Q9BXN2 (CLC7A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
C-type lectin domain family 7 member A

Alternative name(s):
Beta-glucan receptor
C-type lectin superfamily member 12
Dendritic cell-associated C-type lectin 1
Short name=DC-associated C-type lectin 1
Short name=Dectin-1

Gene names

Name:	CLEC7A
Synonyms:	BGR, CLECSF12, DECTIN1
ORF Names:	UNQ539/PRO1082

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	247 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Lectin that functions as pattern receptor specific for beta-1,3-linked and beta-1,6-linked glucans, such as cell wall constituents from pathogenic bacteria and fungi. Necessary for the TLR2-mediated inflammatory response and for TLR2-mediated activation of NF-kappa-B. Enhances cytokine production in macrophages and dendritic cells. Mediates production of reactive oxygen species in the cell. Mediates phagocytosis of C.albicans conidia. Binds T-cells in a way that does not involve their surface glycans and plays a role in T-cell activation. Stimulates T-cell proliferation By similarity. Ref.4 Ref.5 Ref.12
Subunit structure	Homodimer By similarity. Interacts with SYK; participates in leukocyte activation in presence of fungal pathogens By similarity. Isoform 5 interacts with RANBP9. Ref.11
Subcellular location	Cell membrane; Single-pass type II membrane protein Ref.1 Ref.11 Ref.12. Isoform 5: Cytoplasm Ref.1 Ref.11 Ref.12. Isoform 6: Cytoplasm Probable Ref.1 Ref.11 Ref.12. Isoform 7: Cytoplasm Probable Ref.1 Ref.11 Ref.12.
Tissue specificity	Highly expressed in peripheral blood leukocytes and dendritic cells. Detected in spleen, bone marrow, lung, muscle, stomach and placenta. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5
Induction	Up-regulated during differentiation from monocytes into dendritic cells. Ref.5
Post-translational modification	Phosphorylated on tyrosine residues in response to glucan binding By similarity.
Polymorphism	A stop polymorphism at position 238 may be associated with invasive aspergillosis following hematopoietic stem cell transplantation. The risk is highest when the polymorphism is present in both donors and recipients [MIM:614079].
Involvement in disease	Familial candidiasis 4 (CANDF4) [MIM:613108]: A primary immunodeficiency disorder with altered immune responses and impaired clearance of fungal infections, selective against Candida. It is characterized by persistent and/or recurrent infections of the skin, nails and mucous membranes caused by organisms of the genus Candida, mainly Candida albicans. Note: The disease may be caused by mutations affecting the gene represented in this entry. Ref.13
Sequence similarities	Contains 1 C-type lectin domain.

Ontologies

Keywords
Biological process	Immunity Inflammatory response Innate immunity
Cellular component	Cell membrane Cytoplasm Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Lectin Metal-binding
Molecular function	Receptor
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	T cell activation Traceable author statement Ref.4. Source: UniProtKB carbohydrate mediated signaling Traceable author statement Ref.4. Source: UniProtKB defense response to protozoan Non-traceable author statement Ref.4. Source: UniProtKB inflammatory response Inferred from electronic annotation. Source: UniProtKB-KW innate immune response Inferred from electronic annotation. Source: UniProtKB-KW phagocytosis, recognition Inferred from direct assay Ref.4. Source: UniProtKB
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Traceable author statement Ref.4. Source: UniProtKB plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	MHC protein binding Non-traceable author statement Ref.4. Source: UniProtKB carbohydrate binding Inferred from direct assay Ref.4. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW pattern recognition receptor activity Inferred from direct assay Ref.4. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 9 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9BXN2-1)

Also known as: A;

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: Q9BXN2-2)

Also known as: Beta; B;

The sequence of this isoform differs from the canonical sequence as follows:
     68-113: Missing.

Note: Predominant isoform.

Isoform 3 (identifier: Q9BXN2-3)

Also known as: C;

The sequence of this isoform differs from the canonical sequence as follows:
     165-189: GFIVKQVSSQPDNSFWIGLSRPQTE → ISDQNHSYPRKPISKLCMDSRVSHL
     190-247: Missing.

Isoform 4 (identifier: Q9BXN2-4)

Also known as: G;

The sequence of this isoform differs from the canonical sequence as follows:
     165-196: GFIVKQVSSQPDNSFWIGLSRPQTEVPWLWED → SLTLLPKLECSEAATSQAQVILPPQLPE
     197-247: Missing.

