CACO2_BOVIN
ID CACO2_BOVIN Reviewed; 450 AA.
AC O18737;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 100.
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};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ishiguro N.;
RT "Bovine NDP52.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) 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; AB008852; BAA23587.1; -; mRNA.
DR EMBL; BC146237; AAI46238.1; -; mRNA.
DR RefSeq; NP_776825.1; NM_174400.2.
DR AlphaFoldDB; O18737; -.
DR SMR; O18737; -.
DR STRING; 9913.ENSBTAP00000010432; -.
DR PaxDb; O18737; -.
DR GeneID; 281942; -.
DR KEGG; bta:281942; -.
DR CTD; 10241; -.
DR eggNOG; ENOG502QT1M; Eukaryota.
DR HOGENOM; CLU_021315_0_0_1; -.
DR InParanoid; O18737; -.
DR OrthoDB; 179838at2759; -.
DR TreeFam; TF329501; -.
DR Proteomes; UP000009136; Unplaced.
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:0016605; C:PML body; IBA:GO_Central.
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; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..450
FT /note="Calcium-binding and coiled-coil domain-containing
FT protein 2"
FT /id="PRO_0000312336"
FT ZN_FING 423..448
FT /note="UBZ1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT REGION 371..381
FT /note="Interaction with LGALS8"
FT /evidence="ECO:0000250|UniProtKB:Q13137"
FT REGION 395..450
FT /note="Interaction with MYO6"
FT /evidence="ECO:0000250|UniProtKB:Q13137"
FT COILED 135..349
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 426
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT BINDING 429
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 BINDING 448
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
SQ SEQUENCE 450 AA; 52551 MW; 60A96E3E58A64B26 CRC64;
MEETVDDPPT SAVLLDHCHF SQVIFNSVEK FYIPGGDITC YYTLTQHFIP RRKDWIGIFR
VGWKTTREYY TFMWVTLPVD LNSESAKQQE VQFKAYYLPK DDEYYQFCYV DQDGVVRGAS
IPFQFRPENE EDILVVTTQS EVEEIEQHNK ELCKENRELK DSCVSLQKQN SDMQATLQKK
QEELETLKSI NKKLEQTMKE QKDCWEIELL QLKEQNQKMS SENEKMGVRV DQLQAQLSNQ
GREMEKLVQG VQDKTEQLEH LKEENGQLFL SLTEQREHQK KLEQTVEEMK QKETTAAKKQ
QELTDQNMDL SKRLSENMII HDVLQREKEK MEKENDYLKR ENNRLLSYMG LDCDSLSYQV
PTSNQGGTRQ DPGLVFGNPY SGIQESSAPS LLSIKKCPTC KSDFAADVFD HNLALEQHLQ
TLSLNCPICD KTFPAKEKQI FEDHVFCHTL
