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

HLA class I histocompatibility antigen, alpha chain F (CDA12) (HLA F antigen) (Leukocyte antigen F) (MHC class I antigen F)

 HLAF_HUMAN              Reviewed;         346 AA.
P30511; Q5JQI8; Q5JQJ1; Q5SPT5; Q860R0; Q8MGQ1; Q8WLP5; Q95HC0;
Q9TP68;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 3.
16-JAN-2019, entry version 171.
RecName: Full=HLA class I histocompatibility antigen, alpha chain F;
AltName: Full=CDA12;
AltName: Full=HLA F antigen;
AltName: Full=Leukocyte antigen F {ECO:0000303|PubMed:1688605};
AltName: Full=MHC class I antigen F;
Flags: Precursor;
Name=HLA-F {ECO:0000303|PubMed:1688605, ECO:0000303|PubMed:1707659,
ECO:0000312|HGNC:HGNC:4963};
Synonyms=HLA-5.4 {ECO:0000303|PubMed:1688605,
ECO:0000303|PubMed:1707659}, HLAF;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 1),
AND VARIANT SER-272.
PubMed=1688605; DOI=10.1084/jem.171.1.1;
Geraghty D.E., Wei X., Orr H.T., Koller B.H.;
"Human leukocyte antigen F (HLA-F). An expressed HLA gene composed of
a class I coding sequence linked to a novel transcribed repetitive
element.";
J. Exp. Med. 171:1-18(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 1),
AND VARIANT SER-272.
PubMed=1707659; DOI=10.1093/intimm/2.6.531;
Lury D., Epstein H., Holmes N.;
"The human class I MHC gene HLA-F is expressed in lymphocytes.";
Int. Immunol. 2:531-537(1990).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 1),
AND VARIANT SER-272.
PubMed=10727083; DOI=10.3109/10425179909033955;
Hampe A., Coriton O., Andrieux N., Carn G., Lepourcelet M.,
Mottier S., Dreano S., Gatius M.T., Hitte C., Soriano N., Galibert F.;
"A 356-Kb sequence of the subtelomeric part of the MHC class I
region.";
DNA Seq. 10:263-299(1999).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANT SER-272.
PubMed=14705989; DOI=10.1111/j.1399-0039.2004.00145.x;
He X., Xu L., Liu Y., Zeng Y.;
"Identification of a novel HLA-F allele - HLA-F*010102.";
Tissue Antigens 63:181-183(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 1),
AND VARIANT SER-272.
PubMed=16570139; DOI=10.1007/s00251-005-0076-z;
Pyo C.W., Williams L.M., Moore Y., Hyodo H., Li S.S., Zhao L.P.,
Sageshima N., Ishitani A., Geraghty D.E.;
"HLA-E, HLA-F, and HLA-G polymorphism: genomic sequence defines
haplotype structure and variation spanning the nonclassical class I
genes.";
Immunogenetics 58:241-251(2006).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT SER-272.
Gharwan H., Sageshima N., Ishitani A., Geraghty D.E.;
"A comparative study of the MHC-F expression patterns between humans
and nonhuman primates.";
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT SER-272.
Shiina S., Tamiya G., Oka A., Inoko H.;
"Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region.";
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT SER-272.
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
SER-272.
TISSUE=Lung, and Lymph;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
SUBUNIT, INTERACTION WITH LILRB1 AND LILRB2, AND TISSUE SPECIFICITY.
PubMed=11169396;
DOI=10.1002/1521-4141(200012)30:12<3552::AID-IMMU3552>3.0.CO;2-L;
Lepin E.J., Bastin J.M., Allan D.S., Roncador G., Braud V.M.,
Mason D.Y., van der Merwe P.A., McMichael A.J., Bell J.I., Powis S.H.,
O'Callaghan C.A.;
"Functional characterization of HLA-F and binding of HLA-F tetramers
to ILT2 and ILT4 receptors.";
Eur. J. Immunol. 30:3552-3561(2000).
[12]
SUBUNIT, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, GLYCOSYLATION,
INTERACTION WITH TAP1, INTERACTION WITH TAP2, INTERACTION WITH CALR,
AND INTERACTION WITH B2M.
PubMed=10605026;
Wainwright S.D., Biro P.A., Holmes C.H.;
"HLA-F is a predominantly empty, intracellular, TAP-associated MHC
class Ib protein with a restricted expression pattern.";
J. Immunol. 164:319-328(2000).
[13]
SUBCELLULAR LOCATION, MUTAGENESIS OF VAL-346, MUTAGENESIS OF
336-ARG--ARG-338, SUBUNIT, AND MOTIF.
