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O15389 (SIGL5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 127. 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·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sialic acid-binding Ig-like lectin 5

Short name=Siglec-5
Alternative name(s):
CD33 antigen-like 2
Obesity-binding protein 2
Short name=OB-BP2
Short name=OB-binding protein 2
CD_antigen=CD170
Gene names
Name:SIGLEC5
Synonyms:CD33L2, OBBP2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length551 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Binds equally to alpha-2,3-linked and alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface.

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Expressed by monocytic/myeloid lineage cells. Found at high levels in peripheral blood leukocytes, spleen, bone marrow and at lower levels in lymph node, lung, appendix, placenta, pancreas and thymus. Expressed by monocytes and neutrophils but absent from leukemic cell lines representing early stages of myelomonocytic differentiation.

Domain

Contains 1 copy of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is involved in modulation of cellular responses. The phosphorylated ITIM motif can bind the SH2 domain of several SH2-containing phosphatases.

Sequence similarities

Belongs to the immunoglobulin superfamily. SIGLEC (sialic acid binding Ig-like lectin) family.

Contains 2 Ig-like C2-type (immunoglobulin-like) domains.

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

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   LigandLectin
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Potential
Chain17 – 551535Sialic acid-binding Ig-like lectin 5
PRO_0000014944

Regions

Topological domain17 – 441425Extracellular Potential
Transmembrane442 – 46221Helical; Potential
Topological domain463 – 55189Cytoplasmic Potential
Domain19 – 136118Ig-like V-type
Domain146 – 22984Ig-like C2-type 1
Domain236 – 33095Ig-like C2-type 2
Motif518 – 5236ITIM motif
Motif542 – 5476SLAM-like motif

Sites

Binding site1191Sialic acid
Binding site1271Sialic acid
Binding site1291Sialic acid

Amino acid modifications

Glycosylation1001N-linked (GlcNAc...) Potential
Glycosylation2101N-linked (GlcNAc...) Potential
Glycosylation2311N-linked (GlcNAc...) Potential
Glycosylation2531N-linked (GlcNAc...) Potential
Glycosylation3281N-linked (GlcNAc...) Potential
Glycosylation3751N-linked (GlcNAc...) Potential
Glycosylation3841N-linked (GlcNAc...) Potential
Glycosylation3931N-linked (GlcNAc...) Potential
Disulfide bond36 ↔ 170 Ref.6
Disulfide bond41 ↔ 101 Ref.6
Disulfide bond164 ↔ 213 Ref.6
Disulfide bond269 ↔ 314 By similarity

Natural variations

Natural variant721V → A.
Corresponds to variant rs1973019 [ dbSNP | Ensembl ].
VAR_014249
Natural variant2151M → V.
Corresponds to variant rs1807124 [ dbSNP | Ensembl ].
VAR_014250
Natural variant3221F → S.
Corresponds to variant rs2278831 [ dbSNP | Ensembl ].
VAR_014251
Natural variant3581R → W. Ref.1
Corresponds to variant rs8108074 [ dbSNP | Ensembl ].
VAR_049929
Natural variant4991P → A. Ref.5
Corresponds to variant rs3829655 [ dbSNP | Ensembl ].
VAR_020087

Experimental info

Sequence conflict3091E → K in AAD50978. Ref.1
Sequence conflict3881A → P in AAD50978. Ref.1
Sequence conflict4031S → N in AAD50978. Ref.1

Secondary structure

.................................................... 551
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O15389 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 2FEA2B6B341EFEAF

FASTA55160,715
        10         20         30         40         50         60 
MLPLLLLPLL WGGSLQEKPV YELQVQKSVT VQEGLCVLVP CSFSYPWRSW YSSPPLYVYW 

        70         80         90        100        110        120 
FRDGEIPYYA EVVATNNPDR RVKPETQGRF RLLGDVQKKN CSLSIGDARM EDTGSYFFRV 

       130        140        150        160        170        180 
ERGRDVKYSY QQNKLNLEVT ALIEKPDIHF LEPLESGRPT RLSCSLPGSC EAGPPLTFSW 

       190        200        210        220        230        240 
TGNALSPLDP ETTRSSELTL TPRPEDHGTN LTCQMKRQGA QVTTERTVQL NVSYAPQTIT 

       250        260        270        280        290        300 
IFRNGIALEI LQNTSYLPVL EGQALRLLCD APSNPPAHLS WFQGSPALNA TPISNTGILE 

       310        320        330        340        350        360 
LRRVRSAEEG GFTCRAQHPL GFLQIFLNLS VYSLPQLLGP SCSWEAEGLH CRCSFRARPA 

