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Database: UniProt
Entry: M3ZUT2_XIPMA
LinkDB: M3ZUT2_XIPMA
Original site: M3ZUT2_XIPMA 
ID   M3ZUT2_XIPMA            Unreviewed;       135 AA.
AC   M3ZUT2;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=CDGSH iron-sulfur domain-containing protein 2 {ECO:0000256|RuleBase:RU369084};
OS   Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Xiphophorus.
OX   NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000005975.1, ECO:0000313|Proteomes:UP000002852};
RN   [1] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA   Walter R., Schartl M., Warren W.;
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX   PubMed=23542700; DOI=10.1038/ng.2604;
RA   Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA   Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA   Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA   Postlethwait J.H., Warren W.C.;
RT   "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT   evolutionary adaptation and several complex traits.";
RL   Nat. Genet. 45:567-572(2013).
RN   [3] {ECO:0000313|Ensembl:ENSXMAP00000005975.1}
RP   IDENTIFICATION.
RC   STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000005975.1};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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       {ECO:0000256|RuleBase:RU369084}.
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|RuleBase:RU369084};
CC       Note=Binds 1 [2Fe-2S] cluster. {ECO:0000256|RuleBase:RU369084};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738,
CC       ECO:0000256|RuleBase:RU369084}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|RuleBase:RU369084}; Single-pass membrane protein
CC       {ECO:0000256|RuleBase:RU369084}. Mitochondrion outer membrane
CC       {ECO:0000256|RuleBase:RU369084}; Single-pass membrane protein
CC       {ECO:0000256|RuleBase:RU369084}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004167}.
CC   -!- SIMILARITY: Belongs to the CISD protein family. CISD2 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008624, ECO:0000256|RuleBase:RU369084}.
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DR   RefSeq; XP_005807220.1; XM_005807163.2.
DR   AlphaFoldDB; M3ZUT2; -.
DR   STRING; 8083.ENSXMAP00000005975; -.
DR   Ensembl; ENSXMAT00000005981.2; ENSXMAP00000005975.1; ENSXMAG00000005961.2.
DR   GeneID; 102235582; -.
DR   KEGG; xma:102235582; -.
DR   CTD; 493856; -.
DR   eggNOG; KOG3461; Eukaryota.
DR   GeneTree; ENSGT00940000156660; -.
DR   HOGENOM; CLU_132293_1_0_1; -.
DR   InParanoid; M3ZUT2; -.
DR   OMA; PKCDGSH; -.
DR   OrthoDB; 1204967at2759; -.
DR   Proteomes; UP000002852; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0010506; P:regulation of autophagy; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.5.90; CDGSH iron-sulfur domain, mitoNEET-type; 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; CDGSH IRON-SULFUR DOMAIN-CONTAINING PROTEIN 1; 1.
DR   PANTHER; PTHR13680:SF5; CDGSH IRON-SULFUR DOMAIN-CONTAINING PROTEIN 2; 1.
DR   Pfam; PF10660; MitoNEET_N; 1.
DR   Pfam; PF09360; zf-CDGSH; 1.
DR   SMART; SM00704; ZnF_CDGSH; 1.
PE   3: Inferred from homology;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714, ECO:0000256|RuleBase:RU369084};
KW   Autophagy {ECO:0000256|ARBA:ARBA00023006};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW   ECO:0000256|RuleBase:RU369084};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU369084};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU369084};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU369084};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU369084};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00022787};
KW   Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002852};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU369084};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU369084}.
FT   TRANSMEM        38..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU369084"
FT   DOMAIN          81..120
FT                   /note="Iron-binding zinc finger CDGSH type"
FT                   /evidence="ECO:0000259|SMART:SM00704"
SQ   SEQUENCE   135 AA;  15471 MW;  F066D9F6FEA8D072 CRC64;
     MVLETISKII KVQLPAYLKK LPLPETIGGF ARLTVSEWLR LLPLLGILAL LGYLTIRPFL
     PKKKKQRDSL INLKIQKENP RVVNEIDIED LNSANVCYCR CWRSKTFPVC DRSHLKHNEL
     TGDNVGPLIL KKKIL
//
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