CLC7A_HUMAN
ID CLC7A_HUMAN Reviewed; 247 AA.
AC Q9BXN2; B2R861; B7Z494; B7Z5A9; B7Z5B9; Q6IPS7; Q96D32; Q96DR9; Q96LD3;
AC Q96PA4; Q96PA5; Q96PA6; Q96PA7; Q96PA8; Q9H1K3;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=C-type lectin domain family 7 member A;
DE AltName: Full=Beta-glucan receptor {ECO:0000303|PubMed:11567029};
DE AltName: Full=C-type lectin superfamily member 12;
DE AltName: Full=Dendritic cell-associated C-type lectin 1 {ECO:0000303|PubMed:11745369};
DE Short=DC-associated C-type lectin 1 {ECO:0000303|PubMed:11745369};
DE Short=Dectin-1 {ECO:0000303|PubMed:11745369};
DE AltName: CD_antigen=CD369;
GN Name=CLEC7A {ECO:0000312|HGNC:HGNC:14558};
GN Synonyms=BGR, CLECSF12, DECTIN1 {ECO:0000303|PubMed:11745369};
GN ORFNames=UNQ539/PRO1082;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=11745369;
RX DOI=10.1002/1521-4141(200112)31:12<3493::aid-immu3493>3.0.co;2-9;
RA Sobanov Y., Bernreiter A., Derdak S., Mechtcheriakova D., Schweighofer B.,
RA Duechler M., Kalthoff F., Hofer E.;
RT "A novel cluster of lectin-like receptor genes expressed in monocytic,
RT dendritic and endothelial cells maps close to the NK receptor genes in the
RT human NK gene complex.";
RL Eur. J. Immunol. 31:3493-3503(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RC TISSUE=Peripheral blood leukocyte;
RX PubMed=11470510; DOI=10.1016/s0378-1119(01)00528-5;
RA Yokota K., Takashima A., Bergstresser P.R., Ariizumi K.;
RT "Identification of a human homologue of the dendritic cell-associated C-
RT type lectin-1, dectin-1.";
RL Gene 272:51-60(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 7), AND TISSUE SPECIFICITY.
RC TISSUE=Peripheral blood leukocyte;
RX PubMed=11491532; DOI=10.1007/s002510100326;
RA Hermanz-Falcon P., Arce I., Roda-Navarro P., Fernandez-Ruiz E.;
RT "Cloning of human DECTIN-1, a novel C-type lectin-like receptor gene
RT expressed on dendritic cells.";
RL Immunogenetics 53:288-295(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 7; 8 AND 10), FUNCTION,
RP AND TISSUE SPECIFICITY.
RC TISSUE=Peripheral blood leukocyte;
RX PubMed=11567029; DOI=10.1074/jbc.m107715200;
RA Willment J.A., Gordon S., Brown G.D.;
RT "Characterization of the human beta-glucan receptor and its alternatively
RT spliced isoforms.";
RL J. Biol. Chem. 276:43818-43823(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INDUCTION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Dendritic cell;
RX PubMed=12423684; DOI=10.1016/s0301-472x(02)00928-1;
RA Gruenebach F., Weck M.M., Reichert J., Brossart P.;
RT "Molecular and functional characterization of human Dectin-1.";
RL Exp. Hematol. 30:1309-1315(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 5 AND 7).
RC TISSUE=Umbilical cord blood;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 6 AND 9).
RC TISSUE=Colon, Lung, and Urinary bladder;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [11]
RP INTERACTION WITH RANBP9, AND SUBCELLULAR LOCATION.
RX PubMed=16870151; DOI=10.1016/j.bbrc.2006.07.021;
RA Xie J., Sun M., Guo L., Liu W., Jiang J., Chen X., Zhou L., Gu J.;
RT "Human Dectin-1 isoform E is a cytoplasmic protein and interacts with
RT RanBPM.";
RL Biochem. Biophys. Res. Commun. 347:1067-1073(2006).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17230442; DOI=10.1002/eji.200636653;
RA Kennedy A.D., Willment J.A., Dorward D.W., Williams D.L., Brown G.D.,
RA DeLeo F.R.;
RT "Dectin-1 promotes fungicidal activity of human neutrophils.";
RL Eur. J. Immunol. 37:467-478(2007).
