Entry
stringlengths 6
10
| Entry Name
stringlengths 5
11
| Sequence
stringlengths 2
35.2k
| EC number
stringlengths 7
118
⌀ | Cofactor
stringlengths 38
1.77k
⌀ | Gene Ontology (biological process)
stringlengths 18
11.3k
⌀ | Gene Ontology (cellular component)
stringlengths 17
1.75k
⌀ | Gene Ontology (molecular function)
stringlengths 24
2.09k
⌀ | Pfam
stringlengths 8
232
⌀ | Gene3D
stringlengths 10
250
⌀ | Protein families
stringlengths 9
237
⌀ | Post-translational modification
stringlengths 16
8.52k
⌀ | Subcellular location [CC]
stringlengths 29
6.18k
⌀ | Catalytic activity
stringlengths 64
35.7k
⌀ | Kinetics
stringlengths 69
11.7k
⌀ | Pathway
stringlengths 27
908
⌀ | pH dependence
stringlengths 64
955
⌀ | Temperature dependence
stringlengths 70
1.16k
⌀ | Function [CC]
stringlengths 17
15.3k
⌀ | Organism
stringlengths 8
196
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
P01599
|
KV117_HUMAN
|
MDMRVPAQLLGLLLLWFPGARCDIQMTQSPSSLSASVGDRVTITCRASQGIRNDLGWYQQKPGKAPKRLIYAASSLQSGVPSRFSGSGSGTEFTLTISSLQPEDFATYYCLQHNSYP
| null | null |
adaptive immune response [GO:0002250]; immune response [GO:0006955]
|
blood microparticle [GO:0072562]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; immunoglobulin complex [GO:0019814]; plasma membrane [GO:0005886]
|
antigen binding [GO:0003823]
|
PF07686;
|
2.60.40.10;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
| null | null | null | null | null |
FUNCTION: V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition (PubMed:24600447). Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268). {ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414, ECO:0000303|PubMed:24600447}.
|
Homo sapiens (Human)
|
P01602
|
KV105_HUMAN
|
MDMRVPAQLLGLLLLWLPGAKCDIQMTQSPSTLSASVGDRVTITCRASQSISSWLAWYQQKPGKAPKLLIYKASSLESGVPSRFSGSGSGTEFTLTISSLQPDDFATYYCQQYNSYS
| null | null |
adaptive immune response [GO:0002250]; immune response [GO:0006955]
|
blood microparticle [GO:0072562]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; immunoglobulin complex [GO:0019814]; plasma membrane [GO:0005886]
|
antigen binding [GO:0003823]
|
PF07686;
|
2.60.40.10;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
| null | null | null | null | null |
FUNCTION: V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition (PubMed:24600447). Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268). {ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414, ECO:0000303|PubMed:24600447}.
|
Homo sapiens (Human)
|
P01615
|
KVD28_HUMAN
|
MRLPAQLLGLLMLWVSGSSGDIVMTQSPLSLPVTPGEPASISCRSSQSLLHSNGYNYLDWYLQKPGQSPQLLIYLGSNRASGVPDRFSGSGSGTDFTLKISRVEAEDVGVYYCMQALQTP
| null | null |
adaptive immune response [GO:0002250]; immune response [GO:0006955]
|
blood microparticle [GO:0072562]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; immunoglobulin complex [GO:0019814]; plasma membrane [GO:0005886]
|
antigen binding [GO:0003823]
|
PF07686;
|
2.60.40.10;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
| null | null | null | null | null |
FUNCTION: V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition (PubMed:24600447). Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268). {ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414, ECO:0000303|PubMed:24600447}.
|
Homo sapiens (Human)
|
P01619
|
KV320_HUMAN
|
METPAQLLFLLLLWLPDTTGEIVLTQSPGTLSLSPGERATLSCRASQSVSSSYLAWYQQKPGQAPRLLIYGASSRATGIPDRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYGSSP
| null | null |
adaptive immune response [GO:0002250]; antibacterial humoral response [GO:0019731]; glomerular filtration [GO:0003094]; immune response [GO:0006955]
|
blood microparticle [GO:0072562]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; monomeric IgA immunoglobulin complex [GO:0071748]; pentameric IgM immunoglobulin complex [GO:0071756]; plasma membrane [GO:0005886]; secretory IgA immunoglobulin complex [GO:0071751]
|
antigen binding [GO:0003823]
|
PF07686;
|
2.60.40.10;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
| null | null | null | null | null |
FUNCTION: V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition (PubMed:24600447). Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268). {ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414, ECO:0000303|PubMed:24600447}.
|
Homo sapiens (Human)
|
P01699
|
LV144_HUMAN
|
MASFPLLLTLLTHCAGSWAQSVLTQPPSASGTPGQRVTISCSGSSSNIGSNTVNWYQQLPGTAPKLLIYSNNQRPSGVPDRFSGSKSGTSASLAISGLQSEDEADYYCAAWDDSLNG
| null | null |
adaptive immune response [GO:0002250]; immune response [GO:0006955]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]; immunoglobulin complex [GO:0019814]; plasma membrane [GO:0005886]
|
antigen binding [GO:0003823]
|
PF07686;
|
2.60.40.10;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
| null | null | null | null | null |
FUNCTION: V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition (PubMed:24600447). Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268). {ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414, ECO:0000303|PubMed:24600447}.
|
Homo sapiens (Human)
|
P01700
|
LV147_HUMAN
|
MAGFPLLLTLLTHCAGSWAQSVLTQPPSASGTPGQRVTISCSGSSSNIGSNYVYWYQQLPGTAPKLLIYSNNQRPSGVPDRFSGSKSGTSASLAISGLRSEDEADYYCAAWDDSLSG
| null | null |
adaptive immune response [GO:0002250]; immune response [GO:0006955]
|
blood microparticle [GO:0072562]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; immunoglobulin complex [GO:0019814]; plasma membrane [GO:0005886]
|
antigen binding [GO:0003823]
|
PF07686;
|
2.60.40.10;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
| null | null | null | null | null |
FUNCTION: V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition (PubMed:24600447). Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268). {ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414, ECO:0000303|PubMed:24600447}.
|
Homo sapiens (Human)
|
P01701
|
LV151_HUMAN
|
MTCSPLLLTLLIHCTGSWAQSVLTQPPSVSAAPGQKVTISCSGSSSNIGNNYVSWYQQLPGTAPKLLIYDNNKRPSGIPDRFSGSKSGTSATLGITGLQTGDEADYYCGTWDSSLSA
| null | null |
adaptive immune response [GO:0002250]; immune response [GO:0006955]
|
extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; immunoglobulin complex [GO:0019814]; plasma membrane [GO:0005886]
|
antigen binding [GO:0003823]
|
PF07686;
|
2.60.40.10;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
| null | null | null | null | null |
FUNCTION: V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition (PubMed:24600447). Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268). {ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414, ECO:0000303|PubMed:24600447}.
|
Homo sapiens (Human)
|
P01703
|
LV140_HUMAN
|
MAWSPLLLTLLAHCTGSWAQSVLTQPPSVSGAPGQRVTISCTGSSSNIGAGYDVHWYQQLPGTAPKLLIYGNSNRPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYDSSLSG
| null | null |
adaptive immune response [GO:0002250]; immune response [GO:0006955]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]; immunoglobulin complex [GO:0019814]; plasma membrane [GO:0005886]
|
antigen binding [GO:0003823]
|
PF07686;
|
2.60.40.10;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
| null | null | null | null | null |
FUNCTION: V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition (PubMed:24600447). Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268). {ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414, ECO:0000303|PubMed:24600447}.
|
Homo sapiens (Human)
|
P01704
|
LV214_HUMAN
|
MAWALLLLTLLTQGTGSWAQSALTQPASVSGSPGQSITISCTGTSSDVGGYNYVSWYQQHPGKAPKLMIYEVSNRPSGVSNRFSGSKSGNTASLTISGLQAEDEADYYCSSYTSSSTLHS
| null | null |
adaptive immune response [GO:0002250]; immune response [GO:0006955]
|
extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; immunoglobulin complex [GO:0019814]; plasma membrane [GO:0005886]
|
antigen binding [GO:0003823]
|
PF07686;
|
2.60.40.10;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
| null | null | null | null | null |
FUNCTION: V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition (PubMed:24600447). Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268). {ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414, ECO:0000303|PubMed:24600447}.
|
Homo sapiens (Human)
|
P01705
|
LV223_HUMAN
|
MAWALLLLTLLTQDTGSWAQSALTQPASVSGSPGQSITISCTGTSSDVGSYNLVSWYQQHPGKAPKLMIYEGSKRPSGVSNRFSGSKSGNTASLTISGLQAEDEADYYCCSYA
| null | null |
adaptive immune response [GO:0002250]; immune response [GO:0006955]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]; immunoglobulin complex [GO:0019814]; plasma membrane [GO:0005886]
|
antigen binding [GO:0003823]
|
PF07686;
|
2.60.40.10;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
| null | null | null | null | null |
FUNCTION: V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition (PubMed:24600447). Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268). {ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414, ECO:0000303|PubMed:24600447}.
|
Homo sapiens (Human)
|
P01706
|
LV211_HUMAN
|
MAWALLLLSLLTQGTGSWAQSALTQPRSVSGSPGQSVTISCTGTSSDVGGYNYVSWYQQHPGKAPKLMIYDVSKRPSGVPDRFSGSKSGNTASLTISGLQAEDEADYYCCSYAGSYTFH
| null | null |
adaptive immune response [GO:0002250]; immune response [GO:0006955]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]; immunoglobulin complex [GO:0019814]; plasma membrane [GO:0005886]
|
antigen binding [GO:0003823]
|
PF07686;
|
2.60.40.10;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
| null | null | null | null | null |
FUNCTION: V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition (PubMed:24600447). Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268). {ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414, ECO:0000303|PubMed:24600447}.
|
Homo sapiens (Human)
|
P01709
|
LV208_HUMAN
|
MAWALLLLTLLTQGTGSWAQSALTQPPSASGSPGQSVTISCTGTSSDVGGYNYVSWYQQHPGKAPKLMIYEVSKRPSGVPDRFSGSKSGNTASLTVSGLQAEDEADYYCSSYAGSNNF
| null | null |
adaptive immune response [GO:0002250]; immune response [GO:0006955]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]; immunoglobulin complex [GO:0019814]; plasma membrane [GO:0005886]
|
antigen binding [GO:0003823]
|
PF07686;
|
2.60.40.10;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
| null | null | null | null | null |
FUNCTION: V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition (PubMed:24600447). Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268). {ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414, ECO:0000303|PubMed:24600447}.
|
Homo sapiens (Human)
|
P01721
|
LV657_HUMAN
|
MAWAPLLLTLLAHCTGSWANFMLTQPHSVSESPGKTVTISCTGSSGSIASNYVQWYQQRPGSAPTTVIYEDNQRPSGVPDRFSGSIDSSSNSASLTISGLKTEDEADYYCQSYDSSN
| null | null |
adaptive immune response [GO:0002250]; immune response [GO:0006955]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]; immunoglobulin complex [GO:0019814]; plasma membrane [GO:0005886]
|
antigen binding [GO:0003823]
|
PF07686;
|
2.60.40.10;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
| null | null | null | null | null |
FUNCTION: V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition (PubMed:24600447). Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268). {ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414, ECO:0000303|PubMed:24600447}.
|
Homo sapiens (Human)
|
P01730
|
CD4_HUMAN
|
MNRGVPFRHLLLVLQLALLPAATQGKKVVLGKKGDTVELTCTASQKKSIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRADSRRSLWDQGNFPLIIKNLKIEDSDTYICEVEDQKEEVQLLVFGLTANSDTHLLQGQSLTLTLESPPGSSPSVQCRSPRGKNIQGGKTLSVSQLELQDSGTWTCTVLQNQKKVEFKIDIVVLAFQKASSIVYKKEGEQVEFSFPLAFTVEKLTGSGELWWQAERASSSKSWITFDLKNKEVSVKRVTQDPKLQMGKKLPLHLTLPQALPQYAGSGNLTLALEAKTGKLHQEVNLVVMRATQLQKNLTCEVWGPTSPKLMLSLKLENKEAKVSKREKAVWVLNPEAGMWQCLLSDSGQVLLESNIKVLPTWSTPVQPMALIVLGGVAGLLLFIGLGIFFCVRCRHRRRQAERMSQIKRLLSEKKTCQCPHRFQKTCSPI
| null | null |
adaptive immune response [GO:0002250]; calcium-mediated signaling [GO:0019722]; cell adhesion [GO:0007155]; cell surface receptor signaling pathway [GO:0007166]; cellular response to granulocyte macrophage colony-stimulating factor stimulus [GO:0097011]; defense response to Gram-negative bacterium [GO:0050829]; enzyme-linked receptor protein signaling pathway [GO:0007167]; helper T cell enhancement of adaptive immune response [GO:0035397]; immune response [GO:0006955]; interleukin-15-mediated signaling pathway [GO:0035723]; macrophage differentiation [GO:0030225]; maintenance of protein location in cell [GO:0032507]; positive regulation of calcium-mediated signaling [GO:0050850]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of interleukin-2 production [GO:0032743]; positive regulation of kinase activity [GO:0033674]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of monocyte differentiation [GO:0045657]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of protein kinase activity [GO:0045860]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of T cell activation [GO:0050870]; positive regulation of viral entry into host cell [GO:0046598]; regulation of calcium ion transport [GO:0051924]; regulation of T cell activation [GO:0050863]; signal transduction [GO:0007165]; T cell activation [GO:0042110]; T cell differentiation [GO:0030217]; T cell selection [GO:0045058]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]
|
clathrin-coated endocytic vesicle membrane [GO:0030669]; early endosome [GO:0005769]; endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum membrane [GO:0005789]; external side of plasma membrane [GO:0009897]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]; T cell receptor complex [GO:0042101]
|
coreceptor activity [GO:0015026]; enzyme binding [GO:0019899]; extracellular matrix structural constituent [GO:0005201]; identical protein binding [GO:0042802]; interleukin-16 binding [GO:0042011]; interleukin-16 receptor activity [GO:0042012]; lipid binding [GO:0008289]; MHC class II protein binding [GO:0042289]; MHC class II protein complex binding [GO:0023026]; protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; protein tyrosine kinase binding [GO:1990782]; signaling receptor activity [GO:0038023]; transmembrane signaling receptor activity [GO:0004888]; virus receptor activity [GO:0001618]; zinc ion binding [GO:0008270]
|
PF05790;PF09191;PF00047;PF12104;
|
2.60.40.10;1.20.5.900;
| null |
PTM: Palmitoylation and association with LCK contribute to the enrichment of CD4 in lipid rafts. {ECO:0000269|PubMed:1618861}.; PTM: Phosphorylated by PKC; phosphorylation at Ser-433 plays an important role for CD4 internalization. {ECO:0000269|PubMed:2105883, ECO:0000269|PubMed:2512251}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12089508, ECO:0000269|PubMed:12517957, ECO:0000269|PubMed:2823150, ECO:0000269|PubMed:2990730}; Single-pass type I membrane protein {ECO:0000269|PubMed:12517957, ECO:0000269|PubMed:15340161, ECO:0000269|PubMed:1708753}. Note=Localizes to lipid rafts (PubMed:12517957, PubMed:9168119). Removed from plasma membrane by HIV-1 Nef protein that increases clathrin-dependent endocytosis of this antigen to target it to lysosomal degradation. Cell surface expression is also down-modulated by HIV-1 Envelope polyprotein gp160 that interacts with, and sequesters CD4 in the endoplasmic reticulum.
| null | null | null | null | null |
FUNCTION: Integral membrane glycoprotein that plays an essential role in the immune response and serves multiple functions in responses against both external and internal offenses. In T-cells, functions primarily as a coreceptor for MHC class II molecule:peptide complex. The antigens presented by class II peptides are derived from extracellular proteins while class I peptides are derived from cytosolic proteins. Interacts simultaneously with the T-cell receptor (TCR) and the MHC class II presented by antigen presenting cells (APCs). In turn, recruits the Src kinase LCK to the vicinity of the TCR-CD3 complex. LCK then initiates different intracellular signaling pathways by phosphorylating various substrates ultimately leading to lymphokine production, motility, adhesion and activation of T-helper cells. In other cells such as macrophages or NK cells, plays a role in differentiation/activation, cytokine expression and cell migration in a TCR/LCK-independent pathway. Participates in the development of T-helper cells in the thymus and triggers the differentiation of monocytes into functional mature macrophages. {ECO:0000269|PubMed:16951326, ECO:0000269|PubMed:24942581, ECO:0000269|PubMed:2823150, ECO:0000269|PubMed:7604010}.; FUNCTION: (Microbial infection) Primary receptor for human immunodeficiency virus-1 (HIV-1) (PubMed:12089508, PubMed:16331979, PubMed:2214026, PubMed:9641677). Down-regulated by HIV-1 Vpu (PubMed:17346169). Acts as a receptor for Human Herpes virus 7/HHV-7 (PubMed:7909607). {ECO:0000269|PubMed:12089508, ECO:0000269|PubMed:16331979, ECO:0000269|PubMed:17346169, ECO:0000269|PubMed:2214026, ECO:0000269|PubMed:7909607, ECO:0000269|PubMed:9641677}.
|
Homo sapiens (Human)
|
P01731
|
CD8A_MOUSE
|
MASPLTRFLSLNLLLLGESIILGSGEAKPQAPELRIFPKKMDAELGQKVDLVCEVLGSVSQGCSWLFQNSSSKLPQPTFVVYMASSHNKITWDEKLNSSKLFSAMRDTNNKYVLTLNKFSKENEGYYFCSVISNSVMYFSSVVPVLQKVNSTTTKPVLRTPSPVHPTGTSQPQRPEDCRPRGSVKGTGLDFACDIYIWAPLAGICVALLLSLIITLICYHRSRKRVCKCPRPLVRQEGKPRPSEKIV
| null | null |
adaptive immune response [GO:0002250]; calcium-mediated signaling [GO:0019722]; cell surface receptor signaling pathway [GO:0007166]; cytotoxic T cell differentiation [GO:0045065]; defense response to virus [GO:0051607]; positive regulation of calcium-mediated signaling [GO:0050850]; T cell activation [GO:0042110]; T cell mediated immunity [GO:0002456]; T cell receptor signaling pathway [GO:0050852]
|
cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]
|
identical protein binding [GO:0042802]; protein kinase binding [GO:0019901]
|
PF07686;
|
2.60.40.10;
| null |
PTM: Palmitoylated, but association with CD8B seems to be more important for the enrichment of CdD8A in lipid rafts. {ECO:0000250|UniProtKB:P01732}.; PTM: Phosphorylated in cytotoxic T-lymphocytes (CTLs) following activation. {ECO:0000269|PubMed:2512251}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P01732}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P01732}. Note=Cd8a localizes to lipid rafts only when associated with its partner Cd8b. {ECO:0000250|UniProtKB:P01732}.
| null | null | null | null | null |
FUNCTION: Integral membrane glycoprotein that plays an essential role in the immune response and serves multiple functions in responses against both external and internal offenses. In T-cells, functions primarily as a coreceptor for MHC class I molecule:peptide complex. The antigens presented by class I peptides are derived from cytosolic proteins while class II derived from extracellular proteins. Interacts simultaneously with the T-cell receptor (TCR) and the MHC class I proteins presented by antigen presenting cells (APCs). In turn, recruits the Src kinase LCK to the vicinity of the TCR-CD3 complex. LCK then initiates different intracellular signaling pathways by phosphorylating various substrates ultimately leading to lymphokine production, motility, adhesion and activation of cytotoxic T-lymphocytes (CTLs). This mechanism enables CTLs to recognize and eliminate infected cells and tumor cells. In NK-cells, the presence of CD8A homodimers at the cell surface provides a survival mechanism allowing conjugation and lysis of multiple target cells. CD8A homodimer molecules also promote the survival and differentiation of activated lymphocytes into memory CD8 T-cells. {ECO:0000250|UniProtKB:P01732, ECO:0000269|PubMed:15105501, ECO:0000269|PubMed:1673361}.
|
Mus musculus (Mouse)
|
P01732
|
CD8A_HUMAN
|
MALPVTALLLPLALLLHAARPSQFRVSPLDRTWNLGETVELKCQVLLSNPTSGCSWLFQPRGAAASPTFLLYLSQNKPKAAEGLDTQRFSGKRLGDTFVLTLSDFRRENEGYYFCSALSNSIMYFSHFVPVFLPAKPTTTPAPRPPTPAPTIASQPLSLRPEACRPAAGGAVHTRGLDFACDIYIWAPLAGTCGVLLLSLVITLYCNHRNRRRVCKCPRPVVKSGDKPSLSARYV
| null | null |
adaptive immune response [GO:0002250]; antigen processing and presentation [GO:0019882]; cell surface receptor signaling pathway [GO:0007166]; cytotoxic T cell differentiation [GO:0045065]; immune response [GO:0006955]; T cell activation [GO:0042110]; T cell mediated immunity [GO:0002456]; T cell receptor signaling pathway [GO:0050852]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]
|
external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; plasma membrane [GO:0005886]; plasma membrane raft [GO:0044853]; receptor complex [GO:0043235]; T cell receptor complex [GO:0042101]
|
coreceptor activity [GO:0015026]; MHC class I protein binding [GO:0042288]; MHC class I protein complex binding [GO:0023024]
|
PF07686;
|
2.60.40.10;
| null |
PTM: Palmitoylated, but association with CD8B seems to be more important for the enrichment of CD8A in lipid rafts. {ECO:0000269|PubMed:17341584}.; PTM: O-glycosylated. {ECO:0000269|PubMed:1460019}.; PTM: Phosphorylated in cytotoxic T-lymphocytes (CTLs) following activation. {ECO:0000269|PubMed:2512251}.