PubMed=16709803;
Boyle L.H., Gillingham A.K., Munro S., Trowsdale J.;
"Selective export of HLA-F by its cytoplasmic tail.";
J. Immunol. 176:6464-6472(2006).
[14]
TISSUE SPECIFICITY.
PubMed=20865824;
Lee N., Ishitani A., Geraghty D.E.;
"HLA-F is a surface marker on activated lymphocytes.";
Eur. J. Immunol. 40:2308-2318(2010).
[15]
SUBUNIT, AND INTERACTION WITH HLA-E.
PubMed=20483783; DOI=10.4049/jimmunol.1000078;
Goodridge J.P., Burian A., Lee N., Geraghty D.E.;
"HLA-F complex without peptide binds to MHC class I protein in the
open conformer form.";
J. Immunol. 184:6199-6208(2010).
[16]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=23851683; DOI=10.4049/jimmunol.1300080;
Goodridge J.P., Lee N., Burian A., Pyo C.W., Tykodi S.S., Warren E.H.,
Yee C., Riddell S.R., Geraghty D.E.;
"HLA-F and MHC-I open conformers cooperate in a MHC-I antigen cross-
presentation pathway.";
J. Immunol. 191:1567-1577(2013).
[17]
FUNCTION, SUBUNIT, INTERACTION WITH KIR3DL2, AND INTERACTION WITH
KIR2DS4.
PubMed=24018270; DOI=10.4049/jimmunol.1300081;
Goodridge J.P., Burian A., Lee N., Geraghty D.E.;
"HLA-F and MHC class I open conformers are ligands for NK cell Ig-like
receptors.";
J. Immunol. 191:3553-3562(2013).
[18]
FUNCTION, SUBUNIT, INTERACTION WITH KIR3DS1, TISSUE SPECIFICITY,
INDUCTION BY HIV-1 INFECTION, GLYCOSYLATION, AND SUBCELLULAR LOCATION.
PubMed=27455421; DOI=10.1038/ni.3513;
Garcia-Beltran W.F., Hoelzemer A., Martrus G., Chung A.W., Pacheco Y.,
Simoneau C.R., Rucevic M., Lamothe-Molina P.A., Pertel T., Kim T.E.,
Dugan H., Alter G., Dechanet-Merville J., Jost S., Carrington M.,
Altfeld M.;
"Open conformers of HLA-F are high-affinity ligands of the activating
NK-cell receptor KIR3DS1.";
Nat. Immunol. 17:1067-1074(2016).
[19]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=26928464; DOI=10.1038/nm.4052;
Song S., Miranda C.J., Braun L., Meyer K., Frakes A.E., Ferraiuolo L.,
Likhite S., Bevan A.K., Foust K.D., McConnell M.J., Walker C.M.,
Kaspar B.K.;
"Major histocompatibility complex class I molecules protect motor
neurons from astrocyte-induced toxicity in amyotrophic lateral
sclerosis.";
Nat. Med. 22:397-403(2016).
[20]
DEVELOPMENTAL STAGE.
PubMed=28185362; DOI=10.1111/aji.12643;
Hackmon R., Pinnaduwage L., Zhang J., Lye S.J., Geraghty D.E.,
Dunk C.E.;
"Definitive class I human leukocyte antigen expression in gestational
placentation: HLA-F, HLA-E, HLA-C, and HLA-G in extravillous
trophoblast invasion on placentation, pregnancy, and parturition.";
Am. J. Reprod. Immunol. 77:0-0(2017).
[21]
X-RAY CRYSTALLOGRAPHY (2.62 ANGSTROMS) OF 22-305 IN COMPLEX WITH
SELF-PEPTIDE, DISULFIDE BOND, FUNCTION, SUBUNIT, INTERACTION WITH
LILRB1, INTERACTION WITH KIR3DS1 AND KIR3DL2, AND MUTAGENESIS OF
TRP-83.
PubMed=28636952; DOI=10.1016/j.immuni.2017.06.002;
Dulberger C.L., McMurtrey C.P., Holzemer A., Neu K.E., Liu V.,
Steinbach A.M., Garcia-Beltran W.F., Sulak M., Jabri B., Lynch V.J.,
Altfeld M., Hildebrand W.H., Adams E.J.;
"Human Leukocyte Antigen F Presents Peptides and Regulates Immunity
through Interactions with NK Cell Receptors.";
Immunity 46:1018-1029.e7(2017).
