen K., Zuchner D., Will H.;
RT "Cellular localization, expression, and structure of the nuclear dot
RT protein 52.";
RL J. Cell Biol. 138:435-448(1997).
RN [9]
RP INTERACTION WITH GEMIN4, AND SUBCELLULAR LOCATION.
RX PubMed=12869526; DOI=10.1093/jb/mvg091;
RA Di Y., Li J., Zhang Y., He X., Lu H., Xu D., Ling J., Huo K., Wan D.,
RA Li Y.Y., Gu J.;
RT "HCC-associated protein HCAP1, a variant of GEMIN4, interacts with zinc-
RT finger proteins.";
RL J. Biochem. 133:713-718(2003).
RN [10]
RP FUNCTION, INTERACTION WITH TAX1BP1 AND MYO6, MUTAGENESIS OF CYS-400 AND
RP CYS-425, AND SUBCELLULAR LOCATION.
RX PubMed=17635994; DOI=10.1242/jcs.007005;
RA Morriswood B., Ryzhakov G., Puri C., Arden S.D., Roberts R., Dendrou C.,
RA Kendrick-Jones J., Buss F.;
RT "T6BP and NDP52 are myosin VI binding partners with potential roles in
RT cytokine signalling and cell adhesion.";
RL J. Cell Sci. 120:2574-2585(2007).
RN [11]
RP FUNCTION, AND INTERACTION WITH LGALS8.
RX PubMed=22246324; DOI=10.1038/nature10744;
RA Thurston T.L., Wandel M.P., von Muhlinen N., Foeglein A., Randow F.;
RT "Galectin 8 targets damaged vesicles for autophagy to defend cells against
RT bacterial invasion.";
RL Nature 482:414-418(2012).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP FUNCTION, DOMAIN, MUTAGENESIS OF CYS-425, INTERACTION WITH MAP1LC3A;
RP MAP1LC3C; MAP1LC3B; GABARAP; GABARAPL1; GABARAPL2 AND LGALS8, AND
RP SUBCELLULAR LOCATION.
RX PubMed=25771791; DOI=10.1016/j.chom.2015.02.008;
RA Verlhac P., Gregoire I.P., Azocar O., Petkova D.S., Baguet J., Viret C.,
RA Faure M.;
RT "Autophagy receptor NDP52 regulates pathogen-containing autophagosome
RT maturation.";
RL Cell Host Microbe 17:515-525(2015).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 21-141 IN COMPLEX WITH MAP1LC3C,
RP FUNCTION, DOMAIN, INTERACTION WITH MAP1LC3C, AND MUTAGENESIS OF VAL-136.
RX PubMed=23022382; DOI=10.1016/j.molcel.2012.08.024;
RA von Muhlinen N., Akutsu M., Ravenhill B.J., Foeglein A., Bloor S.,
RA Rutherford T.J., Freund S.M., Komander D., Randow F.;
RT "LC3C, bound selectively by a noncanonical LIR motif in NDP52, is required
RT for antibacterial autophagy.";
RL Mol. Cell 48:329-342(2012).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 372-385 IN COMPLEX WITH LGALS8,
RP SUBUNIT, DOMAIN, AND MUTAGENESIS OF LEU-374 AND TYR-380.
RX PubMed=23511477; DOI=10.1038/ncomms2606;
RA Kim B.W., Hong S.B., Kim J.H., Kwon do H., Song H.K.;
RT "Structural basis for recognition of autophagic receptor NDP52 by the sugar
RT receptor galectin-8.";
RL Nat. Commun. 4:1613-1613(2013).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS) OF 368-381 IN COMPLEX WITH LGALS8,
RP DOMAIN, MUTAGENESIS OF LEU-374; TYR-376; ASN-378 AND TYR-380, INTERACTION
RP WITH LGALS8, AND FUNCTION.
RX PubMed=23386746; DOI=10.1126/scisignal.2003730;
RA Li S., Wandel M.P., Li F., Liu Z., He C., Wu J., Shi Y., Randow F.;
RT "Sterical hindrance promotes selectivity of the autophagy cargo receptor
RT NDP52 for the danger receptor galectin-8 in antibacterial autophagy.";
RL Sci. Signal. 6:RA9-RA9(2013).
