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P15814 (IGLL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Immunoglobulin lambda-like polypeptide 1
Alternative name(s):
CD179 antigen-like family member B
Ig lambda-5
Immunoglobulin omega polypeptide
Immunoglobulin-related protein 14.1
CD_antigen=CD179b
Gene names
Name:IGLL1
Synonyms:IGL1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length213 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Critical for B-cell development. Ref.7

Subunit structure

Associates non-covalently with VPREB1. Ref.8

Subcellular location

Secreted Ref.7.

Tissue specificity

Expressed only in pre-B-cells and a special B-cell line (which is surface Ig negative). Ref.5

Involvement in disease

Agammaglobulinemia 2, autosomal recessive (AGM2) [MIM:613500]: A primary immunodeficiency characterized by profoundly low or absent serum antibodies and low or absent circulating B cells due to an early block of B-cell development. Affected individuals develop severe infections in the first years of life.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Sequence similarities

Contains 1 Ig-like C1-type (immunoglobulin-like) domain.

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainImmunoglobulin domain
Signal
   PTMDisulfide bond
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processimmune response

Non-traceable author statement Ref.1. Source: UniProtKB

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane

Non-traceable author statement Ref.1. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P15814-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P15814-2)

The sequence of this isoform differs from the canonical sequence as follows:
     70-213: FLLQRGSWTG...EKTVAPAECS → SAQGHPLGHSVPAVL
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3737 Potential
Chain38 – 213176Immunoglobulin lambda-like polypeptide 1
PRO_0000014777

Regions

Domain114 – 20895Ig-like C1-type
Region97 – 10812J region (By similarity to lambda light-chain)
Region109 – 213105C region (By similarity to lambda light-chain)

Amino acid modifications

Disulfide bond135 ↔ 194 Ref.8
Disulfide bond212Interchain (with a heavy chain) By similarity

Natural variations

Alternative sequence70 – 213144FLLQR…PAECS → SAQGHPLGHSVPAVL in isoform 2.
VSP_042748
Natural variant1201P → L.
Corresponds to variant rs1064425 [ dbSNP | Ensembl ].
VAR_049878
Natural variant1421P → L in a patient with agammaglobulinemia. Ref.7
Corresponds to variant rs1064422 [ dbSNP | Ensembl ].
VAR_034869
Natural variant1891R → H.
Corresponds to variant rs8138122 [ dbSNP | Ensembl ].
VAR_059392

Secondary structure

........................... 213
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 9133A7742B943C79

FASTA21322,963
        10         20         30         40         50         60 
MRPGTGQGGL EAPGEPGPNL RQRWPLLLLG LAVVTHGLLR PTAASQSRAL GPGAPGGSSR 

        70         80         90        100        110        120 
SSLRSRWGRF LLQRGSWTGP RCWPRGFQSK HNSVTHVFGS GTQLTVLSQP KATPSVTLFP 

       130        140        150        160        170        180 
PSSEELQANK ATLVCLMNDF YPGILTVTWK ADGTPITQGV EMTTPSKQSN NKYAASSYLS 

       190        200        210 
LTPEQWRSRR SYSCQVMHEG STVEKTVAPA ECS 

« Hide

Isoform 2 [UniParc].

Checksum: 60CEE4A92442032A
Show »

