P01709 (LV206_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Ig lambda chain V-II region MGC
Organism	Homo sapiens (Human)
Taxonomic identifier	9606 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	111 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Miscellaneous	This is a Bence-Jones protein. The MCG-type C region appears to be correlated with a very unusual V-region substitution, 103-Thr above for Gly, suggesting that the V-C joining mechanism is not always random. The C region of this chain has the Kern+ and Mcg+ markers.
Sequence similarities	Contains 1 Ig-like (immunoglobulin-like) domain.

Ontologies

Keywords
Domain	Immunoglobulin V region Immunoglobulin domain
Molecular function	Bence-Jones protein
PTM	Disulfide bond Pyrrolidone carboxylic acid
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	complement activation, classical pathway Traceable author statement. Source: Reactome innate immune response Traceable author statement. Source: Reactome
Cellular component	extracellular region Non-traceable author statement Ref.1. Source: UniProtKB
Molecular function	antigen binding Non-traceable author statement Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – ›111

›111

Ig lambda chain V-II region MGC

PRO_0000059835

Regions

Domain

1 – 108

108

Ig-like

Amino acid modifications

Modified residue

1

1

Pyrrolidone carboxylic acid Ref.1

Disulfide bond

22 ↔ 90

By similarity

Experimental info

Non-terminal residue

111

1

Secondary structure

1

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111

Helix Strand Turn

Details...

Beta strand

8 – 12

5

Beta strand

18 – 33

16

Beta strand

35 – 40

6

Beta strand

47 – 51

5

Turn

52 – 54

3

Beta strand

62 – 68

7

Beta strand

70 – 79

10

Helix

82 – 84

3

Beta strand

86 – 92

7

Beta strand

95 – 97

3

Beta strand

100 – 102

3

Beta strand

105 – 109

5

Sequences

	Sequence		Length	Mass (Da)
	P01709 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 7CC1D6E2FA3377BA	FASTA	111	11,558
	10 20 30 40 50 60 QSALTQPPSA SGSLGQSVTI SCTGTSSDVG GYNYVSWYQQ HAGKAPKVII YEVNKRPSGV 70 80 90 100 110 PDRFSGSKSG NTASLTVSGL QAEDEADYYC SSYEGSDNFV FGTGTKVTVL G

References

[1]	"Primary structure of the Mcg lambda chain." Fett J.W., Deutsch H.F. Biochemistry 13:4102-4114(1974) [PubMed: 4415202] [Abstract] Cited for: PROTEIN SEQUENCE.
[2]	"A new lambda-chain gene." Fett J.W., Deutsch H.F. Immunochemistry 12:643-652(1975) [PubMed: 812801] [Abstract] Cited for: LAMBDA CHAIN GENES.
[3]	"Rotational allomerism and divergent evolution of domains in immunoglobulin light chains." Edmundson A.B., Ely K.R., Abola E.E., Schiffer M., Panagiotopoulos N. Biochemistry 14:3953-3961(1975) Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[4]	"Three-dimensional structure of a light chain dimer crystallized in water. Conformational flexibility of a molecule in two crystal forms." Ely K.R., Herron J.N., Harker M., Edmundson A.B. J. Mol. Biol. 210:601-615(1989) [PubMed: 2515285] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

IPI

IPI00382427.

PIR

L2HUMC. A90381.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A8J	X-ray	2.70	H/L	2-111	[»]
1DCL	X-ray	2.30	A/B	2-111	[»]
2MCG	X-ray	2.00	1/2	2-111	[»]

ProteinModelPortal

P01709.

SMR

P01709. Positions 2-111.

ModBase

Search...

Protein-protein interaction databases

STRING

P01709.

Polymorphism databases

DMDM

126559.

Proteomic databases

PRIDE

P01709.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Phylogenomic databases

HOVERGEN

HBG018013.

Enzyme and pathway databases

Reactome

REACT_6900. Immune System.

Gene expression databases

Genevestigator

P01709.

GermOnline

ENSG00000100208. Homo sapiens.

Family and domain databases

InterPro

IPR007110. Ig-like.
IPR013783. Ig-like_fold.
IPR013106. Ig_V-set.
IPR003596. Ig_V-set_subgr.
[Graphical view]

Gene3D

G3DSA:2.60.40.10. Ig-like_fold. 1 hit.

Pfam

PF07686. V-set. 1 hit.
[Graphical view]

SMART

SM00406. IGv. 1 hit.
[Graphical view]

PROSITE

PS50835. IG_LIKE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

LV206_HUMAN

Accession

Primary (citable) accession number: P01709

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	December 14, 2011
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.