SLC40A1

SLC40A1
Identifikatori
Aliasi	SLC40A1
Vanjski ID-jevi	OMIM: 604653 MGI: 1315204 HomoloGene: 40959 GeneCards: SLC40A1
Lokacija gena (čovjek)
Hrom.	Hromosom 2 (čovjek)
Kraj	189,583,758 bp
Lokacija gena (miš)
Hrom.	Hromosom 1 (miš)
Kraj	45,965,683 bp
Ontologija gena
Molekularna funkcija	• ferrous iron transmembrane transporter activity; • GO:0097689 iron ion transmembrane transporter activity; • peptide hormone binding; • GO:0001948, GO:0016582 vezivanje za proteine; • vezivanje identičnih proteina;
Ćelijska komponenta	• citoplazma; • integral component of membrane; • membrana; • Sinapsna vezikula; • ćelijska membrana; • integral component of plasma membrane; • intracellular anatomical structure; • basolateral plasma membrane; • nukleoplazma; • citosol;
Biološki proces	• iron ion transmembrane transport; • lymphocyte homeostasis; • spleen trabecula formation; • iron ion homeostasis; • negative regulation of apoptotic process; • ion transport; • spleen development; • multicellular organismal iron ion homeostasis; • iron ion transport; • endothelium development; • iron ion export across plasma membrane; • GO:0003257, GO:0010735, GO:1901228, GO:1900622, GO:1904488 positive regulation of transcription by RNA polymerase II; • cellular iron ion homeostasis; • regulation of transcription from RNA polymerase II promoter in response to iron;
	Izvori:Amigo / QuickGO
Ortolozi
	30061
	53945
	ENSG00000138449
	ENSMUSG00000025993
	Q9NP59
	Q9JHI9
	NM_014585
	NM_016917
	NP_055400
	NP_058613
	Wikipodaci
Pogledaj/uredi – čovjek	Pogledaj/uredi – miš

Feroportin-1, znan I kao član 1porodice rastvornih nosača (SLC40A1) ili gožđem-regulirani transporter 1 (IREG1), jest protein koji je kod ljudi kodiran genom SLC40A1 sa hromosoma 2 I dio je porodice feroportina (Fpn) (TC# 2.A.100).^[5] Ferroportinje transmembranski protein koji transportuje gvožđe iz unutrašnjsti na periferiju ćelija. Feroportin je jedini poznati eksporter gvožđa.^[6]

Nakon što se gvožđe iz hrane apsorbira u ćelioje tankog crijeva, feroportin omogućava da se transportira iz tih ćelija u krvotok. Fpn također posreduje u efluksu recikliranog gvopžđa iz makrofaga koji se nalaze u slezeni i jetri.^[7]

Feroportin reguliše hepcidin, hormon koji proizvodi jetra; hepcidin se vezuje za Fpn i ograničava njegovu aktivnost efluksa gvožđa, čime se smanjuje isporuka gvožđa u krvnu plazmu.^[8] Stoga, interakcija između Fpn i hepcidina kontroliše sistemski homeostazu gvožđa.

Aminokiselinska sekvenca

Dužina polipeptidnog lanca je 571 aminokiselina, a molekulska težina 62.542 Da.^[9]