-!- FUNCTION: Non-classical major histocompatibility class Ib molecule
postulated to play a role in immune surveillance, immune tolerance
and inflammation. Functions in two forms, as a heterotrimeric
complex with B2M/beta-2 microglobulin and a peptide (peptide-bound
HLA-F-B2M) and as an open conformer (OC) devoid of peptide and B2M
(peptide-free OC). In complex with B2M, presents non-canonical
self-peptides carrying post-translational modifications,
particularly phosphorylated self-peptides. Peptide-bound HLA-F-B2M
acts as a ligand for LILRB1 inhibitory receptor, a major player in
maternal-fetal tolerance. Peptide-free OC acts as a ligand for
KIR3DS1 and KIR3DL2 receptors (PubMed:28636952). Upon interaction
with activating KIR3DS1 receptor on NK cells, triggers NK cell
degranulation and anti-viral cytokine production
(PubMed:27455421). Through interaction with KIR3DL2 receptor,
inhibits NK and T cell effector functions (PubMed:24018270). May
interact with other MHC class I OCs to cross-present exogenous
viral, tumor or minor histompatibility antigens to cytotoxic CD8+
T cells, triggering effector and memory responses
(PubMed:23851683). May play a role in inflammatory responses in
the peripheral nervous system. Through interaction with KIR3DL2,
may protect motor neurons from astrocyte-induced toxicity
(PubMed:26928464). {ECO:0000269|PubMed:23851683,
ECO:0000269|PubMed:24018270, ECO:0000269|PubMed:26928464,
ECO:0000269|PubMed:27455421, ECO:0000269|PubMed:28636952}.
-!- SUBUNIT: Forms a heterotrimer with B2M and a self-peptide
(PubMed:28636952). Binds a diverse number of peptides ranging from
7 to more than 30 amino acids (PubMed:28636952). Peptide-bound
HLA-F-B2M interacts with LILRB1 and LILRB2 but not with KIR3DS1 or
KIR3DL2; this interaction is direct (PubMed:28636952,
PubMed:11169396). The OC form interacts with KIR3DS1, KIR2DS4 and
KIR3DL2; this interaction is direct (PubMed:28636952,
PubMed:27455421, PubMed:24018270). Interacts with TAP1-TAP2
complex and CALR; this interaction is required for appropriate
folding and peptide loading (PubMed:10605026, PubMed:11169396).
Interacts with the coat protein complex II and 14-3-3 proteins;
these interactions likely control the anterograde ER-to-Golgi
transport of HLA-F (PubMed:16709803). HLA-F-B2M complex interacts
with the heavy chain of other MHC class I molecules including HLA-
A and HLA-E; this interaction may regulate the intracellular
trafficking and the stability of peptide-free MHC class I OCs
(PubMed:20483783). {ECO:0000269|PubMed:10605026,
ECO:0000269|PubMed:11169396, ECO:0000269|PubMed:16709803,
ECO:0000269|PubMed:20483783, ECO:0000269|PubMed:24018270,
ECO:0000269|PubMed:27455421, ECO:0000269|PubMed:28636952}.
-!- INTERACTION:
P13747:HLA-E; NbExp=2; IntAct=EBI-2811134, EBI-726583;
P43632:KIR2DS4; NbExp=4; IntAct=EBI-2811134, EBI-13916812;
P43629:KIR3DL1; NbExp=4; IntAct=EBI-2811134, EBI-3910993;
P43630:KIR3DL2; NbExp=6; IntAct=EBI-2811134, EBI-6165894;
Q14943:KIR3DS1; NbExp=6; IntAct=EBI-2811134, EBI-15316524;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16709803,
ECO:0000269|PubMed:23851683, ECO:0000305|PubMed:27455421}; Single-
pass type I membrane protein. Early endosome membrane
{ECO:0000269|PubMed:23851683}. Lysosome membrane
{ECO:0000269|PubMed:23851683}. Note=For cross-presentation
transits from the cell surface through endosomal pathway to
lysosomes, where the peptide is generated from internalized
exogenous antigen. {ECO:0000269|PubMed:23851683}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P30511-1; Sequence=Displayed;
Name=2;
IsoId=P30511-2; Sequence=VSP_038846;
Name=3;
IsoId=P30511-3; Sequence=VSP_040349;
Note=Ref.10 (AAH09260) sequence is in conflict in position:
353:N->L. {ECO:0000305};
-!- TISSUE SPECIFICITY: Expressed in resting B cells (at protein
level). Expressed in secondary lymphoid organs rich in B and T
cells such as the tonsils, spleen, and thymus (at protein level)
(PubMed:10605026, PubMed:11169396). Expressed in the endothelial
cells of the tonsils (PubMed:11169396). Expressed on activated
lymphoid cells including B cells, NK cells, CD4+ T cells and
memory T cells (at protein level) (PubMed:27455421,
PubMed:20865824). Expressed in motor neurons of spinal cord
(PubMed:26928464). {ECO:0000269|PubMed:10605026,
ECO:0000269|PubMed:11169396, ECO:0000269|PubMed:20865824,
ECO:0000269|PubMed:26928464, ECO:0000269|PubMed:27455421}.
-!- DEVELOPMENTAL STAGE: Expressed in fetal liver (at protein level)
(PubMed:10605026). Expressed in placenta villous mesenchyme,
cytotrophoblast, syncytiotrophoblast and invasive extravillous
trophoblast (at protein level) (PubMed:28185362).
{ECO:0000269|PubMed:10605026, ECO:0000269|PubMed:28185362}.
-!- INDUCTION: Up-regulated in CD4+ T cells upon stimulation via TCR
and upon HIV-1 infection. {ECO:0000269|PubMed:27455421}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:10605026,
ECO:0000269|PubMed:27455421}.
-!- SIMILARITY: Belongs to the MHC class I family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC24827.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=AAH09260.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAB63337.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAA34947.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAB46623.1; Type=Erroneous gene model prediction; Evidence={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; X17093; CAA34947.1; ALT_SEQ; Genomic_DNA.
EMBL; AF055066; AAC24827.1; ALT_SEQ; Genomic_DNA.
EMBL; AY253269; AAO86773.1; -; mRNA.
EMBL; AY253270; AAO86774.1; -; mRNA.
EMBL; AY253271; AAO86775.1; -; mRNA.
EMBL; AF523284; AAM74979.1; -; Genomic_DNA.
EMBL; AF523285; AAM74980.1; -; Genomic_DNA.
EMBL; AF523286; AAM74981.1; -; Genomic_DNA.
EMBL; AF523287; AAM74982.1; -; Genomic_DNA.
EMBL; AF523288; AAM74983.1; -; Genomic_DNA.
EMBL; AF523289; AAM74984.1; -; Genomic_DNA.
EMBL; AF523290; AAM74985.1; -; Genomic_DNA.
EMBL; AF523291; AAM74986.1; -; Genomic_DNA.
EMBL; AF523292; AAM74987.1; -; Genomic_DNA.
EMBL; AF523293; AAM74988.1; -; Genomic_DNA.
EMBL; AF523294; AAM74989.1; -; Genomic_DNA.
EMBL; AF523295; AAM74990.1; -; Genomic_DNA.
EMBL; AF523296; AAM74991.1; -; Genomic_DNA.
EMBL; AF523297; AAM74992.1; -; Genomic_DNA.
EMBL; AY645742; AAT73225.1; -; Genomic_DNA.
EMBL; AY645743; AAT73226.1; -; Genomic_DNA.
EMBL; AY645744; AAT73227.1; -; Genomic_DNA.
EMBL; AY645745; AAT73228.1; -; Genomic_DNA.
EMBL; AY645746; AAT73229.1; -; Genomic_DNA.
EMBL; AY645748; AAT73231.1; -; Genomic_DNA.
EMBL; AY645749; AAT73232.1; -; Genomic_DNA.
EMBL; AY645750; AAT73233.1; -; Genomic_DNA.
EMBL; AY645751; AAT73234.1; -; Genomic_DNA.
EMBL; AY645752; AAT73235.1; -; Genomic_DNA.
EMBL; AY645753; AAT73236.1; -; Genomic_DNA.
EMBL; AY645754; AAT73237.1; -; Genomic_DNA.
EMBL; AY645756; AAT73239.1; -; Genomic_DNA.
EMBL; AY645757; AAT73240.1; -; Genomic_DNA.
EMBL; AY645758; AAT73241.1; -; Genomic_DNA.
EMBL; AY645759; AAT73242.1; -; Genomic_DNA.
EMBL; DQ367723; ABD38924.1; -; mRNA.
EMBL; BA000025; BAB63337.1; ALT_SEQ; Genomic_DNA.
EMBL; AL022723; CAB46623.1; ALT_SEQ; Genomic_DNA.
