Reviewed, UniProtKB/Swiss-Prot Q9P126 (CLC1B_HUMAN)

Names and origin

Protein names

Recommended name:
    C-type lectin domain family 1 member B
Alternative name(s):
    C-type lectin-like receptor 2
      Short name=CLEC-2

Gene names

Name:	CLEC1B
Synonyms:	CLEC2
ORF Names:	UNQ721/PRO1384

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	229 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Acts as a receptor for the platelet-aggregating snake venom protein rhodocytin. Rhodocytin binding leads to tyrosine phosphorylation and this promotes the binding of spleen tyrosine kinase (Syk) and initiation of downstream tyrosine phosphorylation events and activation of PLC-gamma-2. Acts as an attachment factor for human immunodeficiency virus type 1 (HIV-1) and facilitates its capture by platelets. Ref.2 Ref.6
Subunit structure	Monomer. Ref.7
Subcellular location	Membrane; Single-pass type II membrane protein Probable.
Tissue specificity	Expressed preferentially in the liver. Also expressed in immune cells of myeloid origin and on the surface of platelets. Ref.2 Ref.6 Ref.1
Post-translational modification	Glycosylated. Ref.6 Phosphorylated on tyrosine residue in response to rhodocytin binding. Ref.6
Sequence similarities	Contains 1 C-type lectin domain.

Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal-anchor Transmembrane
Ligand	Lectin
Molecular function	Receptor
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	cell surface receptor linked signal transduction Ref.1 Traceable author statement. Source: ProtInc defense response Ref.1 Traceable author statement. Source: ProtInc
Cellular component	integral to plasma membrane Ref.1 Traceable author statement. Source: ProtInc
Molecular function	sugar binding Inferred from electronic annotation. Source: UniProtKB-KW transmembrane receptor activity Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9P126-1)

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: Q9P126-2)

The sequence of this isoform differs from the canonical sequence as follows:
     22-55: VGSASSSWWRVMALILLILCVGMVVGLVALGIWS → A

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 229

229

C-type lectin domain family 1 member B

PRO_0000280043

Regions

Topological domain

1 – 33

33

Cytoplasmic Potential

Transmembrane

34 – 54

21

Signal-anchor for type II membrane protein Potential

Topological domain

55 – 229

175

Extracellular Potential

Domain

109 – 217

109

C-type lectin

Amino acid modifications

Modified residue

7

1

Phosphotyrosine

Glycosylation

68

1

N-linked (GlcNAc...) Potential

Glycosylation

120

1

N-linked (GlcNAc...) Potential

Glycosylation

134

1

N-linked (GlcNAc...) Potential

Disulfide bond

102 ↔ 113

Ref.7

Disulfide bond

130 ↔ 216

Ref.7

Disulfide bond

195 ↔ 208

Ref.7

Natural variations

Alternative sequence

22 – 55

34

VGSAS…LGIWS → A in isoform 2.

VSP_023515

Natural variant

20

1

I → V: dbSNP rs612593. Ref.2 Ref.1 Ref.3 Ref.5

VAR_031047

Natural variant

24

1

S → P: dbSNP rs2273986. Ref.3

VAR_031048

Natural variant

28

1

S → F: dbSNP rs2273987.

VAR_031049

Natural variant

64

1

G → D: dbSNP rs583903. Ref.2 Ref.1 Ref.3 Ref.5

VAR_031050

Experimental info

Mutagenesis

150

1

K → A: Substantial reduction in rhodocytin binding. Ref.7

Mutagenesis

171

1

K → A: Significant reduction in rhodocytin binding. Ref.7

Mutagenesis

184

1

E → A: Significant reduction in rhodocytin binding. Ref.7

Mutagenesis

187

1

E → A: Significant reduction in rhodocytin binding. Ref.7

Mutagenesis

188

1

D → A: Significant reduction in rhodocytin binding. Ref.7

Mutagenesis

190

1

K → A: Significant reduction in rhodocytin binding. Ref.7

Mutagenesis

192

1

N → A: Significant reduction in rhodocytin binding. Ref.7

Sequence conflict

41

1

C → Y in AAF36777. Ref.1

Sequence conflict

41

1

C → Y Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

229

Helix Strand Turn

Details...

