CPN1A_SALSA
ID CPN1A_SALSA Reviewed; 313 AA.
AC B5XEX1; B5DFX9;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Anamorsin-A {ECO:0000255|HAMAP-Rule:MF_03115};
DE AltName: Full=Cytokine-induced apoptosis inhibitor 1-A {ECO:0000255|HAMAP-Rule:MF_03115};
DE AltName: Full=Fe-S cluster assembly protein DRE2 homolog A {ECO:0000255|HAMAP-Rule:MF_03115};
GN Name=ciapin1-A {ECO:0000255|HAMAP-Rule:MF_03115}; Synonyms=ciapin1-1;
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=White muscle;
RX PubMed=19878547; DOI=10.1186/1471-2164-10-502;
RA Andreassen R., Lunner S., Hoyheim B.;
RT "Characterization of full-length sequenced cDNA inserts (FLIcs) from
RT Atlantic salmon (Salmo salar).";
RL BMC Genomics 10:502-502(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
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: 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. Has anti-apoptotic effects in the cell. Involved in negative
CC control of cell death upon cytokine withdrawal. Promotes development of
CC hematopoietic cells. {ECO:0000255|HAMAP-Rule:MF_03115}.
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 -!- 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 -!- 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 -!- SIMILARITY: Belongs to the anamorsin family. {ECO:0000255|HAMAP-
CC Rule:MF_03115}.
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DR EMBL; BT043538; ACH70653.1; -; mRNA.
DR EMBL; BT049590; ACI69391.1; -; mRNA.
DR RefSeq; XP_014004384.1; XM_014148909.1.
DR RefSeq; XP_014004385.1; XM_014148910.1.
DR RefSeq; XP_014004386.1; XM_014148911.1.
DR RefSeq; XP_014004387.1; XM_014148912.1.
DR RefSeq; XP_014004388.1; XM_014148913.1.
DR AlphaFoldDB; B5XEX1; -.
DR SMR; B5XEX1; -.
DR STRING; 8030.ENSSSAP00000035114; -.
DR GeneID; 106573658; -.
DR KEGG; sasa:106573658; -.
DR CTD; 57019; -.
DR Proteomes; UP000087266; Chromosome ssa16.
DR Bgee; ENSSSAG00000041949; Expressed in liver and 16 other tissues.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0030097; P:hemopoiesis; IEA:UniProtKB-UniRule.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:UniProtKB-UniRule.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_03115; Anamorsin; 1.
DR InterPro; IPR007785; Anamorsin.
DR InterPro; IPR046408; CIAPIN1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR13273; PTHR13273; 1.
DR Pfam; PF05093; CIAPIN1; 2.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 2: Evidence at transcript level;
KW 2Fe-2S; 4Fe-4S; Apoptosis; Cytoplasm; Iron; Iron-sulfur; Metal-binding;
KW Mitochondrion; Nucleus; Reference proteome.
FT CHAIN 1..313
FT /note="Anamorsin-A"
FT /id="PRO_0000392304"
FT REGION 6..170
FT /note="N-terminal SAM-like domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT REGION 171..223
FT /note="Linker"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT REGION 236..252
FT /note="Fe-S binding site A"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT REGION 275..289
FT /note="Fe-S binding site B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT MOTIF 275..278
FT /note="Cx2C motif 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT MOTIF 286..289
FT /note="Cx2C motif 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 236
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 250
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 252
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 275
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 278
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 286
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 289
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT CONFLICT 184
FT /note="Missing (in Ref. 2; ACH70653)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 313 AA; 33142 MW; 98A6232A6D5AD94B CRC64;
MADLGVKAGD KVLLVWSQPS SPTTLKKLAE SLGAMVGTDG RVSLENMERL IMSSHAASSY
DWVLSSLLSD SFSVHTSETL AEMARVIKPD GKLVLEEPVT GTDDQKVRTA EKLISALKLS
GLVSVTEVSK EPLTPEAVSA LKTFTGFQGN TLSRVRMSAS KPNFEVGSSS QLKFSFGKKT
SKPVDKPALD PNAAKAWTLS ANDMDDDDVD LVDSDALLDA DDFKKPDAAS LKAPSCGDGT
TKKKKACKNC SCGLAEELEQ ESKGAKTISQ PKSACGSCYL GDAFRCASCP YIGMPAFKPG
EKIVLANTGL NDT