CC -!- FUNCTION: Xenophagy-specific receptor required for autophagy-mediated
CC intracellular bacteria degradation. Acts as an effector protein of
CC galectin-sensed membrane damage that restricts the proliferation of
CC infecting pathogens such as Salmonella typhimurium upon entry into the
CC cytosol by targeting LGALS8-associated bacteria for autophagy
CC (PubMed:22246324). Initially orchestrates bacteria targeting to
CC autophagosomes and subsequently ensures pathogen degradation by
CC regulating pathogen-containing autophagosome maturation
CC (PubMed:23022382, PubMed:25771791). Bacteria targeting to
CC autophagosomes relies on its interaction with MAP1LC3A, MAP1LC3B and/or
CC GABARAPL2, whereas regulation of pathogen-containing autophagosome
CC maturation requires the interaction with MAP3LC3C (PubMed:23022382,
CC PubMed:25771791). May play a role in ruffle formation and actin
CC cytoskeleton organization and seems to negatively regulate constitutive
CC secretion (PubMed:17635994). {ECO:0000269|PubMed:17635994,
CC ECO:0000269|PubMed:22246324, ECO:0000269|PubMed:23022382,
CC ECO:0000269|PubMed:23386746, ECO:0000269|PubMed:25771791}.
CC -!- SUBUNIT: Dimer (PubMed:23511477). Part of a complex consisting of
CC CALCOCO2, TAX1BP1 and MYO6 (PubMed:17635994). Interacts with GEMIN4
CC (PubMed:12869526). Interacts with ATG8 family members MAP1LC3A,
CC MAP1LC3B, GABARAP, GABARAPL1 and GABARAPL2 (PubMed:25771791). Interacts
CC with ATG8 family member MAP1LC3C (PubMed:23022382). Interacts with
CC LGALS8 (PubMed:22246324, PubMed:25771791, PubMed:23511477,
CC PubMed:23386746). {ECO:0000269|PubMed:12869526,
CC ECO:0000269|PubMed:17635994, ECO:0000269|PubMed:22246324,
CC ECO:0000269|PubMed:23022382, ECO:0000269|PubMed:23386746,
CC ECO:0000269|PubMed:23511477, ECO:0000269|PubMed:25771791}.
CC -!- INTERACTION:
CC Q13137; Q02040-3: AKAP17A; NbExp=3; IntAct=EBI-739580, EBI-10222656;
CC Q13137; Q9Y4X0: AMMECR1; NbExp=4; IntAct=EBI-739580, EBI-8583355;
CC Q13137; Q9Y4X0-3: AMMECR1; NbExp=3; IntAct=EBI-739580, EBI-12823597;
CC Q13137; Q6P4J0: ARD1A; NbExp=3; IntAct=EBI-739580, EBI-10252815;
CC Q13137; Q8N4T4: ARHGEF39; NbExp=5; IntAct=EBI-739580, EBI-745468;
CC Q13137; Q12774: ARHGEF5; NbExp=3; IntAct=EBI-739580, EBI-602199;
CC Q13137; A0A0S2Z4M1: AXIN1; NbExp=3; IntAct=EBI-739580, EBI-16429430;
CC Q13137; O15169: AXIN1; NbExp=3; IntAct=EBI-739580, EBI-710484;
CC Q13137; Q8TBE0: BAHD1; NbExp=3; IntAct=EBI-739580, EBI-742750;
CC Q13137; A8KA13: BCL6B; NbExp=3; IntAct=EBI-739580, EBI-10174813;
CC Q13137; Q9BXY8: BEX2; NbExp=3; IntAct=EBI-739580, EBI-745073;
CC Q13137; Q9HC52: CBX8; NbExp=6; IntAct=EBI-739580, EBI-712912;
CC Q13137; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-739580, EBI-744556;
CC Q13137; P51946: CCNH; NbExp=3; IntAct=EBI-739580, EBI-741406;
CC Q13137; O00311: CDC7; NbExp=3; IntAct=EBI-739580, EBI-374980;
CC Q13137; P08218: CELA2B; NbExp=3; IntAct=EBI-739580, EBI-11478642;
CC Q13137; Q8IYX8: CEP57L1; NbExp=3; IntAct=EBI-739580, EBI-1104570;
CC Q13137; Q9NX63: CHCHD3; NbExp=3; IntAct=EBI-739580, EBI-743375;
CC Q13137; Q8NE01: CNNM3; NbExp=3; IntAct=EBI-739580, EBI-741032;
CC Q13137; Q9UBL6-2: CPNE7; NbExp=3; IntAct=EBI-739580, EBI-12012272;