FASTA848,574

References

« Hide 'large scale' references
[1]"Immunoglobulin lambda light-chain-related genes 14.1 and 16.1 are expressed in pre-B cells and may encode the human immunoglobulin omega light-chain protein."
Hollis G.F., Evans R.J., Stafford-Hollis J.M., Korsmeyer S.J., McKearn J.P.
Proc. Natl. Acad. Sci. U.S.A. 86:5552-5556(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Genomic structure of the human Ig lambda 1 gene suggests that it may be expressed as an Ig lambda 14.1-like protein or as a canonical B cell Ig lambda light chain: implications for Ig lambda gene evolution."
Evans R.J., Hollis G.F.
J. Exp. Med. 173:305-311(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Lymphoid tissue.
[3]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Testis.
[5]"The immunoglobulin lambda-like gene cluster (14.1, 16.1 and F lambda 1) contains gene(s) selectively expressed in pre-B cells and is the human counterpart of the mouse lambda 5 gene."
Schiff C., Bensmana M., Guglielmi P., Milili M., Lefranc M.-P., Fougereau M.
Int. Immunol. 2:201-207(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-193, TISSUE SPECIFICITY.
[6]"Identification of three new Ig lambda-like genes in man."
Chang H., Dmitrovsky E., Hieter P.A., Mitchell K., Leder P., Turoczi L., Kirsch I.R., Hollis G.F.
J. Exp. Med. 163:425-435(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 95-213.
[7]"Mutations in the human lambda5/14.1 gene result in B cell deficiency and agammaglobulinemia."
Minegishi Y., Coustan-Smith E., Wang Y.H., Cooper M.D., Campana D., Conley M.E.
J. Exp. Med. 187:71-77(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, VARIANT LEU-142.
[8]"Structural insight into pre-B cell receptor function."
Bankovich A.J., Raunser S., Juo Z.S., Walz T., Davis M.M., Garcia K.C.
Science 316:291-294(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 93-209 IN COMPLEX WITH VPREB1, SUBUNIT, DISULFIDE BOND.
+Additional computationally mapped references.

Web resources

IGLL1base

IGLL1 mutation db

Wikipedia

IGLL1

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M27749 mRNA. Translation: AAA36100.1.
M34513, M34511, M34512 Genomic DNA. Translation: AAA36096.1.
AP000345 Genomic DNA. No translation available.
BC030239 mRNA. Translation: AAH30239.2.
BC012293 mRNA. Translation: AAH12293.1.
X03528 Genomic DNA. Translation: CAA27229.1.
X03530 Genomic DNA. Translation: CAA27231.1.
PIRA33911.
RefSeqNP_064455.1. NM_020070.3.
NP_690594.1. NM_152855.2.
UniGeneHs.348935.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2H32X-ray2.70B93-213[»]
2H3NX-ray2.30B/D94-209[»]
2LKQNMR-A59-82[»]
ProteinModelPortalP15814.
SMRP15814. Positions 13-212.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109759. 1 interaction.
IntActP15814. 5 interactions.
MINTMINT-4657105.
STRING9606.ENSP00000329312.

PTM databases

PhosphoSiteP15814.

Polymorphism databases

DMDM123944.

Proteomic databases

PaxDbP15814.
PeptideAtlasP15814.
PRIDEP15814.

Protocols and materials databases

DNASU3543.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000249053; ENSP00000249053; ENSG00000128322. [P15814-2]
ENST00000330377; ENSP00000329312; ENSG00000128322. [P15814-1]
GeneID3543.
KEGGhsa:3543.
UCSCuc002zxd.3. human. [P15814-1]
uc002zxe.3. human. [P15814-2]

Organism-specific databases

CTD3543.
GeneCardsGC22M023915.
HGNCHGNC:5870. IGLL1.
MIM146770. gene.
613500. phenotype.
neXtProtNX_P15814.
Orphanet33110. Autosomal agammaglobulinemia.
PharmGKBPA29756.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG46716.
HOGENOMHOG000113013.
HOVERGENHBG039526.
InParanoidP15814.
KOK06554.
OMAKHNSVTH.
OrthoDBEOG7X0VQW.
PhylomeDBP15814.
TreeFamTF335549.

Gene expression databases

ArrayExpressP15814.
BgeeP15814.
CleanExHS_IGLL1.
GenevestigatorP15814.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR003597. Ig_C1-set.
[Graphical view]
PfamPF07654. C1-set. 1 hit.
[Graphical view]
SMARTSM00407. IGc1. 1 hit.
[Graphical view]
PROSITEPS50835. IG_LIKE. 1 hit.
PS00290. IG_MHC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP15814.
GeneWikiIGLL1.
GenomeRNAi3543.
NextBio13836.
PROP15814.
SOURCESearch...

Entry information

Entry nameIGLL1_HUMAN
AccessionPrimary (citable) accession number: P15814
Secondary accession number(s): Q0P681
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: April 16, 2014
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries