Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Immunoglobulin kappa variable 1D-33

Gene

IGKV1D-33

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition. 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:20176268, PubMed:17576170).3 Publications

GO - Molecular functioni

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

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Adaptive 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-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-983695. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.

Names & Taxonomyi

Protein namesi
Recommended name:
Immunoglobulin kappa variable 1D-332 Publications
Alternative name(s):
Ig kappa chain V-I region AG1 Publication
Ig kappa chain V-I region Bi1 Publication
Ig kappa chain V-I region Lay2 Publications
Ig kappa chain V-I region Ni1 Publication
Ig kappa chain V-I region Rei1 Publication
Ig kappa chain V-I region Roy1 Publication
Ig kappa chain V-I region Scw1 Publication
Ig kappa chain V-I region WAT2 Publications
Gene namesi
Name:IGKV1D-332 Publications
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:5753. IGKV1D-33.

Subcellular locationi

GO - Cellular componenti

  • blood microparticle Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: UniProtKB
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Organism-specific databases

OpenTargetsiENSG00000239975.
ENSG00000242076.
ENSG00000282811.

Polymorphism and mutation databases

DMDMi1170720.
125756.
125759.
125769.
125771.
125772.
125773.
125777.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 2210 PublicationsAdd BLAST22
ChainiPRO_000005973723 – 117Immunoglobulin kappa variable 1D-339 PublicationsAdd BLAST95

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi45 ↔ 110PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PeptideAtlasiP01593.
PRIDEiP01593.

PTM databases

iPTMnetiP01607.

Interactioni

Subunit structurei

Immunoglobulins are composed of two identical heavy chains and two identical light chains, linked by disulfide bonds.1 Publication

Structurei

Secondary structure

1117
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 7Combined sources4
Beta strandi9 – 13Combined sources5
Beta strandi19 – 27Combined sources9
Beta strandi33 – 38Combined sources6
Beta strandi45 – 49Combined sources5
Turni50 – 52Combined sources3
Beta strandi62 – 67Combined sources6
Beta strandi70 – 77Combined sources8
Helixi80 – 82Combined sources3
Beta strandi84 – 90Combined sources7
Beta strandi92 – 95Combined sources4
Beta strandi102 – 106Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AR2X-ray2.80A23-117[»]
1BWWX-ray1.70A/B23-117[»]
1REIX-ray2.00A/B23-117[»]
1WTLX-ray1.90A/B23-117[»]
4L1HX-ray1.68A23-117[»]
ProteinModelPortaliP01593.
SMRiP01593.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01607.
P80362.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini24 – ›117Ig-likePROSITE-ProRule annotationAdd BLAST›94

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni23 – 45Framework-1Add BLAST23
Regioni46 – 56Complementarity-determining-1Add BLAST11
Regioni57 – 71Framework-2Add BLAST15
Regioni72 – 78Complementarity-determining-27
Regioni79 – 110Framework-3Add BLAST32
Regioni111 – 117Complementarity-determining-37

Sequence similaritiesi

Contains 1 Ig-like (immunoglobulin-like) domain.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Immunoglobulin V region, Signal

