ID   CISD2_BOVIN             Reviewed;         135 AA.
AC   Q05B71;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=CDGSH iron-sulfur domain-containing protein 2;
GN   Name=CISD2; Synonyms=CDGSH2;
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 [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hippocampus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Regulator of autophagy that contributes to antagonize BECN1-
CC       mediated cellular autophagy at the endoplasmic reticulum. Participates
CC       in the interaction of BCL2 with BECN1 and is required for BCL2-mediated
CC       depression of endoplasmic reticulum Ca(2+) stores during autophagy.
CC       Contributes to BIK-initiated autophagy, while it is not involved in
CC       BIK-dependent activation of caspases. Involved in life span control,
CC       probably via its function as regulator of autophagy (By similarity).
CC       {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250};
CC       Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. Interacts with BCL2; the interaction is direct and
CC       disrupted by BIK interaction with BCL2. Interacts with BCL2L1.
CC       Interacts with ITPR1 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Single-pass membrane protein {ECO:0000250}. Mitochondrion outer
CC       membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CISD protein family. CISD2 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BC122676; AAI22677.1; -; mRNA.
DR   RefSeq; NP_001073807.1; NM_001080338.1.
DR   AlphaFoldDB; Q05B71; -.
DR   SMR; Q05B71; -.
DR   STRING; 9913.ENSBTAP00000039580; -.
DR   PaxDb; Q05B71; -.
DR   PRIDE; Q05B71; -.
DR   GeneID; 781260; -.
DR   KEGG; bta:781260; -.
DR   CTD; 493856; -.
DR   eggNOG; KOG3461; Eukaryota.
DR   HOGENOM; CLU_132293_1_0_1; -.
DR   InParanoid; Q05B71; -.
DR   OrthoDB; 1393750at2759; -.
DR   TreeFam; TF324661; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0000422; P:autophagy of mitochondrion; ISS:UniProtKB.
DR   GO; GO:0010506; P:regulation of autophagy; ISS:UniProtKB.
DR   Gene3D; 3.40.5.90; -; 1.
DR   InterPro; IPR045131; CISD1/2.
DR   InterPro; IPR018967; FeS-contain_CDGSH-typ.
DR   InterPro; IPR019610; FeS-contain_mitoNEET_N.
DR   InterPro; IPR042216; MitoNEET_CISD.
DR   PANTHER; PTHR13680; PTHR13680; 1.
DR   Pfam; PF10660; MitoNEET_N; 1.
DR   Pfam; PF09360; zf-CDGSH; 1.
DR   SMART; SM00704; ZnF_CDGSH; 1.
PE   2: Evidence at transcript level;
KW   2Fe-2S; Autophagy; Endoplasmic reticulum; Iron; Iron-sulfur; Membrane;
KW   Metal-binding; Mitochondrion; Mitochondrion outer membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..135
FT                   /note="CDGSH iron-sulfur domain-containing protein 2"
FT                   /id="PRO_0000316004"
FT   TOPO_DOM        1..37
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        38..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        61..135
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   BINDING         99
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250"
FT   BINDING         101
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250"
FT   BINDING         110
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250"
FT   BINDING         114
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   135 AA;  15278 MW;  44AD1817D6C536D6 CRC64;
     MVLESVARIV KVQLPAYLKR LPVPESITGF ARLTVSEWLR LLPFLGVLAL LGYLAVRPFL
     PKKKQQKDSL INLKIQKENP KVVNEINIED LCLTKAAYCR CWRSKTFPAC DGSHNKHNEL
     TGDNVGPLIL KKKEV