Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Ferritin, middle subunit (Ferritin M) (EC 1.16.3.1) (Ferritin H') (Ferritin X)

 FRI2_LITCT              Reviewed;         176 AA.
P07798;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
05-DEC-2018, entry version 108.
RecName: Full=Ferritin, middle subunit;
Short=Ferritin M;
EC=1.16.3.1;
AltName: Full=Ferritin H';
AltName: Full=Ferritin X;
Lithobates catesbeiana (American bullfrog) (Rana catesbeiana).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Amphibia; Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Rana;
Aquarana.
NCBI_TaxID=8400;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3495534;
Dickey L.F., Sreedharan S., Theil E.C., Didsbury J.R., Wang Y.-H.,
Kaufman R.E.;
"Differences in the regulation of messenger RNA for housekeeping and
specialized-cell ferritin. A comparison of three distinct ferritin
complementary DNAs, the corresponding subunits, and identification of
the first processed in amphibia.";
J. Biol. Chem. 262:7901-7907(1987).
[2]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
PubMed=10439069; DOI=10.1007/s007750050310;
Ha Y., Shi D., Small G.W., Theil E.C., Allewell N.M.;
"Crystal structure of bullfrog M ferritin at 2.8 A resolution:
analysis of subunit interactions and the binuclear metal center.";
J. Biol. Inorg. Chem. 4:243-256(1999).
-!- FUNCTION: Stores iron in a soluble, non-toxic, readily available
form. Important for iron homeostasis. Has ferroxidase activity.
Iron is taken up in the ferrous form and deposited as ferric
hydroxides after oxidation.
-!- CATALYTIC ACTIVITY:
Reaction=4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O;
Xref=Rhea:RHEA:11148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034;
EC=1.16.3.1;
-!- SUBUNIT: Oligomer of 24 subunits. The functional molecule is
roughly spherical and contains a central cavity into which the
polymeric mineral iron core is deposited.
-!- MISCELLANEOUS: There are three types of ferritin subunits in
amphibia: L, M and H chains. M and H chains are fast mineralizing;
the L chain is very slow mineralizing.
-!- SIMILARITY: Belongs to the ferritin family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; J02724; AAA49525.1; -; mRNA.
PIR; C27805; C27805.
PDB; 1MFR; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-176.
PDB; 3KA3; X-ray; 1.40 A; A=1-176.
PDB; 3KA4; X-ray; 1.40 A; A=1-176.
PDB; 3KA6; X-ray; 1.40 A; A=1-176.
PDB; 3KA8; X-ray; 1.35 A; A=1-176.
PDB; 3KA9; X-ray; 1.45 A; A=1-176.
PDB; 3RBC; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-176.
PDB; 3RE7; X-ray; 2.82 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-176.
PDB; 3RGD; X-ray; 2.89 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-176.
PDB; 3SE1; X-ray; 1.65 A; A=1-176.
PDB; 3SH6; X-ray; 1.40 A; A=1-176.
PDB; 3SHX; X-ray; 1.35 A; A=1-176.
PDB; 4DAS; X-ray; 2.56 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-176.
PDB; 4LPJ; X-ray; 1.27 A; A=1-176.
PDB; 4LPM; X-ray; 1.65 A; A=2-175.
PDB; 4LPN; X-ray; 1.66 A; A=1-176.
PDB; 4LQH; X-ray; 1.16 A; A=1-176.
PDB; 4LQJ; X-ray; 1.20 A; A=1-176.
PDB; 4LQN; X-ray; 1.59 A; A=1-176.
PDB; 4LQV; X-ray; 1.54 A; A=1-176.
PDB; 4LYU; X-ray; 1.75 A; A=1-176.
PDB; 4LYX; X-ray; 1.23 A; A=1-176.
PDB; 4MJY; X-ray; 1.40 A; A=1-176.
PDB; 4MKU; X-ray; 1.30 A; A=1-176.
PDB; 4ML5; X-ray; 1.22 A; A=1-176.
PDB; 4MN9; X-ray; 1.15 A; A=1-176.
PDB; 4MY7; X-ray; 1.48 A; A=1-176.
PDB; 4P18; X-ray; 1.91 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-176.
PDB; 5J8S; X-ray; 1.50 A; A=1-176.
PDB; 5J8W; X-ray; 1.11 A; A=1-176.
PDB; 5J93; X-ray; 1.10 A; A=1-176.