RN [13]
RP INVOLVEMENT IN CANDF4.
RX PubMed=19864674; DOI=10.1056/nejmoa0901053;
RA Ferwerda B., Ferwerda G., Plantinga T.S., Willment J.A., van Spriel A.B.,
RA Venselaar H., Elbers C.C., Johnson M.D., Cambi A., Huysamen C., Jacobs L.,
RA Jansen T., Verheijen K., Masthoff L., Morre S.A., Vriend G., Williams D.L.,
RA Perfect J.R., Joosten L.A., Wijmenga C., van der Meer J.W., Adema G.J.,
RA Kullberg B.J., Brown G.D., Netea M.G.;
RT "Human dectin-1 deficiency and mucocutaneous fungal infections.";
RL N. Engl. J. Med. 361:1760-1767(2009).
RN [14]
RP POLYMORPHISM, AND VARIANT 238-TYR--MET-247 DEL.
RX PubMed=20807886; DOI=10.1182/blood-2010-04-279307;
RA Cunha C., Di Ianni M., Bozza S., Giovannini G., Zagarella S., Zelante T.,
RA D'Angelo C., Pierini A., Pitzurra L., Falzetti F., Carotti A.,
RA Perruccio K., Latge J.P., Rodrigues F., Velardi A., Aversa F., Romani L.,
RA Carvalho A.;
RT "Dectin-1 Y238X polymorphism associates with susceptibility to invasive
RT aspergillosis in hematopoietic transplantation through impairment of both
RT recipient- and donor-dependent mechanisms of antifungal immunity.";
RL Blood 116:5394-5402(2010).
CC -!- FUNCTION: Lectin that functions as pattern recognizing receptor (PRR)
CC specific for beta-1,3-linked and beta-1,6-linked glucans, which
CC constitute cell wall constituents from pathogenic bacteria and fungi
CC (PubMed:11567029, PubMed:12423684). Necessary for the TLR2-mediated
CC inflammatory response and activation of NF-kappa-B: upon beta-glucan
CC binding, recruits SYK via its ITAM motif and promotes a signaling
CC cascade that activates some CARD domain-BCL10-MALT1 (CBM) signalosomes,
CC leading to the activation of NF-kappa-B and MAP kinase p38 (MAPK11,
CC MAPK12, MAPK13 and/or MAPK14) pathways which stimulate expression of
CC genes encoding pro-inflammatory cytokines and chemokines (By
CC similarity). Enhances cytokine production in macrophages and dendritic
CC cells (By similarity). Mediates production of reactive oxygen species
CC in the cell (By similarity). Mediates phagocytosis of C.albicans
CC conidia (PubMed:17230442). Binds T-cells in a way that does not involve
CC their surface glycans and plays a role in T-cell activation. Stimulates
CC T-cell proliferation. Induces phosphorylation of SCIMP after binding
CC beta-glucans (By similarity). {ECO:0000250|UniProtKB:Q6QLQ4,
CC ECO:0000269|PubMed:11567029, ECO:0000269|PubMed:12423684,
CC ECO:0000269|PubMed:17230442}.
CC -!- SUBUNIT: Homodimer. Interacts with SYK; participates in leukocyte
CC activation in presence of fungal pathogens.
CC {ECO:0000250|UniProtKB:Q6QLQ4}.
CC -!- SUBUNIT: [Isoform 5]: Interacts with RANBP9.
CC {ECO:0000269|PubMed:16870151}.