C: Cistein

D: Asparaginska kiselina

E: Glutaminska kiselina

F: Fenilalanin

G: Glicin

H: Histidin

I: Izoleucin

K: Lizin

L: Leucin

M: Metionin

N: Asparagin

P: Prolin

Q: Glutamin

R: Arginin

S: Serin

T: Treonin

V: Valin

W: Triptofan

Y: Tirozin

10	20	30	40	50
MTRAGDHNRQ	RGCCGSLADY	LTSAKFLLYL	GHSLSTWGDR	MWHFAVSVFL
VELYGNSLLL	TAVYGLVVAG	SVLVLGAIIG	DWVDKNARLK	VAQTSLVVQN
VSVILCGIIL	MMVFLHKHEL	LTMYHGWVLT	SCYILIITIA	NIANLASTAT
AITIQRDWIV	VVAGEDRSKL	ANMNATIRRI	DQLTNILAPM	AVGQIMTFGS
PVIGCGFISG	WNLVSMCVEY	VLLWKVYQKT	PALAVKAGLK	EEETELKQLN
LHKDTEPKPL	EGTHLMGVKD	SNIHELEHEQ	EPTCASQMAE	PFRTFRDGWV
SYYNQPVFLA	GMGLAFLYMT	VLGFDCITTG	YAYTQGLSGS	ILSILMGASA
ITGIMGTVAF	TWLRRKCGLV	RTGLISGLAQ	LSCLILCVIS	VFMPGSPLDL
SVSPFEDIRS	RFIQGESITP	TKIPEITTEI	YMSNGSNSAN	IVPETSPESV
PIISVSLLFA	GVIAARIGLW	SFDLTVTQLL	QENVIESERG	IINGVQNSMN
YLLDLLHFIM	VILAPNPEAF	GLLVLISVSF	VAMGHIMYFR	FAQNTLGNKL
FACGPDAKEV	RKENQANTSV	V

Struktura i funkcija

Članovi porodice feroportina sastoje se od 400-800 aminokiselinskih ostataka,^[10] sa visoko konzerviranim histidin om na poziciji ostatka 32 (H32), i pokazuju 8-12 navodnih transmembranski domena. Ljudski Fpn sastoji se od 571 aminokiselinskog ostatka.^[10] Kada je H32 mutiran kod miševa, aktivnost transporta gvožđa je poremećena.^[11]

Nedavne kristalne strukture generirane iz bakterijskog homologa feroportina (iz " Bdellovibrio bacteriovorus ") otkrile su da struktura Fpn nalikuje onoj transportera natporodice glavnih fasilitatora (MFS).^[12]^[13] Prospektivno mjesto vezanja supstrata nalazi se na interfejsu između N- i C-terminalne polovine proteina, i naizmenično je dostupno sa obje strane ćelijjske membrane,^[13] u skladu sa MFS transporterima.

Feroportin posredovan efluksom gvožđa je kalcij-aktiviran; studije ljudskog Fpn eksprmiranog u oocitima Xenopus laevis pokazale su da je kalcij neophodan kofaktor za Fpn, ali da Fpn ne prenosi kalcij.^[13] Dakle, Fpn ne funkcionira kao antiporter gvožđa/kalcija. Termodinamička pokretačka sila za Fpn ostaje nepoznata.

Profil podloge

Pored gvožđa, pokazalo se da feroportin prenosi kobalt i cink,^[14] kao i nikl.^[13] Ferroportin može također funkcionirati kao eksporter mangana.^[15]

Tkivna distribucija

Feroportin se nalazi na bazolateralnim membranama intestinalnog epitela sisara, uključujući:^[16]^[17]

Uloga u razvoju

Feroportin-1 ima važnu ulogu u zatvaranju nervne cijevi i prednjem mozgu uzorku.^[18] Mišji embrioni bez gena Scl40a1 pobačeni su prije gastrulacija, što sugerira da je kodirani protein Fpn1 neophodan za normalan embrionalni razvoj.^[16] Fpn1 je izražen u sinciciotrofoblastnim ćelijama u placenti i visceralnom endodermu miševa na E7.5.^[5]^[16] Nadalje, nekoliko retrospektivnih studija zabilježilo je povećanu incidenciju spina bifida koji se javlja nakon malog majčinog unosa gvožđa tokom embrionskog i fetusnog razvoja.^[19]^[20]

