Transferin

TF
Dostupne strukture PDB Pretraga ortologa: PDBe RCSB Spisak PDB ID kodova 4X1D, 1A8E, 1A8F, 1B3E, 1BP5, 1BTJ, 1D3K, 1D4N, 1DTG, 1FQE, 1FQF, 1JQF, 1N7W, 1N7X, 1N84, 1OQG, 1OQH, 1RYO, 1SUV, 2HAU, 2HAV, 2O7U, 2O84, 3FGS, 3QYT, 3S9L, 3S9M, 3S9N, 3SKP, 3V83, 3V89, 3V8X, 3VE1, 4H0W, 4X1B, 5DYH
Identifikatori
Aliasi	TF
Vanjski ID-jevi	OMIM: 190000 MGI: 98821 HomoloGene: 68153 GeneCards: TF
Lokacija gena (čovjek) Hrom. Hromosom 3 (čovjek)[1] Bend 3q22.1 Početak 133,746,040 bp[1] Kraj 133,796,641 bp[1]
Lokacija gena (miš) Hrom. Hromosom 9 (miš)[2] Bend 9 F1|9 55.03 cM Početak 103,081,200 bp[2] Kraj 103,107,643 bp[2]
Obrazac RNK ekspresije Više referentnih podataka o ekspresiji
Ontologija gena Molekularna funkcija • ferric iron binding • vezivanje iona metala • GO:0001948, GO:0016582 vezivanje za proteine • ferric iron transmembrane transporter activity • ferrous iron binding • transferrin receptor binding • iron chaperone activity Ćelijska komponenta • reciklirajući endosom • Vezikula • HFE-transferrin receptor complex • late endosome • blood microparticle • basal part of cell • endocytic vesicle • extracellular region • cell surface • basal plasma membrane • extrinsic component of external side of plasma membrane • early endosome • apical plasma membrane • perinuklearno područje citoplazme • clathrin-coated pit • secretory granule lumen • endosome membrane • Egzosom • Vanćelijsko • clathrin-coated vesicle membrane • GO:0016023 citoplazmatska vezikula • endoplasmic reticulum lumen Biološki proces • positive regulation of receptor-mediated endocytosis • cellular response to iron ion • regulation of protein stability • transferrin transport • iron ion homeostasis • platelet degranulation • ion transport • retina homeostasis • iron ion transport • cellular iron ion homeostasis • membrane organization • Posttranslacione modifikacije • GO:0015915 transport • iron ion transmembrane transport • GO:1900400 regulation of iron ion transport Izvori:Amigo / QuickGO
Ortolozi
Vrste	Čovjek	Miš
Entrez	7018	22041
Ensembl	ENSG00000091513	ENSMUSG00000032554
UniProt	P02787	Q921I1
RefSeq (mRNK)	NM_001063 NM_001354704 NM_001354703	NM_133977
RefSeq (bjelančevina)	NP_001054 NP_001341633 NP_001341632	NP_598738
Lokacija (UCSC)	Chr 3: 133.75 – 133.8 Mb	Chr 9: 103.08 – 103.11 Mb
PubMed pretraga	[3]	[4]
Wikipodaci
Pogledaj/uredi – čovjek Pogledaj/uredi – miš

Transferin
Identifikatori
Simbol	TF
Pfam	PF00405
InterPro	IPR001156
PROSITE	PDOC00182
SCOP2	1lcf / SCOPe / SUPFAM
Dostupne proteinske strukture: Pfam   strukture / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum sažetak strukture

Transferini su glikoproteini koji se nalaze u kičmenjacima, a vezuju se za i posljedično posreduju u transportu gvožđa (Fe) kroz krvnu plazmu.^[5] Proizvode se u jetri i sadrže mjesta vezivanja za dva iona Fe³⁺.^[6] Ljudski transferin je kodiran genom TF i proizveden je kao glikoproten od 76 kDa.^[7][8]