Beta strand

106 – 109

4

Beta strand

112 – 121

10

Helix

123 – 132

10

Helix

143 – 150

8

Beta strand

157 – 162

6

Helix

180 – 185

6

Beta strand

195 – 199

5

Beta strand

202 – 206

5

Beta strand

212 – 219

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 6, 2007. Version 2. Checksum: B39BF202AAE6DDD9	FASTA	229	26,596
	10 20 30 40 50 60 MQDEDGYITL NIKTRKPALI SVGSASSSWW RVMALILLIL CVGMVVGLVA LGIWSVMQRN 70 80 90 100 110 120 YLQGENENRT GTLQQLAKRF CQYVVKQSEL KGTFKGHKCS PCDTNWRYYG DSCYGFFRHN 130 140 150 160 170 180 LTWEESKQYC TDMNATLLKI DNRNIVEYIK ARTHLIRWVG LSRQKSNEVW KWEDGSVISE 190 200 210 220 NMFEFLEDGK GNMNCAYFHN GKMHPTFCEN KHYLMCERKA GMTKVDQLP
	Isoform 2. Checksum: 0BFA3D427640C3F5	FASTA	196	23,096
	10 20 30 40 50 60 MQDEDGYITL NIKTRKPALI SAVMQRNYLQ GENENRTGTL QQLAKRFCQY VVKQSELKGT 70 80 90 100 110 120 FKGHKCSPCD TNWRYYGDSC YGFFRHNLTW EESKQYCTDM NATLLKIDNR NIVEYIKART 130 140 150 160 170 180 HLIRWVGLSR QKSNEVWKWE DGSVISENMF EFLEDGKGNM NCAYFHNGKM HPTFCENKHY 190 LMCERKAGMT KVDQLP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular characterization of two novel C-type lectin-like receptors, one of which is selectively expressed in human dendritic cells." Colonna M., Samaridis J., Angman L. Eur. J. Immunol. 30:697-704(2000) [PubMed: 10671229] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANTS VAL-20 AND ASP-64. Tissue: Liver.
[2]	"DC-SIGN and CLEC-2 mediate human immunodeficiency virus type 1 capture by platelets." Chaipan C., Soilleux E.J., Simpson P., Hofmann H., Gramberg T., Marzi A., Geier M., Stewart E.A., Eisemann J., Steinkasserer A., Suzuki-Inoue K., Fuller G.L., Pearce A.C., Watson S.P., Hoxie J.A., Baribaud F., Poehlmann S. J. Virol. 80:8951-8960(2006) [PubMed: 16940507] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, VARIANTS VAL-20 AND ASP-64. Tissue: Liver.
[3]	"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment." Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M. Genome Res. 13:2265-2270(2003) [PubMed: 12975309] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS VAL-20; PRO-24 AND ASP-64.
[4]	"The finished DNA sequence of human chromosome 12." Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A. Nature 440:346-351(2006) [PubMed: 16541075] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANTS VAL-20 AND ASP-64. Tissue: Testis.
[6]	"A novel Syk-dependent mechanism of platelet activation by the C-type lectin receptor CLEC-2." Suzuki-Inoue K., Fuller G.L.J., Garcia A., Eble J.A., Poehlmann S., Inoue O., Gartner T.K., Hughan S.C., Pearce A.C., Laing G.D., Theakston R.D.G., Schweighoffer E., Zitzmann N., Morita T., Tybulewicz V.L.J., Ozaki Y., Watson S.P. Blood 107:542-549(2006) [PubMed: 16174766] [Abstract] Cited for: FUNCTION, GLYCOSYLATION, PHOSPHORYLATION, TISSUE SPECIFICITY.
[7]	"The crystal structure and mutational binding analysis of the extracellular domain of the platelet-activating receptor CLEC-2." Watson A.A., Brown J., Harlos K., Eble J.A., Walter T.S., O'Callaghan C.A. J. Biol. Chem. 282:3165-3172(2007) [PubMed: 17132623] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 100-221, SUBUNIT, DISULFIDE BONDS, INTERACTION WITH RHODOCYTIN, MUTAGENESIS OF LYS-150; LYS-171; GLU-184; GLU-187; ASP-188; LYS-190 AND ASN-192.
+	Additional computationally mapped references.

Web resources

Functional Glycomics Gateway - Glycan Binding

CLEC-2

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF124841 mRNA. Translation: AAF36777.1.
AY358599 mRNA. Translation: AAQ88962.1.
AC091814 Genomic DNA. No translation available.
BC029554 mRNA. Translation: AAH29554.1.

IPI

IPI00009457.
IPI00169302.

RefSeq

NP_001092901.1.
NP_057593.3.

UniGene

Hs.409794

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2C6U	X-ray	1.60	A	100-221	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9P126. 1 interaction.

Proteomic databases

PRIDE

Q9P126.

Genome annotation databases

Ensembl

ENSG00000165682. Homo sapiens. [Contig view]

GeneID

51266.

KEGG

hsa:51266.

NMPDR

fig|9606.3.peg.7146.

Organism-specific databases

GeneCards

GC12M010037.

HGNC

HGNC:24356. CLEC1B.

MIM

606783. gene.

PharmGKB

PA142672098.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

Q9P126.

OMA

Q9P126. IMSVTQQ.

Gene expression databases

ArrayExpress

Q9P126.

Bgee

Q9P126.

CleanEx

HS_CLEC1B.

Family and domain databases

InterPro

IPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
[Graphical view]

Gene3D

G3DSA:3.10.100.10. C-type_lectin-like. 1 hit.

Pfam

PF00059. Lectin_C. 1 hit.
[Graphical view]

SMART

SM00034. CLECT. 1 hit.
[Graphical view]

PROSITE

PS00615. C_TYPE_LECTIN_1. False negative.
PS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

54453.

SOURCE

Search...

Entry information

Entry name

CLC1B_HUMAN

Accession

Primary (citable) accession number: Q9P126
Secondary accession number(s): Q6UWX7, Q8NHR6

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 6, 2007
Last sequence update:	March 6, 2007
Last modified:	June 16, 2009
This is version 49 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)