EMBL; AL645939; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL669813; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL844851; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BX005428; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CR753818; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BX927250; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471081; EAX03223.1; -; Genomic_DNA.
EMBL; CH471081; EAX03226.1; -; Genomic_DNA.
EMBL; BC009260; AAH09260.2; ALT_INIT; mRNA.
EMBL; BC062991; AAH62991.1; -; mRNA.
CCDS; CCDS43437.1; -. [P30511-3]
CCDS; CCDS43438.1; -. [P30511-1]
CCDS; CCDS43439.1; -. [P30511-2]
PIR; A60384; A60384.
RefSeq; NP_001091948.1; NM_001098478.1. [P30511-2]
RefSeq; NP_001091949.1; NM_001098479.1. [P30511-3]
RefSeq; NP_061823.2; NM_018950.2. [P30511-1]
UniGene; Hs.519972; -.
PDB; 5IUE; X-ray; 2.62 A; A/E/G/I=22-305.
PDB; 5KNM; X-ray; 3.30 A; A=22-305.
PDBsum; 5IUE; -.
PDBsum; 5KNM; -.
ProteinModelPortal; P30511; -.
SMR; P30511; -.
BioGrid; 109379; 21.
IntAct; P30511; 11.
STRING; 9606.ENSP00000259951; -.
iPTMnet; P30511; -.
PhosphoSitePlus; P30511; -.
BioMuta; HLA-F; -.
DMDM; 317373438; -.
EPD; P30511; -.
jPOST; P30511; -.
PaxDb; P30511; -.
PeptideAtlas; P30511; -.
PRIDE; P30511; -.
ProteomicsDB; 54704; -.
ProteomicsDB; 54705; -. [P30511-2]
ProteomicsDB; 54706; -. [P30511-3]
DNASU; 3134; -.
Ensembl; ENST00000259951; ENSP00000259951; ENSG00000204642. [P30511-3]
Ensembl; ENST00000334668; ENSP00000334263; ENSG00000204642. [P30511-1]
Ensembl; ENST00000359076; ENSP00000351977; ENSG00000206509. [P30511-2]
Ensembl; ENST00000376848; ENSP00000366044; ENSG00000229698. [P30511-2]
Ensembl; ENST00000376861; ENSP00000366057; ENSG00000204642. [P30511-1]
Ensembl; ENST00000383515; ENSP00000373007; ENSG00000137403. [P30511-2]
Ensembl; ENST00000420067; ENSP00000393535; ENSG00000235220. [P30511-2]
Ensembl; ENST00000434407; ENSP00000397376; ENSG00000204642. [P30511-2]
Ensembl; ENST00000440590; ENSP00000399835; ENSG00000237508. [P30511-2]
GeneID; 3134; -.
KEGG; hsa:3134; -.
UCSC; uc003nnm.5; human. [P30511-1]
CTD; 3134; -.
DisGeNET; 3134; -.
EuPathDB; HostDB:ENSG00000204642.13; -.
GeneCards; HLA-F; -.
HGNC; HGNC:4963; HLA-F.
MIM; 143110; gene.
neXtProt; NX_P30511; -.
OpenTargets; ENSG00000204642; -.
PharmGKB; PA35082; -.
eggNOG; ENOG410IUXN; Eukaryota.
eggNOG; ENOG4111K8F; LUCA.
GeneTree; ENSGT00940000153382; -.
HOGENOM; HOG000296917; -.
HOVERGEN; HBG016709; -.
InParanoid; P30511; -.
KO; K06751; -.
OMA; RITQRFY; -.
OrthoDB; 1390181at2759; -.
PhylomeDB; P30511; -.
TreeFam; TF336617; -.
Reactome; R-HSA-1236974; ER-Phagosome pathway.
Reactome; R-HSA-1236977; Endosomal/Vacuolar pathway.
Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
Reactome; R-HSA-877300; Interferon gamma signaling.
Reactome; R-HSA-909733; Interferon alpha/beta signaling.
Reactome; R-HSA-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
SIGNOR; P30511; -.
ChiTaRS; HLA-F; human.
GeneWiki; HLA-F; -.
GenomeRNAi; 3134; -.
PRO; PR:P30511; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000204642; Expressed in 237 organ(s), highest expression level in blood.
CleanEx; HS_HLA-F; -.
ExpressionAtlas; P30511; baseline and differential.
Genevisible; P30511; HS.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0031901; C:early endosome membrane; TAS:Reactome.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0042612; C:MHC class I protein complex; IEA:UniProtKB-KW.
GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0055038; C:recycling endosome membrane; TAS:Reactome.
GO; GO:0042605; F:peptide antigen binding; IBA:GO_Central.
GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
GO; GO:0046978; F:TAP1 binding; IPI:UniProtKB.
GO; GO:0046979; F:TAP2 binding; IPI:UniProtKB.
GO; GO:0002476; P:antigen processing and presentation of endogenous peptide antigen via MHC class Ib; IBA:GO_Central.
GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
GO; GO:0002480; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent; TAS:Reactome.
GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:Reactome.
GO; GO:0006955; P:immune response; IBA:GO_Central.
GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome.
GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IBA:GO_Central.
GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
GO; GO:0060337; P:type I interferon signaling pathway; TAS:Reactome.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 3.30.500.10; -; 1.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003006; Ig/MHC_CS.
InterPro; IPR003597; Ig_C1-set.
InterPro; IPR011161; MHC_I-like_Ag-recog.
InterPro; IPR037055; MHC_I-like_Ag-recog_sf.
InterPro; IPR011162; MHC_I/II-like_Ag-recog.
InterPro; IPR001039; MHC_I_a_a1/a2.
Pfam; PF07654; C1-set; 1.
Pfam; PF00129; MHC_I; 1.
PRINTS; PR01638; MHCCLASSI.
SMART; SM00407; IGc1; 1.
SUPFAM; SSF48726; SSF48726; 1.
SUPFAM; SSF54452; SSF54452; 1.
PROSITE; PS50835; IG_LIKE; 1.
PROSITE; PS00290; IG_MHC; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Disulfide bond; Endosome; Glycoprotein; Immunity; Lysosome; Membrane;
MHC I; Polymorphism; Reference proteome; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 21 {ECO:0000255}.
CHAIN 22 346 HLA class I histocompatibility antigen,
alpha chain F.
/FTId=PRO_0000018884.
TOPO_DOM 22 305 Extracellular. {ECO:0000255}.
TRANSMEM 306 329 Helical. {ECO:0000255}.
TOPO_DOM 330 346 Cytoplasmic. {ECO:0000255}.
DOMAIN 206 296 Ig-like C1-type. {ECO:0000255}.
REGION 22 111 Alpha-1.
REGION 112 203 Alpha-2.
REGION 204 295 Alpha-3.
REGION 296 305 Connecting peptide.
MOTIF 336 338 Sorting signal sequence; Golgi-retention
signal; ER-retention signal.
{ECO:0000269|PubMed:16709803}.
BINDING 91 91 Self-peptide antigen.
{ECO:0000269|PubMed:28636952}.
BINDING 105 105 Self-peptide antigen.
{ECO:0000269|PubMed:28636952}.
BINDING 164 164 Self-peptide antigen.
{ECO:0000269|PubMed:28636952}.
BINDING 168 168 Self-peptide antigen.
{ECO:0000269|PubMed:28636952}.
BINDING 176 176 Self-peptide antigen.
{ECO:0000269|PubMed:28636952}.
CARBOHYD 107 107 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
DISULFID 122 185 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:28636952}.
DISULFID 224 280 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:28636952}.
VAR_SEQ 204 295 Missing (in isoform 2).
{ECO:0000303|PubMed:14705989}.
/FTId=VSP_038846.
VAR_SEQ 346 346 V -> AYSVVSGNLMITWWSSLFLLGVLFQGYLGCLRSHSV
LGRRKVGDMWILFFLWLWTSFNTAFLALQSLRFGFGFRRGR
SFLLRSWHHLMKRVQIKIFD (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_040349.
VARIANT 13 13 A -> V (in dbSNP:rs17875379).
/FTId=VAR_056525.
VARIANT 71 71 P -> Q (in dbSNP:rs17875380).
/FTId=VAR_056526.
VARIANT 272 272 P -> S (in dbSNP:rs1736924).
{ECO:0000269|PubMed:10727083,
ECO:0000269|PubMed:14574404,
ECO:0000269|PubMed:14705989,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:16570139,
ECO:0000269|PubMed:1688605,
ECO:0000269|PubMed:1707659,
ECO:0000269|Ref.6, ECO:0000269|Ref.7}.
/FTId=VAR_018327.
MUTAGEN 83 83 W->R: Impairs peptide binding.
{ECO:0000269|PubMed:28636952}.
