CPIN1_BOVIN
ID CPIN1_BOVIN Reviewed; 310 AA.
AC Q5EAC7; Q0VCL8;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal pons;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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}.
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; BT020642; AAX08659.1; -; mRNA.
DR EMBL; BC120105; AAI20106.1; -; mRNA.
DR RefSeq; NP_001015659.1; NM_001015659.1.
DR AlphaFoldDB; Q5EAC7; -.
DR SMR; Q5EAC7; -.
DR STRING; 9913.ENSBTAP00000002418; -.
DR PaxDb; Q5EAC7; -.
DR PRIDE; Q5EAC7; -.
DR Ensembl; ENSBTAT00000002418; ENSBTAP00000002418; ENSBTAG00000001854.
DR GeneID; 535119; -.
DR KEGG; bta:535119; -.
DR CTD; 57019; -.
DR VEuPathDB; HostDB:ENSBTAG00000001854; -.
DR VGNC; VGNC:27357; CIAPIN1.
DR eggNOG; KOG4020; Eukaryota.
DR GeneTree; ENSGT00390000011417; -.
DR HOGENOM; CLU_064393_2_0_1; -.
DR InParanoid; Q5EAC7; -.
DR OMA; QRVAIIW; -.
DR OrthoDB; 1588798at2759; -.
DR TreeFam; TF314449; -.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000001854; Expressed in spermatocyte and 105 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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; IBA:GO_Central.
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; Phosphoprotein; Reference proteome.
FT CHAIN 1..310
FT /note="Anamorsin"
FT /id="PRO_0000325004"
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 272..286
FT /note="Fe-S binding site B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT MOTIF 272..275
FT /note="Cx2C motif 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT MOTIF 283..286
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 272
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
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 283
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 MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6FI81"
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 270
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WTY4"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6FI81"
FT MOD_RES 305
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6FI81"
FT CONFLICT 103
FT /note="V -> VA (in Ref. 2; AAI20106)"
FT /evidence="ECO:0000305"
FT CONFLICT 308..310
FT /note="HDA -> TSHHMVPPISSDLGPWQGG (in Ref. 2; AAI20106)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 310 AA; 33205 MW; C2EBE532E92152B2 CRC64;
MADFGISAGQ FVAVIWDKSS PVEALKDLVD KLQALTGDEG RVSVENINQL LQSAHKESSF
DIVLSGIIPG STTLHSADIL AEMARILRPG GCLFLKEPVE TAVVNNSKVK TASKLCSALT
LSGLVEVKEL QRESLSPEEI QSVREHLGYH SDSLLSLQIT GKKPNFEVGS SSQLKLSIAK
KSSGKPAVDP AAAKLWTLSA NDMEDESVDL IDSDELLDAE DLKKPDPASL RAPSCGEGKK
RKACKNCTCG LAEELEKEKS RDQISSQPKS ACGNCYLGDA FRCASCPYLG MPAFKPGEKV
LLSDSNLHDA