|
SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:1460019, ECO:0000269|PubMed:17341584, ECO:0000269|PubMed:17678538}; Single-pass type I membrane protein. Note=CD8A localizes to lipid rafts only when associated with its partner CD8B. {ECO:0000269|PubMed:17341584}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000269|PubMed:7923932}.
| null | null | null | null | null |
FUNCTION: Integral membrane glycoprotein that plays an essential role in the immune response and serves multiple functions in responses against both external and internal offenses. In T-cells, functions primarily as a coreceptor for MHC class I molecule:peptide complex. The antigens presented by class I peptides are derived from cytosolic proteins while class II derived from extracellular proteins. Interacts simultaneously with the T-cell receptor (TCR) and the MHC class I proteins presented by antigen presenting cells (APCs). In turn, recruits the Src kinase LCK to the vicinity of the TCR-CD3 complex. LCK then initiates different intracellular signaling pathways by phosphorylating various substrates ultimately leading to lymphokine production, motility, adhesion and activation of cytotoxic T-lymphocytes (CTLs). This mechanism enables CTLs to recognize and eliminate infected cells and tumor cells. In NK-cells, the presence of CD8A homodimers at the cell surface provides a survival mechanism allowing conjugation and lysis of multiple target cells. CD8A homodimer molecules also promote the survival and differentiation of activated lymphocytes into memory CD8 T-cells. {ECO:0000269|PubMed:16236125, ECO:0000269|PubMed:17678538, ECO:0000269|PubMed:23657257, ECO:0000269|PubMed:26082771}.
|
Homo sapiens (Human)
|
P01742
|
HV169_HUMAN
|
MDWTWRFLFVVAAATGVQSQVQLVQSGAEVKKPGSSVKVSCKASGGTFSSYAISWVRQAPGQGLEWMGGIIPIFGTANYAQKFQGRVTITADKSTSTAYMELSSLRSEDTAVYYCAR
| null | null |
immune response [GO:0006955]; immunoglobulin mediated immune response [GO:0016064]
|
blood microparticle [GO:0072562]; extracellular region [GO:0005576]; immunoglobulin complex [GO:0019814]; plasma membrane [GO:0005886]
|
antigen binding [GO:0003823]
|
PF07686;
|
2.60.40.10;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
| null | null | null | null | null |
FUNCTION: V region of the variable domain of immunoglobulin heavy chains that participates in the antigen recognition (PubMed:24600447). Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268). {ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414, ECO:0000303|PubMed:24600447}.
|
Homo sapiens (Human)
|
P01762
|
HV311_HUMAN
|
MEFGLSWVFLVAIIKGVQCQVQLVESGGGLVKPGGSLRLSCAASGFTFSDYYMSWIRQAPGKGLEWVSYISSSSSYTNYADSVKGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCAR
| null | null |
immune response [GO:0006955]; immunoglobulin mediated immune response [GO:0016064]
|
blood microparticle [GO:0072562]; extracellular region [GO:0005576]; immunoglobulin complex [GO:0019814]; plasma membrane [GO:0005886]
|
antigen binding [GO:0003823]
|
PF07686;
|
2.60.40.10;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
| null | null | null | null | null |
FUNCTION: V region of the variable domain of immunoglobulin heavy chains that participates in the antigen recognition (PubMed:24600447). Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268). {ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414, ECO:0000303|PubMed:24600447}.
|
Homo sapiens (Human)
|
P01764
|
HV323_HUMAN
|
MEFGLSWLFLVAILKGVQCEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYAMSWVRQAPGKGLEWVSAISGSGGSTYYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAK
| null | null |
immune response [GO:0006955]; immunoglobulin mediated immune response [GO:0016064]
|
blood microparticle [GO:0072562]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; immunoglobulin complex [GO:0019814]; plasma membrane [GO:0005886]
|
antigen binding [GO:0003823]
|
PF07686;
|
2.60.40.10;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
| null | null | null | null | null |
FUNCTION: V region of the variable domain of immunoglobulin heavy chains that participates in the antigen recognition (PubMed:24600447). Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268). {ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414, ECO:0000303|PubMed:24600447}.
|
Homo sapiens (Human)
|
P01768
|
HV330_HUMAN
|
MEFGLSWVFLVALLRGVQCQVQLVESGGGVVQPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAVISYDGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAK
| null | null |
immune response [GO:0006955]; immunoglobulin mediated immune response [GO:0016064]
|
blood microparticle [GO:0072562]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; immunoglobulin complex [GO:0019814]; plasma membrane [GO:0005886]
|
antigen binding [GO:0003823]
|
PF07686;
|
2.60.40.10;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
| null | null | null | null | null |
FUNCTION: V region of the variable domain of immunoglobulin heavy chains that participates in the antigen recognition (PubMed:24600447). Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268). {ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414, ECO:0000303|PubMed:24600447}.
|
Homo sapiens (Human)
|
P01772
|
HV333_HUMAN
|
MEFGLSWVFLVALLRGVQCQVQLVESGGGVVQPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAVIWYDGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAR
| null | null |
immune response [GO:0006955]; immunoglobulin mediated immune response [GO:0016064]
|
blood microparticle [GO:0072562]; extracellular region [GO:0005576]; immunoglobulin complex [GO:0019814]; plasma membrane [GO:0005886]
|
antigen binding [GO:0003823]
|
PF07686;
|
2.60.40.10;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
| null | null | null | null | null |
FUNCTION: V region of the variable domain of immunoglobulin heavy chains that participates in the antigen recognition (PubMed:24600447). Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268). {ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414, ECO:0000303|PubMed:24600447}.
|
Homo sapiens (Human)
|
P01780
|
HV307_HUMAN
|
MELGLSWVFLVAILEGVQCEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYWMSWVRQAPGKGLEWVANIKQDGSEKYYVDSVKGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCAR
| null | null |
immune response [GO:0006955]; immunoglobulin mediated immune response [GO:0016064]
|
blood microparticle [GO:0072562]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; immunoglobulin complex [GO:0019814]; plasma membrane [GO:0005886]
|
antigen binding [GO:0003823]
|
PF07686;
|
2.60.40.10;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
| null | null | null | null | null |
FUNCTION: V region of the variable domain of immunoglobulin heavy chains that participates in the antigen recognition (PubMed:24600447). Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268). {ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414, ECO:0000303|PubMed:24600447}.
|
Homo sapiens (Human)
|
P01814
|
HV270_HUMAN
|
MDILCSTLLLLTVPSWVLSQVTLRESGPALVKPTQTLTLTCTFSGFSLSTSGMCVSWIRQPPGKALEWLALIDWDDDKYYSTSLKTRLTISKDTSKNQVVLTMTNMDPVDTATYYCARI
| null | null |
immune response [GO:0006955]; immunoglobulin mediated immune response [GO:0016064]
|
blood microparticle [GO:0072562]; extracellular region [GO:0005576]; immunoglobulin complex [GO:0019814]; plasma membrane [GO:0005886]
|
antigen binding [GO:0003823]
|
PF07686;
|
2.60.40.10;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
| null | null | null | null | null |
FUNCTION: V region of the variable domain of immunoglobulin heavy chains that participates in the antigen recognition (PubMed:24600447). Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268). {ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414, ECO:0000303|PubMed:24600447}.
|
Homo sapiens (Human)
|
P01817
|
HV205_HUMAN
|
MDTLCSTLLLLTIPSWVLSQITLKESGPTLVKPTQTLTLTCTFSGFSLSTSGVGVGWIRQPPGKALEWLALIYWDDDKRYSPSLKSRLTITKDTSKNQVVLTMTNMDPVDTATYYCAHR
| null | null |
immune response [GO:0006955]; immunoglobulin mediated immune response [GO:0016064]
|
blood microparticle [GO:0072562]; extracellular region [GO:0005576]; immunoglobulin complex [GO:0019814]; plasma membrane [GO:0005886]
|
antigen binding [GO:0003823]
|
PF07686;
|
2.60.40.10;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
| null | null | null | null | null |
FUNCTION: V region of the variable domain of immunoglobulin heavy chains that participates in the antigen recognition (PubMed:24600447). Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268). {ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414, ECO:0000303|PubMed:24600447}.
|
Homo sapiens (Human)
|
P01825
|
HV459_HUMAN
|
MKHLWFFLLLVAAPRWVLSQVQLQESGPGLVKPSETLSLTCTVSGGSISSYYWSWIRQPPGKGLEWIGYIYYSGSTNYNPSLKSRVTISVDTSKNQFSLKLSSVTAADTAVYYCAR
| null | null |
immune response [GO:0006955]; immunoglobulin mediated immune response [GO:0016064]
|
blood microparticle [GO:0072562]; extracellular region [GO:0005576]; immunoglobulin complex [GO:0019814]; plasma membrane [GO:0005886]
|
antigen binding [GO:0003823]
|
PF07686;
|
2.60.40.10;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
| null | null | null | null | null |
FUNCTION: V region of the variable domain of immunoglobulin heavy chains that participates in the antigen recognition (PubMed:24600447). Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268). {ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414, ECO:0000303|PubMed:24600447}.
|
Homo sapiens (Human)
|
P01830
|
THY1_RAT
|
MNPVISITLLLSVLQMSRGQRVISLTACLVNQNLRLDCRHENNTNLPIQHEFSLTREKKKHVLSGTLGVPEHTYRSRVNLFSDRFIKVLTLANFTTKDEGDYMCELRVSGQNPTSSNKTINVIRDKLVKCGGISLLVQNTSWLLLLLLSLSFLQATDFISL
| null | null |
angiogenesis [GO:0001525]; cell-cell adhesion [GO:0098609]; cell-cell signaling [GO:0007267]; cytoskeleton organization [GO:0007010]; focal adhesion assembly [GO:0048041]; heterotypic cell-cell adhesion [GO:0034113]; integrin-mediated signaling pathway [GO:0007229]; mast cell activation [GO:0045576]; negative regulation of apoptotic process [GO:0043066]; negative regulation of axonogenesis [GO:0050771]; negative regulation of cell migration [GO:0030336]; negative regulation of fibroblast proliferation [GO:0048147]; negative regulation of neuron projection regeneration [GO:0070571]; negative regulation of protein kinase activity [GO:0006469]; negative regulation of T cell receptor signaling pathway [GO:0050860]; positive regulation of cellular extravasation [GO:0002693]; positive regulation of focal adhesion assembly [GO:0051894]; positive regulation of GTPase activity [GO:0043547]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of release of sequestered calcium ion into cytosol [GO:0051281]; positive regulation of T cell activation [GO:0050870]; protein autophosphorylation [GO:0046777]; receptor clustering [GO:0043113]; regulation of cell-matrix adhesion [GO:0001952]; regulation of Rho-dependent protein serine/threonine kinase activity [GO:2000298]; response to axon injury [GO:0048678]; retinal cone cell development [GO:0046549]; T cell receptor signaling pathway [GO:0050852]
|
apical plasma membrane [GO:0016324]; axolemma [GO:0030673]; cell surface [GO:0009986]; cytosol [GO:0005829]; dendrite [GO:0030425]; dendrite membrane [GO:0032590]; external side of plasma membrane [GO:0009897]; focal adhesion [GO:0005925]; growth cone [GO:0030426]; membrane raft [GO:0045121]; myelin sheath [GO:0043209]; neuronal cell body membrane [GO:0032809]; plasma membrane [GO:0005886]
|
enzyme binding [GO:0019899]; GPI anchor binding [GO:0034235]; GTPase activator activity [GO:0005096]; integrin binding [GO:0005178]; protein kinase binding [GO:0019901]
|
PF00047;
|
2.60.40.10;
| null |
PTM: Glycosylation is tissue specific. Sialylation of N-glycans at Asn-93 in brain and at Asn-42, Asn-93 and Asn-117 in thymus. {ECO:0000269|PubMed:6118137}.
|
SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
| null | null | null | null | null |
FUNCTION: May play a role in cell-cell or cell-ligand interactions during synaptogenesis and other events in the brain.
|
Rattus norvegicus (Rat)
|
P01831
|
THY1_MOUSE
|
MNPAISVALLLSVLQVSRGQKVTSLTACLVNQNLRLDCRHENNTKDNSIQHEFSLTREKRKHVLSGTLGIPEHTYRSRVTLSNQPYIKVLTLANFTTKDEGDYFCELQVSGANPMSSNKSISVYRDKLVKCGGISLLVQNTSWMLLLLLSLSLLQALDFISL
| null | null |
angiogenesis [GO:0001525]; cell-cell adhesion [GO:0098609]; cell-cell signaling [GO:0007267]; cytoskeleton organization [GO:0007010]; focal adhesion assembly [GO:0048041]; heterotypic cell-cell adhesion [GO:0034113]; integrin-mediated signaling pathway [GO:0007229]; negative regulation of axonogenesis [GO:0050771]; negative regulation of cell migration [GO:0030336]; negative regulation of neuron projection regeneration [GO:0070571]; negative regulation of protein kinase activity [GO:0006469]; negative regulation of T cell receptor signaling pathway [GO:0050860]; positive regulation of cellular extravasation [GO:0002693]; positive regulation of focal adhesion assembly [GO:0051894]; positive regulation of GTPase activity [GO:0043547]; positive regulation of release of sequestered calcium ion into cytosol [GO:0051281]; positive regulation of T cell activation [GO:0050870]; receptor clustering [GO:0043113]; regulation of Rho-dependent protein serine/threonine kinase activity [GO:2000298]; retinal cone cell development [GO:0046549]; T cell receptor signaling pathway [GO:0050852]
|
apical plasma membrane [GO:0016324]; axolemma [GO:0030673]; cell surface [GO:0009986]; cytosol [GO:0005829]; dendrite [GO:0030425]; dendrite membrane [GO:0032590]; endoplasmic reticulum [GO:0005783]; external side of plasma membrane [GO:0009897]; focal adhesion [GO:0005925]; growth cone [GO:0030426]; membrane raft [GO:0045121]; myelin sheath [GO:0043209]; neuronal cell body membrane [GO:0032809]; plasma membrane [GO:0005886]
|
enzyme binding [GO:0019899]; GPI anchor binding [GO:0034235]; GTPase activator activity [GO:0005096]; integrin binding [GO:0005178]; protein kinase binding [GO:0019901]
|
PF00047;
|
2.60.40.10;
| null | null |
SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
| null | null | null | null | null |
FUNCTION: May play a role in cell-cell or cell-ligand interactions during synaptogenesis and other events in the brain.
|
Mus musculus (Mouse)
|
P01832
|
PIGR_RABIT
|
MALFLLTCLLAVFSAATAQSSLLGPSSIFGPGEVNVLEGDSVSITCYYPTTSVTRHSRKFWCREEESGRCVTLASTGYTSQEYSGRGKLTDFPDKGEFVVTVDQLTQNDSGSYKCGVGVNGRGLDFGVNVLVSQKPEPDDVVYKQYESYTVTITCPFTYATRQLKKSFYKVEDGELVLIIDSSSKEAKDPRYKGRITLQIQSTTAKEFTVTIKHLQLNDAGQYVCQSGSDPTAEEQNVDLRLLTPGLLYGNLGGSVTFECALDSEDANAVASLRQVRGGNVVIDSQGTIDPAFEGRILFTKAENGHFSVVIAGLRKEDTGNYLCGVQSNGQSGDGPTQLRQLFVNEEIDVSRSPPVLKGFPGGSVTIRCPYNPKRSDSHLQLYLWEGSQTRHLLVDSGEGLVQKDYTGRLALFEEPGNGTFSVVLNQLTAEDEGFYWCVSDDDESLTTSVKLQIVDGEPSPTIDKFTAVQGEPVEITCHFPCKYFSSEKYWCKWNDHGCEDLPTKLSSSGDLVKCNNNLVLTLTLDSVSEDDEGWYWCGAKDGHEFEEVAAVRVELTEPAKVAVEPAKVPVDPAKAAPAPAEEKAKARCPVPRRRQWYPLSRKLRTSCPEPRLLAEEVAVQSAEDPASGSRASVDASSASGQSGSAKVLISTLVPLGLVLAAGAMAVAIARARHRRNVDRVSIGSYRTDISMSDLENSREFGAIDNPSACPDARETALGGKDELATATESTVEIEEPKKAKRSSKEEADLAYSAFLLQSNTIAAEHQDGPKEA
| null | null |
immunoglobulin transcytosis in epithelial cells mediated by polymeric immunoglobulin receptor [GO:0002415]
|
plasma membrane [GO:0005886]; secretory IgA immunoglobulin complex [GO:0071751]
|
transmembrane signaling receptor activity [GO:0004888]
|
PF07686;
|
2.60.40.10;
| null |
PTM: N-glycosylated. N-glycosylation is required for anchoring IgA molecules to mucus, but is not necessary for Ig binding. {ECO:0000250|UniProtKB:P01833}.
|
SUBCELLULAR LOCATION: [Polymeric immunoglobulin receptor]: Cell membrane {ECO:0000250|UniProtKB:P01833}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Secretory component]: Secreted {ECO:0000250|UniProtKB:P01833}.
| null | null | null | null | null |
FUNCTION: [Polymeric immunoglobulin receptor]: Mediates selective transcytosis of polymeric IgA and IgM across mucosal epithelial cells. Binds polymeric IgA and IgM at the basolateral surface of epithelial cells. The complex is then transported across the cell to be secreted at the apical surface. During this process, a cleavage occurs that separates the extracellular (known as the secretory component) from the transmembrane segment. {ECO:0000250|UniProtKB:P01833}.; FUNCTION: [Secretory component]: Through its N-linked glycans ensures anchoring of secretory IgA (sIgA) molecules to mucus lining the epithelial surface to neutralize extracellular pathogens. On its own (free form) may act as a non-specific microbial scavenger to prevent pathogen interaction with epithelial cells. {ECO:0000250|UniProtKB:P01833}.
|
Oryctolagus cuniculus (Rabbit)
|
P01833
|
PIGR_HUMAN
|
MLLFVLTCLLAVFPAISTKSPIFGPEEVNSVEGNSVSITCYYPPTSVNRHTRKYWCRQGARGGCITLISSEGYVSSKYAGRANLTNFPENGTFVVNIAQLSQDDSGRYKCGLGINSRGLSFDVSLEVSQGPGLLNDTKVYTVDLGRTVTINCPFKTENAQKRKSLYKQIGLYPVLVIDSSGYVNPNYTGRIRLDIQGTGQLLFSVVINQLRLSDAGQYLCQAGDDSNSNKKNADLQVLKPEPELVYEDLRGSVTFHCALGPEVANVAKFLCRQSSGENCDVVVNTLGKRAPAFEGRILLNPQDKDGSFSVVITGLRKEDAGRYLCGAHSDGQLQEGSPIQAWQLFVNEESTIPRSPTVVKGVAGGSVAVLCPYNRKESKSIKYWCLWEGAQNGRCPLLVDSEGWVKAQYEGRLSLLEEPGNGTFTVILNQLTSRDAGFYWCLTNGDTLWRTTVEIKIIEGEPNLKVPGNVTAVLGETLKVPCHFPCKFSSYEKYWCKWNNTGCQALPSQDEGPSKAFVNCDENSRLVSLTLNLVTRADEGWYWCGVKQGHFYGETAAVYVAVEERKAAGSRDVSLAKADAAPDEKVLDSGFREIENKAIQDPRLFAEEKAVADTRDQADGSRASVDSGSSEEQGGSSRALVSTLVPLGLVLAVGAVAVGVARARHRKNVDRVSIRSYRTDISMSDFENSREFGANDNMGASSITQETSLGGKEEFVATTESTTETKEPKKAKRSSKEEAEMAYKDFLLQSSTVAAEAQDGPQEA
| null | null |
detection of chemical stimulus involved in sensory perception of bitter taste [GO:0001580]; epidermal growth factor receptor signaling pathway [GO:0007173]; Fc receptor signaling pathway [GO:0038093]; immunoglobulin transcytosis in epithelial cells mediated by polymeric immunoglobulin receptor [GO:0002415]; receptor clustering [GO:0043113]
|
azurophil granule membrane [GO:0035577]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]; secretory IgA immunoglobulin complex [GO:0071751]
|
polymeric immunoglobulin binding [GO:0001790]; polymeric immunoglobulin receptor activity [GO:0001792]
|
PF07686;
|
2.60.40.10;
| null |
PTM: N-glycosylated. N-glycosylation is required for anchoring IgA molecules to mucus, but is not necessary for Ig binding. {ECO:0000269|PubMed:12150896, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16543244, ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:18780401, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:6526384}.
|
SUBCELLULAR LOCATION: [Polymeric immunoglobulin receptor]: Cell membrane {ECO:0000269|PubMed:9379029}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Secretory component]: Secreted {ECO:0000269|PubMed:16543244, ECO:0000269|PubMed:19079336, ECO:0000269|PubMed:8292260}.
| null | null | null | null | null |
FUNCTION: [Polymeric immunoglobulin receptor]: Mediates selective transcytosis of polymeric IgA and IgM across mucosal epithelial cells. Binds polymeric IgA and IgM at the basolateral surface of epithelial cells. The complex is then transported across the cell to be secreted at the apical surface. During this process, a cleavage occurs that separates the extracellular (known as the secretory component) from the transmembrane segment. {ECO:0000269|PubMed:10229845, ECO:0000269|PubMed:15530357, ECO:0000269|PubMed:9379029}.; FUNCTION: [Secretory component]: Through its N-linked glycans ensures anchoring of secretory IgA (sIgA) molecules to mucus lining the epithelial surface to neutralize extracellular pathogens (PubMed:12150896). On its own (free form) may act as a non-specific microbial scavenger to prevent pathogen interaction with epithelial cells (PubMed:16543244). {ECO:0000269|PubMed:12150896, ECO:0000269|PubMed:16543244}.
