CACO2_MOUSE
ID CACO2_MOUSE Reviewed; 331 AA.
AC A2A6M5; Q3TK36; Q3TKZ6; Q3TL30; Q9CWE3;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Calcium-binding and coiled-coil domain-containing protein 2 {ECO:0000250|UniProtKB:Q13137};
DE AltName: Full=Nuclear domain 10 protein NDP52 {ECO:0000250|UniProtKB:Q13137};
DE Short=Nuclear domain 10 protein 52 {ECO:0000250|UniProtKB:Q13137};
GN Name=Calcoco2 {ECO:0000250|UniProtKB:Q13137}; Synonyms=Ndp52, Ndp52l1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND DEVELOPMENTAL STAGE.
RX PubMed=12620990; DOI=10.1242/dev.00366;
RA Bortvin A., Eggan K., Skaletsky H., Akutsu H., Berry D.L., Yanagimachi R.,
RA Page D.C., Jaenisch R.;
RT "Incomplete reactivation of Oct4-related genes in mouse embryos cloned from
RT somatic nuclei.";
RL Development 130:1673-1680(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4 AND 5).
RC STRAIN=C57BL/6J; TISSUE=Blastocyst;
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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
CC -!- FUNCTION: Xenophagy-specific receptor required for autophagy-mediated
CC intracellular bacteria degradation (By similarity). Acts as an effector
CC protein of galectin-sensed membrane damage that restricts the
CC proliferation of infecting pathogens upon entry into the cytosol by
CC targeting LGALS8-associated bacteria for autophagy (By similarity).
CC Initially orchestrates bacteria targeting to autophagosomes and
CC subsequently ensures pathogen degradation by regulating pathogen-
CC containing autophagosome maturation (By similarity). Bacteria targeting
CC to autophagosomes relies on its interaction with MAP1LC3A, MAP1LC3B
CC and/or GABARAPL2, whereas regulation of pathogen-containing
CC autophagosome maturation requires the interaction with MAP3LC3C (By
CC similarity). May play a role in ruffle formation and actin cytoskeleton
CC organization and seems to negatively regulate constitutive secretion
CC (By similarity). {ECO:0000250|UniProtKB:Q13137}.
CC -!- SUBUNIT: Dimer. Part of a complex consisting of CALCOCO2, TAX1BP1 and
CC MYO6. Interacts with GEMIN4. Interacts with ATG8 family members
CC MAP1LC3A, MAP1LC3B, GABARAP, GABARAPL1 and GABARAPL2. Interacts with
CC ATG8 family member MAP1LC3C. Interacts with LGALS8.
CC {ECO:0000250|UniProtKB:Q13137}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q13137}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q13137}. Cytoplasmic vesicle, autophagosome
CC membrane {ECO:0000250|UniProtKB:Q13137}; Peripheral membrane protein
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=A2A6M5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2A6M5-2; Sequence=VSP_029832;
CC Name=3;
CC IsoId=A2A6M5-3; Sequence=VSP_029833;
CC Name=4;
CC IsoId=A2A6M5-4; Sequence=VSP_029830;
CC Name=5;
CC IsoId=A2A6M5-5; Sequence=VSP_029831;
CC -!- DEVELOPMENTAL STAGE: Expression is limited to the pluripotent cells of
CC the early embryo and the germline. Expressed in blastocysts, epiblasts
CC and purified primordial germ cells. {ECO:0000269|PubMed:12620990}.
CC -!- DOMAIN: The LGALS8-binding domain is essential for the recruitment to
CC cytosol-exposed infecting bacteria. {ECO:0000250|UniProtKB:Q13137}.
CC -!- DOMAIN: The CLIR (LC3C-interacting region) motif is required for
CC interaction with MAP1LC3C, but dispensable for CALCOCO2-mediated
CC autophagosome maturation. {ECO:0000250|UniProtKB:Q13137}.
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:0000250|UniProtKB:Q13137}.
CC -!- SIMILARITY: Belongs to the CALCOCO family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE38997.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF490344; AAO84502.1; -; mRNA.
DR EMBL; AK010816; BAB27200.1; -; mRNA.
DR EMBL; AK166710; BAE38963.1; -; mRNA.
DR EMBL; AK166756; BAE38997.1; ALT_FRAME; mRNA.
