HLA-DPA1
entrez
3113
canonical
uniprot
P20036
canonical
ensembl
ENSG00000168384
resolver
ensembl
ENSG00000206291
resolver
ensembl
ENSG00000224103
resolver
ensembl
ENSG00000228163
resolver
ensembl
ENSG00000229685
resolver
ensembl
ENSG00000231389
resolver
ensembl
ENSG00000235844
resolver
ensembl
ENSG00000236177
resolver
ensp
ENSP00000363941
resolver
ensp
ENSP00000372711
resolver
ensp
ENSP00000393566
resolver
ensp
ENSP00000397139
resolver
ensp
ENSP00000397587
resolver
ensp
ENSP00000405838
resolver
ensp
ENSP00000406250
resolver
ensp
ENSP00000427429
resolver
ensp
ENSP00000509163
resolver
ensp
ENSP00000594002
resolver
enst
ENST00000374808
resolver
enst
ENST00000383224
resolver
enst
ENST00000415247
resolver
enst
ENST00000419277
resolver
enst
ENST00000422504
resolver
enst
ENST00000443117
resolver
enst
ENST00000454805
resolver
enst
ENST00000515317
resolver
enst
ENST00000692443
resolver
enst
ENST00000923943
resolver
genesymbol
HLA-DPA1
resolver
genesymbol_syn
HLA-DP1A
resolver
genesymbol_syn
HLASB
resolver
hgnc
HGNC:4938
resolver
uniprot
A9YWH7
resolver
uniprot
B9UKH4
resolver
uniprot
O19722
resolver
uniprot
O46883
resolver
uniprot
P01905
resolver
uniprot
P79554
resolver
uniprot
Q2Q060
resolver
uniprot
Q2Q061
resolver
uniprot
Q5EY03
resolver
uniprot
Q5STP1
resolver
uniprot
Q6DQK4
resolver
uniprot
Q9BCQ1
resolver
uniprot
Q9TPX3
resolver
uniprot
Q9XS10
resolver
uniprot_entry
DPA1_HUMAN
resolver
uniprot_sec
A9YWH7
resolver
uniprot_sec
B9UKH4
resolver
uniprot_sec
O19722
resolver
uniprot_sec
O46883
resolver
uniprot_sec
P01905
resolver
uniprot_sec
P79554
resolver
uniprot_sec
Q2Q060
resolver
uniprot_sec
Q2Q061
resolver
uniprot_sec
Q5EY03
resolver
uniprot_sec
Q5STP1
resolver
uniprot_sec
Q6DQK4
resolver
uniprot_sec
Q9BCQ1
resolver
uniprot_sec
Q9TPX3
resolver
uniprot_sec
Q9XS10
resolver
amino_acid_sequence
MRPEDRMFHIRAVILRALSLAFLLSLRGAGAIKADHVSTYAAFVQTHRPTGEFMFEFDEDEMFYVDLDKKETVWHLEEFGQAFSFEAQGGLANIAILNNNLNTLIQRSNHTQATNDPPEVTVFPKEPVELGQPNTLICHIDKFFPPVLNVTWLCNGELVTEGVAESLFLPRTDYSFHKFHYLTFVPSAEDFYDCRVEHWGLDQPLLKHWEAQEPIQMPETTETVLCALGLVLGLVGIIVGTVLIIKSLRSGHDPRAQGTL
uniprot
proteins
function
FUNCTION: Binds peptides derived from antigens that access the endocytic route of antigen presenting cells (APC) and presents them on the cell surface for recognition by the CD4 T-cells. The peptide binding cleft accommodates peptides of 10-30 residues. The peptides presented by MHC class II molecules are generated mostly by degradation of proteins that access the endocytic route, where they are processed by lysosomal proteases and other hydrolases. Exogenous antigens that have been endocytosed by the APC are thus readily available for presentation via MHC II molecules, and for this reason this antigen presentation pathway is usually referred to as exogenous. As membrane proteins on their way to degradation in lysosomes as part of their normal turn-over are also contained in the endosomal/lysosomal compartments, exogenous antigens must compete with those derived from endogenous components. Autophagy is also a source of endogenous peptides, autophagosomes constitutively fuse with MHC class II loading compartments. In addition to APCs, other cells of the gastrointestinal tract, such as epithelial cells, express MHC class II molecules and CD74 and act as APCs, which is an unusual trait of the GI tract. To produce a MHC class II molecule that presents an antigen, three MHC class II molecules (heterodimers of an alpha and a beta chain) associate with a CD74 trimer in the ER to form a heterononamer. Soon after the entry of this complex into the endosomal/lysosomal system where antigen processing occurs, CD74 undergoes a sequential degradation by various proteases, including CTSS and CTSL, leaving a small fragment termed CLIP (class-II-associated invariant chain peptide). The removal of CLIP is facilitated by HLA-DM via direct binding to the alpha-beta-CLIP complex so that CLIP is released. HLA-DM stabilizes MHC class II molecules until primary high affinity antigenic peptides are bound. The MHC II molecule bound to a peptide is then transported to the cell membrane surface. In B-cells, the interaction between HLA-DM and MHC class II molecules is regulated by HLA-DO. Primary dendritic cells (DCs) also to express HLA-DO. Lysosomal microenvironment has been implicated in the regulation of antigen loading into MHC II molecules, increased acidification produces increased proteolysis and efficient peptide loading.
uniprot
proteins
mass_dalton
29381
uniprot
proteins
protein_family
MHC class II family
uniprot
proteins
pubmed
11019928
uniprot
proteins
pubmed
11684289
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15663751
uniprot
proteins
pubmed
17241953
uniprot
proteins
pubmed
18046453
uniprot
proteins
pubmed
18380777
uniprot
proteins
pubmed
18489436
uniprot
proteins
pubmed
18838095
uniprot
proteins
pubmed
19092054
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
19533806
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
2461352
uniprot
proteins
pubmed
2997750
uniprot
proteins
pubmed
3036829
uniprot
proteins
pubmed
6300884
uniprot
proteins
pubmed
6584734
uniprot
proteins
pubmed
7725312
uniprot
proteins
pubmed
7806277
uniprot
proteins
pubmed
8598037
uniprot
proteins
pubmed
8988544
uniprot
proteins
pubmed
9234495
uniprot
proteins
pubmed
9694359
uniprot
proteins
sequence_length
260
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Endoplasmic reticulum membrane; Single-pass type I membrane protein. Golgi apparatus, trans-Golgi network membrane; Single-pass type I membrane protein. Endosome membrane; Single-pass type I membrane protein. Lysosome membrane; Single-pass type I membrane protein. Note=The MHC class II complex transits through a number of intracellular compartments in the endocytic pathway until it reaches the cell membrane for antigen presentation.
uniprot
proteins
transmembrane_region
TRANSMEM 223..245; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins