CISD2_HUMAN
ID CISD2_HUMAN Reviewed; 135 AA.
AC Q8N5K1; Q7Z3D5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=CDGSH iron-sulfur domain-containing protein 2;
DE AltName: Full=Endoplasmic reticulum intermembrane small protein;
DE AltName: Full=MitoNEET-related 1 protein;
DE Short=Miner1;
DE AltName: Full=Nutrient-deprivation autophagy factor-1;
DE Short=NAF-1;
GN Name=CISD2; Synonyms=CDGSH2, ERIS, ZCD2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INVOLVEMENT IN WFS2.
RX PubMed=17846994; DOI=10.1086/520961;
RA Amr S., Heisey C., Zhang M., Xia X.J., Shows K.H., Ajlouni K., Pandya A.,
RA Satin L.S., El-Shanti H., Shiang R.;
RT "A homozygous mutation in a novel zinc-finger protein, ERIS, is responsible
RT for Wolfram syndrome 2.";
RL Am. J. Hum. Genet. 81:673-683(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Synovium;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Retina;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 21-32; 82-95 AND 117-131, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (JUN-2005) to UniProtKB.
RN [7]
RP COFACTOR, AND SUBCELLULAR LOCATION.
RX PubMed=17376863; DOI=10.1073/pnas.0701078104;
RA Wiley S.E., Murphy A.N., Ross S.A., van der Geer P., Dixon J.E.;
RT "MitoNEET is an iron-containing outer mitochondrial membrane protein that
RT regulates oxidative capacity.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5318-5323(2007).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BCL2; BCL2L1 AND ITPR1,
RP AND MUTAGENESIS OF CYS-99; CYS-101; CYS-110 AND HIS-114.
RX PubMed=20010695; DOI=10.1038/emboj.2009.369;
RA Chang N.C., Nguyen M., Germain M., Shore G.C.;
RT "Antagonism of Beclin 1-dependent autophagy by BCL-2 at the endoplasmic
RT reticulum requires NAF-1.";
RL EMBO J. 29:606-618(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 57-135 OF MUTANT CYS-92 IN COMPLEX
RP WITH 2FE-2S, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF CYS-92.
RX PubMed=19580816; DOI=10.1016/j.jmb.2009.06.079;
RA Conlan A.R., Axelrod H.L., Cohen A.E., Abresch E.C., Zuris J., Yee D.,
RA Nechushtai R., Jennings P.A., Paddock M.L.;
RT "Crystal structure of Miner1: The redox-active 2Fe-2S protein causative in
RT Wolfram Syndrome 2.";
RL J. Mol. Biol. 392:143-153(2009).
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.
CC {ECO:0000269|PubMed:17846994, ECO:0000269|PubMed:20010695}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000269|PubMed:17376863};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000269|PubMed:17376863};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Redox potential:
CC E is 0 +/- 10 mV for 2Fe-2S at pH 7.5. {ECO:0000269|PubMed:19580816};
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. {ECO:0000269|PubMed:19580816,
CC ECO:0000269|PubMed:20010695}.
CC -!- INTERACTION:
CC Q8N5K1; P26436: ACRV1; NbExp=3; IntAct=EBI-1045797, EBI-25884472;
CC Q8N5K1; Q9NVV5-2: AIG1; NbExp=3; IntAct=EBI-1045797, EBI-11957045;
CC Q8N5K1; Q9BQE5: APOL2; NbExp=3; IntAct=EBI-1045797, EBI-4290634;
CC Q8N5K1; Q96PS8: AQP10; NbExp=3; IntAct=EBI-1045797, EBI-12820279;
CC Q8N5K1; Q8WXF7: ATL1; NbExp=3; IntAct=EBI-1045797, EBI-2410266;
