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Database: UniProt
Entry: H2Q9W5_PANTR
LinkDB: H2Q9W5_PANTR
Original site: H2Q9W5_PANTR 
ID   H2Q9W5_PANTR            Unreviewed;       963 AA.
AC   H2Q9W5; A0A2J8KCK3;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   24-JAN-2024, entry version 70.
DE   RecName: Full=Iron-responsive element-binding protein 2 {ECO:0000256|ARBA:ARBA00015385};
GN   Name=IREB2 {ECO:0000313|EMBL:JAA10203.1,
GN   ECO:0000313|Ensembl:ENSPTRP00000012550.3, ECO:0000313|VGNC:VGNC:1935};
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000012550.3, ECO:0000313|Proteomes:UP000002277};
RN   [1] {ECO:0000313|Ensembl:ENSPTRP00000012550.3, ECO:0000313|Proteomes:UP000002277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16136131; DOI=10.1038/nature04072;
RG   Chimpanzee sequencing and analysis consortium;
RT   "Initial sequence of the chimpanzee genome and comparison with the human
RT   genome.";
RL   Nature 437:69-87(2005).
RN   [2] {ECO:0000313|EMBL:JAA10203.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Adipose stromal {ECO:0000313|EMBL:JAA10203.1}, Skeletal muscle
RC   {ECO:0000313|EMBL:JAA33564.1}, Skin {ECO:0000313|EMBL:JAA25900.1}, and
RC   Smooth vascular {ECO:0000313|EMBL:JAA21313.1};
RA   Maudhoo M.D., Meehan D.T., Norgren R.B.Jr.;
RT   "De novo assembly of the reference chimpanzee transcriptome from NextGen
RT   mRNA sequences.";
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSPTRP00000012550.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- FUNCTION: RNA-binding protein that binds to iron-responsive elements
CC       (IRES), which are stem-loop structures found in the 5'-UTR of ferritin,
CC       and delta aminolevulinic acid synthase mRNAs, and in the 3'-UTR of
CC       transferrin receptor mRNA. Binding to the IRE element in ferritin
CC       results in the repression of its mRNA translation. Binding of the
CC       protein to the transferrin receptor mRNA inhibits the degradation of
CC       this otherwise rapidly degraded mRNA. {ECO:0000256|ARBA:ARBA00003938}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|RuleBase:RU361275}.
CC   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC       {ECO:0000256|ARBA:ARBA00007185, ECO:0000256|RuleBase:RU361275}.
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DR   EMBL; AACZ04065419; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; GABC01001135; JAA10203.1; -; mRNA.
DR   EMBL; GABF01000832; JAA21313.1; -; mRNA.
DR   EMBL; GABD01007200; JAA25900.1; -; mRNA.
DR   EMBL; GABE01011175; JAA33564.1; -; mRNA.
DR   RefSeq; XP_523125.2; XM_523125.5.
DR   STRING; 9598.ENSPTRP00000012550; -.
DR   PaxDb; 9598-ENSPTRP00000012550; -.
DR   Ensembl; ENSPTRT00000013538.4; ENSPTRP00000012550.3; ENSPTRG00000007342.4.
DR   GeneID; 467731; -.
DR   CTD; 3658; -.
DR   VGNC; VGNC:1935; IREB2.
DR   eggNOG; KOG0452; Eukaryota.
DR   GeneTree; ENSGT00940000157796; -.
DR   HOGENOM; CLU_013476_2_1_1; -.
DR   OMA; HVEVPFC; -.
DR   OrthoDB; 176941at2759; -.
DR   TreeFam; TF313476; -.
DR   Proteomes; UP000002277; Chromosome 15.
DR   Bgee; ENSPTRG00000007342; Expressed in hindlimb stylopod muscle and 20 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
DR   GO; GO:0003994; F:aconitate hydratase activity; IBA:GO_Central.
DR   GO; GO:0030350; F:iron-responsive element binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006101; P:citrate metabolic process; IBA:GO_Central.
DR   GO; GO:0034101; P:erythrocyte homeostasis; IEA:Ensembl.
DR   GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR   GO; GO:0050892; P:intestinal absorption; IEA:Ensembl.
DR   GO; GO:0006879; P:intracellular iron ion homeostasis; IEA:Ensembl.
