ID   CID2B_SALSA             Reviewed;         135 AA.
AC   B5X8S2;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=CDGSH iron-sulfur domain-containing protein 2B;
GN   Name=cisd2b;
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thyroid;
RX   PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA   Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA   Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA   Koop B.F.;
RT   "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT   evolutionary pressures on a post-tetraploidization genome.";
RL   BMC Genomics 11:279-279(2010).
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 (By
CC       similarity). {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. {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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BT047441; ACI67242.1; -; mRNA.
DR   RefSeq; NP_001134369.1; NM_001140897.1.
DR   AlphaFoldDB; B5X8S2; -.
DR   SMR; B5X8S2; -.
DR   STRING; 8030.ENSSSAP00000017072; -.
DR   GeneID; 100195868; -.
DR   KEGG; sasa:100195868; -.
DR   CTD; 493856; -.
DR   OMA; VVDMIDI; -.
DR   OrthoDB; 1393750at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa08.
DR   Bgee; ENSSSAG00000008170; Expressed in camera-type eye and 14 other tissues.
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 2B"
FT                   /id="PRO_0000392020"
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;  15479 MW;  53FD35FC4699CDD6 CRC64;
     MVLETISKII KTQLPAYLKK FPLPETIGGF ARLTVLDWLR LLPLLGILAL LGYLTIRPFL
     PKKKKQKDSL INLKIQKENP KVVNEIDIED LKSTNVCYCR CWRSKTFPVC DKSHIKHNEL
     TGDNVGPLIL KKKIL