CC Q8N5K1; P10415: BCL2; NbExp=2; IntAct=EBI-1045797, EBI-77694;
CC Q8N5K1; Q92843: BCL2L2; NbExp=3; IntAct=EBI-1045797, EBI-707714;
CC Q8N5K1; O15155: BET1; NbExp=3; IntAct=EBI-1045797, EBI-749204;
CC Q8N5K1; O95393: BMP10; NbExp=3; IntAct=EBI-1045797, EBI-3922513;
CC Q8N5K1; Q8WVV5: BTN2A2; NbExp=3; IntAct=EBI-1045797, EBI-8648738;
CC Q8N5K1; Q8TAB5: C1orf216; NbExp=3; IntAct=EBI-1045797, EBI-747505;
CC Q8N5K1; O14523: C2CD2L; NbExp=3; IntAct=EBI-1045797, EBI-12822627;
CC Q8N5K1; Q8WVX3-2: C4orf3; NbExp=3; IntAct=EBI-1045797, EBI-12003442;
CC Q8N5K1; O14735: CDIPT; NbExp=3; IntAct=EBI-1045797, EBI-358858;
CC Q8N5K1; Q9BXR6: CFHR5; NbExp=3; IntAct=EBI-1045797, EBI-11579371;
CC Q8N5K1; P78369: CLDN10; NbExp=3; IntAct=EBI-1045797, EBI-13372810;
CC Q8N5K1; Q9NWW5: CLN6; NbExp=3; IntAct=EBI-1045797, EBI-6165897;
CC Q8N5K1; Q9BQA9: CYBC1; NbExp=3; IntAct=EBI-1045797, EBI-2680384;
CC Q8N5K1; Q08426: EHHADH; NbExp=3; IntAct=EBI-1045797, EBI-2339219;
CC Q8N5K1; P50402: EMD; NbExp=3; IntAct=EBI-1045797, EBI-489887;
CC Q8N5K1; Q96D05-2: FAM241B; NbExp=3; IntAct=EBI-1045797, EBI-12118888;
CC Q8N5K1; Q8N3T1: GALNT15; NbExp=3; IntAct=EBI-1045797, EBI-3925203;
CC Q8N5K1; P01350: GAST; NbExp=3; IntAct=EBI-1045797, EBI-3436637;
CC Q8N5K1; O60883: GPR37L1; NbExp=3; IntAct=EBI-1045797, EBI-2927498;
CC Q8N5K1; Q9HCP6: HHATL; NbExp=3; IntAct=EBI-1045797, EBI-5916693;
CC Q8N5K1; P46695: IER3; NbExp=3; IntAct=EBI-1045797, EBI-1748945;
CC Q8N5K1; P43628: KIR2DL3; NbExp=3; IntAct=EBI-1045797, EBI-8632435;
CC Q8N5K1; O95214: LEPROTL1; NbExp=3; IntAct=EBI-1045797, EBI-750776;
CC Q8N5K1; Q7Z4F1: LRP10; NbExp=3; IntAct=EBI-1045797, EBI-2830349;
CC Q8N5K1; Q9Y2E5: MAN2B2; NbExp=3; IntAct=EBI-1045797, EBI-12243024;
CC Q8N5K1; P30301: MIP; NbExp=3; IntAct=EBI-1045797, EBI-8449636;
CC Q8N5K1; Q9H115: NAPB; NbExp=3; IntAct=EBI-1045797, EBI-3921185;
CC Q8N5K1; Q8N912: NRAC; NbExp=3; IntAct=EBI-1045797, EBI-12051377;
CC Q8N5K1; Q8WWG1: NRG4; NbExp=3; IntAct=EBI-1045797, EBI-8637292;
CC Q8N5K1; P42857: NSG1; NbExp=3; IntAct=EBI-1045797, EBI-6380741;
CC Q8N5K1; Q9UHJ9-5: PGAP2; NbExp=3; IntAct=EBI-1045797, EBI-12092917;
CC Q8N5K1; Q5VZY2: PLPP4; NbExp=3; IntAct=EBI-1045797, EBI-10485931;
CC Q8N5K1; Q96GM1: PLPPR2; NbExp=3; IntAct=EBI-1045797, EBI-12955265;
CC Q8N5K1; Q96T60: PNKP; NbExp=3; IntAct=EBI-1045797, EBI-1045072;
CC Q8N5K1; Q8WZA1: POMGNT1; NbExp=3; IntAct=EBI-1045797, EBI-3912424;
CC Q8N5K1; Q5QGT7: RTP2; NbExp=3; IntAct=EBI-1045797, EBI-10244780;
CC Q8N5K1; Q96GQ5: RUSF1; NbExp=3; IntAct=EBI-1045797, EBI-8636004;
CC Q8N5K1; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-1045797, EBI-8652744;
CC Q8N5K1; Q8N6R1: SERP2; NbExp=3; IntAct=EBI-1045797, EBI-749270;
CC Q8N5K1; Q8WWT9: SLC13A3; NbExp=3; IntAct=EBI-1045797, EBI-12938720;
CC Q8N5K1; Q969S0: SLC35B4; NbExp=3; IntAct=EBI-1045797, EBI-10281213;
CC Q8N5K1; B2RUZ4: SMIM1; NbExp=3; IntAct=EBI-1045797, EBI-12188413;
CC Q8N5K1; Q6UX34: SNORC; NbExp=3; IntAct=EBI-1045797, EBI-11957067;
CC Q8N5K1; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-1045797, EBI-11959123;
CC Q8N5K1; Q9UNE7: STUB1; NbExp=3; IntAct=EBI-1045797, EBI-357085;
CC Q8N5K1; Q86Y82: STX12; NbExp=3; IntAct=EBI-1045797, EBI-2691717;