Studija koja je ispitivala posljedice nekoliko različitih mutacija mišjeg gena "Slc40a1" sugerira da je kao rezultat nastalo nekoliko ozbiljnih defekata nervne cijevi i uzorka, uključujući spina bifida, egzencefaliju i skraćenje prednjeg mozga, između ostalog.^[18] S obzirom na nalaze dosadašnjih studija, čini se da postoje značajni dokazi da su mehanizmi transporta netaknutog gvođđa kritični za normalno zatvaranje nervne cijevi. Nadalje, drugi eksperimenti su sugerirali da su "Fpn1" proizvod i aktivnost potrebni duž cijele prednje-stražnje ose životinje kako bi se osiguralo pravilno zatvaranje nrvne cijevi.^[18]

Uloga u plodnosti

Poznato je da je gen za feroportin (SLC40A1) izražen na niskom nivou kod neplodnih žena. Otkriveno je da su njeni nivoi iRNK smanjeni kod ovih žena, posebno u granuloznim ćelijama. Štaviše, niska ekspresija feroportina je takođe povezana sa neplodnošću kada se uzmu u obzir neke karakteristike kao što su starost i navike pušenja.

Također je važno napomenuti da, ne samo da je feroportin smanjen u granulastim ćelijamama, već iu ćelijama grlića maternice neplodnih žena, te da se veza između neplodnosti i niskog nivoa feroportina u ovim ćelijama može vidjeti, opet, kada nivoi feroportinske iRNK nisz prilagođeni godinama i pušačkom statusu.^[21]

Uloga u metabolizmu gvožđa

Feroportin inhibira hepcidin, koji se veže za feroportin i internalizira ga unutar ćelije.^[8] To rezultira zadržavanjem gvođđa u enterocitima, hepatocitima i makrofagima s posljedičnim smanjenjem nivoa u krvnom serumu. Ovo je posebno značajno za enterocite koji, kada se isprazne na kraju svog životnog vijeka, rezultiraju značajnim gubitkom gvožđa. Ovo je dio mehanizma koji uzrokuje anemiju srčene bolesti; hepcidin se oslobađa iz jetre kao odgovor na upalne citokine, naime interleukin-6, što rezultira povećanom koncentracijom hepcidina i posljedičnim smanjenjem nivoa gvožđa u plazmi.^[22]

Ekspresija feroportina je takođe regulirana regulatornim mehanizmom protein koji reaguje na gvožđeIRP. Ako je koncentracija gvožđa preniska, koncentracija IRP se povećava, čime se inhibira translacija feroportina. Prevođenje feroportina je također regulirano putem mikroRNk miR-485-3p.^[23]

Klinički značaj

Poznato je da mutacije u genu feroportina uzrokuju autosomno dominantni oblik preopterećenja gvožđem poznat kao tip IV hemohromatoza ili feroportinska bolest. Učinci mutacija općenito nisu ozbiljni, ali se kod različitih mutacija vidi čitav spektar kliničkih ishoda. Feroportin je takođe povezan sa afričkim preopterećenjem gvožđem. Feroportin i hepcidin su kritični proteini za regulaciju sistemske homeostaze gvožđa.