CC Q13137; Q2TBE0: CWF19L2; NbExp=3; IntAct=EBI-739580, EBI-5453285;
CC Q13137; Q15038: DAZAP2; NbExp=4; IntAct=EBI-739580, EBI-724310;
CC Q13137; Q9UJW0: DCTN4; NbExp=3; IntAct=EBI-739580, EBI-2134033;
CC Q13137; O43602: DCX; NbExp=3; IntAct=EBI-739580, EBI-8646694;
CC Q13137; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-739580, EBI-742054;
CC Q13137; P26196: DDX6; NbExp=6; IntAct=EBI-739580, EBI-351257;
CC Q13137; Q92608: DOCK2; NbExp=3; IntAct=EBI-739580, EBI-448771;
CC Q13137; Q9UNI6: DUSP12; NbExp=5; IntAct=EBI-739580, EBI-715161;
CC Q13137; Q9BV47: DUSP26; NbExp=3; IntAct=EBI-739580, EBI-2924519;
CC Q13137; O43324: EEF1E1; NbExp=3; IntAct=EBI-739580, EBI-1048486;
CC Q13137; Q5JVL4: EFHC1; NbExp=3; IntAct=EBI-739580, EBI-743105;
CC Q13137; Q9H0I2: ENKD1; NbExp=4; IntAct=EBI-739580, EBI-744099;
CC Q13137; Q9NQT4: EXOSC5; NbExp=3; IntAct=EBI-739580, EBI-371876;
CC Q13137; Q3B820: FAM161A; NbExp=6; IntAct=EBI-739580, EBI-719941;
CC Q13137; Q92567: FAM168A; NbExp=3; IntAct=EBI-739580, EBI-7957930;
CC Q13137; Q7L5A3: FAM214B; NbExp=3; IntAct=EBI-739580, EBI-745689;
CC Q13137; Q86YD7: FAM90A1; NbExp=7; IntAct=EBI-739580, EBI-6658203;
CC Q13137; O95363: FARS2; NbExp=7; IntAct=EBI-739580, EBI-2513774;
CC Q13137; Q8TES7-6: FBF1; NbExp=3; IntAct=EBI-739580, EBI-10244131;
CC Q13137; Q96D16: FBXL18; NbExp=4; IntAct=EBI-739580, EBI-744419;
CC Q13137; Q9UIM3: FKBPL; NbExp=3; IntAct=EBI-739580, EBI-719882;
CC Q13137; Q9BVV2: FNDC11; NbExp=4; IntAct=EBI-739580, EBI-744935;
CC Q13137; Q6VB84: FOXD4L3; NbExp=3; IntAct=EBI-739580, EBI-11961494;
CC Q13137; Q9H0R8: GABARAPL1; NbExp=7; IntAct=EBI-739580, EBI-746969;
CC Q13137; P60520: GABARAPL2; NbExp=7; IntAct=EBI-739580, EBI-720116;
CC Q13137; Q8WXI9: GATAD2B; NbExp=3; IntAct=EBI-739580, EBI-923440;
CC Q13137; P28676: GCA; NbExp=3; IntAct=EBI-739580, EBI-947242;
CC Q13137; Q8IVS8: GLYCTK; NbExp=3; IntAct=EBI-739580, EBI-748515;
CC Q13137; P56524-2: HDAC4; NbExp=3; IntAct=EBI-739580, EBI-11953488;
CC Q13137; Q8WUI4-5: HDAC7; NbExp=3; IntAct=EBI-739580, EBI-10276431;
CC Q13137; Q8WUI4-6: HDAC7; NbExp=3; IntAct=EBI-739580, EBI-12094670;
CC Q13137; P09067: HOXB5; NbExp=3; IntAct=EBI-739580, EBI-3893317;
CC Q13137; P17482: HOXB9; NbExp=3; IntAct=EBI-739580, EBI-745290;
CC Q13137; Q14005-2: IL16; NbExp=3; IntAct=EBI-739580, EBI-17178971;
CC Q13137; Q8NA54: IQUB; NbExp=3; IntAct=EBI-739580, EBI-10220600;
CC Q13137; Q7Z3B3: KANSL1; NbExp=5; IntAct=EBI-739580, EBI-740244;
CC Q13137; Q6PF15: KLHL35; NbExp=3; IntAct=EBI-739580, EBI-9477654;
CC Q13137; Q9P2K6: KLHL42; NbExp=3; IntAct=EBI-739580, EBI-739890;
CC Q13137; Q96BZ8: LENG1; NbExp=3; IntAct=EBI-739580, EBI-726510;
CC Q13137; O00214: LGALS8; NbExp=7; IntAct=EBI-739580, EBI-740058;
CC Q13137; O00214-2: LGALS8; NbExp=3; IntAct=EBI-739580, EBI-12069522;
CC Q13137; Q7Z4I7-5: LIMS2; NbExp=3; IntAct=EBI-739580, EBI-10257651;
CC Q13137; Q99732: LITAF; NbExp=7; IntAct=EBI-739580, EBI-725647;
CC Q13137; Q9BU23: LMF2; NbExp=3; IntAct=EBI-739580, EBI-10298556;
CC Q13137; P25791: LMO2; NbExp=3; IntAct=EBI-739580, EBI-739696;
CC Q13137; P61968: LMO4; NbExp=3; IntAct=EBI-739580, EBI-2798728;
CC Q13137; Q17RB8: LONRF1; NbExp=3; IntAct=EBI-739580, EBI-2341787;
CC Q13137; Q9Y4Z0: LSM4; NbExp=7; IntAct=EBI-739580, EBI-372521;