DR   GO; GO:0060586; P:multicellular organismal-level iron ion homeostasis; IEA:Ensembl.
DR   GO; GO:0030316; P:osteoclast differentiation; IEA:Ensembl.
DR   GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR   GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:Ensembl.
DR   GO; GO:0006417; P:regulation of translation; IEA:Ensembl.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR   CDD; cd01586; AcnA_IRP; 1.
DR   CDD; cd01580; AcnA_IRP_Swivel; 1.
DR   Gene3D; 6.10.190.10; -; 1.
DR   Gene3D; 3.30.499.10; Aconitase, domain 3; 3.
DR   Gene3D; 3.20.19.10; Aconitase, domain 4; 1.
DR   InterPro; IPR044137; AcnA_IRP_Swivel.
DR   InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
DR   InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR   InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR   InterPro; IPR006249; Aconitase/IRP2.
DR   InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR   InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR   InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR   NCBIfam; TIGR01341; aconitase_1; 1.
DR   PANTHER; PTHR11670; ACONITASE/IRON-RESPONSIVE ELEMENT FAMILY MEMBER; 1.
DR   PANTHER; PTHR11670:SF31; IRON-RESPONSIVE ELEMENT-BINDING PROTEIN 2; 1.
DR   Pfam; PF00330; Aconitase; 2.
DR   Pfam; PF00694; Aconitase_C; 1.
DR   PRINTS; PR00415; ACONITASE.
DR   SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1.
DR   SUPFAM; SSF52016; LeuD/IlvD-like; 1.
DR   PROSITE; PS00450; ACONITASE_1; 1.
DR   PROSITE; PS01244; ACONITASE_2; 1.
PE   2: Evidence at transcript level;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|RuleBase:RU361275};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU361275};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU361275};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU361275};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   DOMAIN          70..131
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          212..639
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          768..894
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
SQ   SEQUENCE   963 AA;  105011 MW;  8250BE889E31BCAC CRC64;
     MDAPTAGYAF EYLIETLNDS SRKKFFDVSK LGTKYDVLPY SIRVLLEAAV RNCDGFLMTK
     EDVMNILDWK TKQSNVEVPF FPARVLLQDF TGIPAMVDFA AMREAVKTLG GDPEKVHPAC
     PTDLTVDHSL QIDFSKCAIQ NAPNPGGGDL QKAGKLSPLK VQPKKLPCRG QTTCRGSCDS
     GELGRNSGTF SSQIENTPIL CPFHLQPVPE PETVLKNQEV EFGRNRERLQ FFKWSSRVFK
     NVAVIPPGTG MAHQINLEYL SRVVFEEKDL LFPDSVVGTD SHITMVNGLG ILGWGVGGIE
     TEAVMLGLPV SLTLPEVVGC ELTGSSNPFV TSIDVVLGIT KHLRQVGVAG KFVEFFGSGV
     SQLSIVDRTT IANMCPEYGA ILSFFPVDNV TLKHLEHTGF SKAKLESMET YLKAVKLFRN
     DQNSSGEPEY SQVIQINLNS IVPSVSGPKR PQDRVAVTDM KSDFQACLNE KVGFKGFQIA
     AEKQKDIVSI HYEGSEYKLS HGSVVIAAVI SCTNNCNPSV MLAAGLLAKK AVEAGLRVKP
     YIRTSLSPGS GMVTHYLSSS GVLPYLSKLG FEIVGYGCST CVGNTAPLSD AVLNAVKQGD
     LVTCGILSGN KNFEGRLCDC VRANYLASPP LVVAYAIAGT VNIDFQTEPL GTDPTGKNIY
     LHDIWPSREE VHRVEEEHVI LSMFKALKDK IEMGNKRWNS LEAPDSVLFP WDLKSTYIRC
     PSFFDKLTKE PIALQAIENA HVLLYLGDSV TTDHISPAGS IARNSAAAKY LTNRGLTPRE
     FNSYGARRGN DAVMTRGTFA NIKLFNKFIG KPAPKTIHFP SGQTLDVFEA AELYQKEGIP
     LIILAGKKYG SGNSRDWAAK GPYLLGVKAV LAESYEKIHK DHLIGIGIAP LQFLPGENAD
     SLGLSGRETF SLTFPEELSP GITLNIQTST GKVFSVIASF EDDVEITLYK HGGLLNFVAR
     KFS
//
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