Phylogenomic databases

HOVERGENiHBG018013.
OMAiCHASQSI.
PhylomeDBiP01593.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
[Graphical view]
PfamiPF07686. V-set. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
SM00406. IGv. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P01593-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDMRVPAQLL GLLLLWLSGA RCDIQMTQSP SSLSASVGDR VTITCQASQD
60 70 80 90 100
ISNYLNWYQQ KPGKAPKLLI YDASNLETGV PSRFSGSGSG TDFTFTISSL
110
QPEDIATYYC QQYDNLP
Length:117
Mass (Da):12,848
Last modified:November 2, 2016 - v2
Checksum:iEE4F871C54A514FB
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti32S → P AA sequence (PubMed:4563064).Curated1
Sequence conflicti35A → V AA sequence (PubMed:824717).Curated1
Sequence conflicti35A → V AA sequence (PubMed:2496160).Curated1
Sequence conflicti36S → T AA sequence (PubMed:4709625).Curated1
Sequence conflicti40R → S AA sequence (PubMed:4563064).Curated1
Sequence conflicti43 – 46ITCQ → LLCE AA sequence (PubMed:4709625).Curated4
Sequence conflicti46Q → R AA sequence (PubMed:7993911).Curated1
Sequence conflicti46Q → R AA sequence (PubMed:6167731).Curated1
Sequence conflicti50 – 56DISNYLN → SVLESGNTFLA AA sequence (PubMed:4709625).Curated7
Sequence conflicti50 – 53DISN → NVNA AA sequence (PubMed:824717).Curated4
Sequence conflicti50 – 53DISN → NVNA AA sequence (PubMed:2496160).Curated4
Sequence conflicti52 – 56SNYLN → RNSLI AA sequence (PubMed:4563064).Curated5
Sequence conflicti52 – 54SNY → RKH AA sequence (PubMed:4435756).Curated3
Sequence conflicti52 – 53SN → IK AA sequence (PubMed:809329).Curated2
Sequence conflicti52 – 53SN → NH AA sequence (PubMed:4893682).Curated2
Sequence conflicti52S → T AA sequence (PubMed:7993911).Curated1
Sequence conflicti52S → T AA sequence (PubMed:6167731).Curated1
Sequence conflicti53 – 54NY → IF AA sequence (PubMed:5595110).Curated2
Sequence conflicti53N → D AA sequence (PubMed:6167731).Curated1
Sequence conflicti55L → V AA sequence (PubMed:7993911).Curated1
Sequence conflicti55L → V AA sequence (PubMed:6167731).Curated1
Sequence conflicti58Y → F AA sequence (PubMed:7993911).Curated1
Sequence conflicti59Q → D AA sequence (PubMed:4435756).Curated1
Sequence conflicti61K → G AA sequence (PubMed:4893682).Curated1
Sequence conflicti61K → R AA sequence (PubMed:7993911).Curated1
Sequence conflicti61K → T AA sequence (PubMed:809329).Curated1
Sequence conflicti63G → K AA sequence (PubMed:4709625).Curated1
Sequence conflicti63G → K AA sequence (PubMed:4893682).Curated1
Sequence conflicti64K → L AA sequence (PubMed:824717).Curated1
Sequence conflicti64K → L AA sequence (PubMed:2496160).Curated1
Sequence conflicti64K → Q AA sequence (PubMed:7993911).Curated1
Sequence conflicti67K → R AA sequence (PubMed:4435756).Curated1
Sequence conflicti68L → F AA sequence (PubMed:4563064).Curated1
Sequence conflicti68L → I AA sequence (PubMed:4893682).Curated1
Sequence conflicti68L → V AA sequence (PubMed:7993911).Curated1
Sequence conflicti72D → E AA sequence (PubMed:809329).Curated1
Sequence conflicti72D → G AA sequence (PubMed:7993911).Curated1
Sequence conflicti72D → G AA sequence (PubMed:4435756).Curated1
Sequence conflicti72D → G AA sequence (PubMed:824717).Curated1
Sequence conflicti72D → G AA sequence (PubMed:2496160).Curated1
Sequence conflicti74S → E AA sequence (PubMed:4563064).Curated1
Sequence conflicti75N → I AA sequence (PubMed:7993911).Curated1
Sequence conflicti75N → K AA sequence (PubMed:5595110).Curated1
Sequence conflicti75N → T AA sequence (PubMed:4435756).Curated1
Sequence conflicti75N → T AA sequence (PubMed:824717).Curated1
Sequence conflicti75N → T AA sequence (PubMed:2496160).Curated1
Sequence conflicti76L → R AA sequence (PubMed:824717).Curated1
Sequence conflicti76L → R AA sequence (PubMed:2496160).Curated1
Sequence conflicti77E → Q AA sequence (PubMed:809329).Curated1
Sequence conflicti78T → A AA sequence (PubMed:5595110).Curated1
Sequence conflicti78T → A AA sequence (PubMed:824717).Curated1
Sequence conflicti78T → A AA sequence (PubMed:2496160).Curated1
Sequence conflicti78T → A AA sequence (PubMed:809329).Curated1
Sequence conflicti78T → I AA sequence (PubMed:4563064).Curated1
Sequence conflicti85S → R AA sequence (PubMed:4563064).Curated1
Sequence conflicti86G → E AA sequence (PubMed:4709625).Curated1
Sequence conflicti87S → T AA sequence (PubMed:5595110).Curated1
Sequence conflicti89S → F AA sequence (PubMed:4893682).Curated1
Sequence conflicti93F → Y AA sequence (PubMed:809329).Curated1
Sequence conflicti94 – 96TFT → ALS AA sequence (PubMed:4563064).Curated3
Sequence conflicti95F → L AA sequence (PubMed:4435756).Curated1
Sequence conflicti99S → G AA sequence (PubMed:4893682).Curated1
Sequence conflicti99S → G AA sequence (PubMed:4709625).Curated1
Sequence conflicti99S → T AA sequence (PubMed:4435756).Curated1
Sequence conflicti105I → F AA sequence (PubMed:4563064).Curated1
Sequence conflicti105I → F AA sequence (PubMed:4709625).Curated1
Sequence conflicti106 – 107AT → GN AA sequence (PubMed:4435756).Curated2
Sequence conflicti107T → V AA sequence (PubMed:4709625).Curated1
Sequence conflicti113Y → F AA sequence (PubMed:5595110).Curated1
Sequence conflicti114 – 116DNL → NNW AA sequence (PubMed:824717).Curated3
Sequence conflicti114 – 116DNL → NNW AA sequence (PubMed:2496160).Curated3
Sequence conflicti114 – 115DN → QS AA sequence (PubMed:809329).Curated2
Sequence conflicti114D → Y AA sequence (PubMed:4563064).Curated1
Sequence conflicti115N → T AA sequence (PubMed:7993911).Curated1
Sequence conflicti115N → T AA sequence (PubMed:4709625).Curated1
Sequence conflicti115N → T AA sequence (PubMed:4893682).Curated1
Sequence conflicti116L → V AA sequence (PubMed:4435756).Curated1
Non-terminal residuei1171