CC Q13137; Q96A72: MAGOHB; NbExp=6; IntAct=EBI-739580, EBI-746778;
CC Q13137; Q9BXW4: MAP1LC3C; NbExp=3; IntAct=EBI-739580, EBI-2603996;
CC Q13137; Q7Z434: MAVS; NbExp=3; IntAct=EBI-739580, EBI-995373;
CC Q13137; Q9H7H0: METTL17; NbExp=7; IntAct=EBI-739580, EBI-749353;
CC Q13137; Q9H7H0-2: METTL17; NbExp=3; IntAct=EBI-739580, EBI-11098807;
CC Q13137; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-739580, EBI-10172526;
CC Q13137; P00540: MOS; NbExp=8; IntAct=EBI-739580, EBI-1757866;
CC Q13137; Q9NVV4: MTPAP; NbExp=2; IntAct=EBI-739580, EBI-2556166;
CC Q13137; P50539: MXI1; NbExp=3; IntAct=EBI-739580, EBI-752241;
CC Q13137; P50539-3: MXI1; NbExp=6; IntAct=EBI-739580, EBI-10211940;
CC Q13137; P41227: NAA10; NbExp=7; IntAct=EBI-739580, EBI-747693;
CC Q13137; Q9UMS0: NFU1; NbExp=3; IntAct=EBI-739580, EBI-725252;
CC Q13137; Q9UBV8: PEF1; NbExp=4; IntAct=EBI-739580, EBI-724639;
CC Q13137; Q86TG7: PEG10; NbExp=4; IntAct=EBI-739580, EBI-2858265;
CC Q13137; Q99471: PFDN5; NbExp=4; IntAct=EBI-739580, EBI-357275;
CC Q13137; O43189: PHF1; NbExp=3; IntAct=EBI-739580, EBI-530034;
CC Q13137; Q494U1-3: PLEKHN1; NbExp=3; IntAct=EBI-739580, EBI-12014286;
CC Q13137; Q6NYC8: PPP1R18; NbExp=3; IntAct=EBI-739580, EBI-2557469;
CC Q13137; P54646: PRKAA2; NbExp=3; IntAct=EBI-739580, EBI-1383852;
CC Q13137; Q99633: PRPF18; NbExp=3; IntAct=EBI-739580, EBI-2798416;
CC Q13137; Q8WWY3: PRPF31; NbExp=6; IntAct=EBI-739580, EBI-1567797;
CC Q13137; P25786: PSMA1; NbExp=4; IntAct=EBI-739580, EBI-359352;
CC Q13137; Q14997: PSME4; NbExp=3; IntAct=EBI-739580, EBI-1236916;
CC Q13137; P47897: QARS1; NbExp=3; IntAct=EBI-739580, EBI-347462;
CC Q13137; Q96T37: RBM15; NbExp=3; IntAct=EBI-739580, EBI-2514922;
CC Q13137; Q13671: RIN1; NbExp=4; IntAct=EBI-739580, EBI-366017;
CC Q13137; P32969: RPL9P9; NbExp=3; IntAct=EBI-739580, EBI-358122;
CC Q13137; P62979: RPS27A; NbExp=3; IntAct=EBI-739580, EBI-357375;
CC Q13137; Q14D33: RTP5; NbExp=6; IntAct=EBI-739580, EBI-10217913;
CC Q13137; P28702-3: RXRB; NbExp=3; IntAct=EBI-739580, EBI-16429492;
CC Q13137; P57086: SCAND1; NbExp=3; IntAct=EBI-739580, EBI-745846;
CC Q13137; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-739580, EBI-748391;
CC Q13137; O00560: SDCBP; NbExp=3; IntAct=EBI-739580, EBI-727004;
CC Q13137; Q9C0A6-3: SETD5; NbExp=3; IntAct=EBI-739580, EBI-12233047;
CC Q13137; P29353: SHC1; NbExp=3; IntAct=EBI-739580, EBI-78835;
CC Q13137; Q05CH4: SLC15A3; NbExp=3; IntAct=EBI-739580, EBI-10223741;
CC Q13137; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-739580, EBI-358489;
CC Q13137; P49901: SMCP; NbExp=3; IntAct=EBI-739580, EBI-750494;
CC Q13137; P14678-2: SNRPB; NbExp=3; IntAct=EBI-739580, EBI-372475;
CC Q13137; Q86W54: SPATA24; NbExp=3; IntAct=EBI-739580, EBI-3916986;
CC Q13137; P30626: SRI; NbExp=5; IntAct=EBI-739580, EBI-750459;
CC Q13137; Q96FJ0: STAMBPL1; NbExp=3; IntAct=EBI-739580, EBI-745021;
CC Q13137; O75716: STK16; NbExp=3; IntAct=EBI-739580, EBI-749295;
CC Q13137; Q9BSH4: TACO1; NbExp=3; IntAct=EBI-739580, EBI-747797;
CC Q13137; Q9NU19: TBC1D22B; NbExp=3; IntAct=EBI-739580, EBI-8787464;
CC Q13137; Q9UHD2: TBK1; NbExp=7; IntAct=EBI-739580, EBI-356402;
CC Q13137; Q969Z0: TBRG4; NbExp=3; IntAct=EBI-739580, EBI-702328;