CC -!- INTERACTION:
CC Q9BXN2; Q9BZ11-2: ADAM33; NbExp=3; IntAct=EBI-3939278, EBI-10303054;
CC Q9BXN2; Q12983: BNIP3; NbExp=3; IntAct=EBI-3939278, EBI-749464;
CC Q9BXN2; O60238: BNIP3L; NbExp=6; IntAct=EBI-3939278, EBI-849893;
CC Q9BXN2; Q9BU27: FAM3A; NbExp=3; IntAct=EBI-3939278, EBI-10298603;
CC Q9BXN2; Q01638: IL1RL1; NbExp=3; IntAct=EBI-3939278, EBI-993762;
CC Q9BXN2; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-3939278, EBI-10266796;
CC Q9BXN2; Q86UP2: KTN1; NbExp=3; IntAct=EBI-3939278, EBI-359761;
CC Q9BXN2; Q9NZG7: NINJ2; NbExp=3; IntAct=EBI-3939278, EBI-10317425;
CC Q9BXN2; Q16625: OCLN; NbExp=3; IntAct=EBI-3939278, EBI-2903088;
CC Q9BXN2; P53801: PTTG1IP; NbExp=3; IntAct=EBI-3939278, EBI-3906138;
CC Q9BXN2; Q9BZL3: SMIM3; NbExp=3; IntAct=EBI-3939278, EBI-741850;
CC Q9BXN2; Q8N205: SYNE4; NbExp=7; IntAct=EBI-3939278, EBI-7131783;
CC Q9BXN2; Q9BSE2: TMEM79; NbExp=4; IntAct=EBI-3939278, EBI-8649725;
CC Q9BXN2; Q9NRS4-3: TMPRSS4; NbExp=3; IntAct=EBI-3939278, EBI-10312990;
CC Q9BXN2; Q9BRL5; NbExp=3; IntAct=EBI-3939278, EBI-10296986;
CC Q9BXN2-6; Q08AM2: ADAM33; NbExp=3; IntAct=EBI-11989440, EBI-10225815;
CC Q9BXN2-6; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-11989440, EBI-11343438;
CC Q9BXN2-6; P07307-3: ASGR2; NbExp=3; IntAct=EBI-11989440, EBI-12808270;
CC Q9BXN2-6; Q12983: BNIP3; NbExp=3; IntAct=EBI-11989440, EBI-749464;
CC Q9BXN2-6; O60238: BNIP3L; NbExp=3; IntAct=EBI-11989440, EBI-849893;
CC Q9BXN2-6; P19397: CD53; NbExp=3; IntAct=EBI-11989440, EBI-6657396;
CC Q9BXN2-6; P04233-2: CD74; NbExp=3; IntAct=EBI-11989440, EBI-12222807;
CC Q9BXN2-6; Q9BXN2-6: CLEC7A; NbExp=3; IntAct=EBI-11989440, EBI-11989440;
CC Q9BXN2-6; Q4LDR2: CTXN3; NbExp=3; IntAct=EBI-11989440, EBI-12019274;
CC Q9BXN2-6; Q07325: CXCL9; NbExp=3; IntAct=EBI-11989440, EBI-3911467;
CC Q9BXN2-6; P12314: FCGR1A; NbExp=3; IntAct=EBI-11989440, EBI-2869867;
CC Q9BXN2-6; Q8TBE3: FNDC9; NbExp=3; IntAct=EBI-11989440, EBI-12142257;
CC Q9BXN2-6; P08034: GJB1; NbExp=3; IntAct=EBI-11989440, EBI-17565645;
CC Q9BXN2-6; P38484: IFNGR2; NbExp=3; IntAct=EBI-11989440, EBI-3905457;
CC Q9BXN2-6; P26715: KLRC1; NbExp=3; IntAct=EBI-11989440, EBI-9018187;
CC Q9BXN2-6; Q9H2K0: MTIF3; NbExp=3; IntAct=EBI-11989440, EBI-3923617;
CC Q9BXN2-6; O14524-2: NEMP1; NbExp=3; IntAct=EBI-11989440, EBI-10969203;
CC Q9BXN2-6; Q8N912: NRAC; NbExp=3; IntAct=EBI-11989440, EBI-12051377;
CC Q9BXN2-6; Q9Y328: NSG2; NbExp=3; IntAct=EBI-11989440, EBI-7101695;
CC Q9BXN2-6; Q6UX06: OLFM4; NbExp=3; IntAct=EBI-11989440, EBI-2804156;
CC Q9BXN2-6; P35372-10: OPRM1; NbExp=3; IntAct=EBI-11989440, EBI-12807478;
CC Q9BXN2-6; P53801: PTTG1IP; NbExp=3; IntAct=EBI-11989440, EBI-3906138;
CC Q9BXN2-6; Q9NR31: SAR1A; NbExp=3; IntAct=EBI-11989440, EBI-3920694;
CC Q9BXN2-6; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-11989440, EBI-8652744;
