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Protein

Immunoglobulin heavy variable 3-7

Gene

IGHV3-7

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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:22158414, PubMed:20176268). 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:20176268, PubMed:17576170).4 Publications

Caution

For examples of full-length immunoglobulin heavy chains (of different isotypes) see AC P0DOX2, AC P0DOX3, AC P0DOX4, AC P0DOX5 and AC P0DOX6.Curated

GO - Molecular functioni

  • antigen binding Source: UniProtKB
  • serine-type endopeptidase activity Source: Reactome

GO - Biological processi

Keywordsi

Biological processAdaptive immunity, Immunity

Enzyme and pathway databases

ReactomeiR-HSA-166663 Initial triggering of complement
R-HSA-173623 Classical antibody-mediated complement activation
R-HSA-198933 Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell
R-HSA-202733 Cell surface interactions at the vascular wall
R-HSA-2029481 FCGR activation
R-HSA-2029482 Regulation of actin dynamics for phagocytic cup formation
R-HSA-2029485 Role of phospholipids in phagocytosis
R-HSA-2168880 Scavenging of heme from plasma
R-HSA-2454202 Fc epsilon receptor (FCERI) signaling
R-HSA-2730905 Role of LAT2/NTAL/LAB on calcium mobilization
R-HSA-2871796 FCERI mediated MAPK activation
R-HSA-2871809 FCERI mediated Ca+2 mobilization
R-HSA-2871837 FCERI mediated NF-kB activation
R-HSA-5690714 CD22 mediated BCR regulation
R-HSA-977606 Regulation of Complement cascade
R-HSA-983695 Antigen activates B Cell Receptor (BCR) leading to generation of second messengers

Protein family/group databases

IMGT/GENE-DBIGHV3-7

Names & Taxonomyi

Protein namesi
Recommended name:
Immunoglobulin heavy variable 3-72 Publications
Alternative name(s):
Ig heavy chain V-III region GAL1 Publication
Ig heavy chain V-III region GAR1 Publication
Ig heavy chain V-III region JON1 Publication
Gene namesi
Name:IGHV3-72 Publications
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

EuPathDBiHostDB:ENSG00000211938.2
HGNCiHGNC:5620 IGHV3-7
neXtProtiNX_P01780

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Organism-specific databases

DisGeNETi28452
OpenTargetsiENSG00000211938

Polymorphism and mutation databases

DMDMi123859
123860

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 193 PublicationsAdd BLAST19
ChainiPRO_000005993120 – 117Immunoglobulin heavy variable 3-73 PublicationsAdd BLAST98

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi41 ↔ 115PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PeptideAtlasiP01780
PRIDEiP01780
ProteomicsDBi51479
51480
57684

Expressioni

Gene expression databases

BgeeiENSG00000211938

Interactioni

Subunit structurei

Immunoglobulins are composed of two identical heavy chains and two identical light chains; disulfide-linked.1 Publication

Protein-protein interaction databases

IntActiP01780, 1 interactor

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2FL5X-ray3.00B/D/F/H20-117[»]
ProteinModelPortaliP01780
SMRiP01780
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini20 – ›117Ig-likePROSITE-ProRule annotationAdd BLAST›98

Keywords - Domaini

Immunoglobulin domain, Immunoglobulin V region, Signal

Phylogenomic databases

GeneTreeiENSGT00760000118963
HOVERGENiHBG018013
OMAiWVATITS
PhylomeDBiP01780

Family and domain databases

Gene3Di2.60.40.10, 1 hit
InterProiView protein in InterPro
IPR007110 Ig-like_dom
IPR036179 Ig-like_dom_sf
IPR013783 Ig-like_fold
IPR013106 Ig_V-set
PfamiView protein in Pfam
PF07686 V-set, 1 hit
SMARTiView protein in SMART
SM00406 IGv, 1 hit
SUPFAMiSSF48726 SSF48726, 1 hit
PROSITEiView protein in PROSITE
PS50835 IG_LIKE, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P01780-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELGLSWVFL VAILEGVQCE VQLVESGGGL VQPGGSLRLS CAASGFTFSS
60 70 80 90 100
YWMSWVRQAP GKGLEWVANI KQDGSEKYYV DSVKGRFTIS RDNAKNSLYL
110
QMNSLRAEDT AVYYCAR
Length:117
Mass (Da):12,943
Last modified:October 5, 2016 - v2
Checksum:i32001F95FCA6C2FC
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti20E → D AA sequence (PubMed:4522793).Curated1
Sequence conflicti29G → D AA sequence (PubMed:4803843).Curated1
Sequence conflicti32Q → K AA sequence (PubMed:4522793).Curated1
Sequence conflicti35G → E AA sequence (PubMed:7737190).Curated1
Sequence conflicti35G → R AA sequence (PubMed:4803843).Curated1
Sequence conflicti38R → K AA sequence (PubMed:7737190).Curated1
Sequence conflicti42A → T AA sequence (PubMed:7737190).Curated1
Sequence conflicti47 – 54TFSSYWMS → BFBBLGMT AA sequence (PubMed:4803843).Curated8
Sequence conflicti47 – 54TFSSYWMS → SYSNYVMT AA sequence (PubMed:7737190).Curated8
Sequence conflicti50 – 51SY → TA AA sequence (PubMed:4522793).Curated2
Sequence conflicti54S → K AA sequence (PubMed:4522793).Curated1
Sequence conflicti68 – 75ANIKQDGS → VWRVEQVV AA sequence (PubMed:4522793).Curated8
Sequence conflicti68A → T AA sequence (PubMed:7737190).Curated1
Sequence conflicti71 – 75KQDGS → RPDET AA sequence (PubMed:7737190).Curated5
Sequence conflicti77 – 78KY → ZB AA sequence (PubMed:4803843).Curated2
Sequence conflicti78 – 81YYVD → AFAN AA sequence (PubMed:4522793).Curated4
Sequence conflicti78 – 80YYV → FYS AA sequence (PubMed:7737190).Curated3
Sequence conflicti84 – 85Missing AA sequence (PubMed:7737190).Curated2
Sequence conflicti84K → N AA sequence (PubMed:4522793).Curated1
Sequence conflicti89I → V AA sequence (PubMed:7737190).Curated1
Sequence conflicti92 – 94DNA → NDS AA sequence (PubMed:4522793).Curated3
Sequence conflicti95K → R AA sequence (PubMed:7737190).Curated1
Sequence conflicti97S → T AA sequence (PubMed:4522793).Curated1
Sequence conflicti98 – 107LYLQMNSLRA → VSNSMFLQRV AA sequence (PubMed:7737190).Curated10
Sequence conflicti103 – 107NSLRA → ISVTP AA sequence (PubMed:4522793).Curated5
Sequence conflicti107A → V AA sequence (PubMed:4803843).Curated1
Sequence conflicti112V → L AA sequence (PubMed:4803843).Curated1
Sequence conflicti112V → T AA sequence (PubMed:7737190).Curated1
Non-terminal residuei1171

Polymorphismi

There are several alleles. The sequence shown is that of IMGT allele IGHV3-7*03.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC244226 Genomic DNA No translation available.
PIRiA02063 G3HUJN
A02064 M3HUGL
S69132

Genome annotation databases

EnsembliENST00000390598; ENSP00000375007; ENSG00000211938
ENST00000633988; ENSP00000487659; ENSG00000282211

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiHV307_HUMAN
AccessioniPrimary (citable) accession number: P01780
Secondary accession number(s): A0A0B4J1U8, P01781, P80419
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 5, 2016
Last modified: June 20, 2018
This is version 96 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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