Polymorphismi

There are several alleles. The sequence shown is that of IMGT allele IGKV1D-33*01.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC233264 Genomic DNA. No translation available.
PIRiA01861. K1HUAG.
A01863. K1HUBI.
A01871. K1HULY.
A01875. K1HUSW.
A01880. K1HUNY.
A91638. K1HURY.
A91663. K1HURE.

Genome annotation databases

EnsembliENST00000390265; ENSP00000374800; ENSG00000239975.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

IMGT/GENE-DB

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC233264 Genomic DNA. No translation available.
PIRiA01861. K1HUAG.
A01863. K1HUBI.
A01871. K1HULY.
A01875. K1HUSW.
A01880. K1HUNY.
A91638. K1HURY.
A91663. K1HURE.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AR2X-ray2.80A23-117[»]
1BWWX-ray1.70A/B23-117[»]
1REIX-ray2.00A/B23-117[»]
1WTLX-ray1.90A/B23-117[»]
4L1HX-ray1.68A23-117[»]
ProteinModelPortaliP01593.
SMRiP01593.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

IMGTiSearch...

PTM databases

iPTMnetiP01607.

Polymorphism and mutation databases

DMDMi1170720.
125756.
125759.
125769.
125771.
125772.
125773.
125777.

Proteomic databases

PeptideAtlasiP01593.
PRIDEiP01593.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000390265; ENSP00000374800; ENSG00000239975.

Organism-specific databases

HGNCiHGNC:5753. IGKV1D-33.
OpenTargetsiENSG00000239975.
ENSG00000242076.
ENSG00000282811.
GenAtlasiSearch...

Phylogenomic databases

HOVERGENiHBG018013.
OMAiCHASQSI.
PhylomeDBiP01593.

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-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-983695. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.

Miscellaneous databases

EvolutionaryTraceiP01607.
P80362.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
[Graphical view]
PfamiPF07686. V-set. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
SM00406. IGv. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiKVD33_HUMAN
AccessioniPrimary (citable) accession number: P01593
Secondary accession number(s): A0A0B4J1U0
, P01595, P01605, P01607, P01608, P01609, P01613, P80362
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 2, 2016
Last modified: November 30, 2016
This is version 97 of the entry and version 2 of the sequence. [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 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.