Isoform 5 (identifier: Q9BXN2-5)

Also known as: E;

The sequence of this isoform differs from the canonical sequence as follows:
     36-114: Missing.

Isoform 6 (identifier: Q9BXN2-6)

The sequence of this isoform differs from the canonical sequence as follows:
     68-113: Missing.
     165-178: GFIVKQVSSQPDNS → VSVDFCYDYLWCVS
     179-247: Missing.

Isoform 7 (identifier: Q9BXN2-7)

Also known as: D;

The sequence of this isoform differs from the canonical sequence as follows:
     68-113: Missing.
     165-189: GFIVKQVSSQPDNSFWIGLSRPQTE → ISDQNHSYPRKPISKLCMDSRVSHL
     190-247: Missing.

Isoform 8 (identifier: Q9BXN2-8)

Also known as: F;

The sequence of this isoform differs from the canonical sequence as follows:
     36-45: SCAASPPWRL → IYSKTSVFPT
     46-247: Missing.

Isoform 9 (identifier: Q9BXN2-9)

The sequence of this isoform differs from the canonical sequence as follows:
     69-77: IWRSNSGSN → GFKAVEFKG
     78-247: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 247	247	C-type lectin domain family 7 member A		PRO_0000269491
Regions
	Topological domain	1 – 44	44	Cytoplasmic Potential
	Transmembrane	45 – 65	21	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	66 – 247	182	Extracellular Potential
	Domain	127 – 242	116	C-type lectin
	Motif	15 – 18	4	ITAM-like
Sites
	Metal binding	157	1	Divalent metal cation By similarity
	Metal binding	159	1	Divalent metal cation By similarity
	Metal binding	163	1	Divalent metal cation By similarity
	Metal binding	242	1	Divalent metal cation By similarity
Amino acid modifications
	Glycosylation	91	1	N-linked (GlcNAc...) Potential
	Disulfide bond	120 ↔ 131		By similarity
	Disulfide bond	148 ↔ 241		By similarity
	Disulfide bond	220 ↔ 233		By similarity
Natural variations
	Alternative sequence	36 – 114	79	Missing in isoform 5.		VSP_022048
	Alternative sequence	36 – 45	10	SCAASPPWRL → IYSKTSVFPT in isoform 8.		VSP_022049
	Alternative sequence	46 – 247	202	Missing in isoform 8.		VSP_022050
	Alternative sequence	68 – 113	46	Missing in isoform 2, isoform 6 and isoform 7.		VSP_022051
	Alternative sequence	69 – 77	9	IWRSNSGSN → GFKAVEFKG in isoform 9.		VSP_043298
	Alternative sequence	78 – 247	170	Missing in isoform 9.		VSP_043299
	Alternative sequence	165 – 196	32	GFIVK…WLWED → SLTLLPKLECSEAATSQAQV ILPPQLPE in isoform 4.		VSP_022052
	Alternative sequence	165 – 189	25	GFIVK…RPQTE → ISDQNHSYPRKPISKLCMDS RVSHL in isoform 3 and isoform 7.		VSP_022053
	Alternative sequence	165 – 178	14	GFIVK…QPDNS → VSVDFCYDYLWCVS in isoform 6.		VSP_022054
	Alternative sequence	179 – 247	69	Missing in isoform 6.		VSP_022055
	Alternative sequence	190 – 247	58	Missing in isoform 3 and isoform 7.		VSP_022056
	Alternative sequence	197 – 247	51	Missing in isoform 4.		VSP_022057
	Natural variant	223	1	I → S. Corresponds to variant rs16910527 [ dbSNP | Ensembl ].		VAR_050111
Experimental info
	Sequence conflict	31	1	V → I in AAL11714. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (A) [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 98393E36976111B9	FASTA	247	27,627
	10 20 30 40 50 60 MEYHPDLENL DEDGYTQLHF DSQSNTRIAV VSEKGSCAAS PPWRLIAVIL GILCLVILVI 70 80 90 100 110 120 AVVLGTMAIW RSNSGSNTLE NGYFLSRNKE NHSQPTQSSL EDSVTPTKAV KTTGVLSSPC 130 140 150 160 170 180 PPNWIIYEKS CYLFSMSLNS WDGSKRQCWQ LGSNLLKIDS SNELGFIVKQ VSSQPDNSFW 190 200 210 220 230 240 IGLSRPQTEV PWLWEDGSTF SSNLFQIRTT ATQENPSPNC VWIHVSVIYD QLCSVPSYSI CEKKFSM