CC Q13137; P56279: TCL1A; NbExp=10; IntAct=EBI-739580, EBI-749995;
CC Q13137; Q9BXF9: TEKT3; NbExp=5; IntAct=EBI-739580, EBI-8644516;
CC Q13137; Q6PIY7: TENT2; NbExp=3; IntAct=EBI-739580, EBI-2802204;
CC Q13137; Q08117: TLE5; NbExp=3; IntAct=EBI-739580, EBI-717810;
CC Q13137; Q96S44: TP53RK; NbExp=5; IntAct=EBI-739580, EBI-739588;
CC Q13137; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-739580, EBI-10241197;
CC Q13137; Q8NBM4: UBAC2; NbExp=3; IntAct=EBI-739580, EBI-724045;
CC Q13137; Q5U5U6: UBB; NbExp=3; IntAct=EBI-739580, EBI-1642104;
CC Q13137; Q96C32: UBC; NbExp=3; IntAct=EBI-739580, EBI-745483;
CC Q13137; O75604: USP2; NbExp=3; IntAct=EBI-739580, EBI-743272;
CC Q13137; P26640: VARS1; NbExp=3; IntAct=EBI-739580, EBI-355765;
CC Q13137; Q9P1Z0: ZBTB4; NbExp=3; IntAct=EBI-739580, EBI-2564133;
CC Q13137; Q9Y3M9: ZNF337; NbExp=3; IntAct=EBI-739580, EBI-714987;
CC Q13137; Q9H9D4: ZNF408; NbExp=4; IntAct=EBI-739580, EBI-347633;
CC Q13137; Q96IQ9: ZNF414; NbExp=3; IntAct=EBI-739580, EBI-744257;
CC Q13137; Q8TBZ8: ZNF564; NbExp=3; IntAct=EBI-739580, EBI-10273713;
CC Q13137; Q9P0T4: ZNF581; NbExp=3; IntAct=EBI-739580, EBI-745520;
CC Q13137; Q5T619: ZNF648; NbExp=3; IntAct=EBI-739580, EBI-11985915;
CC Q13137; A0A0S2Z5X4: ZNF688; NbExp=3; IntAct=EBI-739580, EBI-16429014;
CC Q13137; Q9H7X3: ZNF696; NbExp=3; IntAct=EBI-739580, EBI-11090299;
CC Q13137; Q6NX45: ZNF774; NbExp=3; IntAct=EBI-739580, EBI-10251462;
CC Q13137; P51504: ZNF80; NbExp=3; IntAct=EBI-739580, EBI-12013828;
CC Q13137; B2R9Y1; NbExp=3; IntAct=EBI-739580, EBI-10175746;
CC Q13137; Q8WU02; NbExp=3; IntAct=EBI-739580, EBI-747182;
CC Q13137; PRO_0000037548 [Q9WMX2]; Xeno; NbExp=3; IntAct=EBI-739580, EBI-6863741;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:12869526, ECO:0000269|PubMed:17635994,
CC ECO:0000269|PubMed:9230084}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:17635994}. Cytoplasmic vesicle, autophagosome
CC membrane {ECO:0000269|PubMed:25771791}; Peripheral membrane protein
CC {ECO:0000305}. Note=According to PubMed:7540613, localizes to nuclear
CC dots. According to PubMed:9230084 and PubMed:12869526, it is not a
CC nuclear dot-associated protein but localizes predominantly in the
CC cytoplasm with a coarse-grained distribution preferentially close to
CC the nucleus. {ECO:0000269|PubMed:12869526, ECO:0000269|PubMed:7540613,
CC ECO:0000269|PubMed:9230084}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q13137-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13137-2; Sequence=VSP_044728;
CC Name=3;
CC IsoId=Q13137-3; Sequence=VSP_046766;
CC Name=4;
CC IsoId=Q13137-4; Sequence=VSP_046767;
CC Name=5;
CC IsoId=Q13137-5; Sequence=VSP_047414;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested with highest
CC expression in skeletal muscle and lowest in brain.
CC {ECO:0000269|PubMed:7540613}.
CC -!- INDUCTION: Treatment with IFNB1/IFN-beta and IFNG/IFN-gamma show an
CC increase in number and size of CALCOCO2-specific dots and partial
CC redistribution to the cytoplasm (PubMed:7540613). IFNG/IFN-gamma
CC increases gene expression only slightly and IFNB does not increase
CC expression (PubMed:9230084). {ECO:0000269|PubMed:7540613,
CC ECO:0000269|PubMed:9230084}.