Transferinski glikoprotein vezuje gvožđe čvrsto, ali reverzibilno. Iako je gvožđe vezano za transferin manje od 0,1% (4 mg) ukupnog gvožđa u tijelu, ono čini najvitalniji bazen gvožđa sa najvećom stopom obrtanja (25 mg/24 h). Transferin ima molekulsku težinu od oko 80 kDa i sadrži dva specifična mjesta visokog afiniteta Fe(III) vezivanja. Afinitet transferina prema Fe(III) je izuzetno visok (konstanta disocijacije je 10²⁰ M⁻¹ na pH 7.4)^[9] ali se progresivno smanjuje sa smanjenjem pH ispod neutralnosti. Transferini nisu ograničeni samo na vezivanje za gvožđe, već i za različite ione metala.^[10] Ovi glikoproteini nalaze se u različitim tjelesnim tekućinama kičmenjaka.^[11][12] Neki beskičmenjaci imaju proteine koji se ponašaju kao transferin koji se nalazi u hemolimfi.^[11][13]

Kada nije vezan za željezo, transferin je poznat kao "apotransferin" (vidi također Apoprotein).

1. ^ ^{a b c} GRCh38: Ensembl release 89: ENSG00000091513 - Ensembl, maj 2017
2. ^ ^{a b c} GRCm38: Ensembl release 89: ENSMUSG00000032554 - Ensembl, maj 2017
3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. ^ Crichton RR, Charloteaux-Wauters M (maj 1987). "Iron transport and storage". European Journal of Biochemistry. 164 (3): 485–506. doi:10.1111/j.1432-1033.1987.tb11155.x. PMID 3032619.
6. ^ Hall DR, Hadden JM, Leonard GA, Bailey S, Neu M, Winn M, Lindley PF (januar 2002). "The crystal and molecular structures of diferric porcine and rabbit serum transferrins at resolutions of 2.15 and 2.60 A, respectively". Acta Crystallographica. Section D, Biological Crystallography. 58 (Pt 1): 70–80. doi:10.1107/s0907444901017309. PMID 11752780.
7. ^ Yang F, Lum JB, McGill JR, Moore CM, Naylor SL, van Bragt PH, et al. (maj 1984). "Human transferrin: cDNA characterization and chromosomal localization". Proceedings of the National Academy of Sciences of the United States of America. 81 (9): 2752–6. Bibcode:1984PNAS...81.2752Y. doi:10.1073/pnas.81.9.2752. PMC 345148. PMID 6585826.
8. ^ Kawabata H (mart 2019). "Transferrin and transferrin receptors update". Free Radical Biology & Medicine. 133: 46–54. doi:10.1016/j.freeradbiomed.2018.06.037. PMID 29969719. S2CID 49674402.
9. ^ Aisen P, Leibman A, Zweier J (mart 1978). "Stoichiometric and site characteristics of the binding of iron to human transferrin". The Journal of Biological Chemistry. 253 (6): 1930–7. doi:10.1016/S0021-9258(19)62337-9. PMID 204636.
10. ^ Nicotra S, Sorio D, Filippi G, De Gioia L, Paterlini V, De Palo EF, et al. (novembar 2017). "Terbium chelation, a specific fluorescent tagging of human transferrin. Optimization of conditions in view of its application to the HPLC analysis of carbohydrate-deficient transferrin (CDT)". Analytical and Bioanalytical Chemistry. 409 (28): 6605–6612. doi:10.1007/s00216-017-0616-z. PMID 28971232. S2CID 13929228.
11. ^ ^{a b} MacGillivray RT, Moore SA, Chen J, Anderson BF, Baker H, Luo Y, et al. (juni 1998). "Two high-resolution crystal structures of the recombinant N-lobe of human transferrin reveal a structural change implicated in iron release". Biochemistry. 37 (22): 7919–28. doi:10.1021/bi980355j. PMID 9609685.
12. ^ Dewan JC, Mikami B, Hirose M, Sacchettini JC (novembar 1993). "Structural evidence for a pH-sensitive dilysine trigger in the hen ovotransferrin N-lobe: implications for transferrin iron release". Biochemistry. 32 (45): 11963–8. doi:10.1021/bi00096a004. PMID 8218271.
13. ^ Baker EN, Lindley PF (august 1992). "New perspectives on the structure and function of transferrins". Journal of Inorganic Biochemistry. 47 (3–4): 147–60. doi:10.1016/0162-0134(92)84061-q. PMID 1431877.