CIA2A_MOUSE
ID CIA2A_MOUSE Reviewed; 160 AA.
AC Q9DCL2; Q3TD02; Q9D171;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Cytosolic iron-sulfur assembly component 2A {ECO:0000305};
DE AltName: Full=MIP18 family protein FAM96A;
GN Name=Ciao2a; Synonyms=Fam96a {ECO:0000312|MGI:MGI:1915500};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, and Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP FUNCTION, IDENTIFICATION IN THE CIA COMPLEX, AND INTERACTION WITH CIAO1 AND
RP IREB2.
RX PubMed=23891004; DOI=10.1016/j.cmet.2013.06.015;
RA Stehling O., Mascarenhas J., Vashisht A.A., Sheftel A.D., Niggemeyer B.,
RA Roesser R., Pierik A.J., Wohlschlegel J.A., Lill R.;
RT "Human CIA2A-FAM96A and CIA2B-FAM96B integrate iron homeostasis and
RT maturation of different subsets of cytosolic-nuclear iron-sulfur
RT proteins.";
RL Cell Metab. 18:187-198(2013).
RN [5]
RP ERRATUM OF PUBMED:23891004.
RX PubMed=29320706; DOI=10.1016/j.cmet.2017.12.009;
RA Stehling O., Mascarenhas J., Vashisht A.A., Sheftel A.D., Niggemeyer B.,
RA Roesser R., Pierik A.J., Wohlschlegel J.A., Lill R.;
RT "Human CIA2A-FAM96A and CIA2B-FAM96B Integrate Iron Homeostasis and
RT Maturation of Different Subsets of Cytosolic-Nuclear Iron-Sulfur
RT Proteins.";
RL Cell Metab. 27:263-263(2018).
RN [6]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=25716227; DOI=10.1002/ijc.29498;
RA Schwamb B., Pick R., Fernandez S.B., Voelp K., Heering J., Doetsch V.,
RA Boesser S., Jung J., Beinoraviciute-Kellner R., Wesely J., Zoernig I.,
RA Hammerschmidt M., Nowak M., Penzel R., Zatloukal K., Joos S., Rieker R.J.,
RA Agaimy A., Soeder S., Reid-Lombardo K.M., Kendrick M.L., Bardsley M.R.,
RA Hayashi Y., Asuzu D.T., Syed S.A., Ordog T., Zoernig M.;
RT "FAM96A is a novel pro-apoptotic tumor suppressor in gastrointestinal
RT stromal tumors.";
RL Int. J. Cancer 137:1318-1329(2015).
CC -!- FUNCTION: Component of the cytosolic iron-sulfur protein assembly (CIA)
CC complex, a multiprotein complex that mediates the incorporation of
CC iron-sulfur cluster into extramitochondrial Fe/S proteins
CC (PubMed:23891004). As a CIA complex component and in collaboration with
CC CIAO1 specifically matures ACO1 and stabilizes IREB2 (PubMed:23891004).
CC May play a role in chromosome segregation through establishment of
CC sister chromatid cohesion. May induce apoptosis in collaboration with
CC APAF1 (PubMed:25716227). {ECO:0000250, ECO:0000269|PubMed:23891004,
CC ECO:0000269|PubMed:25716227}.
CC -!- SUBUNIT: Monomer and homodimer (By similarity). Component of the CIA
CC complex (PubMed:23891004). Interacts with CIAO1 (PubMed:23891004).
CC Interacts with IREB2 (PubMed:23891004). Interacts with APAF1 (By
CC similarity). {ECO:0000250|UniProtKB:Q9H5X1,
CC ECO:0000269|PubMed:23891004}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in interstitial cell lineages.
CC {ECO:0000269|PubMed:25716227}.
CC -!- SIMILARITY: Belongs to the MIP18 family. {ECO:0000305}.
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DR EMBL; AK002690; BAB22285.1; -; mRNA.
DR EMBL; AK003870; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK077700; BAC36966.1; -; mRNA.
DR EMBL; AK170445; BAE41803.1; -; mRNA.
DR EMBL; BC005745; AAH05745.1; -; mRNA.
DR CCDS; CCDS23302.1; -.
DR RefSeq; NP_080911.1; NM_026635.3.
DR AlphaFoldDB; Q9DCL2; -.
DR BMRB; Q9DCL2; -.
DR SMR; Q9DCL2; -.
DR BioGRID; 212761; 1.
DR IntAct; Q9DCL2; 1.
DR MINT; Q9DCL2; -.
DR STRING; 10090.ENSMUSP00000034945; -.
DR PhosphoSitePlus; Q9DCL2; -.
DR EPD; Q9DCL2; -.
DR MaxQB; Q9DCL2; -.
DR PaxDb; Q9DCL2; -.
DR PeptideAtlas; Q9DCL2; -.
DR PRIDE; Q9DCL2; -.
DR ProteomicsDB; 277032; -.
DR Antibodypedia; 25761; 114 antibodies from 18 providers.
DR DNASU; 68250; -.
DR Ensembl; ENSMUST00000034945; ENSMUSP00000034945; ENSMUSG00000032381.
DR GeneID; 68250; -.
DR KEGG; mmu:68250; -.
DR UCSC; uc009qel.1; mouse.
DR CTD; 84191; -.
DR MGI; MGI:1915500; Ciao2a.
DR VEuPathDB; HostDB:ENSMUSG00000032381; -.
DR eggNOG; KOG3381; Eukaryota.
DR GeneTree; ENSGT00390000017697; -.
DR HOGENOM; CLU_075876_4_0_1; -.
DR InParanoid; Q9DCL2; -.
DR OMA; YISEGAH; -.
DR OrthoDB; 1408004at2759; -.
DR PhylomeDB; Q9DCL2; -.
DR TreeFam; TF323934; -.
DR BioGRID-ORCS; 68250; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Ciao2a; mouse.
DR PRO; PR:Q9DCL2; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9DCL2; protein.
DR Bgee; ENSMUSG00000032381; Expressed in pharyngeal arch 2 and 259 other tissues.
DR Genevisible; Q9DCL2; MM.
DR GO; GO:0097361; C:CIA complex; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; ISS:UniProtKB.
DR GO; GO:0106035; P:protein maturation by [4Fe-4S] cluster transfer; IEA:InterPro.
DR GO; GO:0097428; P:protein maturation by iron-sulfur cluster transfer; ISS:UniProtKB.
DR Gene3D; 3.30.300.130; -; 1.
DR InterPro; IPR034904; FSCA_dom_sf.
DR InterPro; IPR039796; MIP18.
DR InterPro; IPR002744; MIP18-like.
DR PANTHER; PTHR12377; PTHR12377; 1.
DR Pfam; PF01883; FeS_assembly_P; 1.
DR SUPFAM; SSF117916; SSF117916; 1.
PE 1: Evidence at protein level;
KW Chromosome partition; Cytoplasm; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..160
FT /note="Cytosolic iron-sulfur assembly component 2A"
FT /id="PRO_0000212690"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
SQ SEQUENCE 160 AA; 18418 MW; 8DB6322DE7CC7A20 CRC64;
MERVSGLLSW TLSRVLWLSG FSEHGAAWQP RIMEEKALEV YDLIRTIRDP EKPNTLEELE
VVTESCVEVQ EINEDDYLVI IKFTPTVPHC SLATLIGLCL RVKLQRCLPF KHKLEIYISE
GTHSTEEDIN KQINDKERVA AAMENPNLRE IVEQCVLEPD