CC -!- DOMAIN: The MYO6-binding domain is required for autophagy-mediated
CC degradation of infecting bacteria such as Salmonella typhimurium, but
CC not for bacteria targeting to autophagosomes.
CC {ECO:0000269|PubMed:25771791}.
CC -!- DOMAIN: The CLIR (LC3C-interacting region) motif is required for
CC interaction with MAP1LC3C, but dispensable for CALCOCO2-mediated
CC autophagosome maturation. {ECO:0000269|PubMed:23022382,
CC ECO:0000269|PubMed:25771791}.
CC -!- DOMAIN: The LIR-like motif is required for interaction with MAP1LC3A,
CC MAP1LC3B and GABARAPL2, as well as for CALCOCO2-mediated autophagosome
CC maturation. {ECO:0000269|PubMed:25771791}.
CC -!- DOMAIN: The LGALS8-binding domain is essential for the recruitment to
CC cytosol-exposed infecting bacteria. {ECO:0000269|PubMed:23386746}.
CC -!- SIMILARITY: Belongs to the CALCOCO family. {ECO:0000305}.
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DR EMBL; U22897; AAA75297.1; -; mRNA.
DR EMBL; AK293137; BAG56685.1; -; mRNA.
DR EMBL; AK293329; BAG56845.1; -; mRNA.
DR EMBL; AK298177; BAG60448.1; -; mRNA.
DR EMBL; AK303313; BAG64382.1; -; mRNA.
DR EMBL; AK314796; BAG37327.1; -; mRNA.
DR EMBL; CR456763; CAG33044.1; -; mRNA.
DR EMBL; AK222666; BAD96386.1; -; mRNA.
DR EMBL; AK223227; BAD96947.1; -; mRNA.
DR EMBL; AC068531; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471109; EAW94707.1; -; Genomic_DNA.
DR EMBL; BC004130; AAH04130.1; -; mRNA.
DR EMBL; BC015893; AAH15893.1; -; mRNA.
DR CCDS; CCDS11538.1; -. [Q13137-1]
DR CCDS; CCDS58558.1; -. [Q13137-3]
DR CCDS; CCDS58559.1; -. [Q13137-4]
DR CCDS; CCDS58560.1; -. [Q13137-2]
DR CCDS; CCDS58561.1; -. [Q13137-5]
DR PIR; A56733; A56733.
DR RefSeq; NP_001248319.1; NM_001261390.1. [Q13137-4]
DR RefSeq; NP_001248320.1; NM_001261391.1. [Q13137-3]
DR RefSeq; NP_001248322.1; NM_001261393.1. [Q13137-2]
DR RefSeq; NP_001248324.1; NM_001261395.1. [Q13137-5]
DR RefSeq; NP_005822.1; NM_005831.4. [Q13137-1]
DR PDB; 2MXP; NMR; -; A=414-446.
DR PDB; 3VVV; X-ray; 1.35 A; A=21-141.
DR PDB; 3VVW; X-ray; 2.50 A; A=21-141.
DR PDB; 4GXL; X-ray; 2.02 A; B=368-381.
DR PDB; 4HAN; X-ray; 2.55 A; C/D=372-385.
DR PDB; 4XKL; X-ray; 2.10 A; B/D=414-446.
DR PDB; 5AAQ; NMR; -; A=388-446.
DR PDB; 5Z7A; X-ray; 2.38 A; A/B=1-126.
DR PDB; 5Z7L; X-ray; 2.02 A; A/B=10-126.
DR PDB; 7EAA; X-ray; 2.60 A; A/B=10-141.
DR PDBsum; 2MXP; -.
DR PDBsum; 3VVV; -.
DR PDBsum; 3VVW; -.
DR PDBsum; 4GXL; -.
DR PDBsum; 4HAN; -.
DR PDBsum; 4XKL; -.
DR PDBsum; 5AAQ; -.
DR PDBsum; 5Z7A; -.
DR PDBsum; 5Z7L; -.
DR PDBsum; 7EAA; -.
DR AlphaFoldDB; Q13137; -.
DR BMRB; Q13137; -.
DR SMR; Q13137; -.
DR BioGRID; 115535; 491.
DR DIP; DIP-57534N; -.
DR IntAct; Q13137; 214.
DR MINT; Q13137; -.
DR STRING; 9606.ENSP00000398523; -.
DR iPTMnet; Q13137; -.
DR PhosphoSitePlus; Q13137; -.
DR BioMuta; CALCOCO2; -.
DR DMDM; 74735623; -.
DR CPTAC; CPTAC-1312; -.
DR EPD; Q13137; -.
DR jPOST; Q13137; -.
DR MassIVE; Q13137; -.
DR MaxQB; Q13137; -.