CC Q8N5K1; O15400: STX7; NbExp=3; IntAct=EBI-1045797, EBI-3221827;
CC Q8N5K1; C9JKN6: THSD7B; NbExp=3; IntAct=EBI-1045797, EBI-17192156;
CC Q8N5K1; Q14656: TMEM187; NbExp=3; IntAct=EBI-1045797, EBI-13046724;
CC Q8N5K1; Q9BU79: TMEM243; NbExp=3; IntAct=EBI-1045797, EBI-12887458;
CC Q8N5K1; Q9BTV4: TMEM43; NbExp=3; IntAct=EBI-1045797, EBI-721293;
CC Q8N5K1; Q8N2M4: TMEM86A; NbExp=3; IntAct=EBI-1045797, EBI-12015604;
CC Q8N5K1; Q86UF1: TSPAN33; NbExp=3; IntAct=EBI-1045797, EBI-12045841;
CC Q8N5K1; P49638: TTPA; NbExp=5; IntAct=EBI-1045797, EBI-10210710;
CC Q8N5K1; O75379: VAMP4; NbExp=3; IntAct=EBI-1045797, EBI-744953;
CC Q8N5K1; Q8N0U8: VKORC1L1; NbExp=3; IntAct=EBI-1045797, EBI-11337915;
CC Q8N5K1; Q96EC8: YIPF6; NbExp=3; IntAct=EBI-1045797, EBI-751210;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC membrane protein. Mitochondrion outer membrane; Single-pass membrane
CC protein. Note=According to PubMed:20010695, it mainly localizes to the
CC endoplasmic reticulum. However, experiments in mouse showed that it
CC mainly localizes to the mitochondrion outer membrane.
CC -!- TISSUE SPECIFICITY: Testis, small intestine, kidney, lung, brain,
CC heart, pancreas and platelets. {ECO:0000269|PubMed:17846994}.
CC -!- DISEASE: Wolfram syndrome 2 (WFS2) [MIM:604928]: A rare disorder
CC characterized by juvenile-onset insulin-dependent diabetes mellitus
CC with optic atrophy. Other manifestations include diabetes insipidus,
CC sensorineural deafness, dementia, psychiatric illnesses. WFS2 patients
CC additionally show a strong bleeding tendency and gastrointestinal
CC ulceration. Diabetes insipidus may be absent.
CC {ECO:0000269|PubMed:17846994}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the CISD protein family. CISD2 subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Although initially thought (PubMed:17846994) to be a zinc-
CC finger protein, it was later shown (PubMed:17376863) that it binds 1
CC 2Fe-2S cluster instead. {ECO:0000305|PubMed:17376863,
CC ECO:0000305|PubMed:17846994}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD97935.1; Type=Erroneous initiation; Evidence={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; AK292134; BAF84823.1; -; mRNA.
DR EMBL; BX537971; CAD97935.1; ALT_INIT; mRNA.
DR EMBL; CH471057; EAX06148.1; -; Genomic_DNA.
DR EMBL; BC032300; AAH32300.1; -; mRNA.
DR CCDS; CCDS34040.1; -.
DR RefSeq; NP_001008389.1; NM_001008388.4.
DR PDB; 3FNV; X-ray; 2.10 A; A/B=57-135.
DR PDB; 4OO7; X-ray; 1.65 A; A/B=68-135.
DR PDB; 4OOA; X-ray; 1.58 A; A/B/C/D/E/F=68-135.
DR PDBsum; 3FNV; -.
DR PDBsum; 4OO7; -.
DR PDBsum; 4OOA; -.
DR AlphaFoldDB; Q8N5K1; -.
DR SMR; Q8N5K1; -.
DR BioGRID; 138922; 213.
DR CORUM; Q8N5K1; -.
DR IntAct; Q8N5K1; 99.
DR MINT; Q8N5K1; -.
DR STRING; 9606.ENSP00000273986; -.
DR BindingDB; Q8N5K1; -.
DR ChEMBL; CHEMBL4523399; -.
DR iPTMnet; Q8N5K1; -.
DR PhosphoSitePlus; Q8N5K1; -.
DR SwissPalm; Q8N5K1; -.
DR BioMuta; CISD2; -.
DR DMDM; 74729013; -.
DR EPD; Q8N5K1; -.
DR jPOST; Q8N5K1; -.
DR MassIVE; Q8N5K1; -.
DR MaxQB; Q8N5K1; -.
DR PaxDb; Q8N5K1; -.
DR PeptideAtlas; Q8N5K1; -.
DR PRIDE; Q8N5K1; -.
DR ProteomicsDB; 72071; -.