PDB; 5J9V; X-ray; 1.16 A; A=1-176.
PDB; 5JAC; X-ray; 1.18 A; A=1-176.
PDB; 5XHI; X-ray; 1.26 A; A=2-175.
PDB; 5XHM; X-ray; 1.70 A; A=2-175.
PDB; 5XHN; X-ray; 1.63 A; A=2-175.
PDB; 5XHO; X-ray; 1.73 A; A=2-175.
PDBsum; 1MFR; -.
PDBsum; 3KA3; -.
PDBsum; 3KA4; -.
PDBsum; 3KA6; -.
PDBsum; 3KA8; -.
PDBsum; 3KA9; -.
PDBsum; 3RBC; -.
PDBsum; 3RE7; -.
PDBsum; 3RGD; -.
PDBsum; 3SE1; -.
PDBsum; 3SH6; -.
PDBsum; 3SHX; -.
PDBsum; 4DAS; -.
PDBsum; 4LPJ; -.
PDBsum; 4LPM; -.
PDBsum; 4LPN; -.
PDBsum; 4LQH; -.
PDBsum; 4LQJ; -.
PDBsum; 4LQN; -.
PDBsum; 4LQV; -.
PDBsum; 4LYU; -.
PDBsum; 4LYX; -.
PDBsum; 4MJY; -.
PDBsum; 4MKU; -.
PDBsum; 4ML5; -.
PDBsum; 4MN9; -.
PDBsum; 4MY7; -.
PDBsum; 4P18; -.
PDBsum; 5J8S; -.
PDBsum; 5J8W; -.
PDBsum; 5J93; -.
PDBsum; 5J9V; -.
PDBsum; 5JAC; -.
PDBsum; 5XHI; -.
PDBsum; 5XHM; -.
PDBsum; 5XHN; -.
PDBsum; 5XHO; -.
ProteinModelPortal; P07798; -.
SMR; P07798; -.
HOVERGEN; HBG000410; -.
SABIO-RK; P07798; -.
EvolutionaryTrace; P07798; -.
GO; GO:0005623; C:cell; IEA:GOC.
GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
GO; GO:0004322; F:ferroxidase activity; IEA:UniProtKB-EC.
GO; GO:0006879; P:cellular iron ion homeostasis; IEA:UniProtKB-KW.
GO; GO:0006826; P:iron ion transport; IEA:InterPro.
Gene3D; 1.20.1260.10; -; 1.
InterPro; IPR001519; Ferritin.
InterPro; IPR012347; Ferritin-like.
InterPro; IPR009040; Ferritin-like_diiron.
InterPro; IPR009078; Ferritin-like_SF.
InterPro; IPR014034; Ferritin_CS.
InterPro; IPR008331; Ferritin_DPS_dom.
PANTHER; PTHR11431; PTHR11431; 1.
Pfam; PF00210; Ferritin; 1.
SUPFAM; SSF47240; SSF47240; 1.
PROSITE; PS00540; FERRITIN_1; 1.
PROSITE; PS00204; FERRITIN_2; 1.
PROSITE; PS50905; FERRITIN_LIKE; 1.
1: Evidence at protein level;
3D-structure; Iron; Iron storage; Metal-binding; Oxidoreductase.
INIT_MET 1 1 Removed. {ECO:0000250}.
CHAIN 2 176 Ferritin, middle subunit.
/FTId=PRO_0000201073.
DOMAIN 7 156 Ferritin-like diiron.
{ECO:0000255|PROSITE-ProRule:PRU00085}.
METAL 24 24 Iron 1.
METAL 59 59 Iron 1.
METAL 59 59 Iron 2.
METAL 62 62 Iron 1.
METAL 104 104 Iron 2.
METAL 138 138 Iron 2.
METAL 141 141 Iron 2.
HELIX 11 38 {ECO:0000244|PDB:5J93}.
TURN 41 43 {ECO:0000244|PDB:5J93}.
HELIX 46 73 {ECO:0000244|PDB:5J93}.
HELIX 93 120 {ECO:0000244|PDB:5J93}.
HELIX 124 133 {ECO:0000244|PDB:5J93}.
HELIX 135 154 {ECO:0000244|PDB:5J93}.
TURN 155 159 {ECO:0000244|PDB:5J93}.
HELIX 161 170 {ECO:0000244|PDB:5J93}.