CC Q9BXN2-6; Q16585: SGCB; NbExp=3; IntAct=EBI-11989440, EBI-5663627;
CC Q9BXN2-6; Q9BZL3: SMIM3; NbExp=4; IntAct=EBI-11989440, EBI-741850;
CC Q9BXN2-6; O43278-2: SPINT1; NbExp=3; IntAct=EBI-11989440, EBI-12078338;
CC Q9BXN2-6; Q96L08: SUSD3; NbExp=3; IntAct=EBI-11989440, EBI-18194029;
CC Q9BXN2-6; Q8N6K0: TEX29; NbExp=3; IntAct=EBI-11989440, EBI-19027521;
CC Q9BXN2-6; Q96MV1: TLCD4; NbExp=3; IntAct=EBI-11989440, EBI-12947623;
CC Q9BXN2-6; Q9BSE2: TMEM79; NbExp=3; IntAct=EBI-11989440, EBI-8649725;
CC Q9BXN2-6; O15393-2: TMPRSS2; NbExp=3; IntAct=EBI-11989440, EBI-12345267;
CC Q9BXN2-6; O00526: UPK2; NbExp=3; IntAct=EBI-11989440, EBI-10179682;
CC Q9BXN2-6; Q9H7M9: VSIR; NbExp=3; IntAct=EBI-11989440, EBI-744988;
CC Q9BXN2-6; O95159: ZFPL1; NbExp=3; IntAct=EBI-11989440, EBI-718439;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11745369,
CC ECO:0000269|PubMed:16870151, ECO:0000269|PubMed:17230442}; Single-pass
CC type II membrane protein {ECO:0000269|PubMed:11745369,
CC ECO:0000269|PubMed:16870151, ECO:0000269|PubMed:17230442}.
CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 6]: Cytoplasm {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 7]: Cytoplasm {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=10;
CC Name=1; Synonyms=A;
CC IsoId=Q9BXN2-1; Sequence=Displayed;
CC Name=2; Synonyms=Beta, B;
CC IsoId=Q9BXN2-2; Sequence=VSP_022051;
CC Name=3; Synonyms=C;
CC IsoId=Q9BXN2-3; Sequence=VSP_022053, VSP_022056;
CC Name=4; Synonyms=G;
CC IsoId=Q9BXN2-4; Sequence=VSP_022052, VSP_022057;
CC Name=5; Synonyms=E;
CC IsoId=Q9BXN2-5; Sequence=VSP_022048;
CC Name=6;
CC IsoId=Q9BXN2-6; Sequence=VSP_022051, VSP_022054, VSP_022055;
CC Name=7; Synonyms=D;
CC IsoId=Q9BXN2-7; Sequence=VSP_022051, VSP_022053, VSP_022056;
CC Name=8; Synonyms=F;
CC IsoId=Q9BXN2-8; Sequence=VSP_022049, VSP_022050;
CC Name=9;
CC IsoId=Q9BXN2-9; Sequence=VSP_043298, VSP_043299;
CC Name=10;
CC IsoId=Q9BXN2-10; Sequence=VSP_047589, VSP_047590;
CC -!- TISSUE SPECIFICITY: Highly expressed in peripheral blood leukocytes and
CC dendritic cells. Detected in spleen, bone marrow, lung, muscle, stomach
CC and placenta. {ECO:0000269|PubMed:11470510,
CC ECO:0000269|PubMed:11491532, ECO:0000269|PubMed:11567029,
CC ECO:0000269|PubMed:11745369, ECO:0000269|PubMed:12423684}.
CC -!- INDUCTION: Up-regulated during differentiation from monocytes into
CC dendritic cells. {ECO:0000269|PubMed:12423684}.
CC -!- PTM: Phosphorylated on tyrosine residues in response to beta-glucan
CC binding. {ECO:0000250|UniProtKB:Q6QLQ4}.
CC -!- POLYMORPHISM: A stop polymorphism at position 238 may be associated
CC with invasive aspergillosis following hematopoietic stem cell
CC transplantation (PubMed:20807886). The risk is highest when the
CC polymorphism is present in both donors and recipients [MIM:614079]
CC (PubMed:20807886). {ECO:0000269|PubMed:20807886}.
