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CIA2A_BOVIN
ID   CIA2A_BOVIN             Reviewed;         160 AA.
AC   Q3T0U7;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Cytosolic iron-sulfur assembly component 2A {ECO:0000305};
DE   AltName: Full=MIP18 family protein FAM96A;
GN   Name=CIAO2A {ECO:0000250|UniProtKB:Q9H5X1}; Synonyms=FAM96A;
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].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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. As a CIA
CC       complex component and in collaboration with CIAO1 specifically matures
CC       ACO1 and stabilizes IREB2, connecting cytosolic iron-sulfur protein
CC       maturation with cellular iron regulation. May play a role in chromosome
CC       segregation through establishment of sister chromatid cohesion. May
CC       induce apoptosis in collaboration with APAF1. {ECO:0000250,
CC       ECO:0000250|UniProtKB:Q9H5X1}.
CC   -!- SUBUNIT: Monomer and homodimer. Component of the CIA complex. Interacts
CC       with CIAO1. Interacts with IREB2. Interacts with APAF1.
CC       {ECO:0000250|UniProtKB:Q9H5X1}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H5X1}.
CC   -!- SIMILARITY: Belongs to the MIP18 family. {ECO:0000305}.
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DR   EMBL; BC102256; AAI02257.1; -; mRNA.
DR   RefSeq; NP_001030282.1; NM_001035110.1.
DR   AlphaFoldDB; Q3T0U7; -.
DR   BMRB; Q3T0U7; -.
DR   SMR; Q3T0U7; -.
DR   STRING; 9913.ENSBTAP00000002607; -.
DR   PaxDb; Q3T0U7; -.
DR   PRIDE; Q3T0U7; -.
DR   GeneID; 512871; -.
DR   KEGG; bta:512871; -.
DR   CTD; 84191; -.
DR   eggNOG; KOG3381; Eukaryota.
DR   InParanoid; Q3T0U7; -.
DR   OrthoDB; 1408004at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0097361; C:CIA complex; ISS:UniProtKB.
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   2: Evidence at transcript 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_0000245580"
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;  18390 MW;  5651D62B6C85DE17 CRC64;
     MERVSGLLSW TLSRFLWLSG LSEPGAARQP RIMEEKALEV YDLIRTIRDP EKPNTLEELE
     VVTESCVEVQ EINEDDYLVI IRFTPTVPHC SLATLIGLCL RVKLQRCLPF KHKLEIYISE
     GTHSTEEDIN KQINDKERVA AAMENPNLRE IVEQCVLEPD
 
 
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