SEQUENCE 176 AA; 20592 MW; A9F0F5BEB8584D46 CRC64;
MVSQVRQNYH SDCEAAVNRM LNLELYASYT YSSMYAFFDR DDVALHNVAE FFKEHSHEER
EHAEKFMKYQ NKRGGRVVLQ DIKKPERDEW GNTLEAMQAA LQLEKTVNQA LLDLHKLATD
KVDPHLCDFL ESEYLEEQVK DIKRIGDFIT NLKRLGLPEN GMGEYLFDKH SVKESS


Related products :

Catalog number Product name Quantity
26-843 FTL is the light subunit of the ferritin protein. Ferritin is the major intracellular iron storage protein in prokaryotes and eukaryotes. It is composed of 24 subunits of the heavy and light ferritin 0.05 mg
20-272-190048 Ferritin - Mouse monoclonal [F23] to Ferritin; Ferritin L subunit Monoclonal 0.1 mg
20-272-190049 Ferritin - Mouse monoclonal [F31] to Ferritin; Ferritin L subunit Monoclonal 0.1 mg
U1905b CLIA Bos taurus,Bovine,Ferritin L subunit,Ferritin light chain,FTL 96T
U0518p CLIA Ferritin H subunit,Ferritin heavy chain,FTH,FTH1,Pig,Sus scrofa 96T
E1905b ELISA Bos taurus,Bovine,Ferritin L subunit,Ferritin light chain,FTL 96T
U1905b CLIA kit Bos taurus,Bovine,Ferritin L subunit,Ferritin light chain,FTL 96T
E1905b ELISA kit Bos taurus,Bovine,Ferritin L subunit,Ferritin light chain,FTL 96T
E0518p ELISA Ferritin H subunit,Ferritin heavy chain,FTH,FTH1,Pig,Sus scrofa 96T
E0518p ELISA kit Ferritin H subunit,Ferritin heavy chain,FTH,FTH1,Pig,Sus scrofa 96T
U1905p CLIA kit Ferritin L subunit,Ferritin light chain,FTL,Pig,Sus scrofa 96T
E1905p ELISA kit Ferritin L subunit,Ferritin light chain,FTL,Pig,Sus scrofa 96T
U1905p CLIA Ferritin L subunit,Ferritin light chain,FTL,Pig,Sus scrofa 96T
E1905p ELISA Ferritin L subunit,Ferritin light chain,FTL,Pig,Sus scrofa 96T
U1905h CLIA Ferritin L subunit,Ferritin light chain,FTL,Homo sapiens,Human 96T
E0518m ELISA Ferritin H subunit,Ferritin heavy chain,Fth,Fth1,Mouse,Mus musculus 96T
U1905Rb CLIA kit Ferritin L subunit,Ferritin light chain,FTL,Oryctolagus cuniculus,Rabbit 96T
E0518r ELISA kit Ferritin H subunit,Ferritin heavy chain,Fth,Fth1,Rat,Rattus norvegicus 96T
E1905Rb ELISA kit Ferritin L subunit,Ferritin light chain,FTL,Oryctolagus cuniculus,Rabbit 96T
E0518b ELISA Bos taurus,Bovine,Ferritin H subunit,Ferritin heavy chain,FTH,FTH1 96T
E0518r ELISA Ferritin H subunit,Ferritin heavy chain,Fth,Fth1,Rat,Rattus norvegicus 96T
E1905h ELISA kit Ferritin L subunit,Ferritin light chain,FTL,Homo sapiens,Human 96T
U0518r CLIA Ferritin H subunit,Ferritin heavy chain,Fth,Fth1,Rat,Rattus norvegicus 96T
U0518b CLIA Bos taurus,Bovine,Ferritin H subunit,Ferritin heavy chain,FTH,FTH1 96T
E1905Rb ELISA Ferritin L subunit,Ferritin light chain,FTL,Oryctolagus cuniculus,Rabbit 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur | Gentaur





GENTAUR Ltd.
Unicorn House, Station Cl
Hertfordshire, Potters Bar EN6 1TL
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017
RIB 30004 00187 00010092253 10
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
IBAN FR76 3000 4001 8700 0100 9225 310
france@gentaur.com | Gentaur | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: +49 0241 40 08 90 86, +49 0241 95 78 94 78, +49 0241 40 08 90 86
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur | Gentaur