MUTAGEN 336 338 RNR->AAA: Impairs the interaction with
14-3-3 proteins.
{ECO:0000269|PubMed:16709803}.
MUTAGEN 336 338 RNR->GKG: Impairs the anterograde ER-to-
Golgi transport.
{ECO:0000269|PubMed:16709803}.
MUTAGEN 346 346 V->S: Impairs the anterograde ER-to-Golgi
transport. {ECO:0000269|PubMed:16709803}.
MUTAGEN 346 346 Missing: Impairs the interaction with
coat protein complex II; impairs the
anterograde ER-to-Golgi transport.
{ECO:0000269|PubMed:16709803}.
STRAND 24 35 {ECO:0000244|PDB:5IUE}.
TURN 36 38 {ECO:0000244|PDB:5IUE}.
STRAND 39 49 {ECO:0000244|PDB:5IUE}.
STRAND 52 58 {ECO:0000244|PDB:5IUE}.
STRAND 61 63 {ECO:0000244|PDB:5IUE}.
STRAND 67 70 {ECO:0000244|PDB:5IUE}.
HELIX 71 73 {ECO:0000244|PDB:5IUE}.
HELIX 78 105 {ECO:0000244|PDB:5IUE}.
STRAND 115 124 {ECO:0000244|PDB:5IUE}.
STRAND 128 139 {ECO:0000244|PDB:5IUE}.
STRAND 142 147 {ECO:0000244|PDB:5IUE}.
STRAND 154 158 {ECO:0000244|PDB:5IUE}.
HELIX 161 170 {ECO:0000244|PDB:5IUE}.
HELIX 173 182 {ECO:0000244|PDB:5IUE}.
HELIX 184 195 {ECO:0000244|PDB:5IUE}.
HELIX 197 200 {ECO:0000244|PDB:5IUE}.
STRAND 207 214 {ECO:0000244|PDB:5IUE}.
STRAND 216 232 {ECO:0000244|PDB:5IUE}.
STRAND 235 240 {ECO:0000244|PDB:5IUE}.
TURN 246 248 {ECO:0000244|PDB:5KNM}.
STRAND 249 251 {ECO:0000244|PDB:5IUE}.
STRAND 258 260 {ECO:0000244|PDB:5IUE}.
STRAND 262 271 {ECO:0000244|PDB:5IUE}.
HELIX 275 277 {ECO:0000244|PDB:5IUE}.
STRAND 278 283 {ECO:0000244|PDB:5IUE}.
STRAND 287 289 {ECO:0000244|PDB:5IUE}.
STRAND 291 293 {ECO:0000244|PDB:5IUE}.
SEQUENCE 346 AA; 39062 MW; D4782968A67E9B7D CRC64;
MAPRSLLLLL SGALALTDTW AGSHSLRYFS TAVSRPGRGE PRYIAVEYVD DTQFLRFDSD
AAIPRMEPRE PWVEQEGPQY WEWTTGYAKA NAQTDRVALR NLLRRYNQSE AGSHTLQGMN
GCDMGPDGRL LRGYHQHAYD GKDYISLNED LRSWTAADTV AQITQRFYEA EEYAEEFRTY
LEGECLELLR RYLENGKETL QRADPPKAHV AHHPISDHEA TLRCWALGFY PAEITLTWQR
DGEEQTQDTE LVETRPAGDG TFQKWAAVVV PPGEEQRYTC HVQHEGLPQP LILRWEQSPQ
PTIPIVGIVA GLVVLGAVVT GAVVAAVMWR KKSSDRNRGS YSQAAV


Related products :

Catalog number Product name Quantity
E1386h ELISA HLA class I histocompatibility antigen, alpha chain G,HLA G antigen,HLA-6.0,HLAG,HLA-G,Homo sapiens,Human,MHC class I antigen G 96T
E1386h ELISA kit HLA class I histocompatibility antigen, alpha chain G,HLA G antigen,HLA-6.0,HLAG,HLA-G,Homo sapiens,Human,MHC class I antigen G 96T
U1386h CLIA HLA class I histocompatibility antigen, alpha chain G,HLA G antigen,HLA-6.0,HLAG,HLA-G,Homo sapiens,Human,MHC class I antigen G 96T
E1752h ELISA HLA class I histocompatibility antigen, alpha chain E,HLA-6.2,HLAE,HLA-E,Homo sapiens,Human,MHC class I antigen E 96T
U1752h CLIA HLA class I histocompatibility antigen, alpha chain E,HLA-6.2,HLAE,HLA-E,Homo sapiens,Human,MHC class I antigen E 96T
E1752h ELISA kit HLA class I histocompatibility antigen, alpha chain E,HLA-6.2,HLAE,HLA-E,Homo sapiens,Human,MHC class I antigen E 96T
EIAAB11895 HLA class II histocompatibility antigen, DR alpha chain,HLA-DRA,HLA-DRA1,Homo sapiens,Human,MHC class II antigen DRA