|
Homo sapiens (Human)
|
P01834
|
IGKC_HUMAN
|
RTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
| null | null |
adaptive immune response [GO:0002250]; B cell receptor signaling pathway [GO:0050853]; immune response [GO:0006955]; immunoglobulin mediated immune response [GO:0016064]
|
blood microparticle [GO:0072562]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; IgA immunoglobulin complex [GO:0071745]; IgD immunoglobulin complex [GO:0071738]; IgE immunoglobulin complex [GO:0071742]; IgG immunoglobulin complex [GO:0071735]; IgM immunoglobulin complex [GO:0071753]; plasma membrane [GO:0005886]
|
antigen binding [GO:0003823]
|
PF07654;
|
2.60.40.10;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
| null | null | null | null | null |
FUNCTION: Constant region of immunoglobulin light chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268). {ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
|
Homo sapiens (Human)
|
P01848
|
TRAC_HUMAN
|
IQNPDPAVYQLRDSKSSDKSVCLFTDFDSQTNVSQSKDSDVYITDKTVLDMRSMDFKSNSAVAWSNKSDFACANAFNNSIIPEDTFFPSPESSCDVKLVEKSFETDTNLNFQNLSVIGFRILLLKVAGFNLLMTLRLWSS
| null | null |
adaptive immune response [GO:0002250]; alpha-beta T cell activation [GO:0046631]; response to bacterium [GO:0009617]; T cell receptor signaling pathway [GO:0050852]
|
alpha-beta T cell receptor complex [GO:0042105]; plasma membrane [GO:0005886]
| null |
PF09291;
|
2.60.40.10;
| null | null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000303|PubMed:20452950}.
| null | null | null | null | null |
FUNCTION: Constant region of T cell receptor (TR) alpha chain (PubMed:24600447). Alpha-beta T cell receptors are antigen specific receptors which are essential to the immune response and are present on the cell surface of T lymphocytes. Recognize peptide-major histocompatibility (MH) (pMH) complexes that are displayed by antigen presenting cells (APC), a prerequisite for efficient T cell adaptive immunity against pathogens (PubMed:25493333). Binding of alpha-beta TR to pMH complex initiates TR-CD3 clustering on the cell surface and intracellular activation of LCK that phosphorylates the ITAM motifs of CD3G, CD3D, CD3E and CD247 enabling the recruitment of ZAP70. In turn, ZAP70 phosphorylates LAT, which recruits numerous signaling molecules to form the LAT signalosome. The LAT signalosome propagates signal branching to three major signaling pathways, the calcium, the mitogen-activated protein kinase (MAPK) kinase and the nuclear factor NF-kappa-B (NF-kB) pathways, leading to the mobilization of transcription factors that are critical for gene expression and essential for T cell growth and differentiation (PubMed:23524462). The T cell repertoire is generated in the thymus, by V-(D)-J rearrangement. This repertoire is then shaped by intrathymic selection events to generate a peripheral T cell pool of self-MH restricted, non-autoaggressive T cells. Post-thymic interaction of alpha-beta TR with the pMH complexes shapes TR structural and functional avidity (PubMed:15040585). {ECO:0000303|PubMed:15040585, ECO:0000303|PubMed:23524462, ECO:0000303|PubMed:24600447, ECO:0000303|PubMed:25493333}.
|
Homo sapiens (Human)
|
P01850
|
TRBC1_HUMAN
|
DLNKVFPPEVAVFEPSEAEISHTQKATLVCLATGFFPDHVELSWWVNGKEVHSGVSTDPQPLKEQPALNDSRYCLSSRLRVSATFWQNPRNHFRCQVQFYGLSENDEWTQDRAKPVTQIVSAEAWGRADCGFTSVSYQQGVLSATILYEILLGKATLYAVLVSALVLMAMVKRKDF
| null | null |
adaptive immune response [GO:0002250]; alpha-beta T cell activation [GO:0046631]; antibacterial humoral response [GO:0019731]; complement activation, classical pathway [GO:0006958]; immune response [GO:0006955]; T cell receptor signaling pathway [GO:0050852]
|
alpha-beta T cell receptor complex [GO:0042105]; blood microparticle [GO:0072562]; extracellular exosome [GO:0070062]; immunoglobulin complex, circulating [GO:0042571]; membrane [GO:0016020]; plasma membrane [GO:0005886]
|
antigen binding [GO:0003823]; immunoglobulin receptor binding [GO:0034987]
|
PF07654;
|
2.60.40.10;
| null | null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000303|PubMed:20452950}.
| null | null | null | null | null |
FUNCTION: Constant region of T cell receptor (TR) beta chain (PubMed:24600447). Alpha-beta T cell receptors are antigen specific receptors which are essential to the immune response and are present on the cell surface of T lymphocytes. Recognize peptide-major histocompatibility (MH) (pMH) complexes that are displayed by antigen presenting cells (APC), a prerequisite for efficient T cell adaptive immunity against pathogens (PubMed:25493333). Binding of alpha-beta TR to pMH complex initiates TR-CD3 clustering on the cell surface and intracellular activation of LCK that phosphorylates the ITAM motifs of CD3G, CD3D, CD3E and CD247 enabling the recruitment of ZAP70. In turn, ZAP70 phosphorylates LAT, which recruits numerous signaling molecules to form the LAT signalosome. The LAT signalosome propagates signal branching to three major signaling pathways, the calcium, the mitogen-activated protein kinase (MAPK) kinase and the nuclear factor NF-kappa-B (NF-kB) pathways, leading to the mobilization of transcription factors that are critical for gene expression and essential for T cell growth and differentiation (PubMed:23524462, PubMed:9382891). The T cell repertoire is generated in the thymus, by V-(D)-J rearrangement. This repertoire is then shaped by intrathymic selection events to generate a peripheral T cell pool of self-MH restricted, non-autoaggressive T cells. Post-thymic interaction of alpha-beta TR with the pMH complexes shapes TR structural and functional avidity (PubMed:15040585). {ECO:0000269|PubMed:9382891, ECO:0000303|PubMed:15040585, ECO:0000303|PubMed:23524462, ECO:0000303|PubMed:24600447, ECO:0000303|PubMed:25493333}.
|
Homo sapiens (Human)
|
P01854
|
IGHE_HUMAN
|
ASTQSPSVFPLTRCCKNIPSNATSVTLGCLATGYFPEPVMVTWDTGSLNGTTMTLPATTLTLSGHYATISLLTVSGAWAKQMFTCRVAHTPSSTDWVDNKTFSVCSRDFTPPTVKILQSSCDGGGHFPPTIQLLCLVSGYTPGTINITWLEDGQVMDVDLSTASTTQEGELASTQSELTLSQKHWLSDRTYTCQVTYQGHTFEDSTKKCADSNPRGVSAYLSRPSPFDLFIRKSPTITCLVVDLAPSKGTVNLTWSRASGKPVNHSTRKEEKQRNGTLTVTSTLPVGTRDWIEGETYQCRVTHPHLPRALMRSTTKTSGPRAAPEVYAFATPEWPGSRDKRTLACLIQNFMPEDISVQWLHNEVQLPDARHSTTQPRKTKGSGFFVFSRLEVTRAEWEQKDEFICRAVHEAASPSQTVQRAVSVNPGLAGGSAQSQRAPDRVLCHSGQQQGLPRAAGGSVPHPRCHCGAGRADWPGPPELDVCVEEAEGEAPWTWTGLCIFAALFLLSVSYSAAITLLMVQRFLSATRQGRPQTSLDYTNVLQPHA
| null | null |
adaptive immune memory response [GO:0090716]; adaptive immune response [GO:0002250]; antibacterial humoral response [GO:0019731]; antibody-dependent cellular cytotoxicity [GO:0001788]; B cell antigen processing and presentation [GO:0002450]; B cell proliferation [GO:0042100]; B cell receptor signaling pathway [GO:0050853]; complement activation, classical pathway [GO:0006958]; eosinophil degranulation [GO:0043308]; Fc receptor-mediated immune complex endocytosis [GO:0160006]; immune response [GO:0006955]; inflammatory response [GO:0006954]; macrophage activation [GO:0042116]; macrophage differentiation [GO:0030225]; mast cell degranulation [GO:0043303]; primary adaptive immune response [GO:0090720]; type 2 immune response [GO:0042092]; type I hypersensitivity [GO:0016068]
|
blood microparticle [GO:0072562]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; IgE B cell receptor complex [GO:0071744]; IgE immunoglobulin complex [GO:0071742]; immunoglobulin complex, circulating [GO:0042571]; plasma membrane [GO:0005886]
|
antigen binding [GO:0003823]; immunoglobulin receptor binding [GO:0034987]
|
PF07654;
|
2.60.40.10;
| null | null |
SUBCELLULAR LOCATION: [Isoform 1]: Secreted {ECO:0000269|PubMed:7995941}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000269|PubMed:20458139, ECO:0000269|PubMed:7995941, ECO:0000269|PubMed:8976175}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 3]: Cell membrane {ECO:0000269|PubMed:8976175}; Single-pass type I membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Constant region of immunoglobulin heavy chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268). {ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.; FUNCTION: [Isoform 1]: Constant region of secreted IgE, also known as the Fc region of IgE antibody. Mediates IgE effector functions on myeloid and lymphoid cells primarily via two Fc receptors, the high-affinity IgE Fc receptor complex/FCER1A:MS4A2:FCGR1A and the low-affinity FCER2 receptor, which upon antigen/allergen cross-linking initiate signaling pathways that lead to immune cell activation and differentiation (PubMed:2167225, PubMed:25629393, PubMed:33840121, PubMed:7544003, PubMed:8114916, PubMed:8551243). Triggers the immediate hypersensitivity response to allergens as a host defense mechanism against helminth parasites, pathogenic bacteria and venom toxicity. When dysregulated, it can elicit harmful life-threatening allergic and anaphylactic reactions (PubMed:25629393, PubMed:33840121, PubMed:7544003, PubMed:8114916, PubMed:8551243). Stimulates the high-affinity IgE Fc receptor complex/FCER1A:MS4A2:FCGR1A on mast cells, basophils and eosinophils leading to secretion of vasoactive amines, lipid mediators and cytokines that contribute to inflammatory response, tissue remodeling and cytotoxicity against microbes (PubMed:25629393, PubMed:8114916, PubMed:8551243). On macrophages, cross-linking of FCER2 by IgE immune complexes induces intracellular killing of parasites through activation of L-Arginine-nitric oxide pathway (PubMed:7544003). Activates macrophages to kill tumor cells via antigen-specific antibody-dependent cytotoxicity (ADCC). Triggers differentiation of quiescent M0 macrophages toward M1 state and reprograms M2 macrophages toward a proinflammatory state with antitumor functions (PubMed:30956175). Stimulates FCER2 on B cells and initiates IgE-dependent antigen uptake and presentation to T cells (PubMed:2167225). {ECO:0000269|PubMed:2167225, ECO:0000269|PubMed:25629393, ECO:0000269|PubMed:30956175, ECO:0000269|PubMed:33840121, ECO:0000269|PubMed:7544003, ECO:0000269|PubMed:8114916, ECO:0000269|PubMed:8551243, ECO:0000303|PubMed:20176268, ECO:0000305|PubMed:10917520, ECO:0000305|PubMed:7995941}.; FUNCTION: [Isoform 2]: Constant region of membrane-bound IgE (long mIgE), part of the B cell receptor complex (BCR). Upon antigen cross-linking triggers quick BCR signaling, ensuring survival of IgE-switched B cells and differentiation into plasma cells, thus regulating both primary and memory IgE responses. {ECO:0000269|PubMed:20458139, ECO:0000269|PubMed:8976175}.; FUNCTION: [Isoform 3]: Constant region of membrane-bound IgE (short mIgE), part of the B cell receptor complex (BCR). Upon antigen cross-linking initiates slower but sustained BCR signaling that negatively regulates mature B cell proliferation. {ECO:0000269|PubMed:8976175}.
|
Homo sapiens (Human)
|
P01857
|
IGHG1_HUMAN
|
ASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPELQLEESCAEAQDGELDGLWTTITIFITLFLLSVCYSATVTFFKVKWIFSSVVDLKQTIIPDYRNMIGQGA
| null | null |
adaptive immune response [GO:0002250]; antibacterial humoral response [GO:0019731]; antibody-dependent cellular cytotoxicity [GO:0001788]; B cell receptor signaling pathway [GO:0050853]; complement activation, classical pathway [GO:0006958]; complement-dependent cytotoxicity [GO:0097278]
|
blood microparticle [GO:0072562]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; IgG immunoglobulin complex [GO:0071735]; immunoglobulin complex, circulating [GO:0042571]; plasma membrane [GO:0005886]
|
antigen binding [GO:0003823]; Fc-gamma receptor I complex binding [GO:0034988]; immunoglobulin receptor binding [GO:0034987]
|
PF07654;
|
2.60.40.10;
| null |
PTM: Glycosylation on Asn-180 is required for interaction with Fc receptors and ability to activate the complement pathway. {ECO:0000269|PubMed:20357243}.; PTM: (Microbial infection) Deglycosylation on Asn-180 by S.pyogenes EndoS or Endos2 endoglucosidases prevents interaction between immunoglobulin-gamma (IgG) and Fc receptors, impairing ability to activate the complement pathway. {ECO:0000269|PubMed:11406581, ECO:0000269|PubMed:20357243, ECO:0000269|PubMed:23865566}.
|
SUBCELLULAR LOCATION: [Isoform 1]: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}; Single-pass membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Constant region of immunoglobulin heavy chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268). Mediates IgG effector functions on monocytes triggering ADCC of virus-infected cells. {ECO:0000269|PubMed:11711607, ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
|
Homo sapiens (Human)
|
P01859
|
IGHG2_HUMAN
|
ASTKGPSVFPLAPCSRSTSESTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSNFGTQTYTCNVDHKPSNTKVDKTVERKCCVECPPCPAPPVAGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTFRVVSVLTVVHQDWLNGKEYKCKVSNKGLPAPIEKTISKTKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDISVEWESNGQPENNYKTTPPMLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPELQLEESCAEAQDGELDGLWTTITIFITLFLLSVCYSATITFFKVKWIFSSVVDLKQTIVPDYRNMIRQGA
| null | null |
adaptive immune response [GO:0002250]; antibacterial humoral response [GO:0019731]; B cell receptor signaling pathway [GO:0050853]; complement activation, classical pathway [GO:0006958]
|
blood microparticle [GO:0072562]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; IgG immunoglobulin complex [GO:0071735]; immunoglobulin complex, circulating [GO:0042571]; plasma membrane [GO:0005886]
|
antigen binding [GO:0003823]; immunoglobulin receptor binding [GO:0034987]
|
PF07654;
|
2.60.40.10;
| null |
PTM: Glycosylation on Asn-176 is required for interaction with Fc receptors and ability to activate the complement pathway. {ECO:0000269|PubMed:20357243}.; PTM: (Microbial infection) Deglycosylation on Asn-176 by S.pyogenes EndoS or Endos2 endoglucosidases prevents interaction between immunoglobulin-gamma (IgG) and Fc receptors, impairing ability to activate the complement pathway. {ECO:0000269|PubMed:11406581, ECO:0000269|PubMed:20357243, ECO:0000269|PubMed:23865566}.
|
SUBCELLULAR LOCATION: [Isoform 1]: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}; Single-pass membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Constant region of immunoglobulin heavy chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268). {ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
|
Homo sapiens (Human)
|
P01860
|
IGHG3_HUMAN
|
ASTKGPSVFPLAPCSRSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYTCNVNHKPSNTKVDKRVELKTPLGDTTHTCPRCPEPKSCDTPPPCPRCPEPKSCDTPPPCPRCPEPKSCDTPPPCPRCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVQFKWYVDGVEVHNAKTKPREEQYNSTFRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKTKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESSGQPENNYNTTPPMLDSDGSFFLYSKLTVDKSRWQQGNIFSCSVMHEALHNRFTQKSLSLSPELQLEESCAEAQDGELDGLWTTITIFITLFLLSVCYSATVTFFKVKWIFSSVVDLKQTIIPDYRNMIGQGA
| null | null |
adaptive immune response [GO:0002250]; antibacterial humoral response [GO:0019731]; B cell receptor signaling pathway [GO:0050853]; complement activation, classical pathway [GO:0006958]
|
blood microparticle [GO:0072562]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; IgG immunoglobulin complex [GO:0071735]; immunoglobulin complex, circulating [GO:0042571]; plasma membrane [GO:0005886]
|
antigen binding [GO:0003823]; immunoglobulin receptor binding [GO:0034987]
|
PF07654;
|
2.60.40.10;
| null |
PTM: N-linked glycans at Asn-322 are noncore fucosylated and the vast majority are diantennary species with a bisecting GlcNAc. Among them the most dominant glycans are HexNAc5Hex4, HexNAc5Hex5, and HexNAc5Hex5Sia1. {ECO:0000269|PubMed:26536155}.; PTM: N-linked glycans at Asn-227 are diantennary core fucosylated structures without bisecting GlcNAc (HexNAc4Hex4Fuc1, HexNAc4Hex5Fuc1, and HexNAc4Hex5Fuc1Sia1) (PubMed:26536155). Glycosylation on Asn-227 is required for interaction with Fc receptors and ability to activate the complement pathway (PubMed:20357243). {ECO:0000269|PubMed:20357243, ECO:0000269|PubMed:26536155}.; PTM: (Microbial infection) Deglycosylation on Asn-227 by S.pyogenes EndoS or Endos2 endoglucosidases prevents interaction between immunoglobulin-gamma (IgG) and Fc receptors, impairing ability to activate the complement pathway. {ECO:0000269|PubMed:11406581, ECO:0000269|PubMed:20357243, ECO:0000269|PubMed:23865566}.; PTM: O-linked glycans are non-, mono- and disialylated core 1-type O-glycans. {ECO:0000269|PubMed:25759508}.
|
SUBCELLULAR LOCATION: [Isoform 1]: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}; Single-pass membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Constant region of immunoglobulin heavy chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268). {ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
|
Homo sapiens (Human)
|
P01861
|
IGHG4_HUMAN
|
ASTKGPSVFPLAPCSRSTSESTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTKTYTCNVDHKPSNTKVDKRVESKYGPPCPSCPAPEFLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSQEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKGLPSSIEKTISKAKGQPREPQVYTLPPSQEEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSRLTVDKSRWQEGNVFSCSVMHEALHNHYTQKSLSLSLELQLEESCAEAQDGELDGLWTTITIFITLFLLSVCYSATVTFFKVKWIFSSVVDLKQTIVPDYRNMIRQGA
| null | null |
adaptive immune response [GO:0002250]; antibacterial humoral response [GO:0019731]; B cell receptor signaling pathway [GO:0050853]; complement activation, classical pathway [GO:0006958]
|
blood microparticle [GO:0072562]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; IgG immunoglobulin complex [GO:0071735]; immunoglobulin complex, circulating [GO:0042571]; plasma membrane [GO:0005886]
|
antigen binding [GO:0003823]; immunoglobulin receptor binding [GO:0034987]
|
PF07654;
|
2.60.40.10;
| null |
PTM: Glycosylation on Asn-177 is required for interaction with Fc receptors and ability to activate the complement pathway. {ECO:0000269|PubMed:20357243}.; PTM: (Microbial infection) Deglycosylation on Asn-177 by S.pyogenes EndoS or Endos2 endoglucosidases prevents interaction between immunoglobulin-gamma (IgG) and Fc receptors, impairing ability to activate the complement pathway. {ECO:0000269|PubMed:11406581, ECO:0000269|PubMed:20357243, ECO:0000269|PubMed:23865566}.
|
SUBCELLULAR LOCATION: [Isoform 1]: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}; Single-pass membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Constant region of immunoglobulin heavy chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268). {ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
|
Homo sapiens (Human)
|
P01865
|
GCAM_MOUSE
|
KTTAPSVYPLAPVCGDTTGSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVTSSTWPSQSITCNVAHPASSTKVDKKIEPRGPTIKPCPPCKCPAPNLLGGPSVFIFPPKIKDVLMISLSPIVTCVVVDVSEDDPDVQISWFVNNVEVHTAQTQTHREDYNSTLRVVSALPIQHQDWMSGKEFKCKVNNKDLPAPIERTISKPKGSVRAPQVYVLPPPEEEMTKKQVTLTCMVTDFMPEDIYVEWTNNGKTELNYKNTEPVLDSDGSYFMYSKLRVEKKNWVERNSYSCSVVHEGLHNHHTTKSFSRTPGLDLDDVCAEAQDGELDGLWTTITIFISLFLLSVCYSASVTLFKVKWIFSSVVELKQTISPDYRNMIGQGA
| null | null |
antibacterial humoral response [GO:0019731]; antibody-dependent cellular cytotoxicity [GO:0001788]; antigen processing and presentation [GO:0019882]; complement activation, classical pathway [GO:0006958]; early endosome to late endosome transport [GO:0045022]; endosome to lysosome transport [GO:0008333]; humoral immune response mediated by circulating immunoglobulin [GO:0002455]; immunoglobulin mediated immune response [GO:0016064]; phagocytosis, engulfment [GO:0006911]; phagocytosis, recognition [GO:0006910]; positive regulation of B cell activation [GO:0050871]; positive regulation of endocytosis [GO:0045807]; positive regulation of immune response [GO:0050778]; positive regulation of phagocytosis [GO:0050766]; positive regulation of type I hypersensitivity [GO:0001812]; positive regulation of type IIa hypersensitivity [GO:0001798]; regulation of proteolysis [GO:0030162]; response to bacterium [GO:0009617]
|
blood microparticle [GO:0072562]; extracellular exosome [GO:0070062]; immunoglobulin complex, circulating [GO:0042571]; multivesicular body [GO:0005771]; plasma membrane [GO:0005886]
|
antigen binding [GO:0003823]; immunoglobulin receptor binding [GO:0034987]
|
PF07654;
|
2.60.40.10;
| null | null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
| null | null | null | null | null | null |
Mus musculus (Mouse)
|
P01867
|
IGG2B_MOUSE
|
KTTPPSVYPLAPGCGDTTGSSVTLGCLVKGYFPESVTVTWNSGSLSSSVHTFPALLQSGLYTMSSSVTVPSSTWPSQTVTCSVAHPASSTTVDKKLEPSGPISTINPCPPCKECHKCPAPNLEGGPSVFIFPPNIKDVLMISLTPKVTCVVVDVSEDDPDVQISWFVNNVEVHTAQTQTHREDYNSTIRVVSTLPIQHQDWMSGKEFKCKVNNKDLPSPIERTISKIKGLVRAPQVYILPPPAEQLSRKDVSLTCLVVGFNPGDISVEWTSNGHTEENYKDTAPVLDSDGSYFIYSKLNMKTSKWEKTDSFSCNVRHEGLKNYYLKKTISRSPGLDLDDICAEAKDGELDGLWTTITIFISLFLLSVCYSASVTLFKVKWIFSSVVELKQKISPDYRNMIGQGA
| null | null |
antibacterial humoral response [GO:0019731]; complement activation, classical pathway [GO:0006958]; humoral immune response mediated by circulating immunoglobulin [GO:0002455]; immunoglobulin mediated immune response [GO:0016064]; phagocytosis, engulfment [GO:0006911]; phagocytosis, recognition [GO:0006910]; positive regulation of immune response [GO:0050778]; positive regulation of phagocytosis [GO:0050766]; positive regulation of type I hypersensitivity [GO:0001812]; positive regulation of type IIa hypersensitivity [GO:0001798]
|
blood microparticle [GO:0072562]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; immunoglobulin complex, circulating [GO:0042571]; plasma membrane [GO:0005886]
|
antigen binding [GO:0003823]; immunoglobulin receptor binding [GO:0034987]
|
PF07654;
|
2.60.40.10;
| null |
PTM: O-linked glycan consists of Gal-GalNAc disaccharide which is modified with 2 sialic acid residues. {ECO:0000269|PubMed:7512967}.
