CACO2_XENTR
ID CACO2_XENTR Reviewed; 470 AA.
AC Q6DF48;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Calcium-binding and coiled-coil domain-containing protein 2 {ECO:0000250|UniProtKB:Q13137};
GN Name=calcoco2 {ECO:0000250|UniProtKB:Q13137}; ORFNames=TEgg035o03.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Egg;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) 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 galectin-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). May play a role in
CC ruffle formation and actin cytoskeleton organization and seems to
CC negatively regulate constitutive secretion (By similarity).
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 CLIR and LIR-like motifs are required for interaction with
CC AT8 family proteins. {ECO:0000250|UniProtKB:Q13137}.
CC -!- SIMILARITY: Belongs to the CALCOCO family. {ECO:0000305}.
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DR EMBL; CR926335; CAJ81818.1; -; mRNA.
DR EMBL; BC076895; AAH76895.1; -; mRNA.
DR RefSeq; NP_001006828.1; NM_001006827.1.
DR AlphaFoldDB; Q6DF48; -.
DR SMR; Q6DF48; -.
DR STRING; 8364.ENSXETP00000049360; -.
DR PaxDb; Q6DF48; -.
DR DNASU; 448562; -.
DR Ensembl; ENSXETT00000049360; ENSXETP00000049360; ENSXETG00000022806.
DR GeneID; 448562; -.
DR KEGG; xtr:448562; -.
DR CTD; 10241; -.
DR Xenbase; XB-GENE-1006016; calcoco2.
DR eggNOG; ENOG502QT1M; Eukaryota.
DR HOGENOM; CLU_021315_0_0_1; -.
DR InParanoid; Q6DF48; -.
DR OMA; WIGIFRA; -.
DR OrthoDB; 179838at2759; -.
DR PhylomeDB; Q6DF48; -.
DR TreeFam; TF329501; -.
DR Proteomes; UP000008143; Chromosome 10.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000022806; Expressed in heart and 15 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 InterPro; IPR013087; Znf_C2H2_type.
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..470
FT /note="Calcium-binding and coiled-coil domain-containing
FT protein 2"
FT /id="PRO_0000312341"
FT ZN_FING 441..464
FT /note="UBZ1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT COILED 132..368
FT /evidence="ECO:0000255"
FT MOTIF 131..134
FT /note="CLIR"
FT /evidence="ECO:0000250|UniProtKB:Q13137"
FT MOTIF 201..204
FT /note="LIR-like"
FT /evidence="ECO:0000250|UniProtKB:Q13137"
FT BINDING 444
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT BINDING 447
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT BINDING 460
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT BINDING 464
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
SQ SEQUENCE 470 AA; 54948 MW; C36340386FBACE1A CRC64;
MASDAPPTSM LQPEERNYSQ VVFSRVEQSY VPGIDIICYF TYTSGFHPAK KDWVGIFKVS
WKTTREYYTW VSADCEEQGL EKRVTFKAYY LPKESDDYYQ FCYVDQKGEV RGVSIPFQLC
RKIQDEGEED ILLVTTEEEA QGMKEKQRVL EEKVAALEKD KCTLQDECTQ LALEQKNKAA
LIESLQAQQL ECAKKNEELD QQNQELERQL EEEKCKNGSL HLKVVSAEEE RERVQNDIRS
LQLEQNQLKE ENMELHKHTN DMEFSLKKYS EEAKNQEEEV QELKDKLWDA EAKHHLLQVQ
LQDIQMEKKK DKYSIELLTK EAEKVADLRQ NLEKKDKTME TMEKQLAQLQ RENATVLRQM
EDLSYTLELR KAEISDMQQQ RVRDGAEIEH LNRLLTEQSS STPRNQGLFF QNPYESESLI
SFANEPQPGE APGGSSVRHV QMQCPECGSE FENFQVFQDH IFCHDLESTE