DR TopDownProteomics; Q8N5K1; -.
DR ABCD; Q8N5K1; 4 sequenced antibodies.
DR Antibodypedia; 2500; 175 antibodies from 30 providers.
DR DNASU; 493856; -.
DR Ensembl; ENST00000273986.10; ENSP00000273986.4; ENSG00000145354.12.
DR GeneID; 493856; -.
DR KEGG; hsa:493856; -.
DR MANE-Select; ENST00000273986.10; ENSP00000273986.4; NM_001008388.5; NP_001008389.1.
DR UCSC; uc003hwt.5; human.
DR CTD; 493856; -.
DR DisGeNET; 493856; -.
DR GeneCards; CISD2; -.
DR HGNC; HGNC:24212; CISD2.
DR HPA; ENSG00000145354; Tissue enhanced (liver).
DR MalaCards; CISD2; -.
DR MIM; 604928; phenotype.
DR MIM; 611507; gene.
DR neXtProt; NX_Q8N5K1; -.
DR OpenTargets; ENSG00000145354; -.
DR Orphanet; 3463; Wolfram syndrome.
DR PharmGKB; PA162382300; -.
DR VEuPathDB; HostDB:ENSG00000145354; -.
DR eggNOG; KOG3461; Eukaryota.
DR GeneTree; ENSGT00940000156660; -.
DR HOGENOM; CLU_132293_1_0_1; -.
DR InParanoid; Q8N5K1; -.
DR OMA; PKCDGSH; -.
DR OrthoDB; 1393750at2759; -.
DR PhylomeDB; Q8N5K1; -.
DR TreeFam; TF324661; -.
DR PathwayCommons; Q8N5K1; -.
DR SignaLink; Q8N5K1; -.
DR BioGRID-ORCS; 493856; 10 hits in 1083 CRISPR screens.
DR EvolutionaryTrace; Q8N5K1; -.
DR GenomeRNAi; 493856; -.
DR Pharos; Q8N5K1; Tbio.
DR PRO; PR:Q8N5K1; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q8N5K1; protein.
DR Bgee; ENSG00000145354; Expressed in epithelial cell of pancreas and 180 other tissues.
DR ExpressionAtlas; Q8N5K1; baseline and differential.
DR Genevisible; Q8N5K1; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:LIFEdb.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0010506; P:regulation of autophagy; IMP: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 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Autophagy; Deafness; Diabetes mellitus;
KW Direct protein sequencing; Endoplasmic reticulum; Iron; Iron-sulfur;
KW Membrane; Metal-binding; Mitochondrion; Mitochondrion outer membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:25944712"
FT CHAIN 2..135
FT /note="CDGSH iron-sulfur domain-containing protein 2"
FT /id="PRO_0000316005"
FT TOPO_DOM 2..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 BINDING 101
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 110
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 114
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT MUTAGEN 92
FT /note="C->S: Has the same optical signature of the native
FT protein and improves yields of purified protein and a
FT decreased tendency to aggregate."
FT /evidence="ECO:0000269|PubMed:19580816"
FT MUTAGEN 99
FT /note="C->S: Impairs interaction with BCL2; when associated
FT with S-101; S-110 and Q-114."
FT /evidence="ECO:0000269|PubMed:20010695"
FT MUTAGEN 101
FT /note="C->S: Impairs interaction with BCL2; when associated
FT with S-99; S-110 and Q-114."
FT /evidence="ECO:0000269|PubMed:20010695"
FT MUTAGEN 110
FT /note="C->S: Impairs interaction with BCL2; when associated
FT with S-99; S-101 and Q-114."
FT /evidence="ECO:0000269|PubMed:20010695"
FT MUTAGEN 114
FT /note="H->Q: Impairs interaction with BCL2; when associated
FT with S-99; S-101 and S-110."
FT /evidence="ECO:0000269|PubMed:20010695"
FT TURN 75..78
FT /evidence="ECO:0007829|PDB:4OOA"
FT STRAND 79..87
FT /evidence="ECO:0007829|PDB:4OOA"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:4OOA"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:4OOA"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:4OOA"
FT TURN 105..108
FT /evidence="ECO:0007829|PDB:4OOA"
FT HELIX 113..121
FT /evidence="ECO:0007829|PDB:4OOA"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:4OOA"
SQ SEQUENCE 135 AA; 15278 MW; 44AD1817D6C536D6 CRC64;
MVLESVARIV KVQLPAYLKR LPVPESITGF ARLTVSEWLR LLPFLGVLAL LGYLAVRPFL
PKKKQQKDSL INLKIQKENP KVVNEINIED LCLTKAAYCR CWRSKTFPAC DGSHNKHNEL
TGDNVGPLIL KKKEV