	Isoform 2 (Beta) (B) [UniParc]. Checksum: C6ADEE762B2CE968	FASTA	201	22,563
	10 20 30 40 50 60 MEYHPDLENL DEDGYTQLHF DSQSNTRIAV VSEKGSCAAS PPWRLIAVIL GILCLVILVI 70 80 90 100 110 120 AVVLGTMGVL SSPCPPNWII YEKSCYLFSM SLNSWDGSKR QCWQLGSNLL KIDSSNELGF 130 140 150 160 170 180 IVKQVSSQPD NSFWIGLSRP QTEVPWLWED GSTFSSNLFQ IRTTATQENP SPNCVWIHVS 190 200 VIYDQLCSVP SYSICEKKFS M
	Isoform 3 (C) [UniParc]. Checksum: F7DF9F76EA4B6B59	FASTA	189	21,065
	10 20 30 40 50 60 MEYHPDLENL DEDGYTQLHF DSQSNTRIAV VSEKGSCAAS PPWRLIAVIL GILCLVILVI 70 80 90 100 110 120 AVVLGTMAIW RSNSGSNTLE NGYFLSRNKE NHSQPTQSSL EDSVTPTKAV KTTGVLSSPC 130 140 150 160 170 180 PPNWIIYEKS CYLFSMSLNS WDGSKRQCWQ LGSNLLKIDS SNELISDQNH SYPRKPISKL CMDSRVSHL
	Isoform 4 (G) [UniParc]. Checksum: 6F3350B1DFBEC921	FASTA	192	21,130
	10 20 30 40 50 60 MEYHPDLENL DEDGYTQLHF DSQSNTRIAV VSEKGSCAAS PPWRLIAVIL GILCLVILVI 70 80 90 100 110 120 AVVLGTMAIW RSNSGSNTLE NGYFLSRNKE NHSQPTQSSL EDSVTPTKAV KTTGVLSSPC 130 140 150 160 170 180 PPNWIIYEKS CYLFSMSLNS WDGSKRQCWQ LGSNLLKIDS SNELSLTLLP KLECSEAATS 190 QAQVILPPQL PE
	Isoform 5 (E) [UniParc]. Checksum: AFD3A88F89BBFFC6	FASTA	168	19,218
	10 20 30 40 50 60 MEYHPDLENL DEDGYTQLHF DSQSNTRIAV VSEKGVLSSP CPPNWIIYEK SCYLFSMSLN 70 80 90 100 110 120 SWDGSKRQCW QLGSNLLKID SSNELGFIVK QVSSQPDNSF WIGLSRPQTE VPWLWEDGST 130 140 150 160 FSSNLFQIRT TATQENPSPN CVWIHVSVIY DQLCSVPSYS ICEKKFSM
	Isoform 6 [UniParc]. Checksum: 997EEE918BC63102	FASTA	132	14,787
	10 20 30 40 50 60 MEYHPDLENL DEDGYTQLHF DSQSNTRIAV VSEKGSCAAS PPWRLIAVIL GILCLVILVI 70 80 90 100 110 120 AVVLGTMGVL SSPCPPNWII YEKSCYLFSM SLNSWDGSKR QCWQLGSNLL KIDSSNELVS 130 VDFCYDYLWC VS
	Isoform 7 (D) [UniParc]. Checksum: 3BD7AE116DDB4305	FASTA	143	16,000
	10 20 30 40 50 60 MEYHPDLENL DEDGYTQLHF DSQSNTRIAV VSEKGSCAAS PPWRLIAVIL GILCLVILVI 70 80 90 100 110 120 AVVLGTMGVL SSPCPPNWII YEKSCYLFSM SLNSWDGSKR QCWQLGSNLL KIDSSNELIS 130 140 DQNHSYPRKP ISKLCMDSRV SHL
	Isoform 8 (F) [UniParc]. Checksum: ED83111E8DE75169	FASTA	45	5,164
	10 20 30 40 MEYHPDLENL DEDGYTQLHF DSQSNTRIAV VSEKGIYSKT SVFPT
	Isoform 9 [UniParc]. Checksum: 488D685E42698CCB	FASTA	77	8,363
	10 20 30 40 50 60 MEYHPDLENL DEDGYTQLHF DSQSNTRIAV VSEKGSCAAS PPWRLIAVIL GILCLVILVI 70 AVVLGTMAGF KAVEFKG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel cluster of lectin-like receptor genes expressed in monocytic, dendritic and endothelial cells maps close to the NK receptor genes in the human NK gene complex." Sobanov Y., Bernreiter A., Derdak S., Mechtcheriakova D., Schweighofer B., Duechler M., Kalthoff F., Hofer E. Eur. J. Immunol. 31:3493-3503(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[2]	"Identification of a human homologue of the dendritic cell-associated C-type lectin-1, dectin-1." Yokota K., Takashima A., Bergstresser P.R., Ariizumi K. Gene 272:51-60(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY. Tissue: Peripheral blood leukocyte.
[3]	"Cloning of human DECTIN-1, a novel C-type lectin-like receptor gene expressed on dendritic cells." Hermanz-Falcon P., Arce I., Roda-Navarro P., Fernandez-Ruiz E. Immunogenetics 53:288-295(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 7), TISSUE SPECIFICITY. Tissue: Peripheral blood leukocyte.
[4]	"Characterization of the human beta-glucan receptor and its alternatively spliced isoforms." Willment J.A., Gordon S., Brown G.D. J. Biol. Chem. 276:43818-43823(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 7 AND 8), FUNCTION, TISSUE SPECIFICITY. Tissue: Peripheral blood leukocyte.
[5]	"Molecular and functional characterization of human Dectin-1." Gruenebach F., Weck M.M., Reichert J., Brossart P. Exp. Hematol. 30:1309-1315(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INDUCTION, TISSUE SPECIFICITY. Tissue: Dendritic cell.
[6]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[7]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 5 AND 7). Tissue: Umbilical cord blood.
[8]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]	"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 6 AND 9). Tissue: Colon, Lung and Urinary bladder.
[11]	"Human Dectin-1 isoform E is a cytoplasmic protein and interacts with RanBPM." Xie J., Sun M., Guo L., Liu W., Jiang J., Chen X., Zhou L., Gu J. Biochem. Biophys. Res. Commun. 347:1067-1073(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RANBP9, SUBCELLULAR LOCATION.
[12]	"Dectin-1 promotes fungicidal activity of human neutrophils." Kennedy A.D., Willment J.A., Dorward D.W., Williams D.L., Brown G.D., DeLeo F.R. Eur. J. Immunol. 37:467-478(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[13]	"Human dectin-1 deficiency and mucocutaneous fungal infections." Ferwerda B., Ferwerda G., Plantinga T.S., Willment J.A., van Spriel A.B., Venselaar H., Elbers C.C., Johnson M.D., Cambi A., Huysamen C., Jacobs L., Jansen T., Verheijen K., Masthoff L., Morre S.A., Vriend G., Williams D.L., Perfect J.R. , Joosten L.A., Wijmenga C., van der Meer J.W., Adema G.J., Kullberg B.J., Brown G.D., Netea M.G. N. Engl. J. Med. 361:1760-1767(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN CANDF4.
[14]	"Dectin-1 Y238X polymorphism associates with susceptibility to invasive aspergillosis in hematopoietic transplantation through impairment of both recipient- and donor-dependent mechanisms of antifungal immunity." Cunha C., Di Ianni M., Bozza S., Giovannini G., Zagarella S., Zelante T., D'Angelo C., Pierini A., Pitzurra L., Falzetti F., Carotti A., Perruccio K., Latge J.P., Rodrigues F., Velardi A., Aversa F., Romani L., Carvalho A. Blood 116:5394-5402(2010) [PubMed] [Europe PMC] [Abstract] Cited for: POLYMORPHISM.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY026769 mRNA. Translation: AAK20114.2. AY026770 mRNA. Translation: AAK20115.1. AY026771 mRNA. Translation: AAK20116.1. AF313468 mRNA. Translation: AAK37473.1. AF313469 mRNA. Translation: AAK37474.1. AF400595 mRNA. Translation: AAL11711.1. AF400596 mRNA. Translation: AAL11712.1. AF400597 mRNA. Translation: AAL11713.1. AF400598 mRNA. Translation: AAL11714.1. AF400599 mRNA. Translation: AAL11715.1. AF400600 mRNA. Translation: AAL11716.1. AF400601 mRNA. Translation: AAL11717.1. AJ312372 mRNA. Translation: CAC43846.1. AJ312373 mRNA. Translation: CAC43847.1. AY009090 mRNA. Translation: AAG33923.2. AY359002 mRNA. Translation: AAQ89361.1. AK297028 mRNA. Translation: BAH12480.1. AK298679 mRNA. Translation: BAH12845.1. AK298724 mRNA. Translation: BAH12855.1. AK313247 mRNA. Translation: BAG36058.1. AC024224 Genomic DNA. No translation available. CH471094 Genomic DNA. Translation: EAW96144.1. CH471094 Genomic DNA. Translation: EAW96145.1. CH471094 Genomic DNA. Translation: EAW96146.1. CH471094 Genomic DNA. Translation: EAW96150.1. BC013385 mRNA. Translation: AAH13385.1. BC071746 mRNA. Translation: AAH71746.1. BC093829 mRNA. Translation: AAH93829.1. BC093831 mRNA. Translation: AAH93831.1.
IPI	IPI00021735. IPI00044331. IPI00044332. IPI00060623. IPI00155858. IPI00170475. IPI00186897. IPI00411381. IPI00815987.
RefSeq	NP_072092.2. NM_022570.4. NP_922938.1. NM_197947.2. NP_922939.1. NM_197948.2. NP_922940.1. NM_197949.2. NP_922941.1. NM_197950.2. NP_922945.1. NM_197954.2.
UniGene	Hs.143929.
3D structure databases
HSSP	HSSP built from PDB template 1KCG based on UniProtKB P26718.
ProteinModelPortal	Q9BXN2.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9BXN2. 3 interactions.
PTM databases
PhosphoSite	Q9BXN2.
Polymorphism databases
DMDM	74752433.
Proteomic databases
PaxDb	Q9BXN2.
PRIDE	Q9BXN2.
Protocols and materials databases
DNASU	64581.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000298523; ENSP00000298523; ENSG00000172243. ENST00000304084; ENSP00000302569; ENSG00000172243. ENST00000310002; ENSP00000312089; ENSG00000172243. ENST00000349926; ENSP00000344723; ENSG00000172243. ENST00000353231; ENSP00000266456; ENSG00000172243. ENST00000396484; ENSP00000379743; ENSG00000172243. ENST00000529761; ENSP00000432876; ENSG00000172243. ENST00000531192; ENSP00000434392; ENSG00000172243. ENST00000533022; ENSP00000431461; ENSG00000172243.
GeneID	64581.
KEGG	hsa:64581.
UCSC	uc001qxf.2. human. uc001qxg.2. human. uc001qxh.2. human. uc001qxi.2. human. uc001qxj.2. human. uc021quz.1. human.
Organism-specific databases
CTD	64581.
GeneCards	GC12M010269.
H-InvDB	HIX0010422.
HGNC	HGNC:14558. CLEC7A.
HPA	HPA043244.
MIM	606264. gene. 613108. phenotype. 614079. phenotype.
neXtProt	NX_Q9BXN2.
Orphanet	1334. Chronic mucocutaneous candidiasis.
PharmGKB	PA26581.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG327853.
HOGENOM	HOG000151249.
HOVERGEN	HBG105854.
InParanoid	Q9BXN2.
KO	K10074.
OMA	QPDNSFW.
Gene expression databases
ArrayExpress	Q9BXN2.
Bgee	Q9BXN2.
Genevestigator	Q9BXN2.
Family and domain databases
Gene3D	3.10.100.10. 1 hit.
InterPro	IPR001304. C-type_lectin. IPR016186. C-type_lectin-like. IPR016187. C-type_lectin_fold. [Graphical view]
Pfam	PF00059. Lectin_C. 1 hit. [Graphical view]
SMART	SM00034. CLECT. 1 hit. [Graphical view]
SUPFAM	SSF56436. C-type_lectin_fold. 1 hit.
PROSITE	PS00615. C_TYPE_LECTIN_1. False negative. PS50041. C_TYPE_LECTIN_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	64581.
NextBio	66517.
SOURCE	Search...

Entry information

Entry name

CLC7A_HUMAN

Accession

Primary (citable) accession number: Q9BXN2
Secondary accession number(s): B2R861 , B7Z494, B7Z5A9, B7Z5B9, Q6IPS7, Q96D32, Q96DR9, Q96LD3, Q96PA5, Q96PA6, Q96PA7, Q96PA8, Q9H1K3

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	June 1, 2001
Last modified:	May 1, 2013
This is version 98 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.