CACO2_MACFA
ID CACO2_MACFA Reviewed; 398 AA.
AC Q4R914;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Calcium-binding and coiled-coil domain-containing protein 2 {ECO:0000250|UniProtKB:Q13137};
DE AltName: Full=Antigen nuclear dot 52 kDa protein {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};
DE AltName: Full=Nuclear dot protein 52 {ECO:0000250|UniProtKB:Q13137};
GN Name=CALCOCO2 {ECO:0000250|UniProtKB:Q13137};
GN Synonyms=NDP52 {ECO:0000250|UniProtKB:Q13137}; ORFNames=QtsA-10956;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:0000250|UniProtKB:Q13137}.
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}.
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DR EMBL; AB168283; BAE00407.1; -; mRNA.
DR AlphaFoldDB; Q4R914; -.
DR SMR; Q4R914; -.
DR PRIDE; Q4R914; -.
DR Ensembl; ENSMFAT00000087204; ENSMFAP00000050859; ENSMFAG00000000840.
DR GeneTree; ENSGT00950000183025; -.
DR Proteomes; UP000233100; Chromosome 16.
DR Bgee; ENSMFAG00000000840; Expressed in heart and 13 other tissues.
DR GO; GO:0005776; C:autophagosome; ISS:GO_Central.
DR GO; GO:0000421; C:autophagosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1901098; P:positive regulation of autophagosome maturation; ISS:GO_Central.
DR GO; GO:0098792; P:xenophagy; ISS: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 2: Evidence at transcript level;
KW Autophagy; Coiled coil; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW Membrane; Metal-binding; Phosphoprotein; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..398
FT /note="Calcium-binding and coiled-coil domain-containing
FT protein 2"
FT /id="PRO_0000312338"
FT ZN_FING 371..396
FT /note="UBZ1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT REGION 314..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..333
FT /note="Interaction with LGALS8"
FT /evidence="ECO:0000250|UniProtKB:Q13137"
FT REGION 347..398
FT /note="Interaction with MYO6"
FT /evidence="ECO:0000250|UniProtKB:Q13137"
FT COILED 137..301
FT /evidence="ECO:0000255"
FT MOTIF 133..136
FT /note="CLIR"
FT /evidence="ECO:0000250|UniProtKB:Q13137"
FT MOTIF 203..206
FT /note="LIR-like"
FT /evidence="ECO:0000250|UniProtKB:Q13137"
FT BINDING 374
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT BINDING 377
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT BINDING 392
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT BINDING 396
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT MOD_RES 397
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13137"
SQ SEQUENCE 398 AA; 46589 MW; 80113BD1C11E0583 CRC64;
MEKTIEDPPT SAVLLDHCHF SQVIFNSVEK FYIPGGDVTC RYTFTQNFIP RQKDWIGIFR
VGWKTVREYY TFMWVTLPID LNNKSAKQQE VQFKAYYLPK DDEYYQFCYV DQDGVVRGAS
IPFQFRPENE EDILVVTTQG EVEEIEQHNK ELCKENQELK DSCVSLQKQN SDMQAELQKK
QEELETLQSI NKKLELKVKE QKDYWETEQL EHLKKENGHL FLSLTEQRKD QKKLEQTVEE
MKQNETTAMK KQQELMDENF DLSRRLSEKK MIYNALQREK ERLEGENDLL KRENSRLLSY
MGLDFNSLPY QVPTSDEGGA GQNPGLVYGN PYSGIQESSS PSQLSIKKCP ICKADDICDH
TLEQQQMQAL CLNCPICDKI FPATEKQIFE DHVFCHSL