|
SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted.
| null | null | null | null | null | null |
Mus musculus (Mouse)
|
P01868
|
IGHG1_MOUSE
|
AKTTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVPSSPRPSETVTCNVAHPASSTKVDKKIVPRDCGCKPCICTVPEVSSVFIFPPKPKDVLTITLTPKVTCVVVDISKDDPEVQFSWFVDDVEVHTAQTQPREEQFNSTFRSVSELPIMHQDWLNGKEFKCRVNSAAFPAPIEKTISKTKGRPKAPQVYTIPPPKEQMAKDKVSLTCMITDFFPEDITVEWQWNGQPAENYKNTQPIMNTNGSYFVYSKLNVQKSNWEAGNTFTCSVLHEGLHNHHTEKSLSHSPGK
| null | null |
antibacterial humoral response [GO:0019731]; antibody-dependent cellular cytotoxicity [GO:0001788]; B cell differentiation [GO:0030183]; complement activation, classical pathway [GO:0006958]; defense response to bacterium [GO:0042742]; humoral immune response mediated by circulating immunoglobulin [GO:0002455]; immunoglobulin mediated immune response [GO:0016064]; phagocytosis, engulfment [GO:0006911]; phagocytosis, recognition [GO:0006910]; positive regulation of immune response [GO:0050778]; positive regulation of phagocytosis [GO:0050766]; positive regulation of type I hypersensitivity [GO:0001812]; positive regulation of type IIa hypersensitivity [GO:0001798]
|
blood microparticle [GO:0072562]; cytoplasm [GO:0005737]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; immunoglobulin complex, circulating [GO:0042571]
|
antigen binding [GO:0003823]; immunoglobulin receptor binding [GO:0034987]
|
PF07654;
|
2.60.40.10;
| null | null |
SUBCELLULAR LOCATION: [Isoform Secreted]: Secreted.
| null | null | null | null | null | null |
Mus musculus (Mouse)
|
P01869
|
IGH1M_MOUSE
|
AKTTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVPSSPRPSETVTCNVAHPASSTKVDKKIVPRDCGCKPCICTVPEVSSVFIFPPKPKDVLTITLTPKVTCVVVDISKDDPEVQFSWFVDDVEVHTAQTQPREEQFNSTFRSVSELPIMHQDWLNGKEFKCRVNSAAFPAPIEKTISKTKGRPKAPQVYTIPPPKEQMAKDKVSLTCMITDFFPEDITVEWQWNGQPAENYKNTQPIMNTNGSYFVYSKLNVQKSNWEAGNTFTCSVLHEGLHNHHTEKSLSHSPGLQLDETCAEAQDGELDGLWTTITIFISLFLLSVCYSAAVTLFKVKWIFSSVVELKQTLVPEYKNMIGQAP
| null | null |
antibacterial humoral response [GO:0019731]; antibody-dependent cellular cytotoxicity [GO:0001788]; B cell differentiation [GO:0030183]; complement activation, classical pathway [GO:0006958]; defense response to bacterium [GO:0042742]; humoral immune response mediated by circulating immunoglobulin [GO:0002455]; immunoglobulin mediated immune response [GO:0016064]; phagocytosis, engulfment [GO:0006911]; phagocytosis, recognition [GO:0006910]; positive regulation of immune response [GO:0050778]; positive regulation of phagocytosis [GO:0050766]; positive regulation of type I hypersensitivity [GO:0001812]; positive regulation of type IIa hypersensitivity [GO:0001798]
|
blood microparticle [GO:0072562]; cytoplasm [GO:0005737]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; immunoglobulin complex, circulating [GO:0042571]
|
antigen binding [GO:0003823]; immunoglobulin receptor binding [GO:0034987]
|
PF07654;
|
2.60.40.10;
| null | null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
| null | null | null | null | null | null |
Mus musculus (Mouse)
|
P01871
|
IGHM_HUMAN
|
GSASAPTLFPLVSCENSPSDTSSVAVGCLAQDFLPDSITFSWKYKNNSDISSTRGFPSVLRGGKYAATSQVLLPSKDVMQGTDEHVVCKVQHPNGNKEKNVPLPVIAELPPKVSVFVPPRDGFFGNPRKSKLICQATGFSPRQIQVSWLREGKQVGSGVTTDQVQAEAKESGPTTYKVTSTLTIKESDWLGQSMFTCRVDHRGLTFQQNASSMCVPDQDTAIRVFAIPPSFASIFLTKSTKLTCLVTDLTTYDSVTISWTRQNGEAVKTHTNISESHPNATFSAVGEASICEDDWNSGERFTCTVTHTDLPSPLKQTISRPKGVALHRPDVYLLPPAREQLNLRESATITCLVTGFSPADVFVQWMQRGQPLSPEKYVTSAPMPEPQAPGRYFAHSILTVSEEEWNTGETYTCVVAHEALPNRVTERTVDKSTEGEVSADEEGFENLWATASTFIVLFLLSLFYSTTVTLFKVK
| null | null |
adaptive immune response [GO:0002250]; antibacterial humoral response [GO:0019731]; B cell receptor signaling pathway [GO:0050853]; complement activation, classical pathway [GO:0006958]; defense response to Gram-negative bacterium [GO:0050829]; innate immune response [GO:0045087]; pre-B cell allelic exclusion [GO:0002331]
|
blood microparticle [GO:0072562]; cell surface [GO:0009986]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; hexameric IgM immunoglobulin complex [GO:0071757]; IgM B cell receptor complex [GO:0071755]; IgM immunoglobulin complex [GO:0071753]; immunoglobulin complex, circulating [GO:0042571]; pentameric IgM immunoglobulin complex [GO:0071756]; plasma membrane [GO:0005886]
|
antigen binding [GO:0003823]; immunoglobulin receptor binding [GO:0034987]
|
PF07654;
|
2.60.40.10;
| null |
PTM: N-glycosylated; important for IgM secretion and its localization at the plasma membrane. The interaction with FCMR is glycan-independent. {ECO:0000269|PubMed:28230186, ECO:0000269|PubMed:32029689, ECO:0000269|PubMed:35981043}.
|
SUBCELLULAR LOCATION: [Isoform 1]: Secreted. Note=During differentiation, B-lymphocytes switch from expression of membrane-bound IgM to secretion of IgM. {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane; Single-pass membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Constant region of immunoglobulin heavy chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268). {ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.; FUNCTION: [Isoform 1]: Constant region of secreted IgM (sIgM), also known as the Fc region of IgM antibody. Able to multimerize, forms high order polymers, mainly pentamers and occasionally hexamers, providing for multivalency and high avidity recognition of antigens (PubMed:32029689, PubMed:37095205). Natural sIgM are polyreactive and recognize conserved self- and pathogen-derived structures, whereas immune sIgM are secreted only upon exposure to pathogens and are antigen-specific. Both natural and immune sIgM are required for an efficient humoral immune response to infection (By similarity). Mediates sIgM effector functions mostly via Fc receptors and the complement system. On lymphoid cells binds high-affinity Fc receptor FCMR and promotes induction of an efficient neutralizing IgG response while maintaining tolerance to self-antigens. Recruits C1q complement component to initiate the classical complement pathway, facilitating the recognition and neutralization of pathogens by the host. Together with C1q and mannose-binding lectin promotes the phagocytosis of apoptotic cells by macrophages, ensuring the clearance of potential autoimmune epitopes from tissues (By similarity) (PubMed:12847249, PubMed:19006321, PubMed:28230186, PubMed:32029689). Involved in mucosal immunity. It is transported by transcytosis across mucosal epithelium by PIGR and secreted on the apical side in complex with PIGR secretory component to scan mucosal lining for pathogens. IgM-antigen complexes undergo FCMR-mediated retrotranscytosis across mucosal M cells toward antigen-presenting cells in mucosal lymphoid tissues (By similarity) (PubMed:32029689). {ECO:0000250|UniProtKB:P01872, ECO:0000269|PubMed:12847249, ECO:0000269|PubMed:19006321, ECO:0000269|PubMed:28230186, ECO:0000269|PubMed:32029689, ECO:0000269|PubMed:37095205}.; FUNCTION: [Isoform 2]: Constant region of membrane-bound IgM, part of the B cell receptor complex (BCR). IgM BCR provides constitutive tonic signaling for B cell survival. Mediates pre-BCR signaling that regulates B cell selection and rearrangement of Ig genes via allelic exclusion. {ECO:0000250|UniProtKB:P01872, ECO:0000269|PubMed:35981043}.
|
Homo sapiens (Human)
|
P01872
|
IGHM_MOUSE
|
SQSFPNVFPLVSCESPLSDKNLVAMGCLARDFLPSTISFTWNYQNNTEVIQGIRTFPTLRTGGKYLATSQVLLSPKSILEGSDEYLVCKIHYGGKNRDLHVPIPAVAEMNPNVNVFVPPRDGFSGPAPRKSKLICEATNFTPKPITVSWLKDGKLVESGFTTDPVTIENKGSTPQTYKVISTLTISEIDWLNLNVYTCRVDHRGLTFLKNVSSTCAASPSTDILTFTIPPSFADIFLSKSANLTCLVSNLATYETLNISWASQSGEPLETKIKIMESHPNGTFSAKGVASVCVEDWNNRKEFVCTVTHRDLPSPQKKFISKPNEVHKHPPAVYLLPPAREQLNLRESATVTCLVKGFSPADISVQWLQRGQLLPQEKYVTSAPMPEPGAPGFYFTHSILTVTEEEWNSGETYTCVVGHEALPHLVTERTVDKSTGKPTLYNVSLIMSDTGGTCY
| null | null |
antibacterial humoral response [GO:0019731]; antigen processing and presentation [GO:0019882]; B cell activation [GO:0042113]; B cell affinity maturation [GO:0002344]; B cell proliferation [GO:0042100]; B cell receptor signaling pathway [GO:0050853]; complement activation, classical pathway [GO:0006958]; defense response to Gram-negative bacterium [GO:0050829]; early endosome to late endosome transport [GO:0045022]; humoral immune response mediated by circulating immunoglobulin [GO:0002455]; immunoglobulin mediated immune response [GO:0016064]; MAPK cascade [GO:0000165]; positive regulation of B cell activation [GO:0050871]; positive regulation of B cell proliferation [GO:0030890]; positive regulation of endocytosis [GO:0045807]; positive regulation of immune response [GO:0050778]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; pre-B cell allelic exclusion [GO:0002331]; regulation of cell morphogenesis [GO:0022604]; regulation of immunoglobulin production [GO:0002637]
|
B cell receptor complex [GO:0019815]; blood microparticle [GO:0072562]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; IgM B cell receptor complex [GO:0071755]; immunoglobulin complex, circulating [GO:0042571]; membrane [GO:0016020]; pentameric IgM immunoglobulin complex [GO:0071756]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]
|
antigen binding [GO:0003823]; identical protein binding [GO:0042802]; immunoglobulin receptor binding [GO:0034987]; transmembrane signaling receptor activity [GO:0004888]
|
PF07654;
|
2.60.40.10;
| null |
PTM: Cleaved by a non-enzymatic process after Asn-96, yielding a glycosylated protein of 55 kDa. The process is induced by other proteins, and requires neutral or alkaline pH. {ECO:0000269|PubMed:29323348}.; PTM: N-glycosylated; important for IgM secretion and its localization at the plasma membrane. The interaction with FCMR is glycan-independent. {ECO:0000250|UniProtKB:P01871}.
|
SUBCELLULAR LOCATION: [Isoform 1]: Secreted {ECO:0000269|PubMed:10899913, ECO:0000269|PubMed:11062505}. Note=During differentiation, B-lymphocytes switch from expression of membrane-bound IgM to secretion of IgM.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000269|PubMed:10899913}; Single-pass membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Constant region of immunoglobulin heavy chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (By similarity). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (By similarity). {ECO:0000250|UniProtKB:P01871}.; FUNCTION: [Isoform 1]: Constant region of secreted IgM (sIgM), also known as the Fc region of IgM antibody. Able to multimerize, forms high order polymers, mainly pentamers and occasionally hexamers, providing for multivalency and high avidity recognition of antigens (By similarity). Natural sIgM are polyreactive and recognize conserved self- and pathogen-derived structures, whereas immune sIgM are secreted only upon exposure to pathogens and are antigen-specific. Both natural and immune sIgM are required for an efficient humoral immune response to infection (PubMed:10899913, PubMed:28135254, PubMed:34788614). Mediates sIgM effector functions mostly via Fc receptors and the complement system. On lymphoid cells binds high-affinity Fc receptor FCMR and promotes induction of an efficient neutralizing IgG response while maintaining tolerance to self-antigens. Recruits C1q complement component to initiate the classical complement pathway, facilitating the recognition and neutralization of pathogens by the host. Together with C1q and mannose-binding lectin promotes the phagocytosis of apoptotic cells by macrophages, ensuring the clearance of potential autoimmune epitopes from tissues (By similarity) (PubMed:10899913, PubMed:11062505, PubMed:28135254). Involved in mucosal immunity. It is transported by transcytosis across mucosal epithelium by PIGR and secreted on the apical side in complex with PIGR secretory component to scan mucosal lining for pathogens. IgM-antigen complexes undergo FCMR-mediated retrotranscytosis across mucosal M cells toward antigen-presenting cells in mucosal lymphoid tissues (PubMed:34788614). {ECO:0000250|UniProtKB:P01871, ECO:0000269|PubMed:10899913, ECO:0000269|PubMed:11062505, ECO:0000269|PubMed:28135254, ECO:0000269|PubMed:34788614}.; FUNCTION: [Isoform 2]: Constant region of membrane-bound IgM, part of the B cell receptor complex (BCR). IgM BCR provides constitutive tonic signaling for B cell survival. Mediates pre-BCR signaling that regulates B cell selection and rearrangement of Ig genes via allelic exclusion. {ECO:0000269|PubMed:1545868, ECO:0000269|PubMed:1901381, ECO:0000269|PubMed:28135254}.
|
Mus musculus (Mouse)
|
P01876
|
IGHA1_HUMAN
|
ASPTSPKVFPLSLCSTQPDGNVVIACLVQGFFPQEPLSVTWSESGQGVTARNFPPSQDASGDLYTTSSQLTLPATQCLAGKSVTCHVKHYTNPSQDVTVPCPVPSTPPTPSPSTPPTPSPSCCHPRLSLHRPALEDLLLGSEANLTCTLTGLRDASGVTFTWTPSSGKSAVQGPPERDLCGCYSVSSVLPGCAEPWNHGKTFTCTAAYPESKTPLTATLSKSGNTFRPEVHLLPPPSEELALNELVTLTCLARGFSPKDVLVRWLQGSQELPREKYLTWASRQEPSQGTTTFAVTSILRVAAEDWKKGDTFSCMVGHEALPLAFTQKTIDRLADWQMPPPYVVLDLPQETLEEETPGANLWPTTITFLTLFLLSLFYSTALTVTSVRGPSGNREGPQY
| null | null |
adaptive immune response [GO:0002250]; antibacterial humoral response [GO:0019731]; B cell receptor signaling pathway [GO:0050853]; complement activation, classical pathway [GO:0006958]; glomerular filtration [GO:0003094]; immune response [GO:0006955]; positive regulation of respiratory burst [GO:0060267]
|
blood microparticle [GO:0072562]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; IgA immunoglobulin complex [GO:0071745]; IgG immunoglobulin complex [GO:0071735]; immunoglobulin complex, circulating [GO:0042571]; monomeric IgA immunoglobulin complex [GO:0071748]; plasma membrane [GO:0005886]; secretory dimeric IgA immunoglobulin complex [GO:0071752]; secretory IgA immunoglobulin complex [GO:0071751]
|
antigen binding [GO:0003823]; immunoglobulin receptor binding [GO:0034987]
|
PF07654;PF00047;
|
2.60.40.10;
| null |
PTM: [Isoform 1]: 3-Hydroxykynurenine, an oxidized tryptophan metabolite that is common in biological fluids, reacts with alpha-1-microglobulin to form heterogeneous polycyclic chromophores including hydroxanthommatin. The chromophore reacts with accessible cysteines forming non-reducible thioether cross-links with Ig alpha-1 chain C region Cys-352. {ECO:0000269|PubMed:7506257}.; PTM: N- and O-glycosylated. N-glycan at Asn-144: Hex5HexNAc4. {ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:22171320}.
|
SUBCELLULAR LOCATION: [Isoform 1]: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}; Single-pass type I membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Constant region of immunoglobulin heavy chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268). Ig alpha is the major immunoglobulin class in body secretions (PubMed:2241915). {ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414, ECO:0000303|PubMed:2241915}.
|
Homo sapiens (Human)
|
P01877
|
IGHA2_HUMAN
|
ASPTSPKVFPLSLDSTPQDGNVVVACLVQGFFPQEPLSVTWSESGQNVTARNFPPSQDASGDLYTTSSQLTLPATQCPDGKSVTCHVKHYTNSSQDVTVPCRVPPPPPCCHPRLSLHRPALEDLLLGSEANLTCTLTGLRDASGATFTWTPSSGKSAVQGPPERDLCGCYSVSSVLPGCAQPWNHGETFTCTAAHPELKTPLTANITKSGNTFRPEVHLLPPPSEELALNELVTLTCLARGFSPKDVLVRWLQGSQELPREKYLTWASRQEPSQGTTTYAVTSILRVAAEDWKKGETFSCMVGHEALPLAFTQKTIDRMAGSCCVADWQMPPPYVVLDLPQETLEEETPGANLWPTTITFLTLFLLSLFYSTALTVTSVRGPSGKREGPQY
| null | null |
adaptive immune response [GO:0002250]; antibacterial humoral response [GO:0019731]; B cell receptor signaling pathway [GO:0050853]; complement activation, classical pathway [GO:0006958]; glomerular filtration [GO:0003094]; immune response [GO:0006955]; positive regulation of respiratory burst [GO:0060267]
|
blood microparticle [GO:0072562]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; IgA immunoglobulin complex [GO:0071745]; immunoglobulin complex, circulating [GO:0042571]; monomeric IgA immunoglobulin complex [GO:0071748]; plasma membrane [GO:0005886]; secretory dimeric IgA immunoglobulin complex [GO:0071752]; secretory IgA immunoglobulin complex [GO:0071751]
|
antigen binding [GO:0003823]; immunoglobulin receptor binding [GO:0034987]
|
PF07654;PF00047;
|
2.60.40.10;
| null | null |
SUBCELLULAR LOCATION: [Isoform 1]: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.; SUBCELLULAR LOCATION: Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}; Single-pass type I membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Constant region of immunoglobulin heavy chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268). Ig alpha is the major immunoglobulin class in body secretions (PubMed:2241915). {ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414, ECO:0000303|PubMed:2241915}.
|
Homo sapiens (Human)
|
P01878
|
IGHA_MOUSE
|
ESARNPTIYPLTLPPALSSDPVIIGCLIHDYFPSGTMNVTWGKSGKDITTVNFPPALASGGRYTMSNQLTLPAVECPEGESVKCSVQHDSNPVQELDVNCSGPTPPPPITIPSCQPSLSLQRPALEDLLLGSDASITCTLNGLRNPEGAVFTWEPSTGKDAVQKKAVQNSCGCYSVSSVLPGCAERWNSGASFKCTVTHPESGTLTGTIAKVTVNTFPPQVHLLPPPSEELALNELLSLTCLVRAFNPKEVLVRWLHGNEELSPESYLVFEPLKEPGEGATTYLVTSVLRVSAETWKQGDQYSCMVGHEALPMNFTQKTIDRLSGKPTNVSVSVIMSEGDGICY
| null | null |
antibacterial humoral response [GO:0019731]; complement activation, classical pathway [GO:0006958]
|
blood microparticle [GO:0072562]; extracellular exosome [GO:0070062]; immunoglobulin complex, circulating [GO:0042571]
|
antigen binding [GO:0003823]; immunoglobulin receptor binding [GO:0034987]
|
PF07654;
|
2.60.40.10;
| null | null | null | null | null | null | null | null |
FUNCTION: Ig alpha is the major immunoglobulin class in body secretions. It may serve both to defend against local infection and to prevent access of foreign antigens to the general immunologic system.
