B12 vitamiiniasiaa .Geeni GIF gastrinen " Intrinsic factor", Kr 11q12.1

https://www.ncbi.nlm.nih.gov/gene/?term=IF+intrinsic+factor
 GIF gastrinen  "intrinsic factor ". Tämän proteiinin geeni on  IF ja se kuuluu kobalamiinin kuljettajaproteiinien perheeseen . Se koodaa mahalaukun limakalvon parietaalisoluista  erittyvää  glykoproteiinia   ja  se on tarpeellinen, jota B12-vitamiini voisi imeytyä kehoon  asianmukaisesti. Vitamiini B12 on  välttämätön punasolujen kypsymiselle ja tämän geenin mutaatio voi  johtaa synnynnäiseen pernisiöösianemiaan. Geeni IF sijaitsee kromosomissa 11q12.1. Sen muita nimiä on TCN3, IFMH, INF, IF.

This gene is a member of the cobalamin transport protein family. It encodes a glycoprotein secreted by parietal cells of the gastric mucosa and is required for adequate absorption of vitamin B12. Vitamin B12 is necessary for erythrocyte maturation and mutations in this gene may lead to congenital pernicious anemia. [provided by RefSeq, J

Related articles in PubMed

1. Acute lymphoblastic leukemia and vitamin B12 deficiency secondary to a gastric intrinsic factor gene mutation. Zia A, et al. Pediatr Blood Cancer, 2012 Oct. PMID 22556038
2. Juvenile cobalamin deficiency in individuals of African ancestry is caused by a founder mutation in the intrinsic factor gene GIF. Ament AE, et al. Br J Haematol, 2009 Feb. PMID 19036097, Free PMC Article
3. Role of (Glu --> Arg, Q5R) mutation of the intrinsic factor in pernicious anemia and other causes of low vitamin B12. Remacha AF, et al. Ann Hematol, 2008 Jul. PMID 18338170
4. Crystal structure of human intrinsic factor: cobalamin complex at 2.6-A resolution. Mathews FS, et al. Proc Natl Acad Sci U S A, 2007 Oct 30. PMID 17954916, Free PMC Article
5. Identification of a 4-base deletion in the gene in inherited intrinsic factor deficiency. Yassin F, et al. Blood, 2004 Feb 15. PMID 14576042

See all (24) citations in PubMed

See citations in PubMed for homologs of this gene provided by HomoloGene

GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

1. the present findings reveal that High-altitude polycythemia -induced gastric mucosal lesion inspires the protection responses by up-regulating APOA4 and APOC3, and down-regulating GIF.
2. study reports that FUT2 secretor variant influences GIF secretion in B12 deficient cases bearing GIF heterozygous mutations, in absence of H. pylori related gastritis
3. Our genetic screening of 154 families of patients with inherited cobalamin malabsorption revealed population-specific mutations, mutational hotspots, and functionally distinct regions in the three causal genes: CUBN, AMN, and GIF.
4. Acute lymphoblastic leukemia and vitamin B12 deficiency secondary to a gastric intrinsic factor gene mutation
5. Observational study of gene-disease association and gene-environment interaction. (HuGE Navigator)
6. crystal structure of the complex between IF-Cbl and the cubilin IF-Cbl-binding-region (CUB(5-8)) determined at 3.3 A resolution
7. a specific GIF mutation to be responsible for all Juvenile cobalamin deficiency cases of West-African origin so far was identified
8. The Q5R mutation of the intrinsic factor gene predisposes to adult-onset pernicious anemia & other causes of low vitamin B12. In this mutation, intrinsic factor secretion is preserved but B12 absorption may be impaired.
9. possible basis for the lack of interchangeability of human and rat IF receptors is presented
10. The parameters obtained for ligand and receptor binding in this study indicate that both full-length 50-kDA intrinsic factor and its 30-kDa and 20-kDa fragments may be involved in assimilation of cobalamin.

PROTEIINI GIF

 https://www.ncbi.nlm.nih.gov/protein/NP_005133.2

ORIGIN      
        1 mawfalylls llwatagtst qtqsscsvps aqeplvngiq vlmensvtss aypnpsilia
       61 mnlagaynlk aqklltyqlm ssdnndltig qlgltimalt sscrdpgdkv silqrqmenw
      121 apsspnaeas afygpslail alcqknseat lpiavrfakt llansspfnv dtgamatlal
      181 tcmynkipvg seegyrslfg qvlkdiveki smkikdngii gdiystglam qalsvtpeps
      241 kkewnckktt dmilneikqg kfhnpmsiaq ilpslkgkty ldvpqvtcsp dhevqptlps
      301 npgpgptsas nitviytinn qlrgvellfn etinvsvksg svllvvleea qrknpmfkfe
      361 ttmtswglvv ssinniaenv nhktywqfls gvtplnegva dyipfnhehi tanftqy
//

KIDERAKENNE IF-Cobalamiini kompleksi

https://www.ncbi.nlm.nih.gov/Structure/mmdb/mmdbsrv.cgi?Dopt=s&uid=60169 

Proc Natl Acad Sci U S A. 2007 Oct 30;104(44):17311-6. Epub 2007 Oct 22.

Crystal structure of human intrinsic factor: cobalamin complex at 2.6-A resolution.

Mathews FS¹, Gordon MM, Chen Z, Rajashankar KR, Ealick SE, Alpers DH, Sukumar N.

Abstract

The structure of intrinsic factor (IF) in complex with cobalamin (Cbl) was determined at 2.6-A resolution. The overall fold of the molecule is that of an alpha(6)/alpha(6) barrel. It is a two-domain protein, and the Cbl is bound at the interface of the domains in a base-on conformation. Surprisingly, two full-length molecules, each comprising an alpha- and a beta-domain and one Cbl, and two truncated molecules with only an alpha- domain are present in the same asymmetric unit. The environment around Cbl is dominated by uncharged residues, and the sixth coordinate position of Co(2+) is empty. A detailed comparison between the IF-B12 complex and another Cbl transport protein complex, trans-Cbl-B12, has been made. The pH effect on the binding of Cbl analogues in transport proteins is analyzed. A possible basis for the lack of interchangeability of human and rat IF receptors is presented.

PMID:

17954916

PMCID:

PMC2077253

DOI:

10.1073/pnas.0703228104