CPIN1_MOUSE
ID CPIN1_MOUSE Reviewed; 309 AA.
AC Q8WTY4; Q3UJW5; Q8VC24; Q91W83;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Anamorsin {ECO:0000255|HAMAP-Rule:MF_03115};
DE AltName: Full=Cytokine-induced apoptosis inhibitor 1 {ECO:0000255|HAMAP-Rule:MF_03115};
DE AltName: Full=Fe-S cluster assembly protein DRE2 homolog {ECO:0000255|HAMAP-Rule:MF_03115};
GN Name=Ciapin1 {ECO:0000255|HAMAP-Rule:MF_03115};
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=14970183; DOI=10.1084/jem.20031858;
RA Shibayama H., Takai E., Matsumura I., Kouno M., Morii E., Kitamura Y.,
RA Takeda J., Kanakura Y.;
RT "Identification of a cytokine-induced antiapoptotic molecule anamorsin
RT essential for definitive hematopoiesis.";
RL J. Exp. Med. 199:581-592(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, DBA/2J, and NOD;
RC TISSUE=Cerebellum, Diencephalon, Spinal cord, and Thymus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver, and Salivary gland;
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 [4]
RP SUBCELLULAR LOCATION.
RX PubMed=16957168; DOI=10.1369/jhc.6a6960.2006;
RA Hao Z., Li X., Qiao T., Du R., Zhang G., Fan D.;
RT "Subcellular localization of CIAPIN1.";
RL J. Histochem. Cytochem. 54:1437-1444(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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).
CC -!- FUNCTION: Component of the cytosolic iron-sulfur (Fe-S) protein
CC assembly (CIA) machinery required for the maturation of
CC extramitochondrial Fe-S proteins. Part of an electron transfer chain
CC functioning in an early step of cytosolic Fe-S biogenesis, facilitating
CC the de novo assembly of a [4Fe-4S] cluster on the scaffold complex
CC NUBP1-NUBP2. Electrons are transferred to CIAPIN1 from NADPH via the
CC FAD- and FMN-containing protein NDOR1. NDOR1-CIAPIN1 are also required
CC for the assembly of the diferric tyrosyl radical cofactor of
CC ribonucleotide reductase (RNR), probably by providing electrons for
CC reduction during radical cofactor maturation in the catalytic small
CC subunit (By similarity). Has anti-apoptotic effects in the cell.
CC Involved in negative control of cell death upon cytokine withdrawal.
CC Promotes development of hematopoietic cells (PubMed:14970183).
CC {ECO:0000255|HAMAP-Rule:MF_03115, ECO:0000269|PubMed:14970183}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03115};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03115};
CC -!- SUBUNIT: Monomer. Interacts with NDOR1. Interacts with CHCHD4.
CC {ECO:0000255|HAMAP-Rule:MF_03115}.
CC -!- INTERACTION:
CC Q8WTY4; Q9CQM9: Glrx3; NbExp=4; IntAct=EBI-2943068, EBI-4319195;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03115}.
CC Nucleus {ECO:0000255|HAMAP-Rule:MF_03115}. Mitochondrion intermembrane
CC space {ECO:0000255|HAMAP-Rule:MF_03115}.
CC -!- DEVELOPMENTAL STAGE: Expressed from early embryogenesis.
CC -!- INDUCTION: By cytokines such as IL3 and THPO.
CC {ECO:0000269|PubMed:14970183}.
CC -!- DOMAIN: The twin Cx2C motifs are involved in the recognition by the
CC mitochondrial CHCHD4/MIA40-GFER/ERV1 disulfide relay system. The
CC formation of 2 disulfide bonds in the Cx2C motifs through
CC dithiol/disulfide exchange reactions effectively traps the protein in
CC the mitochondrial intermembrane space. {ECO:0000255|HAMAP-
CC Rule:MF_03115}.
CC -!- DOMAIN: The C-terminal domain binds 2 Fe-S clusters but is otherwise
CC mostly in an intrinsically disordered conformation. {ECO:0000255|HAMAP-
CC Rule:MF_03115}.
CC -!- DOMAIN: The N-terminal domain has structural similarity with S-
CC adenosyl-L-methionine-dependent methyltransferases, but does not bind
CC S-adenosyl-L-methionine. It is required for correct assembly of the 2
CC Fe-S clusters. {ECO:0000255|HAMAP-Rule:MF_03115}.
CC -!- DISRUPTION PHENOTYPE: Death in late gestation due to defective
CC definitive hematopoiesis in the fetal liver, possibly due to initiated
CC apoptosis in erythroid cells during terminal maturation.
CC {ECO:0000269|PubMed:14970183}.
CC -!- MISCELLANEOUS: 'Ana-mors-in' means 'anti-death molecule' in Latin.
CC -!- SIMILARITY: Belongs to the anamorsin family. {ECO:0000255|HAMAP-
CC Rule:MF_03115}.
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DR EMBL; AY523555; AAS09959.1; -; mRNA.
DR EMBL; AK076116; BAC36196.1; -; mRNA.