|
Mus musculus (Mouse)
|
P01880
|
IGHD_HUMAN
|
APTKAPDVFPIISGCRHPKDNSPVVLACLITGYHPTSVTVTWYMGTQSQPQRTFPEIQRRDSYYMTSSQLSTPLQQWRQGEYKCVVQHTASKSKKEIFRWPESPKAQASSVPTAQPQAEGSLAKATTAPATTRNTGRGGEEKKKEKEKEEQEERETKTPECPSHTQPLGVYLLTPAVQDLWLRDKATFTCFVVGSDLKDAHLTWEVAGKVPTGGVEEGLLERHSNGSQSQHSRLTLPRSLWNAGTSVTCTLNHPSLPPQRLMALREPAAQAPVKLSLNLLASSDPPEAASWLLCEVSGFSPPNILLMWLEDQREVNTSGFAPARPPPQPRSTTFWAWSVLRVPAPPSPQPATYTCVVSHEDSRTLLNASRSLEVSYLAMTPLIPQSKDENSDDYTTFDDVGSLWTTLSTFVALFILTLLYSGIVTFIKVK
| null | null |
adaptive immune response [GO:0002250]; antibacterial humoral response [GO:0019731]; B cell receptor signaling pathway [GO:0050853]; complement activation, classical pathway [GO:0006958]; immune response [GO:0006955]; immunoglobulin mediated immune response [GO:0016064]; positive regulation of interleukin-1 production [GO:0032732]
|
blood microparticle [GO:0072562]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; IgD immunoglobulin complex [GO:0071738]; immunoglobulin complex, circulating [GO:0042571]; plasma membrane [GO:0005886]
|
antigen binding [GO:0003823]; immunoglobulin receptor binding [GO:0034987]
|
PF07654;PF00047;PF20838;
|
2.60.40.10;
| null | null |
SUBCELLULAR LOCATION: [Isoform 1]: Secreted {ECO:0000303|PubMed:11282392}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane; Single-pass type I membrane protein {ECO:0000303|PubMed:11282392}.
| null | null | null | null | null |
FUNCTION: Constant region of immunoglobulin heavy chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268). IgD is the major antigen receptor isotype on the surface of most peripheral B-cells, where it is coexpressed with IgM. The membrane-bound IgD (mIgD) induces the phosphorylation of CD79A and CD79B by the Src family of protein tyrosine kinases. Soluble IgD (sIgD) concentration in serum below those of IgG, IgA, and IgM but much higher than that of IgE. IgM and IgD molecules present on B cells have identical V regions and antigen-binding sites. After the antigen binds to the B-cell receptor, the secreted form sIgD is shut off. IgD is a potent inducer of TNF, IL1B, and IL1RN. IgD also induces release of IL6, IL10, and LIF from peripheral blood mononuclear cells. Monocytes seem to be the main producers of cytokines in vitro in the presence of IgD (PubMed:10702483, PubMed:11282392, PubMed:8774350). {ECO:0000269|PubMed:8774350, ECO:0000303|PubMed:10702483, ECO:0000303|PubMed:11282392, ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
|
Homo sapiens (Human)
|
P01887
|
B2MG_MOUSE
|
MARSVTLVFLVLVSLTGLYAIQKTPQIQVYSRHPPENGKPNILNCYVTQFHPPHIEIQMLKNGKKIPKVEMSDMSFSKDWSFYILAHTEFTPTETDTYACRVKHASMAEPKTVYWDRDM
| null | null |
amyloid fibril formation [GO:1990000]; antigen processing and presentation of endogenous peptide antigen via MHC class I [GO:0019885]; antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; antigen processing and presentation of exogenous protein antigen via MHC class Ib, TAP-dependent [GO:0002481]; cellular defense response [GO:0006968]; cellular response to iron(III) ion [GO:0071283]; cellular response to nicotine [GO:0071316]; intracellular iron ion homeostasis [GO:0006879]; iron ion transport [GO:0006826]; learning or memory [GO:0007611]; multicellular organismal-level iron ion homeostasis [GO:0060586]; negative regulation of epithelial cell proliferation [GO:0050680]; negative regulation of forebrain neuron differentiation [GO:2000978]; negative regulation of neurogenesis [GO:0050768]; negative regulation of neuron projection development [GO:0010977]; peptide antigen assembly with MHC class I protein complex [GO:0002502]; peptide antigen assembly with MHC class II protein complex [GO:0002503]; positive regulation of cellular senescence [GO:2000774]; positive regulation of immune response [GO:0050778]; positive regulation of receptor-mediated endocytosis [GO:0048260]; positive regulation of T cell activation [GO:0050870]; positive regulation of T cell cytokine production [GO:0002726]; positive regulation of T cell mediated cytotoxicity [GO:0001916]; protein homotetramerization [GO:0051289]; protein refolding [GO:0042026]; regulation of erythrocyte differentiation [GO:0045646]; regulation of iron ion transport [GO:0034756]; response to molecule of bacterial origin [GO:0002237]; sensory perception of smell [GO:0007608]; T cell differentiation in thymus [GO:0033077]; T cell mediated cytotoxicity [GO:0001913]
|
cytosol [GO:0005829]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; HFE-transferrin receptor complex [GO:1990712]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; MHC class I peptide loading complex [GO:0042824]; MHC class I protein complex [GO:0042612]; MHC class II protein complex [GO:0042613]; phagocytic vesicle membrane [GO:0030670]
|
MHC class II protein complex binding [GO:0023026]; peptide antigen binding [GO:0042605]; protein homodimerization activity [GO:0042803]; structural molecule activity [GO:0005198]
|
PF07654;
|
2.60.40.10;
|
Beta-2-microglobulin family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system.
|
Mus musculus (Mouse)
|
P01888
|
B2MG_BOVIN
|
MARFVALVLLGLLSLSGLDAIQRPPKIQVYSRHPPEDGKPNYLNCYVYGFHPPQIEIDLLKNGEKIKSEQSDLSFSKDWSFYLLSHAEFTPNSKDQYSCRVKHVTLEQPRIVKWDRDL
| null | null |
antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; immune response [GO:0006955]; peptide antigen assembly with MHC class II protein complex [GO:0002503]; positive regulation of immune response [GO:0050778]; positive regulation of T cell activation [GO:0050870]
|
extracellular region [GO:0005576]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; MHC class I protein complex [GO:0042612]; MHC class II protein complex [GO:0042613]
|
MHC class II protein complex binding [GO:0023026]; peptide antigen binding [GO:0042605]
|
PF07654;
|
2.60.40.10;
|
Beta-2-microglobulin family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system.
|
Bos taurus (Bovine)
|
P01889
|
HLAB_HUMAN
|
MLVMAPRTVLLLLSAALALTETWAGSHSMRYFYTSVSRPGRGEPRFISVGYVDDTQFVRFDSDAASPREEPRAPWIEQEGPEYWDRNTQIYKAQAQTDRESLRNLRGYYNQSEAGSHTLQSMYGCDVGPDGRLLRGHDQYAYDGKDYIALNEDLRSWTAADTAAQITQRKWEAAREAEQRRAYLEGECVEWLRRYLENGKDKLERADPPKTHVTHHPISDHEATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDRTFQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRWEPSSQSTVPIVGIVAGLAVLAVVVIGAVVAAVMCRRKSSGGKGGSYSQAACSDSAQGSDVSLTA
| null | null |
adaptive immune response [GO:0002250]; antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent [GO:0002486]; antigen processing and presentation of endogenous peptide antigen via MHC class Ib [GO:0002476]; defense response [GO:0006952]; detection of bacterium [GO:0016045]; immune response [GO:0006955]; innate immune response [GO:0045087]; positive regulation of T cell mediated cytotoxicity [GO:0001916]; protection from natural killer cell mediated cytotoxicity [GO:0042270]; regulation of dendritic cell differentiation [GO:2001198]; regulation of interleukin-12 production [GO:0032655]; regulation of interleukin-6 production [GO:0032675]; regulation of T cell anergy [GO:0002667]
|
cell surface [GO:0009986]; early endosome membrane [GO:0031901]; endoplasmic reticulum [GO:0005783]; ER to Golgi transport vesicle membrane [GO:0012507]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; lumenal side of endoplasmic reticulum membrane [GO:0098553]; membrane [GO:0016020]; MHC class I protein complex [GO:0042612]; phagocytic vesicle membrane [GO:0030670]; plasma membrane [GO:0005886]; recycling endosome membrane [GO:0055038]; secretory granule membrane [GO:0030667]
|
peptide antigen binding [GO:0042605]; protein-folding chaperone binding [GO:0051087]; signaling receptor binding [GO:0005102]; TAP binding [GO:0046977]
|
PF07654;PF00129;PF06623;
|
2.60.40.10;3.30.500.10;
| null | null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25480565, ECO:0000269|PubMed:26439010, ECO:0000269|PubMed:9620674}; Single-pass type I membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000305|PubMed:9620674}; Single-pass type I membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Antigen-presenting major histocompatibility complex class I (MHCI) molecule. In complex with B2M/beta 2 microglobulin displays primarily viral and tumor-derived peptides on antigen-presenting cells for recognition by alpha-beta T cell receptor (TCR) on HLA-B-restricted CD8-positive T cells, guiding antigen-specific T cell immune response to eliminate infected or transformed cells (PubMed:23209413, PubMed:25808313, PubMed:29531227, PubMed:9620674). May also present self-peptides derived from the signal sequence of secreted or membrane proteins, although T cells specific for these peptides are usually inactivated to prevent autoreactivity (PubMed:18991276, PubMed:7743181). Both the peptide and the MHC molecule are recognized by TCR, the peptide is responsible for the fine specificity of antigen recognition and MHC residues account for the MHC restriction of T cells (PubMed:24600035, PubMed:29531227, PubMed:9620674). Typically presents intracellular peptide antigens of 8 to 13 amino acids that arise from cytosolic proteolysis via constitutive proteasome and IFNG-induced immunoproteasome (PubMed:23209413). Can bind different peptides containing allele-specific binding motifs, which are mainly defined by anchor residues at position 2 and 9 (PubMed:25808313, PubMed:29531227). {ECO:0000269|PubMed:18991276, ECO:0000269|PubMed:23209413, ECO:0000269|PubMed:24600035, ECO:0000269|PubMed:25808313, ECO:0000269|PubMed:29531227, ECO:0000269|PubMed:7743181, ECO:0000269|PubMed:9620674}.; FUNCTION: Allele B*07:02: Displays peptides sharing a common signature motif, namely a Pro residue at position 2 and mainly a Leu anchor residue at the C-terminus (PubMed:7743181). Presents a long peptide (APRGPHGGAASGL) derived from the cancer-testis antigen CTAG1A/NY-ESO-1, eliciting a polyclonal CD8-positive T cell response against tumor cells (PubMed:29531227). Presents viral epitopes derived from HIV-1 gag-pol (TPQDLNTML) and Nef (RPQVPLRPM) (PubMed:25808313). Presents an immunodominant epitope derived from SARS-CoV-2 N/nucleoprotein (SPRWYFYYL) (PubMed:32887977). Displays self-peptides including a peptide derived from the signal sequence of HLA-DPB1 (APRTVALTA) (PubMed:7743181). {ECO:0000269|PubMed:25808313, ECO:0000269|PubMed:29531227, ECO:0000269|PubMed:32887977, ECO:0000269|PubMed:7743181}.; FUNCTION: Allele B*08:01: Presents to CD8-positive T cells viral epitopes derived from EBV/HHV-4 EBNA3 (QAKWRLQTL), eliciting cytotoxic T cell response. {ECO:0000269|PubMed:9620674}.; FUNCTION: Allele B*13:02: Presents multiple HIV-1 epitopes derived from gag (RQANFLGKI, GQMREPRGSDI), nef (RQDILDLWI), gag-pol (RQYDQILIE, GQGQWTYQI) and rev (LQLPPLERL), all having in common a Gln residue at position 2 and mainly hydrophobic amino acids Leu, Ile or Val at the C-terminus. Associated with succesful control of HIV-1 infection. {ECO:0000269|PubMed:17251285}.; FUNCTION: Allele B*18:01: Preferentially presents octomeric and nonameric peptides sharing a common motif, namely a Glu at position 2 and Phe or Tyr anchor residues at the C-terminus (PubMed:14978097, PubMed:18991276, PubMed:23749632). Presents an EBV/HHV-4 epitope derived from BZLF1 (SELEIKRY) (PubMed:23749632). May present to CD8-positive T cells an antigenic peptide derived from MAGEA3 (MEVDPIGHLY), triggering an anti-tumor immune response (PubMed:12366779). May display a broad repertoire of self-peptides with a preference for peptides derived from RNA-binding proteins (PubMed:14978097). {ECO:0000269|PubMed:12366779, ECO:0000269|PubMed:14978097, ECO:0000269|PubMed:18991276, ECO:0000269|PubMed:23749632}.; FUNCTION: Allele B*27:05: Presents to CD8-positive T cells immunodominant viral epitopes derived from HCV POLG (ARMILMTHF), HIV-1 gag (KRWIILGLNK), IAV NP (SRYWAIRTR), SARS-CoV-2 N/nucleoprotein (QRNAPRITF), EBV/HHV-4 EBNA4 (HRCQAIRKK) and EBV/HHV-4 EBNA6 (RRIYDLIEL), conferring longterm protection against viral infection (PubMed:15113903, PubMed:18385228, PubMed:19139562, PubMed:32887977, PubMed:9620674). Can present self-peptides derived from cytosolic and nuclear proteins. All peptides carry an Arg at position 2 (PubMed:1922338). The peptide-bound form interacts with NK cell inhibitory receptor KIR3DL1 and inhibits NK cell activation in a peptide-specific way, being particularly sensitive to the nature of the amino acid side chain at position 8 of the antigenic peptide (PubMed:15657948, PubMed:8879234). KIR3DL1 fails to recognize HLA-B*27:05 in complex with B2M and EBV/HHV-4 EBNA6 (RRIYDLIEL) peptide, which can lead to increased activation of NK cells during infection (PubMed:15657948). May present an altered repertoire of peptides in the absence of TAP1-TAP2 and TAPBPL (PubMed:9620674). {ECO:0000269|PubMed:15113903, ECO:0000269|PubMed:15657948, ECO:0000269|PubMed:18385228, ECO:0000269|PubMed:19139562, ECO:0000269|PubMed:1922338, ECO:0000269|PubMed:8879234, ECO:0000269|PubMed:9620674}.; FUNCTION: Allele B*40:01: Presents immunodominant viral epitopes derived from EBV/HHV-4 LMP2 (IEDPPFNSL) and SARS-CoV-2 N/nucleoprotein (MEVTPSGTWL), triggering memory CD8-positive T cell response (PubMed:18991276, PubMed:32887977). Displays self-peptides sharing a signature motif, namely a Glu at position 2 and a Leu anchor residue at the C-terminus (PubMed:18991276). {ECO:0000269|PubMed:18991276, ECO:0000269|PubMed:32887977}.; FUNCTION: Allele B*41:01: Displays self-peptides sharing a signature motif, namely a Glu at position 2 and Ala or Pro anchor residues at the C-terminus. {ECO:0000269|PubMed:18991276}.; FUNCTION: Allele B*44:02: Presents immunodominant viral epitopes derived from EBV/HHV-4 EBNA4 (VEITPYKPTW) and EBNA6 (AEGGVGWRHW, EENLLDFVRF), triggering memory CD8-positive T cell response (PubMed:18991276, PubMed:9620674). Displays self-peptides sharing a signature motif, namely a Glu at position 2 and Phe, Tyr or Trp anchor residues at the C-terminus (PubMed:18991276). {ECO:0000269|PubMed:18991276, ECO:0000269|PubMed:9620674}.; FUNCTION: Allele B*45:01: Displays self-peptides sharing a signature motif, namely a Glu at position 2 and Ala or Pro anchor residues at the C-terminus. {ECO:0000269|PubMed:18991276}.; FUNCTION: Allele B*46:01: Preferentially presents nonameric peptides sharing a signature motif, namely Ala and Leu at position 2 and Tyr, Phe, Leu, or Met anchor residues at the C-terminus. The peptide-bound form interacts with KIR2DL3 and inhibits NK cell cytotoxic response in a peptide-specific way. {ECO:0000269|PubMed:28514659}.; FUNCTION: Allele B*47:01: Displays self-peptides sharing a signature motif, namely an Asp at position 2 and Leu or Met anchor residues at the C-terminus. {ECO:0000269|PubMed:18991276}.; FUNCTION: Allele B*49:01: Displays self-peptides sharing a signature motif, namely a Glu at position 2 and Ile or Val anchor residues at the C-terminus. {ECO:0000269|PubMed:18991276}.; FUNCTION: Allele B*50:01: Displays self-peptides sharing a signature motif, namely a Glu at position 2 and Ala or Pro anchor residues at the C-terminus. {ECO:0000269|PubMed:18991276}.; FUNCTION: Allele B*51:01: Presents an octomeric HIV-1 epitope derived from gag-pol (TAFTIPSI) to the public TRAV17/TRBV7-3 TCR clonotype, strongly suppressing HIV-1 replication. {ECO:0000269|PubMed:24600035}.; FUNCTION: Allele B*54:01: Displays peptides sharing a common signature motif, namely a Pro residue at position 2 and Ala anchor residue at the C-terminus. {ECO:0000269|PubMed:7743181}.; FUNCTION: Allele B*55:01: Displays peptides sharing a common signature motif, namely a Pro residue at position 2 and Ala anchor residue at the C-terminus. {ECO:0000269|PubMed:7743181}.; FUNCTION: Allele B*56:01: Displays peptides sharing a common signature motif, namely a Pro residue at position 2 and Ala anchor residue at the C-terminus. {ECO:0000269|PubMed:7743181}.; FUNCTION: Allele B*57:01: The peptide-bound form recognizes KIR3DL1 and inhibits NK cell cytotoxic response. Presents HIV gag peptides (immunodominant KAFSPEVIPMF and subdominant KALGPAATL epitopes) predominantly to CD8-positive T cell clones expressing a TRAV41-containing TCR, triggering HLA-B-restricted T cell responses. {ECO:0000269|PubMed:22020283, ECO:0000269|PubMed:25480565, ECO:0000269|PubMed:34228645}.; FUNCTION: Allele B*67:01: Displays peptides sharing a common signature motif, namely a Pro residue at position 2 and Leu anchor residue at the C-terminus. {ECO:0000269|PubMed:7743181}.
|
Homo sapiens (Human)
|
P01893
|
HLAH_HUMAN
|
MVLMAPRTLLLLLSGALALTQTWARSHSMRYFYTTMSRPGAGEPRFISVGYVDDTQFVRFDSDDASPREEPRAPWMEREGPKYWDRNTQICKAQAQTERENLRIALRYYNQSEGGSHTMQVMYGCDVGPDGPFLRGYEQHAYDGKDYIALNEDLRSWTAADMAAQITKRKWEAARRAEQRRVYLEGEFVEWLRRYLENGKETLQRADPPKTHMTHHPISDHEATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPLTLRWEPSSQPTVPIVGIVAGLVLLVAVVTGAVVAAVMWRKKSSDRKGGSYSQAASSNSAQGSDVSLTA
| null | null |
antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent [GO:0002486]; antigen processing and presentation of endogenous peptide antigen via MHC class Ib [GO:0002476]; immune response [GO:0006955]; positive regulation of T cell mediated cytotoxicity [GO:0001916]
|
azurophil granule membrane [GO:0035577]; cell surface [GO:0009986]; early endosome membrane [GO:0031901]; ER to Golgi transport vesicle membrane [GO:0012507]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; Golgi membrane [GO:0000139]; lumenal side of endoplasmic reticulum membrane [GO:0098553]; MHC class I protein complex [GO:0042612]; phagocytic vesicle membrane [GO:0030670]; plasma membrane [GO:0005886]; recycling endosome membrane [GO:0055038]
|
beta-2-microglobulin binding [GO:0030881]; peptide antigen binding [GO:0042605]; signaling receptor binding [GO:0005102]
|
PF07654;PF00129;PF06623;
|
2.60.40.10;3.30.500.10;
|
MHC class I family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Involved in the presentation of foreign antigens to the immune system.
|
Homo sapiens (Human)
|
P01894
|
HA1A_RABIT
|
MGSMAPRTLLLLLAGALTLKDTQAGSHSMRYFYTSVSRPGLGEPRFIIVGYVDDTQFVRFDSDAASPRMEQRAPWMGQVEPEYWDQQTQIAKDTAQTFRVNLNTALRYYNQSAAGSHTFQTMFGCEVWADGRFFHGYRQYAYDGADYIALNEDLRSWTAADTAAQNTQRKWEAAGEAERHRAYLERECVEWLRRYLEMGKETLQRADPPKAHVTHHPASDREATLRCWALGFYPAEISLTWQRDGEDQTQDTELVETRPGGDGTFQKWAAVVVPSGEEQRYTCRVQHEGLPEPLTLTWEPPAQPTALIVGIVAGVLGVLLILGAVVAVVRRKKHSSDGKGGRYTPAAGGHRDQGSDDSLMP
| null | null |
antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent [GO:0002486]; antigen processing and presentation of endogenous peptide antigen via MHC class Ib [GO:0002476]; immune response [GO:0006955]; positive regulation of T cell mediated cytotoxicity [GO:0001916]
|
external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; lumenal side of endoplasmic reticulum membrane [GO:0098553]; MHC class I protein complex [GO:0042612]; phagocytic vesicle membrane [GO:0030670]
|
peptide antigen binding [GO:0042605]; signaling receptor binding [GO:0005102]
|
PF07654;PF00129;PF06623;
|
2.60.40.10;3.30.500.10;
|
MHC class I family
| null |
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
| null | null | null | null | null |
FUNCTION: Involved in the presentation of foreign antigens to the immune system.