Reference

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000138449 - Ensembl, maj 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000025993 - Ensembl, maj 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ ^a ^b Donovan A, Brownlie A, Zhou Y, Shepard J, Pratt SJ, Moynihan J, et al. (februar 2000). "Positional cloning of zebrafish ferroportin1 identifies a conserved vertebrate iron exporter". Nature. 403 (6771): 776–81. Bibcode:2000Natur.403..776D. doi:10.1038/35001596. PMID 10693807. S2CID 4429026.
^ Ward DM, Kaplan J (septembar 2012). "Ferroportin-mediated iron transport: expression and regulation". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1823 (9): 1426–33. doi:10.1016/j.bbamcr.2012.03.004. PMC 3718258. PMID 22440327.
^ Canonne-Hergaux F, Donovan A, Delaby C, Wang HJ, Gros P (januar 2006). "Comparative studies of duodenal and macrophage ferroportin proteins". American Journal of Physiology. Gastrointestinal and Liver Physiology. 290 (1): G156-63. doi:10.1152/ajpgi.00227.2005. PMID 16081760.
^ ^a ^b Nemeth E, Tuttle MS, Powelson J, Vaughn MB, Donovan A, Ward DM, et al. (decembar 2004). "Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization". Science. 306 (5704): 2090–3. Bibcode:2004Sci...306.2090N. doi:10.1126/science.1104742. PMID 15514116. S2CID 24035970.
^ "UniProt, Q9NP59" (jezik: англ.). Pristupljeno 19. 11. 2021.CS1 održavanje: nepoznati jezik (link)
^ ^a ^b "SLC11A3 iron transporter [Homo sapiens]". Protein - NCBI.
^ Zohn IE, De Domenico I, Pollock A, Ward DM, Goodman JF, Liang X, et al. (maj 2007). "The flatiron mutation in mouse ferroportin acts as a dominant negative to cause ferroportin disease". Blood. 109 (10): 4174–80. doi:10.1182/blood-2007-01-066068. PMC 1885502. PMID 17289807.
^ Taniguchi R, Kato HE, Font J, Deshpande CN, Wada M, Ito K, et al. (oktobar 2015). "Outward- and inward-facing structures of a putative bacterial transition-metal transporter with homology to ferroportin". Nature Communications. 6 (1): 8545. Bibcode:2015NatCo...6.8545T. doi:10.1038/ncomms9545. PMC 4633820. PMID 26461048.
^ ^a ^b ^c ^d Deshpande CN, Ruwe TA, Shawki A, Xin V, Vieth KR, Valore EV, et al. (august 2018). "Calcium is an essential cofactor for metal efflux by the ferroportin transporter family". Nature Communications. 9 (1): 3075. Bibcode:2018NatCo...9.3075D. doi:10.1038/s41467-018-05446-4. PMC 6079014. PMID 30082682.
^ Mitchell CJ, Shawki A, Ganz T, Nemeth E, Mackenzie B (mart 2014). "Functional properties of human ferroportin, a cellular iron exporter reactive also with cobalt and zinc". American Journal of Physiology. Cell Physiology. 306 (5): C450-9. doi:10.1152/ajpcell.00348.2013. PMC 4042619. PMID 24304836.
^ Madejczyk MS, Ballatori N (mart 2012). "The iron transporter ferroportin can also function as a manganese exporter". Biochimica et Biophysica Acta (BBA) - Biomembranes. 1818 (3): 651–7. doi:10.1016/j.bbamem.2011.12.002. PMC 5695046. PMID 22178646.
^ ^a ^b ^c Donovan A, Lima CA, Pinkus JL, Pinkus GS, Zon LI, Robine S, Andrews NC (mart 2005). "The iron exporter ferroportin/Slc40a1 is essential for iron homeostasis". Cell Metabolism. 1 (3): 191–200. doi:10.1016/j.cmet.2005.01.003. PMID 16054062.
^ Delaby C, Pilard N, Puy H, Canonne-Hergaux F (april 2008). "Sequential regulation of ferroportin expression after erythrophagocytosis in murine macrophages: early mRNA induction by haem, followed by iron-dependent protein expression" (PDF). The Biochemical Journal. 411 (1): 123–31. doi:10.1042/BJ20071474. PMID 18072938.
^ ^a ^b ^c Mao J, McKean DM, Warrier S, Corbin JG, Niswander L, Zohn IE (septembar 2010). "The iron exporter ferroportin 1 is essential for development of the mouse embryo, forebrain patterning and neural tube closure". Development. 137 (18): 3079–88. doi:10.1242/dev.048744. PMC 2926957. PMID 20702562.
^ Felkner MM, Suarez L, Brender J, Scaife B, Hendricks K (decembar 2005). "Iron status indicators in women with prior neural tube defect-affected pregnancies". Maternal and Child Health Journal. 9 (4): 421–8. doi:10.1007/s10995-005-0017-3. PMID 16315101. S2CID 13415844.
^ Groenen PM, van Rooij IA, Peer PG, Ocké MC, Zielhuis GA, Steegers-Theunissen RP (juni 2004). "Low maternal dietary intakes of iron, magnesium, and niacin are associated with spina bifida in the offspring". The Journal of Nutrition. 134 (6): 1516–22. doi:10.1093/jn/134.6.1516. PMID 15173422.
^ Moreno-Navarrete JM, López-Navarro E, Candenas L, Pinto F, Ortega FJ, Sabater-Masdeu M, et al.Ferroportin mRNA is down-regulated in granulosa and cervical cells from infertile women.Fertil Steril. 2017 Jan;107(1):236-242.
^ Nemeth E, Rivera S, Gabayan V, Keller C, Taudorf S, Pedersen BK, Ganz T (maj 2004). "IL-6 mediates hypoferremia of inflammation by inducing the synthesis of the iron regulatory hormone hepcidin". The Journal of Clinical Investigation. 113 (9): 1271–6. doi:10.1172/JCI20945. PMC 398432. PMID 15124018.
^ Sangokoya C, Doss JF, Chi JT (april 2013). "Iron-responsive miR-485-3p regulates cellular iron homeostasis by targeting ferroportin". PLOS Genetics. 9 (4): e1003408. doi:10.1371/journal.pgen.1003408. PMC 3616902. PMID 23593016.

Dopunska literatura

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Pietrangelo A (2004). "The ferroportin disease". Blood Cells, Molecules & Diseases. 32 (1): 131–8. doi:10.1016/j.bcmd.2003.08.003. PMID 14757427.
Robson KJ, Merryweather-Clarke AT, Cadet E, Viprakasit V, Zaahl MG, Pointon JJ, et al. (oktobar 2004). "Recent advances in understanding haemochromatosis: a transition state". Journal of Medical Genetics. 41 (10): 721–30. doi:10.1136/jmg.2004.020644. PMC 1735598. PMID 15466004.
Maruyama K, Sugano S (januar 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (oktobar 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Abboud S, Haile DJ (juni 2000). "A novel mammalian iron-regulated protein involved in intracellular iron metabolism". The Journal of Biological Chemistry. 275 (26): 19906–12. doi:10.1074/jbc.M000713200. PMID 10747949.
Haile DJ (2000). "Assignment of Slc11a3 to mouse chromosome 1 band 1B and SLC11A3 to human chromosome 2q32 by in situ hybridization". Cytogenetics and Cell Genetics. 88 (3–4): 328–9. doi:10.1159/000015522. PMID 10828623. S2CID 6098716.
McKie AT, Marciani P, Rolfs A, Brennan K, Wehr K, Barrow D, et al. (februar 2000). "A novel duodenal iron-regulated transporter, IREG1, implicated in the basolateral transfer of iron to the circulation". Molecular Cell. 5 (2): 299–309. doi:10.1016/S1097-2765(00)80425-6. PMID 10882071.
Hartley JL, Temple GF, Brasch MA (novembar 2000). "DNA cloning using in vitro site-specific recombination". Genome Research. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
Njajou OT, Vaessen N, Joosse M, Berghuis B, van Dongen JW, Breuning MH, et al. (juli 2001). "A mutation in SLC11A3 is associated with autosomal dominant hemochromatosis". Nature Genetics. 28 (3): 213–4. doi:10.1038/90038. PMID 11431687. S2CID 7345473.
Montosi G, Donovan A, Totaro A, Garuti C, Pignatti E, Cassanelli S, et al. (august 2001). "Autosomal-dominant hemochromatosis is associated with a mutation in the ferroportin (SLC11A3) gene". The Journal of Clinical Investigation. 108 (4): 619–23. doi:10.1172/JCI13468. PMC 209405. PMID 11518736.
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Vanjski linksovi

ferroportin1 protein na US National Library of Medicine Medical Subject Headings (MeSH)

Šablon:Porodica rastvotnih nosača Šablon:Metabolizam gvožđa

As of ovo uređivanje, ovaj članak koristi sadžaj iz "2.A.100 The Ferroportin (Fpn) Family", koji je licenciran na način da dozvoljava korištenje pod Creative Commons Attribution-ShareAlike 3.0 Unported License, ali ne pod GFDL. Svi odgovarajući uslovi moraju biti praćeni.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000138449 - Ensembl, maj 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000025993 - 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.

[Donovan_2000-5] Donovan A, Brownlie A, Zhou Y, Shepard J, Pratt SJ, Moynihan J, et al. (februar 2000). "Positional cloning of zebrafish ferroportin1 identifies a conserved vertebrate iron exporter". Nature. 403 (6771): 776–81. Bibcode:2000Natur.403..776D. doi:10.1038/35001596. PMID 10693807. S2CID 4429026.

[6] Ward DM, Kaplan J (septembar 2012). "Ferroportin-mediated iron transport: expression and regulation". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1823 (9): 1426–33. doi:10.1016/j.bbamcr.2012.03.004. PMC 3718258. PMID 22440327.

[7] Canonne-Hergaux F, Donovan A, Delaby C, Wang HJ, Gros P (januar 2006). "Comparative studies of duodenal and macrophage ferroportin proteins". American Journal of Physiology. Gastrointestinal and Liver Physiology. 290 (1): G156-63. doi:10.1152/ajpgi.00227.2005. PMID 16081760.

[pmid15514116-8] Nemeth E, Tuttle MS, Powelson J, Vaughn MB, Donovan A, Ward DM, et al. (decembar 2004). "Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization". Science. 306 (5704): 2090–3. Bibcode:2004Sci...306.2090N. doi:10.1126/science.1104742. PMID 15514116. S2CID 24035970.

[UniProt-9] "UniProt, Q9NP59" (jezik: англ.). Pristupljeno 19. 11. 2021.CS1 održavanje: nepoznati jezik (link)

[url_SLC11A3_NCBI-10] "SLC11A3 iron transporter [Homo sapiens]". Protein - NCBI.

[pmid17289807-11] Zohn IE, De Domenico I, Pollock A, Ward DM, Goodman JF, Liang X, et al. (maj 2007). "The flatiron mutation in mouse ferroportin acts as a dominant negative to cause ferroportin disease". Blood. 109 (10): 4174–80. doi:10.1182/blood-2007-01-066068. PMC 1885502. PMID 17289807.

[12] Taniguchi R, Kato HE, Font J, Deshpande CN, Wada M, Ito K, et al. (oktobar 2015). "Outward- and inward-facing structures of a putative bacterial transition-metal transporter with homology to ferroportin". Nature Communications. 6 (1): 8545. Bibcode:2015NatCo...6.8545T. doi:10.1038/ncomms9545. PMC 4633820. PMID 26461048.

[:0-13] Deshpande CN, Ruwe TA, Shawki A, Xin V, Vieth KR, Valore EV, et al. (august 2018). "Calcium is an essential cofactor for metal efflux by the ferroportin transporter family". Nature Communications. 9 (1): 3075. Bibcode:2018NatCo...9.3075D. doi:10.1038/s41467-018-05446-4. PMC 6079014. PMID 30082682.

[14] Mitchell CJ, Shawki A, Ganz T, Nemeth E, Mackenzie B (mart 2014). "Functional properties of human ferroportin, a cellular iron exporter reactive also with cobalt and zinc". American Journal of Physiology. Cell Physiology. 306 (5): C450-9. doi:10.1152/ajpcell.00348.2013. PMC 4042619. PMID 24304836.

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