       370        380        390        400        410        420 
PSLCWRLEEK PLEGNSSQGS FKVNSSSAGP WANSSLILHG GLSSDLKVSC KAWNIYGSQS 

       430        440        450        460        470        480 
GSVLLLQGRS NLGTGVVPAA LGGAGVMALL CICLCLIFFL IVKARRKQAA GRPEKMDDED 

       490        500        510        520        530        540 
PIMGTITSGS RKKPWPDSPG DQASPPGDAP PLEEQKELHY ASLSFSEMKS REPKDQEAPS 

       550 
TTEYSEIKTS K 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of siglec-5, a novel glycoprotein expressed on myeloid cells related to CD33."
Cornish A.L., Freeman S., Forbes G., Ni J., Zhang M., Cepeda M., Gentz R., Augustus M., Carter K.C., Crocker P.R.
Blood 92:2123-2132(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT TRP-358.
Tissue: Macrophage.
[2]"OB-BP1/Siglec-6. A leptin- and sialic acid-binding protein of the immunoglobulin superfamily."
Patel N., Brinkman-Van der Linden E.C.M., Altmann S.W., Gish K.C., Balasubramanian S., Timans J.C., Peterson D., Bell M.P., Bazan J.F., Varki A., Kastelein R.A.
J. Biol. Chem. 274:22729-22738(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Erythroleukemia.
[3]Erratum
Patel N., Brinkman-Van der Linden E.C.M., Altmann S.W., Gish K.C., Balasubramanian S., Timans J.C., Peterson D., Bell M.P., Bazan J.F., Varki A., Kastelein R.A.
J. Biol. Chem. 274:28058-28058(1999)
[4]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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], VARIANT ALA-499.
Tissue: Brain.
[6]"Structural implications of Siglec-5-mediated sialoglycan recognition."
Zhuravleva M.A., Trandem K., Sun P.D.
J. Mol. Biol. 375:437-447(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 20-233 ALONE AND IN COMPLEX WITH ALPHA-LINKED SIALYLLACTOSES, DISULFIDE BONDS, SIALIC ACID BINDING SITES.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF170484 mRNA. Translation: AAD50978.1.
U71383 mRNA. Translation: AAB70703.1.
AC018755 Genomic DNA. Translation: AAF87846.1.
BC029896 mRNA. Translation: AAH29896.1.
CCDSCCDS33088.1.
RefSeqNP_003821.1. NM_003830.3.
UniGeneHs.310333.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZG1X-ray2.70A20-233[»]
2ZG2X-ray2.85A20-233[»]
2ZG3X-ray3.00A20-233[»]
ProteinModelPortalO15389.
SMRO15389. Positions 20-233.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114308. 2 interactions.
IntActO15389. 2 interactions.
MINTMINT-1445881.
STRING9606.ENSP00000415200.

PTM databases

PhosphoSiteO15389.

Proteomic databases

PRIDEO15389.

Protocols and materials databases

DNASU8778.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000222107; ENSP00000222107; ENSG00000105501.
ENST00000534261; ENSP00000473238; ENSG00000105501.
ENST00000570106; ENSP00000455510; ENSG00000105501.
GeneID8778.
KEGGhsa:8778.
UCSCuc002pxe.4. human.

Organism-specific databases

CTD8778.
GeneCardsGC19M052114.
HGNCHGNC:10874. SIGLEC5.
HPACAB024900.
HPA009085.
MIM604200. gene.
neXtProtNX_O15389.
PharmGKBPA35775.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHOG000236324.
HOVERGENHBG036161.
InParanoidO15389.
KOK06549.
OMAPEKMDDE.
OrthoDBEOG7JDQXC.
PhylomeDBO15389.
TreeFamTF332441.

Gene expression databases

BgeeO15389.
CleanExHS_SIGLEC5.
GenevestigatorO15389.

Family and domain databases

Gene3D2.60.40.10. 3 hits.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
IPR013151. Immunoglobulin.
[Graphical view]
PfamPF00047. ig. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
SMARTSM00409. IG. 1 hit.
SM00408. IGc2. 1 hit.
[Graphical view]
PROSITEPS50835. IG_LIKE. 3 hits.
PS00290. IG_MHC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO15389.
GeneWikiSIGLEC5.
GenomeRNAi8778.
NextBio32916.
PROO15389.
SOURCESearch...

Entry information

Entry nameSIGL5_HUMAN
AccessionPrimary (citable) accession number: O15389
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 127 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 19

Human chromosome 19: entries, gene names and cross-references to MIM

Human cell differentiation molecules

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