|
Oryctolagus cuniculus (Rabbit)
|
P01895
|
HA1Y_MOUSE
|
RYEPRARWIEQEGPEYWERETRRAKGNEQSFRVDLRTALRYYNQSAGGSHTLQWMAGCDVESDGRLLRGYWQFAYDGCDYIALNEDLKTWTAADMAAQITRRKWEQAGAAERDRAYLEGECVEWLRRYLKNGNATLLRTDPPKAHVTHHRRPEGDVTLRCWALGFYPADITLTWQLNGEELTQEMELVETRPAGDGTFQKWASVVVPLGKEQKYTCHVEHEGLPEPLTLRWGKEEPPSSTKTNTVIIAVPVVLGAVVILGAVMAFVMKRRRNTGGKGGDYALAPVSQSSDMSLPDCKV
| null | null |
antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-dependent [GO:0002485]; antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent [GO:0002486]; antigen processing and presentation of endogenous peptide antigen via MHC class Ib [GO:0002476]; immune response [GO:0006955]; negative regulation of neuron projection development [GO:0010977]; positive regulation of T cell mediated cytotoxicity [GO:0001916]; T cell mediated cytotoxicity [GO:0001913]
|
external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; lumenal side of endoplasmic reticulum membrane [GO:0098553]; MHC class I protein complex [GO:0042612]; phagocytic vesicle membrane [GO:0030670]; plasma membrane [GO:0005886]
|
beta-2-microglobulin binding [GO:0030881]; peptide antigen binding [GO:0042605]; peptide binding [GO:0042277]; protein-containing complex binding [GO:0044877]; signaling receptor binding [GO:0005102]
|
PF07654;PF00129;PF06623;
|
2.60.40.10;3.30.500.10;
|
MHC class I family
| null |
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
| null | null | null | null | null |
FUNCTION: Involved in the presentation of foreign antigens to the immune system.
|
Mus musculus (Mouse)
|
P01897
|
HA1L_MOUSE
|
MGAMAPRTLLLLLAAALAPTQTRAGPHSMRYFETAVSRPGLGEPRYISVGYVDNKEFVRFDSDAENPRYEPQAPWMEQEGPEYWERITQIAKGQEQWFRVNLRTLLGYYNQSAGGTHTLQWMYGCDVGSDGRLLRGYEQFAYDGCDYIALNEDLKTWTAADMAAQITRRKWEQAGAAEYYRAYLEGECVEWLHRYLKNGNATLLRTDSPKAHVTHHPRSKGEVTLRCWALGFYPADITLTWQLNGEELTQDMELVETRPAGDGTFQKWASVVVPLGKEQNYTCRVYHEGLPEPLTLRWEPPPSTDSYMVIVAVLGVLGAMAIIGAVVAFVMKRRRNTGGKGGDYALAPGSQSSEMSLRDCKA
| null | null |
antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent [GO:0002486]; antigen processing and presentation of endogenous peptide antigen via MHC class Ib [GO:0002476]; defense response [GO:0006952]; immune response [GO:0006955]; positive regulation of T cell mediated cytotoxicity [GO:0001916]
|
external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; lumenal side of endoplasmic reticulum membrane [GO:0098553]; MHC class I protein complex [GO:0042612]; phagocytic vesicle membrane [GO:0030670]
|
peptide antigen binding [GO:0042605]; signaling receptor binding [GO:0005102]
|
PF07654;PF00129;PF06623;
|
2.60.40.10;3.30.500.10;
|
MHC class I family
| null |
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
| null | null | null | null | null |
FUNCTION: Involved in the presentation of foreign antigens to the immune system.
|
Mus musculus (Mouse)
|
P01898
|
HA10_MOUSE
|
MGAMAPRTLLLLLAAALAPTQTQAGSHSMRYFETSVSRPGLGEPRFIIVGYVDDTQFVRFDSDAETPRMEPRAPWMEQEGPEYWERETQRAKGNEQSFHVSLRTLLGYYNQSESGSHTIQWMYGCKVGSDGRFLRGYLQYAYDGRDYIALNEDLKTWTAADVAAIITRRKWEQAGAAEYYRAYLEAECVEWLLRYLELGKETLLRTDPPKTHVTHHPGSEGDVTLRCWALGFYPADITLTWQLNGEELTQDMELVETRPAGDGTFQKWASVVVPLGKEQNYTCHVYHEGLPEPLTLRWEPPPSTDSIMSHIADLLWPSLKLWWYL
| null | null |
antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent [GO:0002486]; antigen processing and presentation of endogenous peptide antigen via MHC class Ib [GO:0002476]; immune response [GO:0006955]; positive regulation of T cell mediated cytotoxicity [GO:0001916]
|
external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; lumenal side of endoplasmic reticulum membrane [GO:0098553]; MHC class I protein complex [GO:0042612]; phagocytic vesicle membrane [GO:0030670]
|
beta-2-microglobulin binding [GO:0030881]; peptide antigen binding [GO:0042605]; peptide binding [GO:0042277]; protein-containing complex binding [GO:0044877]; signaling receptor binding [GO:0005102]
|
PF07654;PF00129;
|
2.60.40.10;3.30.500.10;
|
MHC class I family
| null |
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
| null | null | null | null | null |
FUNCTION: Involved in the presentation of foreign antigens to the immune system.
|
Mus musculus (Mouse)
|
P01899
|
HA11_MOUSE
|
MGAMAPRTLLLLLAAALAPTQTRAGPHSMRYFETAVSRPGLEEPRYISVGYVDNKEFVRFDSDAENPRYEPRAPWMEQEGPEYWERETQKAKGQEQWFRVSLRNLLGYYNQSAGGSHTLQQMSGCDLGSDWRLLRGYLQFAYEGRDYIALNEDLKTWTAADMAAQITRRKWEQSGAAEHYKAYLEGECVEWLHRYLKNGNATLLRTDSPKAHVTHHPRSKGEVTLRCWALGFYPADITLTWQLNGEELTQDMELVETRPAGDGTFQKWASVVVPLGKEQNYTCRVYHEGLPEPLTLRWEPPPSTDSYMVIVAVLGVLGAMAIIGAVVAFVMKRRRNTGGKGGDYALAPGSQSSEMSLRDCKA
| null | null |
antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-dependent [GO:0002485]; antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent [GO:0002486]; antigen processing and presentation of endogenous peptide antigen via MHC class Ib [GO:0002476]; immune response [GO:0006955]; negative regulation of neuron projection development [GO:0010977]; positive regulation of T cell mediated cytotoxicity [GO:0001916]; T cell mediated cytotoxicity [GO:0001913]
|
external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; lumenal side of endoplasmic reticulum membrane [GO:0098553]; MHC class I protein complex [GO:0042612]; phagocytic vesicle membrane [GO:0030670]; plasma membrane [GO:0005886]
|
beta-2-microglobulin binding [GO:0030881]; peptide antigen binding [GO:0042605]; peptide binding [GO:0042277]; protein-containing complex binding [GO:0044877]; signaling receptor binding [GO:0005102]
|
PF07654;PF00129;PF06623;
|
2.60.40.10;3.30.500.10;
|
MHC class I family
|
PTM: Polyubiquitinated in case of infection by murid herpesvirus 4, by the viral E3 ligase K3 (mK3). This modification causes the protein to be targeted for rapid degradation by the endoplasmic reticulum-associated degradation (ERAD) system. Ubiquitination occurs on lysine, as well as serine and threonine residues present in the cytoplasmic tail. Serine and threonine residues are subject to ubiquitination via ester bonds instead of the usual isopeptide linkage. {ECO:0000269|PubMed:17502423, ECO:0000269|PubMed:19531064, ECO:0000269|PubMed:19951915}.
|
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
| null | null | null | null | null |
FUNCTION: Involved in the presentation of foreign antigens to the immune system.
|
Mus musculus (Mouse)
|
P01900
|
HA12_MOUSE
|
MGAMAPRTLLLLLAAALGPTQTRAGSHSLRYFVTAVSRPGFGEPRYMEVGYVDNTEFVRFDSDAENPRYEPRARWIEQEGPEYWERETRRAKGNEQSFRVDLRTALRYYNQSAGGSHTLQWMAGCDVESDGRLLRGYWQFAYDGCDYIALNEDLKTWTAADMAAQITRRKWEQAGAAERDRAYLEGECVEWLRRYLKNGNATLLRTDPPKAHVTHHRRPEGDVTLRCWALGFYPADITLTWQLNGEELTQEMELVETRPAGDGTFQKWASVVVPLGKEQKYTCHVEHEGLPEPLTLRWGKEEPPSSTKTNTVIIAVPVVLGAVVILGAVMAFVMKRRRNTGGKGGDYALAPGSQSSDMSLPDCKV
| null | null |
antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-dependent [GO:0002485]; antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent [GO:0002486]; antigen processing and presentation of endogenous peptide antigen via MHC class Ib [GO:0002476]; immune response [GO:0006955]; negative regulation of neuron projection development [GO:0010977]; positive regulation of T cell mediated cytotoxicity [GO:0001916]; T cell mediated cytotoxicity [GO:0001913]
|
external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; lumenal side of endoplasmic reticulum membrane [GO:0098553]; MHC class I protein complex [GO:0042612]; phagocytic vesicle membrane [GO:0030670]; plasma membrane [GO:0005886]
|
beta-2-microglobulin binding [GO:0030881]; peptide antigen binding [GO:0042605]; peptide binding [GO:0042277]; protein-containing complex binding [GO:0044877]; signaling receptor binding [GO:0005102]
|
PF07654;PF00129;PF06623;
|
2.60.40.10;3.30.500.10;
|
MHC class I family
| null |
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
| null | null | null | null | null |
FUNCTION: Involved in the presentation of foreign antigens to the immune system.
|
Mus musculus (Mouse)
|
P01901
|
HA1B_MOUSE
|
MVPCTLLLLLAAALAPTQTRAGPHSLRYFVTAVSRPGLGEPRYMEVGYVDDTEFVRFDSDAENPRYEPRARWMEQEGPEYWERETQKAKGNEQSFRVDLRTLLGYYNQSKGGSHTIQVISGCEVGSDGRLLRGYQQYAYDGCDYIALNEDLKTWTAADMAALITKHKWEQAGEAERLRAYLEGTCVEWLRRYLKNGNATLLRTDSPKAHVTHHSRPEDKVTLRCWALGFYPADITLTWQLNGEELIQDMELVETRPAGDGTFQKWASVVVPLGKEQYYTCHVYHQGLPEPLTLRWEPPPSTVSNMATVAVLVVLGAAIVTGAVVAFVMKMRRRNTGGKGGDYALAPGSQTSDLSLPDCKVMVHDPHSLA
| null | null |
antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-dependent [GO:0002485]; antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent [GO:0002486]; antigen processing and presentation of endogenous peptide antigen via MHC class Ib [GO:0002476]; antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; defense response to bacterium [GO:0042742]; immune response [GO:0006955]; inner ear development [GO:0048839]; negative regulation of neuron projection development [GO:0010977]; positive regulation of T cell mediated cytotoxicity [GO:0001916]; T cell mediated cytotoxicity [GO:0001913]
|
external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; lumenal side of endoplasmic reticulum membrane [GO:0098553]; MHC class I protein complex [GO:0042612]; phagocytic vesicle membrane [GO:0030670]
|
beta-2-microglobulin binding [GO:0030881]; peptide antigen binding [GO:0042605]; peptide binding [GO:0042277]; protein-containing complex binding [GO:0044877]; signaling receptor binding [GO:0005102]
|
PF07654;PF00129;PF06623;
|
2.60.40.10;3.30.500.10;
|
MHC class I family
| null |
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
| null | null | null | null | null |
FUNCTION: Involved in the presentation of foreign antigens to the immune system.
|
Mus musculus (Mouse)
|
P01902
|
HA1D_MOUSE
|
MAPCTLLLLLAAALAPTQTRAGPHSLRYFVTAVSRPGLGEPRFIAVGYVDDTQFVRFDSDADNPRFEPRAPWMEQEGPEYWEEQTQRAKSDEQWFRVSLRTAQRYYNQSKGGSHTFQRMFGCDVGSDWRLLRGYQQFAYDGRDYIALNEDLKTWTAADTAALITRRKWEQAGDAEYYRAYLEGECVEWLRRYLELGNETLLRTDSPKAHVTYHPRSQVDVTLRCWALGFYPADITLTWQLNGEDLTQDMELVETRPAGDGTFQKWAAVVVPLGKEQNYTCHVHHKGLPEPLTLRWKLPPSTVSNTVIIAVLVVLGAAIVTGAVVAFVMKMRRNTGGKGVNYALAPGSQTSDLSLPDGKVMVHDPHSLA
| null | null |
antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-dependent [GO:0002485]; antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent [GO:0002486]; antigen processing and presentation of endogenous peptide antigen via MHC class Ib [GO:0002476]; antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; defense response to bacterium [GO:0042742]; immune response [GO:0006955]; inner ear development [GO:0048839]; negative regulation of neuron projection development [GO:0010977]; positive regulation of T cell mediated cytotoxicity [GO:0001916]; T cell mediated cytotoxicity [GO:0001913]
|
external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; lumenal side of endoplasmic reticulum membrane [GO:0098553]; MHC class I protein complex [GO:0042612]; phagocytic vesicle membrane [GO:0030670]
|
beta-2-microglobulin binding [GO:0030881]; peptide antigen binding [GO:0042605]; peptide binding [GO:0042277]; protein-containing complex binding [GO:0044877]; signaling receptor binding [GO:0005102]
|
PF07654;PF00129;
|
2.60.40.10;3.30.500.10;
|
MHC class I family
| null |
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
| null | null | null | null | null |
FUNCTION: Involved in the presentation of foreign antigens to the immune system.
|
Mus musculus (Mouse)
|
P01903
|
DRA_HUMAN
|
MAISGVPVLGFFIIAVLMSAQESWAIKEEHVIIQAEFYLNPDQSGEFMFDFDGDEIFHVDMAKKETVWRLEEFGRFASFEAQGALANIAVDKANLEIMTKRSNYTPITNVPPEVTVLTNSPVELREPNVLICFIDKFTPPVVNVTWLRNGKPVTTGVSETVFLPREDHLFRKFHYLPFLPSTEDVYDCRVEHWGLDEPLLKHWEFDAPSPLPETTENVVCALGLTVGLVGIIIGTIFIIKGLRKSNAAERRGPL
| null | null |
adaptive immune response [GO:0002250]; antigen processing and presentation of endogenous peptide antigen via MHC class II [GO:0002491]; antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; antigen processing and presentation of peptide or polysaccharide antigen via MHC class II [GO:0002504]; cognition [GO:0050890]; immune response [GO:0006955]; myeloid dendritic cell antigen processing and presentation [GO:0002469]; peptide antigen assembly with MHC class II protein complex [GO:0002503]; positive regulation of CD4-positive, alpha-beta T cell activation [GO:2000516]; positive regulation of CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation [GO:0032831]; positive regulation of immune response [GO:0050778]; positive regulation of memory T cell differentiation [GO:0043382]; positive regulation of T cell activation [GO:0050870]; positive regulation of T cell mediated cytotoxicity [GO:0001916]; regulation of T-helper cell differentiation [GO:0045622]
|
autolysosome membrane [GO:0120281]; cell surface [GO:0009986]; clathrin-coated endocytic vesicle membrane [GO:0030669]; early endosome membrane [GO:0031901]; endocytic vesicle membrane [GO:0030666]; ER to Golgi transport vesicle membrane [GO:0012507]; extracellular exosome [GO:0070062]; Golgi membrane [GO:0000139]; immunological synapse [GO:0001772]; late endosome membrane [GO:0031902]; lumenal side of endoplasmic reticulum membrane [GO:0098553]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; MHC class II protein complex [GO:0042613]; plasma membrane [GO:0005886]; trans-Golgi network membrane [GO:0032588]; transport vesicle membrane [GO:0030658]
|
MHC class II protein complex binding [GO:0023026]; MHC class II receptor activity [GO:0032395]; peptide antigen binding [GO:0042605]; polysaccharide binding [GO:0030247]; T cell receptor binding [GO:0042608]
|
PF07654;PF00993;
|
2.60.40.10;
|
MHC class II family
|
PTM: Ubiquitinated by MARCHF1 or MARCHF8 at Lys-244 leading to down-regulation of MHCII. When associated with ubiquitination of the beta chain at 'Lys-254', the down-regulation of MHCII may be highly effective. {ECO:0000269|PubMed:19117940}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15322540, ECO:0000269|PubMed:18305173, ECO:0000269|PubMed:29884618}; Single-pass type I membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000269|PubMed:19117940}; Single-pass type I membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:18305173, ECO:0000269|PubMed:19117940, ECO:0000269|PubMed:9075930}; Single-pass type I membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:18305173, ECO:0000269|PubMed:9075930}; Single-pass type I membrane protein {ECO:0000255}. Autolysosome membrane {ECO:0000269|PubMed:17182262}; Single-pass type I membrane protein. Note=The MHCII complex transits through a number of intracellular compartments in the endocytic pathway until it reaches the cell membrane for antigen presentation (PubMed:18305173, PubMed:9075930). Component of immunological synapses at the interface between T cell and APC (PubMed:15322540, PubMed:29884618). {ECO:0000269|PubMed:15322540, ECO:0000269|PubMed:18305173, ECO:0000269|PubMed:29884618, ECO:0000269|PubMed:9075930}.
| null | null | null | null | null |
FUNCTION: An alpha chain of antigen-presenting major histocompatibility complex class II (MHCII) molecule. In complex with the beta chain HLA-DRB, displays antigenic peptides on professional antigen presenting cells (APCs) for recognition by alpha-beta T cell receptor (TCR) on HLA-DR-restricted CD4-positive T cells. This guides antigen-specific T-helper effector functions, both antibody-mediated immune response and macrophage activation, to ultimately eliminate the infectious agents and transformed cells (PubMed:15265931, PubMed:15322540, PubMed:17334368, PubMed:22327072, PubMed:24190431, PubMed:27591323, PubMed:29884618, PubMed:31495665, PubMed:8145819, PubMed:9075930). Typically presents extracellular peptide antigens of 10 to 30 amino acids that arise from proteolysis of endocytosed antigens in lysosomes (PubMed:8145819). In the tumor microenvironment, presents antigenic peptides that are primarily generated in tumor-resident APCs likely via phagocytosis of apoptotic tumor cells or macropinocytosis of secreted tumor proteins (PubMed:31495665). Presents peptides derived from intracellular proteins that are trapped in autolysosomes after macroautophagy, a mechanism especially relevant for T cell selection in the thymus and central immune tolerance (PubMed:17182262, PubMed:23783831). The selection of the immunodominant epitopes follows two processing modes: 'bind first, cut/trim later' for pathogen-derived antigenic peptides and 'cut first, bind later' for autoantigens/self-peptides (PubMed:25413013). The anchor residue at position 1 of the peptide N-terminus, usually a large hydrophobic residue, is essential for high affinity interaction with MHCII molecules (PubMed:8145819). {ECO:0000269|PubMed:15265931, ECO:0000269|PubMed:15322540, ECO:0000269|PubMed:17182262, ECO:0000269|PubMed:17334368, ECO:0000269|PubMed:22327072, ECO:0000269|PubMed:23783831, ECO:0000269|PubMed:24190431, ECO:0000269|PubMed:25413013, ECO:0000269|PubMed:27591323, ECO:0000269|PubMed:29884618, ECO:0000269|PubMed:31495665, ECO:0000269|PubMed:8145819, ECO:0000269|PubMed:9075930}.
|
Homo sapiens (Human)
|
P01906
|
DQA2_HUMAN
|
MILNKALLLGALALTAVMSPCGGEDIVADHVASYGVNFYQSHGPSGQYTHEFDGDEEFYVDLETKETVWQLPMFSKFISFDPQSALRNMAVGKHTLEFMMRQSNSTAATNEVPEVTVFSKFPVTLGQPNTLICLVDNIFPPVVNITWLSNGHSVTEGVSETSFLSKSDHSFFKISYLTFLPSADEIYDCKVEHWGLDEPLLKHWEPEIPAPMSELTETLVCALGLSVGLMGIVVGTVFIIQGLRSVGASRHQGLL
| null | null |
adaptive immune response [GO:0002250]; antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; immune response [GO:0006955]; peptide antigen assembly with MHC class II protein complex [GO:0002503]; positive regulation of immune response [GO:0050778]; positive regulation of T cell activation [GO:0050870]
|
clathrin-coated endocytic vesicle membrane [GO:0030669]; endocytic vesicle membrane [GO:0030666]; ER to Golgi transport vesicle membrane [GO:0012507]; Golgi membrane [GO:0000139]; late endosome membrane [GO:0031902]; lumenal side of endoplasmic reticulum membrane [GO:0098553]; lysosomal membrane [GO:0005765]; MHC class II protein complex [GO:0042613]; plasma membrane [GO:0005886]; trans-Golgi network membrane [GO:0032588]; transport vesicle membrane [GO:0030658]
|
MHC class II protein complex binding [GO:0023026]; MHC class II receptor activity [GO:0032395]; peptide antigen binding [GO:0042605]
|
PF07654;PF00993;
|
2.60.40.10;
|
MHC class II family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22407913}; Single-pass type I membrane protein {ECO:0000269|PubMed:22407913}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:22407913}; Single-pass type I membrane protein {ECO:0000269|PubMed:22407913}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:22407913}; Single-pass type I membrane protein {ECO:0000269|PubMed:22407913}. Endosome membrane {ECO:0000269|PubMed:22407913}; Single-pass type I membrane protein {ECO:0000269|PubMed:22407913}. Lysosome membrane {ECO:0000269|PubMed:22407913}; Single-pass type I membrane protein {ECO:0000269|PubMed:22407913}. 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.
| null | null | null | null | null |
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. {ECO:0000269|PubMed:22407913}.
|
Homo sapiens (Human)
|
P01909
|
DQA1_HUMAN
|
MILNKALMLGALALTTVMSPCGGEDIVADHVASYGVNLYQSYGPSGQYTHEFDGDEQFYVDLGRKETVWCLPVLRQFRFDPQFALTNIAVLKHNLNSLIKRSNSTAATNEVPEVTVFSKSPVTLGQPNILICLVDNIFPPVVNITWLSNGHSVTEGVSETSFLSKSDHSFFKISYLTLLPSAEESYDCKVEHWGLDKPLLKHWEPEIPAPMSELTETVVCALGLSVGLVGIVVGTVFIIRGLRSVGASRHQGPL
| null | null |
adaptive immune response [GO:0002250]; antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; immune response [GO:0006955]; peptide antigen assembly with MHC class II protein complex [GO:0002503]; positive regulation of immune response [GO:0050778]; positive regulation of T cell activation [GO:0050870]
|
clathrin-coated endocytic vesicle membrane [GO:0030669]; endocytic vesicle membrane [GO:0030666]; ER to Golgi transport vesicle membrane [GO:0012507]; Golgi membrane [GO:0000139]; late endosome membrane [GO:0031902]; lumenal side of endoplasmic reticulum membrane [GO:0098553]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; MHC class II protein complex [GO:0042613]; plasma membrane [GO:0005886]; trans-Golgi network membrane [GO:0032588]; transport vesicle membrane [GO:0030658]
|
MHC class II protein complex binding [GO:0023026]; MHC class II receptor activity [GO:0032395]; peptide antigen binding [GO:0042605]
|
PF07654;PF00993;
|
2.60.40.10;
|
MHC class II family
| null |
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.
| null | null | null | null | null |
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.
|
Homo sapiens (Human)
|
P01910
|
HA2K_MOUSE
|
MPRSRALILGVLALTTMLSLCGGEDDIEADHVGSYGITVYQSPGDIGQYTFEFDGDELFYVDLDKKETVWMLPEFAQLRRFEPQGGLQNIATGKHNLEILTKRSNSTPATNEAPQATVFPKSPVLLGQPNTLICFVDNIFPPVINITWLRNSKSVTDGVYETSFFVNRDYSFHKLSYLTFIPSDDDIYDCKVEHWGLEEPVLKHWEPEIPAPMSELTETVVCALGLSVGLVGIVVGTIFIIQGLRSGGTSRHPGPL
| null | null |
adaptive immune response [GO:0002250]; antigen processing and presentation [GO:0019882]; antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; antigen processing and presentation of peptide antigen [GO:0048002]; negative regulation of T cell proliferation [GO:0042130]; peptide antigen assembly with MHC class II protein complex [GO:0002503]; positive regulation of immune response [GO:0050778]; positive regulation of T cell activation [GO:0050870]; positive regulation of T cell differentiation [GO:0045582]
|
external side of plasma membrane [GO:0009897]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; MHC class II protein complex [GO:0042613]; plasma membrane [GO:0005886]
|
MHC class II protein complex binding [GO:0023026]; peptide antigen binding [GO:0042605]; protein-containing complex binding [GO:0044877]
|
PF07654;PF00993;
|
2.60.40.10;
|
MHC class II family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
| null | null | null | null | null | null |
Mus musculus (Mouse)
|
P01911
|
DRB1_HUMAN
|
MVCLKLPGGSCMTALTVTLMVLSSPLALSGDTRPRFLWQPKRECHFFNGTERVRFLDRYFYNQEESVRFDSDVGEFRAVTELGRPDAEYWNSQKDILEQARAAVDTYCRHNYGVVESFTVQRRVQPKVTVYPSKTQPLQHHNLLVCSVSGFYPGSIEVRWFLNGQEEKAGMVSTGLIQNGDWTFQTLVMLETVPRSGEVYTCQVEHPSVTSPLTVEWRARSESAQSKMLSGVGGFVLGLLFLGAGLFIYFRNQKGHSGLQPTGFLS
| null | null |
antigen processing and presentation of endogenous peptide antigen via MHC class II [GO:0002491]; antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; detection of bacterium [GO:0016045]; epidermis development [GO:0008544]; humoral immune response [GO:0006959]; immune response [GO:0006955]; inflammatory response to antigenic stimulus [GO:0002437]; macrophage differentiation [GO:0030225]; myeloid dendritic cell antigen processing and presentation [GO:0002469]; negative regulation of inflammatory response to antigenic stimulus [GO:0002862]; negative regulation of T cell proliferation [GO:0042130]; negative regulation of type II interferon production [GO:0032689]; peptide antigen assembly with MHC class II protein complex [GO:0002503]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of CD4-positive, alpha-beta T cell activation [GO:2000516]; positive regulation of CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation [GO:0032831]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of immune response [GO:0050778]; positive regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0035774]; positive regulation of kinase activity [GO:0033674]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of memory T cell differentiation [GO:0043382]; positive regulation of monocyte differentiation [GO:0045657]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of T cell activation [GO:0050870]; positive regulation of T cell mediated cytotoxicity [GO:0001916]; positive regulation of T cell mediated immune response to tumor cell [GO:0002842]; positive regulation of viral entry into host cell [GO:0046598]; protein tetramerization [GO:0051262]; regulation of interleukin-10 production [GO:0032653]; regulation of interleukin-4 production [GO:0032673]; regulation of T-helper cell differentiation [GO:0045622]; signal transduction [GO:0007165]; T cell receptor signaling pathway [GO:0050852]; T-helper 1 type immune response [GO:0042088]
|
autolysosome membrane [GO:0120281]; cell surface [GO:0009986]; clathrin-coated endocytic vesicle membrane [GO:0030669]; endocytic vesicle membrane [GO:0030666]; ER to Golgi transport vesicle membrane [GO:0012507]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; Golgi membrane [GO:0000139]; immunological synapse [GO:0001772]; intermediate filament [GO:0005882]; late endosome membrane [GO:0031902]; lumenal side of endoplasmic reticulum membrane [GO:0098553]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; MHC class II protein complex [GO:0042613]; plasma membrane [GO:0005886]; trans-Golgi network membrane [GO:0032588]; transport vesicle membrane [GO:0030658]
|
CD4 receptor binding [GO:0042609]; MHC class II protein complex binding [GO:0023026]; MHC class II receptor activity [GO:0032395]; peptide antigen binding [GO:0042605]; polysaccharide binding [GO:0030247]; structural constituent of cytoskeleton [GO:0005200]; T cell receptor binding [GO:0042608]
|
PF07654;PF00969;
|
2.60.40.10;
| null |
PTM: Ubiquitinated by MARCHF1 and MARCHF8 at Lys-254 leading to sorting into the endosome system and down-regulation of MHCII. {ECO:0000305|PubMed:18305173}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18305173, ECO:0000269|PubMed:19830726, ECO:0000269|PubMed:29884618}; Single-pass type I membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:18305173, ECO:0000269|PubMed:9075930}; Single-pass type I membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:18305173, ECO:0000269|PubMed:9075930}; Single-pass type I membrane protein {ECO:0000255}. Autolysosome membrane {ECO:0000269|PubMed:17182262}. 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 (PubMed:18305173). Component of immunological synapses at the interface between T cell and APC (PubMed:29884618). {ECO:0000269|PubMed:18305173, ECO:0000269|PubMed:29884618}.
| null | null | null | null | null |
FUNCTION: A beta chain of antigen-presenting major histocompatibility complex class II (MHCII) molecule. In complex with the alpha chain HLA-DRA, displays antigenic peptides on professional antigen presenting cells (APCs) for recognition by alpha-beta T cell receptor (TCR) on HLA-DRB1-restricted CD4-positive T cells. This guides antigen-specific T-helper effector functions, both antibody-mediated immune response and macrophage activation, to ultimately eliminate the infectious agents and transformed cells (PubMed:15265931, PubMed:16148104, PubMed:22327072, PubMed:27591323, PubMed:29884618, PubMed:31495665, PubMed:8642306). Typically presents extracellular peptide antigens of 10 to 30 amino acids that arise from proteolysis of endocytosed antigens in lysosomes (PubMed:8145819). In the tumor microenvironment, presents antigenic peptides that are primarily generated in tumor-resident APCs likely via phagocytosis of apoptotic tumor cells or macropinocytosis of secreted tumor proteins (PubMed:31495665). Presents peptides derived from intracellular proteins that are trapped in autolysosomes after macroautophagy, a mechanism especially relevant for T cell selection in the thymus and central immune tolerance (PubMed:17182262, PubMed:23783831). The selection of the immunodominant epitopes follows two processing modes: 'bind first, cut/trim later' for pathogen-derived antigenic peptides and 'cut first, bind later' for autoantigens/self-peptides (PubMed:25413013). The anchor residue at position 1 of the peptide N-terminus, usually a large hydrophobic residue, is essential for high affinity interaction with MHCII molecules (PubMed:8145819). {ECO:0000269|PubMed:15265931, ECO:0000269|PubMed:17182262, ECO:0000269|PubMed:22327072, ECO:0000269|PubMed:23783831, ECO:0000269|PubMed:25413013, ECO:0000269|PubMed:27591323, ECO:0000269|PubMed:29884618, ECO:0000269|PubMed:31495665, ECO:0000269|PubMed:8145819, ECO:0000269|PubMed:8642306}.; FUNCTION: Allele DRB1*01:01: Displays an immunodominant epitope derived from Bacillus anthracis pagA/protective antigen, PA (KLPLYISNPNYKVNVYAVT), to both naive and PA-specific memory CD4-positive T cells (PubMed:22327072). Presents immunodominant HIV-1 gag peptide (FRDYVDRFYKTLRAEQASQE) on infected dendritic cells for recognition by TRAV24-TRBV2 TCR on CD4-positive T cells and controls viral load (PubMed:29884618). May present to T-helper 1 cells several HRV-16 epitopes derived from capsid proteins VP1 (PRFSLPFLSIASAYYMFYDG) and VP2 (PHQFINLRSNNSATLIVPYV), contributing to viral clearance (PubMed:27591323). Displays commonly recognized peptides derived from IAV external protein HA (PKYVKQNTLKLAT and SNGNFIAPEYAYKIVK) and from internal proteins M, NP and PB1, with M-derived epitope (GLIYNRMGAVTTEV) being the most immunogenic (PubMed:25413013, PubMed:32668259, PubMed:8145819, PubMed:9075930). Presents a self-peptide derived from COL4A3 (GWISLWKGFSF) to TCR (TRAV14 biased) on CD4-positive, FOXP3-positive regulatory T cells and mediates immune tolerance to self (PubMed:28467828). May present peptides derived from oncofetal trophoblast glycoprotein TPBG 5T4, known to be recognized by both T-helper 1 and regulatory T cells (PubMed:31619516). Displays with low affinity a self-peptide derived from MBP (VHFFKNIVTPRTP) (PubMed:9075930). {ECO:0000269|PubMed:22327072, ECO:0000269|PubMed:25413013, ECO:0000269|PubMed:27591323, ECO:0000269|PubMed:28467828, ECO:0000269|PubMed:29884618, ECO:0000269|PubMed:31619516, ECO:0000269|PubMed:32668259, ECO:0000269|PubMed:8145819, ECO:0000269|PubMed:9075930}.; FUNCTION: Allele DRB1*03:01: May present to T-helper 1 cells an HRV-16 epitope derived from capsid protein VP2 (NEKQPSDDNWLNFDGTLLGN), contributing to viral clearance (PubMed:27591323). Displays self-peptides derived from retinal SAG (NRERRGIALDGKIKHE) and thyroid TG (LSSVVVDPSIRHFDV) (PubMed:25413013). Presents viral epitopes derived from HHV-6B gH/U48 and U85 antigens to polyfunctional CD4-positive T cells with cytotoxic activity implicated in control of HHV-6B infection (PubMed:31020640). Presents several immunogenic epitopes derived from C. tetani neurotoxin tetX, playing a role in immune recognition and long-term protection (PubMed:19830726). {ECO:0000269|PubMed:19830726, ECO:0000269|PubMed:25413013, ECO:0000269|PubMed:27591323, ECO:0000269|PubMed:31020640}.; FUNCTION: Allele DRB1*04:01: Presents an immunodominant bacterial epitope derived from M. tuberculosis esxB/culture filtrate antigen CFP-10 (EISTNIRQAGVQYSR), eliciting CD4-positive T cell effector functions such as IFNG production and cytotoxic activity (PubMed:15265931). May present to T-helper 1 cells an HRV-16 epitope derived from capsid protein VP2 (NEKQPSDDNWLNFDGTLLGN), contributing to viral clearance (PubMed:27591323). Presents tumor epitopes derived from melanoma-associated TYR antigen (QNILLSNAPLGPQFP and DYSYLQDSDPDSFQD), triggering CD4-positive T cell effector functions such as GMCSF production (PubMed:8642306). Displays preferentially citrullinated self-peptides derived from VIM (GVYATR/citSSAVR and SAVRAR/citSSVPGVR) and ACAN (VVLLVATEGR/ CitVRVNSAYQDK) (PubMed:24190431). Displays self-peptides derived from COL2A1 (PubMed:9354468). {ECO:0000269|PubMed:15265931, ECO:0000269|PubMed:24190431, ECO:0000269|PubMed:27591323, ECO:0000269|PubMed:8642306, ECO:0000269|PubMed:9354468}.; FUNCTION: Allele DRB1*04:02: Displays native or citrullinated self-peptides derived from VIM. {ECO:0000269|PubMed:24190431}.; FUNCTION: Allele DRB1*04:04: May present to T-helper 1 cells several HRV-16 epitopes derived from capsid proteins VP1 (HIVMQYMYVPPGAPIPTTRN) and VP2 (RGDSTITSQDVANAVVGYGV), contributing to viral clearance (PubMed:27591323). Displays preferentially citrullinated self-peptides derived from VIM (SAVRAR/citSSVPGVR) (PubMed:24190431). {ECO:0000269|PubMed:24190431, ECO:0000269|PubMed:27591323}.; FUNCTION: Allele DRB1*04:05: May present to T-helper 1 cells an immunogenic epitope derived from tumor-associated antigen WT1 (KRYFKLSHLQMHSRKH), likely providing for effective antitumor immunity in a wide range of solid and hematological malignancies. {ECO:0000269|PubMed:19120973}.; FUNCTION: Allele DRB1*05:01: Presents an immunodominant HIV-1 gag peptide (FRDYVDRFYKTLRAEQASQE) on infected dendritic cells for recognition by TRAV24-TRBV2 TCR on CD4-positive T cells and controls viral load. {ECO:0000269|PubMed:29884618}.; FUNCTION: Allele DRB1*07:01: Upon EBV infection, presents latent antigen EBNA2 peptide (PRSPTVFYNIPPMPLPPSQL) to CD4-positive T cells, driving oligoclonal expansion and selection of a dominant virus-specific memory T cell subset with cytotoxic potential to directly eliminate virus-infected B cells (PubMed:31308093). May present to T-helper 1 cells several HRV-16 epitopes derived from capsid proteins VP1 (PRFSLPFLSIASAYYMFYDG) and VP2 (VPYVNAVPMDSMVRHNNWSL), contributing to viral clearance (PubMed:27591323). In the context of tumor immunesurveillance, may present to T-helper 1 cells an immunogenic epitope derived from tumor-associated antigen WT1 (MTEYKLVVVGAVGVGKSALTIQLI), likely providing for effective antitumor immunity in a wide range of solid and hematological malignancies (PubMed:22929521). In metastatic epithelial tumors, presents to intratumoral CD4-positive T cells a KRAS neoantigen (MTEYKLVVVGAVGVGKSALTIQLI) carrying G12V hotspot driver mutation and may mediate tumor regression (PubMed:30282837). {ECO:0000269|PubMed:22929521, ECO:0000269|PubMed:27591323, ECO:0000269|PubMed:30282837, ECO:0000269|PubMed:31308093}.; FUNCTION: Allele DRB1*11:01: Displays an immunodominant HIV-1 gag peptide (FRDYVDRFYKTLRAEQASQE) on infected dendritic cells for recognition by TRAV24-TRBV2 TCR on CD4-positive T cells and controls viral load (PubMed:29884618). May present to T-helper 1 cells an HRV-16 epitope derived from capsid protein VP2 (SDRIIQITRGDSTITSQDVA), contributing to viral clearance (PubMed:27591323). Presents several immunogenic epitopes derived from C. tetani neurotoxin tetX, playing a role in immune recognition and longterm protection (PubMed:19830726). In the context of tumor immunesurveillance, may present tumor-derived neoantigens to CD4-positive T cells and trigger anti-tumor helper functions (PubMed:31495665). {ECO:0000269|PubMed:19830726, ECO:0000269|PubMed:27591323, ECO:0000269|PubMed:29884618, ECO:0000269|PubMed:31495665}.; FUNCTION: Allele DRB1*13:01: Presents viral epitopes derived from HHV-6B antigens to polyfunctional CD4-positive T cells implicated in control of HHV-6B infection. {ECO:0000269|PubMed:31020640}.; FUNCTION: Allele DRB1*15:01: May present to T-helper 1 cells an HRV-16 epitope derived from capsid protein VP2 (SNNSATLIVPYVNAVPMDSM), contributing to viral clearance (PubMed:27591323). Displays a self-peptide derived from MBP (ENPVVHFFKNIVTPR) (PubMed:25413013, PubMed:9782128). May present to T-helper 1 cells an immunogenic epitope derived from tumor-associated antigen WT1 (KRYFKLSHLQMHSRKH), likely providing for effective antitumor immunity in a wide range of solid and hematological malignancies. {ECO:0000269|PubMed:19120973, ECO:0000269|PubMed:27591323, ECO:0000269|PubMed:9782128}.; FUNCTION: Allele DRB1*15:02: Displays an immunodominant HIV-1 gag peptide (FRDYVDRFYKTLRAEQASQE) on infected dendritic cells for recognition by TRAV24-TRBV2 TCR on CD4-positive T cells and controls viral load (PubMed:29884618). May present to T-helper 1 cells an immunogenic epitope derived from tumor-associated antigen WT1 (KRYFKLSHLQMHSRKH), likely providing for effective antitumor immunity in a wide range of solid and hematological malignancies (PubMed:19120973). {ECO:0000269|PubMed:19120973, ECO:0000269|PubMed:29884618}.; FUNCTION: (Microbial infection) Acts as a receptor for Epstein-Barr virus on lymphocytes. {ECO:0000269|PubMed:11864610, ECO:0000269|PubMed:9151859}.
|
Homo sapiens (Human)
|
P01920
|
DQB1_HUMAN
|
MSWKKALRIPGGLRAATVTLMLAMLSTPVAEGRDSPEDFVYQFKAMCYFTNGTERVRYVTRYIYNREEYARFDSDVEVYRAVTPLGPPDAEYWNSQKEVLERTRAELDTVCRHNYQLELRTTLQRRVEPTVTISPSRTEALNHHNLLVCSVTDFYPAQIKVRWFRNDQEETTGVVSTPLIRNGDWTFQILVMLEMTPQHGDVYTCHVEHPSLQNPITVEWRAQSESAQSKMLSGIGGFVLGLIFLGLGLIIHHRSQKGLLH
| null | null |
adaptive immune response [GO:0002250]; antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; humoral immune response [GO:0006959]; immune response [GO:0006955]; peptide antigen assembly with MHC class II protein complex [GO:0002503]; positive regulation of immune response [GO:0050778]; positive regulation of T cell activation [GO:0050870]; T cell receptor signaling pathway [GO:0050852]
|
clathrin-coated endocytic vesicle membrane [GO:0030669]; endocytic vesicle membrane [GO:0030666]; ER to Golgi transport vesicle membrane [GO:0012507]; Golgi membrane [GO:0000139]; late endosome membrane [GO:0031902]; lumenal side of endoplasmic reticulum membrane [GO:0098553]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; MHC class II protein complex [GO:0042613]; plasma membrane [GO:0005886]; trans-Golgi network membrane [GO:0032588]; transport vesicle membrane [GO:0030658]
|
MHC class II protein complex binding [GO:0023026]; MHC class II receptor activity [GO:0032395]; peptide antigen binding [GO:0042605]
|
PF07654;PF00969;
|
2.60.40.10;
|
MHC class II family
| null |
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.
| null | null | null | null | null |
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.
|
Homo sapiens (Human)
|
P01921
|
HB2D_MOUSE
|
MALQIPSLLLSAAVVVLMVLSSPRTEGGNSERHFVVQFKGECYYTNGTQRIRLVTRYIYNREEYVRYDSDVGEYRAVTELGRPDAEYWNSQPEILERTRAEVDTACRHNYEGPETSTSLRRLEQPNVAISLSRTEALNHHNTLVCSVTDFYPAKIKVRWFRNGQEETVGVSSTQLIRNGDWTFQVLVMLEMTPHQGEVYTCHVEHPSLKSPITVEWRAQSESARSKMLSGIGGCVLGVIFLGLGLFIRHRSQKGPRGPPPAGLLQ
| null | null |
adaptive immune response [GO:0002250]; antigen processing and presentation [GO:0019882]; antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; antigen processing and presentation of peptide antigen [GO:0048002]; immune response [GO:0006955]; peptide antigen assembly with MHC class II protein complex [GO:0002503]; positive regulation of immune response [GO:0050778]; positive regulation of T cell activation [GO:0050870]
|
cell surface [GO:0009986]; early endosome [GO:0005769]; external side of plasma membrane [GO:0009897]; Golgi apparatus [GO:0005794]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; MHC class II protein complex [GO:0042613]; multivesicular body [GO:0005771]; plasma membrane [GO:0005886]
|
MHC class II protein complex binding [GO:0023026]; peptide antigen binding [GO:0042605]; protein-containing complex binding [GO:0044877]
|
PF07654;PF00969;
|
2.60.40.10;
|
MHC class II family
|
PTM: Ubiquitinated in immature dendritic cells leading to down-regulation of MHC class II. {ECO:0000269|PubMed:17051151, ECO:0000269|PubMed:17174123}.