DR EMBL; AK079615; BAC37702.1; -; mRNA.
DR EMBL; AK088757; BAC40550.1; -; mRNA.
DR EMBL; AK136821; BAE23137.1; -; mRNA.
DR EMBL; AK146282; BAE27040.1; -; mRNA.
DR EMBL; AK163705; BAE37466.1; -; mRNA.
DR EMBL; AK168252; BAE40202.1; -; mRNA.
DR EMBL; BC016261; AAH16261.1; -; mRNA.
DR EMBL; BC021864; AAH21864.1; -; mRNA.
DR EMBL; BC021949; AAH21949.1; -; mRNA.
DR CCDS; CCDS22549.1; -.
DR RefSeq; NP_598902.1; NM_134141.4.
DR RefSeq; XP_006530623.1; XM_006530560.1.
DR AlphaFoldDB; Q8WTY4; -.
DR SMR; Q8WTY4; -.
DR BioGRID; 224515; 5.
DR IntAct; Q8WTY4; 3.
DR MINT; Q8WTY4; -.
DR STRING; 10090.ENSMUSP00000125451; -.
DR iPTMnet; Q8WTY4; -.
DR PhosphoSitePlus; Q8WTY4; -.
DR EPD; Q8WTY4; -.
DR jPOST; Q8WTY4; -.
DR MaxQB; Q8WTY4; -.
DR PaxDb; Q8WTY4; -.
DR PeptideAtlas; Q8WTY4; -.
DR PRIDE; Q8WTY4; -.
DR ProteomicsDB; 284157; -.
DR Antibodypedia; 28857; 418 antibodies from 32 providers.
DR DNASU; 109006; -.
DR Ensembl; ENSMUST00000034233; ENSMUSP00000034233; ENSMUSG00000031781.
DR Ensembl; ENSMUST00000162538; ENSMUSP00000125451; ENSMUSG00000031781.
DR GeneID; 109006; -.
DR KEGG; mmu:109006; -.
DR UCSC; uc009mxa.2; mouse.
DR CTD; 57019; -.
DR MGI; MGI:1922083; Ciapin1.
DR VEuPathDB; HostDB:ENSMUSG00000031781; -.
DR eggNOG; KOG4020; Eukaryota.
DR GeneTree; ENSGT00390000011417; -.
DR HOGENOM; CLU_064393_2_0_1; -.
DR InParanoid; Q8WTY4; -.
DR OMA; QRVAIIW; -.
DR OrthoDB; 1588798at2759; -.
DR PhylomeDB; Q8WTY4; -.
DR TreeFam; TF314449; -.
DR BioGRID-ORCS; 109006; 10 hits in 75 CRISPR screens.
DR ChiTaRS; Ciapin1; mouse.
DR PRO; PR:Q8WTY4; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8WTY4; protein.
DR Bgee; ENSMUSG00000031781; Expressed in otic placode and 259 other tissues.
DR ExpressionAtlas; Q8WTY4; baseline and differential.
DR Genevisible; Q8WTY4; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; ISS:UniProtKB.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0030097; P:hemopoiesis; IMP:MGI.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_03115; Anamorsin; 1.
DR InterPro; IPR007785; Anamorsin.
DR InterPro; IPR046408; CIAPIN1.
DR InterPro; IPR013216; Methyltransf_11.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR13273; PTHR13273; 1.
DR Pfam; PF05093; CIAPIN1; 2.
DR Pfam; PF08241; Methyltransf_11; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 4Fe-4S; Apoptosis; Cytoplasm; Iron; Iron-sulfur; Metal-binding;
KW Mitochondrion; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..309
FT /note="Anamorsin"
FT /id="PRO_0000079289"
FT REGION 6..172
FT /note="N-terminal SAM-like domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT REGION 173..222
FT /note="Linker"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT REGION 235..249
FT /note="Fe-S binding site A"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT REGION 271..285
FT /note="Fe-S binding site B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT MOTIF 271..274
FT /note="Cx2C motif 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT MOTIF 282..285
FT /note="Cx2C motif 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 235
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 244
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 247
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 249
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 271
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 274
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 282
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 285
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6FI81"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6FI81"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6FI81"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6FI81"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6FI81"
SQ SEQUENCE 309 AA; 33429 MW; 2F1FCB614767C915 CRC64;
MEEFGISPGQ LVAVFWDKSS PEEALKKLVA RLQELTGSEG QVFMENVTQL LQSSHKESSF
DVILSGVVPG STSLHSAEVL AEMARILRPG GCLFLKEPVE TAEVNNDKMK TASKLCSALT
LSGLVEIKEL QREALSPEEV QSVQEHLGYH SDSLRSVRVT GKKPNFEVGS SSQLKLPNKK
SSSVKPVVDP AAAKLWTLSA NDMEDDSVDL IDSDELLDPE DLKRPDPASL KAPSCGEGKK
RKACKNCTCG LAEELEREQS KAQSSQPKSA CGNCYLGDAF RCANCPYLGM PAFKPGEQVL
LSNSNLQDA