DR EMBL; AK167172; BAE39309.1; -; mRNA.
DR EMBL; AL603682; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS59567.1; -. [A2A6M5-1]
DR RefSeq; NP_001257947.1; NM_001271018.1. [A2A6M5-1]
DR AlphaFoldDB; A2A6M5; -.
DR SMR; A2A6M5; -.
DR BioGRID; 218333; 5.
DR STRING; 10090.ENSMUSP00000087407; -.
DR PhosphoSitePlus; A2A6M5; -.
DR PaxDb; A2A6M5; -.
DR PRIDE; A2A6M5; -.
DR Antibodypedia; 17875; 452 antibodies from 28 providers.
DR DNASU; 76815; -.
DR Ensembl; ENSMUST00000068686; ENSMUSP00000087407; ENSMUSG00000006056. [A2A6M5-1]
DR GeneID; 76815; -.
DR KEGG; mmu:76815; -.
DR UCSC; uc033fzk.1; mouse. [A2A6M5-1]
DR CTD; 10241; -.
DR MGI; MGI:1343177; Calcoco2.
DR VEuPathDB; HostDB:ENSMUSG00000006056; -.
DR eggNOG; ENOG502QT1M; Eukaryota.
DR GeneTree; ENSGT00950000183025; -.
DR InParanoid; A2A6M5; -.
DR OMA; ASWEEQK; -.
DR OrthoDB; 179838at2759; -.
DR PhylomeDB; A2A6M5; -.
DR TreeFam; TF329501; -.
DR BioGRID-ORCS; 76815; 1 hit in 69 CRISPR screens.
DR ChiTaRS; Calcoco2; mouse.
DR PRO; PR:A2A6M5; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; A2A6M5; protein.
DR Bgee; ENSMUSG00000006056; Expressed in morula and 50 other tissues.
DR ExpressionAtlas; A2A6M5; baseline and differential.
DR Genevisible; A2A6M5; MM.
DR GO; GO:0005776; C:autophagosome; ISS:GO_Central.
DR GO; GO:0000421; C:autophagosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISS:HGNC-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; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0016605; C:PML body; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:1901098; P:positive regulation of autophagosome maturation; ISS:GO_Central.
DR GO; GO:0034341; P:response to interferon-gamma; ISO:MGI.
DR GO; GO:0098792; P:xenophagy; ISS:GO_Central.
DR InterPro; IPR041611; SKICH.
DR Pfam; PF17751; SKICH; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Autophagy; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; Cytoskeleton; Membrane; Reference proteome.
FT CHAIN 1..331
FT /note="Calcium-binding and coiled-coil domain-containing
FT protein 2"
FT /id="PRO_0000312339"
FT REGION 189..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..302
FT /note="Interaction with LGALS8"
FT /evidence="ECO:0000250|UniProtKB:Q13137"
FT COILED 132..309
FT /evidence="ECO:0000255"
FT MOTIF 128..131
FT /note="CLIR"
FT /evidence="ECO:0000250|UniProtKB:Q13137"
FT MOTIF 190..193
FT /note="LIR-like"
FT /evidence="ECO:0000250|UniProtKB:Q13137"
FT VAR_SEQ 201..291
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029830"
FT VAR_SEQ 208..305
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029831"
FT VAR_SEQ 222..291
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12620990,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_029832"
FT VAR_SEQ 223..320
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029833"
SQ SEQUENCE 331 AA; 40136 MW; A47DAF67DCB89A74 CRC64;
MDQCPIPTLL EHGNFSQVLF NNVEKFYAPR GDIMCYYTLT EKFIPRRKDW IGIFKVGWKT
TQEYYTFMWA PLPKDQNKDS ATQQEIQFKA YYLPKDVERY QFCYVDEDGL VRGTSVPFQF
CPDPDEDIMV VINKEKVEEM EQLSEELYQQ NQELKDKYAD LHEQLQRKQV ALEATQRVNK
TLEHKVEEKA SWEKEKASWE EEKASWEEEK ASWEEEKASW EEEKASWEEE KASWEEEKAS
WEEEKASWEE EKASWEEEKA SWEEEKASWE EEKASWEEEK ASWEEEKASW EKEKASWEEE
KASWEKEKAP WEVEKAPWKE VKAYWWNDLH R