|
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
| null | null | null | null | null | null |
Mus musculus (Mouse)
|
P01942
|
HBA_MOUSE
|
MVLSGEDKSNIKAAWGKIGGHGAEYGAEALERMFASFPTTKTYFPHFDVSHGSAQVKGHGKKVADALASAAGHLDDLPGALSALSDLHAHKLRVDPVNFKLLSHCLLVTLASHHPADFTPAVHASLDKFLASVSTVLTSKYR
| null | null |
carbon dioxide transport [GO:0015670]; erythrocyte development [GO:0048821]; hydrogen peroxide catabolic process [GO:0042744]; in utero embryonic development [GO:0001701]; nitric oxide transport [GO:0030185]; oxygen transport [GO:0015671]; response to bacterium [GO:0009617]; response to stilbenoid [GO:0035634]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]; myelin sheath [GO:0043209]
|
amyloid-beta binding [GO:0001540]; G protein-coupled receptor binding [GO:0001664]; haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]; protein-containing complex binding [GO:0044877]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.; FUNCTION: [Hemopressin]: Hemopressin acts as an antagonist peptide of the cannabinoid receptor CNR1. Hemopressin-binding efficiently blocks cannabinoid receptor CNR1 and subsequent signaling. {ECO:0000250|UniProtKB:P01946}.
|
Mus musculus (Mouse)
|
P01946
|
HBA_RAT
|
MVLSADDKTNIKNCWGKIGGHGGEYGEEALQRMFAAFPTTKTYFSHIDVSPGSAQVKAHGKKVADALAKAADHVEDLPGALSTLSDLHAHKLRVDPVNFKFLSHCLLVTLACHHPGDFTPAMHASLDKFLASVSTVLTSKYR
| null | null |
carbon dioxide transport [GO:0015670]; erythrocyte development [GO:0048821]; hydrogen peroxide catabolic process [GO:0042744]; in utero embryonic development [GO:0001701]; negative regulation of blood pressure [GO:0045776]; nitric oxide transport [GO:0030185]; oxygen transport [GO:0015671]; response to bacterium [GO:0009617]; response to stilbenoid [GO:0035634]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
amyloid-beta binding [GO:0001540]; haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.; FUNCTION: [Hemopressin]: Hemopressin acts as an antagonist peptide of the cannabinoid receptor CNR1 (PubMed:18077343). Hemopressin-binding efficiently blocks cannabinoid receptor CNR1 and subsequent signaling (PubMed:18077343). {ECO:0000269|PubMed:18077343}.
|
Rattus norvegicus (Rat)
|
P01948
|
HBA_RABIT
|
MVLSPADKTNIKTAWEKIGSHGGEYGAEAVERMFLGFPTTKTYFPHFDFTHGSEQIKAHGKKVSEALTKAVGHLDDLPGALSTLSDLHAHKLRVDPVNFKLLSHCLLVTLANHHPSEFTPAVHASLDKFLANVSTVLTSKYR
| null | null |
hydrogen peroxide catabolic process [GO:0042744]; regulation of translation [GO:0006417]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.
|
Oryctolagus cuniculus (Rabbit)
|
P01958
|
HBA_HORSE
|
MVLSAADKTNVKAAWSKVGGHAGEYGAEALERMFLGFPTTKTYFPHFDLSHGSAQVKAHGKKVGDALTLAVGHLDDLPGALSNLSDLHAHKLRVDPVNFKLLSHCLLSTLAVHLPNDFTPAVHASLDKFLSSVSTVLTSKYR
| null | null |
hydrogen peroxide catabolic process [GO:0042744]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.; FUNCTION: [Hemopressin]: Hemopressin acts as an antagonist peptide of the cannabinoid receptor CNR1. Hemopressin-binding efficiently blocks cannabinoid receptor CNR1 and subsequent signaling. {ECO:0000250|UniProtKB:P01946}.
|
Equus caballus (Horse)
|
P01959
|
HBA_EQUAS
|
MVLSAADKTNVKAAWSKVGGNAGEFGAEALERMFLGFPTTKTYFPHFDLSHGSAQVKAHGKKVGDALTLAVGHLDDLPGALSNLSDLHAHKLRVDPVNFKLLSHCLLSTLAVHLPNDFTPAVHASLDKFLSTVSTVLTSKYR
| null | null |
hydrogen peroxide catabolic process [GO:0042744]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.; FUNCTION: [Hemopressin]: Hemopressin acts as an antagonist peptide of the cannabinoid receptor CNR1. Hemopressin-binding efficiently blocks cannabinoid receptor CNR1 and subsequent signaling. {ECO:0000250|UniProtKB:P01946}.
|
Equus asinus (Donkey) (Equus africanus asinus)
|
P01960
|
HBA_EQUZE
|
MVLSAADKTNVKAAWSKVGGNAGEFGAEALERMFLGFPTTKTYFPHFDLSHGSAQVKAHGKKVGDALTLAVGHLDDLPGALSNLSDLHAHKLRVDPVNFKLLSHCLLSTLAVHLPNDFTPAVHASLDKFLSTVSTVLTSKYR
| null | null |
hydrogen peroxide catabolic process [GO:0042744]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.; FUNCTION: [Hemopressin]: Hemopressin acts as an antagonist peptide of the cannabinoid receptor CNR1. Hemopressin-binding efficiently blocks cannabinoid receptor CNR1 and subsequent signaling. {ECO:0000250|UniProtKB:P01946}.
|
Equus zebra (Mountain zebra)
|
P01961
|
HBA_EQUHE
|
MVLSAADKTNVKAAWSKVGGNAGDFGAEALERMFLGFPTTKTYFPHFDLSHGSAQVKAHGKKVGDALTLAVGHLDDLPGALSNLSDLHAHKLRVDPVNFKLLSHCLLSTLAVHLPNDFTPAVHASLDKFLSTVSTVLTSKYR
| null | null |
hydrogen peroxide catabolic process [GO:0042744]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.
|
Equus hemionus kulan (Turkmenian kulan) (Equus onager kulan)
|
P01965
|
HBA_PIG
|
VLSAADKANVKAAWGKVGGQAGAHGAEALERMFLGFPTTKTYFPHFNLSHGSDQVKAHGQKVADALTKAVGHLDDLPGALSALSDLHAHKLRVDPVNFKLLSHCLLVTLAAHHPDDFNPSVHASLDKFLANVSTVLTSKYR
| null | null |
hydrogen peroxide catabolic process [GO:0042744]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.; FUNCTION: [Hemopressin]: Hemopressin acts as an antagonist peptide of the cannabinoid receptor CNR1. Hemopressin-binding efficiently blocks cannabinoid receptor CNR1 and subsequent signaling. {ECO:0000250|UniProtKB:P01946}.
|
Sus scrofa (Pig)
|
P01966
|
HBA_BOVIN
|
MVLSAADKGNVKAAWGKVGGHAAEYGAEALERMFLSFPTTKTYFPHFDLSHGSAQVKGHGAKVAAALTKAVEHLDDLPGALSELSDLHAHKLRVDPVNFKLLSHSLLVTLASHLPSDFTPAVHASLDKFLANVSTVLTSKYR
| null | null |
hydrogen peroxide catabolic process [GO:0042744]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.; FUNCTION: [Hemopressin]: Hemopressin acts as an antagonist peptide of the cannabinoid receptor CNR1. Hemopressin-binding efficiently blocks cannabinoid receptor CNR1 and subsequent signaling. {ECO:0000250|UniProtKB:P01946}.
|
Bos taurus (Bovine)
|
P01971
|
HBA_ALCAA
|
MVLSATDKSNVKAAWGKVGGNAPAYGAEALERMFLSFPTTKTYFPHFDLSHGSAQVKAHGEKVANALTKAVGHLDDLPGTLSDLSDLHAHKLRVDPVNFKLLSHTLLVTLAAHLPSDFTPAVHASLDKFLANVSTVLTSKYR
| null | null |
hydrogen peroxide catabolic process [GO:0042744]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.; FUNCTION: [Hemopressin]: Hemopressin acts as an antagonist peptide of the cannabinoid receptor CNR1. Hemopressin-binding efficiently blocks cannabinoid receptor CNR1 and subsequent signaling. {ECO:0000250|UniProtKB:P01946}.
|
Alces alces alces (European moose) (Elk)
|
P01972
|
HBA_ODOVI
|
VLSAABKSBVKAAWGKVGGNAAPYGAZALZRMFLSFPTTKTYFPHFBLSHGSAZVKAHGZKVABALTKAVGHLBBLPGTLSBLSBLHAHKLRVBPVBFKLLSHSLLVTLATHLPBBFTPAVHASLBKFLABVSTVLTSKYR
| null | null |
hydrogen peroxide catabolic process [GO:0042744]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.
|
Odocoileus virginianus virginianus (Virginia white-tailed deer)
|
P01994
|
HBA_CHICK
|
MVLSAADKNNVKGIFTKIAGHAEEYGAETLERMFTTYPPTKTYFPHFDLSHGSAQIKGHGKKVVAALIEAANHIDDIAGTLSKLSDLHAHKLRVDPVNFKLLGQCFLVVVAIHHPAALTPEVHASLDKFLCAVGTVLTAKYR
| null | null |
hydrogen peroxide catabolic process [GO:0042744]
|
blood microparticle [GO:0072562]; extracellular space [GO:0005615]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.
|
Gallus gallus (Chicken)
|
P02008
|
HBAZ_HUMAN
|
MSLTKTERTIIVSMWAKISTQADTIGTETLERLFLSHPQTKTYFPHFDLHPGSAQLRAHGSKVVAAVGDAVKSIDDIGGALSKLSELHAYILRVDPVNFKLLSHCLLVTLAARFPADFTAEAHAAWDKFLSVVSSVLTEKYR
| null | null |
carbon dioxide transport [GO:0015670]; hydrogen peroxide catabolic process [GO:0042744]; oxygen transport [GO:0015671]
|
blood microparticle [GO:0072562]; extracellular exosome [GO:0070062]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: The zeta chain is an alpha-type chain of mammalian embryonic hemoglobin.
|
Homo sapiens (Human)
|
P02016
|
HBA_CYPCA
|
MSLSDKDKAAVKGLWAKISPKADDIGAEALGRMLTVYPQTKTYFAHWADLSPGSGPVKKHGKVIMGAVGDAVSKIDDLVGGLAALSELHAFKLRVDPANFKILAHNVIVVIGMLYPGDFPPEVHMSVDKFFQNLALALSEKYR
| null | null |
hydrogen peroxide catabolic process [GO:0042744]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from gills to the various peripheral tissues.
|
Cyprinus carpio (Common carp)
|
P02017
|
HBA_CATCL
|
SLSDKDKADVKIAWAKISPRADEIGAEALGRMLTVYPQTKTYFAHWADLSPGSGPVKHGKKVIMGAIGDAVTKFDDLLGGLASLSELHASKLRVDPSNFKILANCITVVIMFYLPGDFPPEVHASVDKFFQNLALALGQKYR
| null | null |
hydrogen peroxide catabolic process [GO:0042744]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from gills to the various peripheral tissues.
|
Catostomus clarkii (Desert sucker)
|
P02024
|
HBB_GORGO
|
MVHLTPEEKSAVTALWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLSTPDAVMGNPKVKAHGKKVLGAFSDGLAHLDNLKGTFATLSELHCDKLHVDPENFKLLGNVLVCVLAHHFGKEFTPPVQAAYQKVVAGVANALAHKYH
| null | null |
hydrogen peroxide catabolic process [GO:0042744]; nitric oxide transport [GO:0030185]; renal absorption [GO:0070293]; response to hydrogen peroxide [GO:0042542]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.
|
Gorilla gorilla gorilla (Western lowland gorilla)
|
P02025
|
HBB_HYLLA
|
VHLTPEEKSAVTALWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLSTPDAVMGNPKVKAHGKKVLGAFSDGLAHLDNLKGTFAQLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGKEFTPQVQAAYQKVVAGVANALAHKYH
| null | null |
hydrogen peroxide catabolic process [GO:0042744]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.
|
Hylobates lar (Lar gibbon) (White-handed gibbon)
|
P02036
|
HBB_SAISC
|
MVHLTGDEKAAVTALWGKVNVEDVGGEALGRLLVVYPWTQRFFESFGDLSTPDAVMNNPKVKAHGKKVLGAFSDGLAHLDNLKGTFAQLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGKEFTPQVQAAYQKVVAGVANALAHKYH
| null | null |
hydrogen peroxide catabolic process [GO:0042744]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.
|
Saimiri sciureus (Common squirrel monkey)
|
P02042
|
HBD_HUMAN
|
MVHLTPEEKTAVNALWGKVNVDAVGGEALGRLLVVYPWTQRFFESFGDLSSPDAVMGNPKVKAHGKKVLGAFSDGLAHLDNLKGTFSQLSELHCDKLHVDPENFRLLGNVLVCVLARNFGKEFTPQMQAAYQKVVAGVANALAHKYH
| null | null |
carbon dioxide transport [GO:0015670]; hydrogen peroxide catabolic process [GO:0042744]; oxygen transport [GO:0015671]
|
blood microparticle [GO:0072562]; cytosol [GO:0005829]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.
|
Homo sapiens (Human)
|
P02050
|
HBB_OTOCR
|
VHLTPDEKNAVCALWGKVNVEEVGGEALGRLLVVYPWTQRFFDSFGDLSSPSAVMGNPKVKAHGKKVLSAFSDGLQHLDNLCGTFAKLSELHCDKLHVNPENFRLLGNVLVCVLAHHFGKDFTPEVQAAYEKVVAGVATALAHKYH
| null | null |
hydrogen peroxide catabolic process [GO:0042744]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.
|
Otolemur crassicaudatus (Brown greater galago) (Galago crassicaudatus)
|
P02053
|
HBB_EULFU
|
MTLLSAEENAHVTSLWGKVDVEKVGGEALGRLLVVYPWTQRFFESFGDLSSPSAVMGNPKVKAHGKKVLSAFSEGLHHLDNLKGTFAQLSELHCDKLHVDPQNFTLLGNVLVVVLAEHFGNAFSPAVQAAFQKVVAGVANALAHKYH
| null | null |
hydrogen peroxide catabolic process [GO:0042744]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.
|
Eulemur fulvus fulvus (Brown lemur)
|
P02057
|
HBB_RABIT
|
MVHLSSEEKSAVTALWGKVNVEEVGGEALGRLLVVYPWTQRFFESFGDLSSANAVMNNPKVKAHGKKVLAAFSEGLSHLDNLKGTFAKLSELHCDKLHVDPENFRLLGNVLVIVLSHHFGKEFTPQVQAAYQKVVAGVANALAHKYH
| null | null |
hydrogen peroxide catabolic process [GO:0042744]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.
|
Oryctolagus cuniculus (Rabbit)
|
P02066
|
HBB_CERSI
|
VELTAEEKAAVLALWDKVKEDEVGGEALGRLLVVYPWTQRFFDSFGDLSTPAAVMGNAKVKAHGKKVLHSFGDGVHHLDNLKGTFAALSELHCDKLHVDPENFRLLGNVLVVVLAKHFGKQFTPELQAAYQKVVAGVANALAHKYH
| null | null |
hydrogen peroxide catabolic process [GO:0042744]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.
|
Ceratotherium simum (White rhinoceros) (Square-lipped rhinoceros)
|
P02067
|
HBB_PIG
|
MVHLSAEEKEAVLGLWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLSNADAVMGNPKVKAHGKKVLQSFSDGLKHLDNLKGTFAKLSELHCDQLHVDPENFRLLGNVIVVVLARRLGHDFNPNVQAAFQKVVAGVANALAHKYH
| null | null |
hydrogen peroxide catabolic process [GO:0042744]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.
|
Sus scrofa (Pig)
|
P02070
|
HBB_BOVIN
|
MLTAEEKAAVTAFWGKVKVDEVGGEALGRLLVVYPWTQRFFESFGDLSTADAVMNNPKVKAHGKKVLDSFSNGMKHLDDLKGTFAALSELHCDKLHVDPENFKLLGNVLVVVLARNFGKEFTPVLQADFQKVVAGVANALAHRYH
| null | null |
hydrogen peroxide catabolic process [GO:0042744]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues. {ECO:0000269|PubMed:8343155}.; FUNCTION: [Spinorphin]: Functions as an endogenous inhibitor of enkephalin-degrading enzymes such as DPP3, and may thereby play a role as a regulator of pain and inflammation. {ECO:0000269|PubMed:8343155}.
|
Bos taurus (Bovine)
|
P02072
|
HBB_BOSMU
|
MLTAEEKAAVTAFWGKVKVDEVGGEALGRLLVVYPWTQRFFESFGDLSSADAVMNNPKVKAHGKKVLDSFSNGMKHLDDLKGTFAALSELHCDKLHVDPENFKLLGNVLVVVLARHFGKEFTPVLQADFQKVVVGVANALAHRYH
| null | null |
hydrogen peroxide catabolic process [GO:0042744]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.
|
Bos mutus grunniens (Wild yak) (Bos grunniens)
|
P02074
|
HBB_ODOVI
|
MLTAEEKAAVTGFWGKVNVDVVGAEALGRLLVVYPWTQRFFEHFGDLSSAGAVMGNPKVKAHGKRVLDAFSEGLKHLDDLKGAFAELSELHCNKLHVDPENFRLLGNVLVVVLARNFGGEFTPLVQADFQKVVAGVANALAHRYH
| null | null |
hydrogen peroxide catabolic process [GO:0042744]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.
|
Odocoileus virginianus virginianus (Virginia white-tailed deer)
|
P02075
|
HBB_SHEEP
|
MLTAEEKAAVTGFWGKVKVDEVGAEALGRLLVVYPWTQRFFEHFGDLSNADAVMNNPKVKAHGKKVLDSFSNGMKHLDDLKGTFAQLSELHCDKLHVDPENFRLLGNVLVVVLARHHGNEFTPVLQADFQKVVAGVANALAHKYH
| null | null |
hydrogen peroxide catabolic process [GO:0042744]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.
|
Ovis aries (Sheep)
|
P02077
|
HBBA_CAPHI
|
MLTAEEKAAVTGFWGKVKVDEVGAEALGRLLVVYPWTQRFFEHFGDLSSADAVMNNAKVKAHGKKVLDSFSNGMKHLDDLKGTFAQLSELHCDKLHVDPENFKLLGNVLVVVLARHHGSEFTPLLQAEFQKVVAGVANALAHRYH
| null | null |
hydrogen peroxide catabolic process [GO:0042744]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.
|
Capra hircus (Goat)
|
P02078
|
HBBC_CAPHI
|
MPNKALITGFWSKVKVDEVGAEALGRLLVVYPWTQRFFEHFGDLSSADAVLGNAKVKAHGKKVLDSFSNGVQHLDDLKGTFAELSELHCDKLHVDPENFRLLGNVLVIVLARHFGKEFTPELQAEFQKVVAGVASALAHRYH
| null | null |
hydrogen peroxide catabolic process [GO:0042744]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.
|
Capra hircus (Goat)
|
P02086
|
HBB_PROHA
|
VHLTDAEKAAVTGLWGKVKVDEYGGEALGRLLVVYPWTQRFFEHFGDLSNADAIMHNPKVLAHGKKVLSSFGDGLNHLDNLKGTFAQLSELHCDKLHVDPENFRLLGNVLVVVLARHFHEEFTPDVQAAFQKVVTGVANALAHKYH
| null | null |
hydrogen peroxide catabolic process [GO:0042744]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.
|
Procavia capensis habessinica (Abyssinian hyrax)
|
P02087
|
HBB_DASNO
|
MVNLTSDEKTAVLALWNKVDVEDCGGEALGRLLVVYPWTQRFFESFGDLSTPAAVFANAKVKAHGKKVLTSFGEGMNHLDNLKGTFAKLSELHCDKLHVDPENFKLLGNMLVVVLARHFGKEFDWHMHACFQKVVAGVANALAHKYH
| null | null |
hydrogen peroxide catabolic process [GO:0042744]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.
|
Dasypus novemcinctus (Nine-banded armadillo)
|
P02088
|
HBB1_MOUSE
|
MVHLTDAEKAAVSCLWGKVNSDEVGGEALGRLLVVYPWTQRYFDSFGDLSSASAIMGNAKVKAHGKKVITAFNDGLNHLDSLKGTFASLSELHCDKLHVDPENFRLLGNMIVIVLGHHLGKDFTPAAQAAFQKVVAGVATALAHKYH
| null | null |
carbon dioxide transport [GO:0015670]; erythrocyte development [GO:0048821]; hemopoiesis [GO:0030097]; hydrogen peroxide catabolic process [GO:0042744]; nitric oxide transport [GO:0030185]; oxygen transport [GO:0015671]; regulation of eIF2 alpha phosphorylation by heme [GO:0010999]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]; myelin sheath [GO:0043209]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; hemoglobin beta binding [GO:0031722]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]; protein-containing complex binding [GO:0044877]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.
|
Mus musculus (Mouse)
|
P02089
|
HBB2_MOUSE
|
MVHLTDAEKSAVSCLWAKVNPDEVGGEALGRLLVVYPWTQRYFDSFGDLSSASAIMGNPKVKAHGKKVITAFNEGLKNLDNLKGTFASLSELHCDKLHVDPENFRLLGNAIVIVLGHHLGKDFTPAAQAAFQKVVAGVATALAHKYH
| null | null |
carbon dioxide transport [GO:0015670]; erythrocyte development [GO:0048821]; hydrogen peroxide catabolic process [GO:0042744]; myeloid cell differentiation [GO:0030099]; nitric oxide transport [GO:0030185]; oxygen transport [GO:0015671]; positive regulation of myeloid cell differentiation [GO:0045639]; regulation of erythrocyte differentiation [GO:0045646]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; hemoglobin beta binding [GO:0031722]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]; protein-containing complex binding [GO:0044877]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.
|
Mus musculus (Mouse)
|
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