EIAAB11449 DMA,HLA class II histocompatibility antigen, DM alpha chain,HLA-DMA,Homo sapiens,Human,MHC class II antigen DMA,Really interesting new gene 6 protein,RING6
EIAAB11884 DX alpha chain,HLA class II histocompatibility antigen, DQ alpha 2 chain,HLA class II histocompatibility antigen, DQ(6) alpha chain,HLA-DQA1,HLA-DQA2,HLA-DXA,Homo sapiens,Human,MHC class II DQA2
EIAAB11729 HLA class II histocompatibility antigen, DP beta 1 chain,HLA class II histocompatibility antigen, DP(W4) beta chain,HLA-DP1B,HLA-DPB1,Homo sapiens,Human,MHC class II antigen DPB1
EIAAB11639 HLA class II histocompatibility antigen, DO alpha chain,HLA-DNA,HLA-DOA,HLA-DZA,Homo sapiens,Human,MHC class II antigen DOA,MHC DN-alpha,MHC DZ alpha
EIAAB11886 HLA class II histocompatibility antigen, DQ beta 2 chain,HLA class II histocompatibility antigen, DX beta chain,HLA-DQB2,HLA-DXB,Homo sapiens,Human,MHC class II antigen DQB2
EIAAB11453 DMB,HLA class II histocompatibility antigen, DM beta chain,HLA-DMB,Homo sapiens,Human,MHC class II antigen DMB,Really interesting new gene 7 protein,RING7
EIAAB11640 HLA class II histocompatibility antigen, DO beta chain,HLA-DOB,Homo sapiens,Human,MHC class II antigen DOB
U1702m CLIA H-2 class I histocompatibility antigen, Q7 alpha chain,H2-Q7,Mouse,Mus musculus,QA-2 antigen 96T
E1702m ELISA kit H-2 class I histocompatibility antigen, Q7 alpha chain,H2-Q7,Mouse,Mus musculus,QA-2 antigen 96T
E1702m ELISA H-2 class I histocompatibility antigen, Q7 alpha chain,H2-Q7,Mouse,Mus musculus,QA-2 antigen 96T
E1555m ELISA H-2 class I histocompatibility antigen, TLA(B) alpha chain,H2-T3,MHC thymus leukemia antigen,Mouse,Mus musculus 96T
U1555m CLIA H-2 class I histocompatibility antigen, TLA(B) alpha chain,H2-T3,MHC thymus leukemia antigen,Mouse,Mus musculus 96T
E1555m ELISA kit H-2 class I histocompatibility antigen, TLA(B) alpha chain,H2-T3,MHC thymus leukemia antigen,Mouse,Mus musculus 96T
EIAAB11885 HLA class II histocompatibility antigen, DQ beta 1 chain,HLA-DQB,HLA-DQB1,Homo sapiens,Human,MHC class II antigen DQB1
EIAAB11903 HLA class II histocompatibility antigen, DR beta 3 chain,HLA-DRB3,Homo sapiens,Human,MHC class II antigen DRB3
EIAAB11904 HLA class II histocompatibility antigen, DR beta 4 chain,HLA-DRB4,Homo sapiens,Human,MHC class II antigen DRB4
EIAAB11726 DP(W3),DP(W4),HLA class II histocompatibility antigen, DP alpha 1 chain,HLA-DP1A,HLA-DPA1,HLASB,HLA-SB alpha chain,Homo sapiens,Human,MHC class II DP3-alpha,MHC class II DPA1
20-321-175233 MHC CLASS II - MONOCLONAL ANTIBODY TO RAT MHC CLASS II; MHC class II antigen; MHC class II histocompatibility antigen SLA-DQB1 Monoclonal 0.1 mg


https://antibody-antibodies.com/ | https://gentaur.com/ | https://gen-script.com/ | https://diagenox.com/ | https://clonagen.com/ | http://gentaursearch.com/ | http://gentaurpub.com/ | https://gentaur-online.com/ | http://anti-anti-pdf.com/ | http://gentaur-worldwide.com/

 

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