DR PaxDb; Q13137; -.
DR PeptideAtlas; Q13137; -.
DR PRIDE; Q13137; -.
DR ProteomicsDB; 17172; -.
DR ProteomicsDB; 18257; -.
DR ProteomicsDB; 19207; -.
DR ProteomicsDB; 4752; -.
DR ProteomicsDB; 59186; -. [Q13137-1]
DR Antibodypedia; 17875; 452 antibodies from 28 providers.
DR DNASU; 10241; -.
DR Ensembl; ENST00000258947.8; ENSP00000258947.3; ENSG00000136436.15. [Q13137-1]
DR Ensembl; ENST00000416445.6; ENSP00000406974.2; ENSG00000136436.15. [Q13137-2]
DR Ensembl; ENST00000448105.6; ENSP00000398523.2; ENSG00000136436.15. [Q13137-4]
DR Ensembl; ENST00000508679.5; ENSP00000423437.1; ENSG00000136436.15. [Q13137-5]
DR Ensembl; ENST00000509507.5; ENSP00000424352.1; ENSG00000136436.15. [Q13137-3]
DR GeneID; 10241; -.
DR KEGG; hsa:10241; -.
DR MANE-Select; ENST00000258947.8; ENSP00000258947.3; NM_005831.5; NP_005822.1.
DR UCSC; uc002iof.4; human. [Q13137-1]
DR CTD; 10241; -.
DR DisGeNET; 10241; -.
DR GeneCards; CALCOCO2; -.
DR HGNC; HGNC:29912; CALCOCO2.
DR HPA; ENSG00000136436; Low tissue specificity.
DR MIM; 604587; gene.
DR neXtProt; NX_Q13137; -.
DR OpenTargets; ENSG00000136436; -.
DR PharmGKB; PA143485407; -.
DR VEuPathDB; HostDB:ENSG00000136436; -.
DR eggNOG; ENOG502QT1M; Eukaryota.
DR GeneTree; ENSGT00950000183025; -.
DR HOGENOM; CLU_021315_0_0_1; -.
DR InParanoid; Q13137; -.
DR OMA; WIGIFRA; -.
DR OrthoDB; 179838at2759; -.
DR PhylomeDB; Q13137; -.
DR TreeFam; TF329501; -.
DR PathwayCommons; Q13137; -.
DR SignaLink; Q13137; -.
DR BioGRID-ORCS; 10241; 13 hits in 1083 CRISPR screens.
DR ChiTaRS; CALCOCO2; human.
DR GeneWiki; CALCOCO2; -.
DR GenomeRNAi; 10241; -.
DR Pharos; Q13137; Tbio.
DR PRO; PR:Q13137; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q13137; protein.
DR Bgee; ENSG00000136436; Expressed in calcaneal tendon and 205 other tissues.
DR ExpressionAtlas; Q13137; baseline and differential.
DR Genevisible; Q13137; HS.
DR GO; GO:0005776; C:autophagosome; IDA:GO_Central.
DR GO; GO:0000421; C:autophagosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
DR GO; GO:0016605; C:PML body; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
DR GO; GO:1901098; P:positive regulation of autophagosome maturation; IMP:GO_Central.
DR GO; GO:0034341; P:response to interferon-gamma; IDA:BHF-UCL.
DR GO; GO:0016032; P:viral process; TAS:ProtInc.
DR GO; GO:0098792; P:xenophagy; IMP:GO_Central.
DR InterPro; IPR041641; CALCOCO1/2_Zn_UBZ1.
DR InterPro; IPR041611; SKICH.
DR Pfam; PF17751; SKICH; 1.
DR PROSITE; PS51905; ZF_UBZ1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Autophagy; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; Cytoskeleton; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..446
FT /note="Calcium-binding and coiled-coil domain-containing
FT protein 2"
FT /id="PRO_0000312337"
FT ZN_FING 419..444
FT /note="UBZ1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT REGION 362..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..381
FT /note="Interaction with LGALS8"
FT /evidence="ECO:0000269|PubMed:23386746,
FT ECO:0000269|PubMed:23511477"
FT REGION 395..446
FT /note="Interaction with MYO6"
FT /evidence="ECO:0000269|PubMed:17635994"
FT COILED 137..349
FT /evidence="ECO:0000255"
FT MOTIF 133..136
FT /note="CLIR"
FT /evidence="ECO:0000305|PubMed:23022382,
FT ECO:0000305|PubMed:25771791"
FT MOTIF 203..206
FT /note="LIR-like"
FT /evidence="ECO:0000305|PubMed:25771791"
FT BINDING 422
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT BINDING 425
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT BINDING 440
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT BINDING 444
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT MOD_RES 445
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..72
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047414"
FT VAR_SEQ 60
FT /note="R -> RCSLNQTIQLLITPDTGSIWHQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046766"
FT VAR_SEQ 60
FT /note="R -> RAFKCFQDKLEQELLKWRSQGQKLQ (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046767"
FT VAR_SEQ 139..180
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044728"
FT VARIANT 140
FT /note="G -> E (in dbSNP:rs550510)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_037489"
FT VARIANT 227
FT /note="G -> R (in dbSNP:rs2303016)"
FT /id="VAR_037490"
FT VARIANT 248
FT /note="V -> A (in dbSNP:rs2303015)"
FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.3"
FT /id="VAR_037491"
FT VARIANT 273
FT /note="T -> A (in dbSNP:rs17849804)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_037492"
FT VARIANT 389
FT /note="P -> A (in dbSNP:rs10278)"
FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.4,
FT ECO:0000269|Ref.6"
FT /id="VAR_037493"
FT MUTAGEN 136
FT /note="V->S: Abrogates the interaction with MAP1LC3C."
FT /evidence="ECO:0000269|PubMed:23022382"
FT MUTAGEN 203..206
FT /note="DYWE->AAAA: Abrogates interaction with MAPLC3A,
FT MAPLC3B and GABARAPL2."
FT /evidence="ECO:0000269|PubMed:25771791"
FT MUTAGEN 374
FT /note="L->A: Severely reduces affinity for LGALS8."
FT /evidence="ECO:0000269|PubMed:23386746,
FT ECO:0000269|PubMed:23511477"
FT MUTAGEN 376
FT /note="Y->A: Severely reduces affinity for LGALS8."
FT /evidence="ECO:0000269|PubMed:23386746"
FT MUTAGEN 378
FT /note="N->A: Prevents interaction with LGALS8."
FT /evidence="ECO:0000269|PubMed:23386746"
FT MUTAGEN 380
FT /note="Y->A,F: Severely reduced affinity for LGALS8."
FT /evidence="ECO:0000269|PubMed:23386746,
FT ECO:0000269|PubMed:23511477"
FT MUTAGEN 400
FT /note="C->A: Does not affect interaction with MYO6."
FT /evidence="ECO:0000269|PubMed:17635994"
FT MUTAGEN 425
FT /note="C->A: Fails interact with MYO6 and to promote
FT maturation of autophagosomes."
FT /evidence="ECO:0000269|PubMed:17635994,
FT ECO:0000269|PubMed:25771791"
FT CONFLICT 102
FT /note="D -> Y (in Ref. 2; BAG64382)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="R -> G (in Ref. 2; BAG56685)"
FT /evidence="ECO:0000305"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:7EAA"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:5Z7L"
FT STRAND 22..27
FT /evidence="ECO:0007829|PDB:3VVV"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:3VVV"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:7EAA"
FT STRAND 38..44
FT /evidence="ECO:0007829|PDB:3VVV"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:7EAA"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:3VVV"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:3VVV"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:3VVV"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:5Z7L"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:3VVV"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:3VVV"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:3VVV"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:3VVV"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:3VVV"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:3VVW"
FT TURN 401..403
FT /evidence="ECO:0007829|PDB:5AAQ"
FT STRAND 404..406
FT /evidence="ECO:0007829|PDB:5AAQ"
FT HELIX 410..413
FT /evidence="ECO:0007829|PDB:5AAQ"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:4XKL"
FT TURN 423..425
FT /evidence="ECO:0007829|PDB:4XKL"
FT STRAND 428..430
FT /evidence="ECO:0007829|PDB:4XKL"
FT HELIX 431..433
FT /evidence="ECO:0007829|PDB:2MXP"
FT HELIX 434..443
FT /evidence="ECO:0007829|PDB:4XKL"
SQ SEQUENCE 446 AA; 52254 MW; 609B121DA1A9DCB8 CRC64;
MEETIKDPPT SAVLLDHCHF SQVIFNSVEK FYIPGGDVTC HYTFTQHFIP RRKDWIGIFR
VGWKTTREYY TFMWVTLPID LNNKSAKQQE VQFKAYYLPK DDEYYQFCYV DEDGVVRGAS
IPFQFRPENE EDILVVTTQG EVEEIEQHNK ELCKENQELK DSCISLQKQN SDMQAELQKK
QEELETLQSI NKKLELKVKE QKDYWETELL QLKEQNQKMS SENEKMGIRV DQLQAQLSTQ
EKEMEKLVQG DQDKTEQLEQ LKKENDHLFL SLTEQRKDQK KLEQTVEQMK QNETTAMKKQ
QELMDENFDL SKRLSENEII CNALQRQKER LEGENDLLKR ENSRLLSYMG LDFNSLPYQV
PTSDEGGARQ NPGLAYGNPY SGIQESSSPS PLSIKKCPIC KADDICDHTL EQQQMQPLCF
NCPICDKIFP ATEKQIFEDH VFCHSL