CC -!- DISEASE: Candidiasis, familial, 4 (CANDF4) [MIM:613108]: A primary
CC immunodeficiency disorder with altered immune responses and impaired
CC clearance of fungal infections, selective against Candida. It is
CC characterized by persistent and/or recurrent infections of the skin,
CC nails and mucous membranes caused by organisms of the genus Candida,
CC mainly Candida albicans. {ECO:0000269|PubMed:19864674}. Note=The
CC disease may be caused by variants affecting the gene represented in
CC this entry.
CC -!- MISCELLANEOUS: [Isoform 2]: Predominant isoform. {ECO:0000305}.
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DR EMBL; AY026769; AAK20114.2; -; mRNA.
DR EMBL; AY026770; AAK20115.1; -; mRNA.
DR EMBL; AY026771; AAK20116.1; -; mRNA.
DR EMBL; AF313468; AAK37473.1; -; mRNA.
DR EMBL; AF313469; AAK37474.1; -; mRNA.
DR EMBL; AF400595; AAL11711.1; -; mRNA.
DR EMBL; AF400596; AAL11712.1; -; mRNA.
DR EMBL; AF400597; AAL11713.1; -; mRNA.
DR EMBL; AF400598; AAL11714.1; -; mRNA.
DR EMBL; AF400599; AAL11715.1; -; mRNA.
DR EMBL; AF400600; AAL11716.1; -; mRNA.
DR EMBL; AF400601; AAL11717.1; -; mRNA.
DR EMBL; AF400602; AAL11718.1; -; mRNA.
DR EMBL; AJ312372; CAC43846.1; -; mRNA.
DR EMBL; AJ312373; CAC43847.1; -; mRNA.
DR EMBL; AY009090; AAG33923.2; -; mRNA.
DR EMBL; AY359002; AAQ89361.1; -; mRNA.
DR EMBL; AK297028; BAH12480.1; -; mRNA.
DR EMBL; AK298679; BAH12845.1; -; mRNA.
DR EMBL; AK298724; BAH12855.1; -; mRNA.
DR EMBL; AK313247; BAG36058.1; -; mRNA.
DR EMBL; AC024224; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471094; EAW96144.1; -; Genomic_DNA.
DR EMBL; CH471094; EAW96145.1; -; Genomic_DNA.
DR EMBL; CH471094; EAW96146.1; -; Genomic_DNA.
DR EMBL; CH471094; EAW96150.1; -; Genomic_DNA.
DR EMBL; CH471094; EAW96154.1; -; Genomic_DNA.
DR EMBL; BC013385; AAH13385.1; -; mRNA.
DR EMBL; BC071746; AAH71746.1; -; mRNA.
DR EMBL; BC093829; AAH93829.1; -; mRNA.
DR EMBL; BC093831; AAH93831.1; -; mRNA.
DR CCDS; CCDS41753.1; -. [Q9BXN2-1]
DR CCDS; CCDS41754.1; -. [Q9BXN2-3]
DR CCDS; CCDS53744.1; -. [Q9BXN2-7]
DR CCDS; CCDS8613.1; -. [Q9BXN2-2]
DR CCDS; CCDS8614.1; -. [Q9BXN2-5]
DR CCDS; CCDS8617.1; -. [Q9BXN2-9]
DR RefSeq; NP_072092.2; NM_022570.4. [Q9BXN2-2]
DR RefSeq; NP_922938.1; NM_197947.2. [Q9BXN2-1]
DR RefSeq; NP_922939.1; NM_197948.2. [Q9BXN2-3]
DR RefSeq; NP_922940.1; NM_197949.2. [Q9BXN2-7]
DR RefSeq; NP_922941.1; NM_197950.2. [Q9BXN2-5]
DR RefSeq; NP_922945.1; NM_197954.2. [Q9BXN2-9]
DR RefSeq; XP_006719198.1; XM_006719135.3. [Q9BXN2-4]
DR AlphaFoldDB; Q9BXN2; -.
DR SMR; Q9BXN2; -.
DR BioGRID; 122206; 52.
DR DIP; DIP-61730N; -.
DR IntAct; Q9BXN2; 51.
DR MINT; Q9BXN2; -.
DR STRING; 9606.ENSP00000302569; -.
DR ChEMBL; CHEMBL2034810; -.
DR GlyGen; Q9BXN2; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BXN2; -.
DR PhosphoSitePlus; Q9BXN2; -.
DR BioMuta; CLEC7A; -.
DR DMDM; 74752433; -.
DR jPOST; Q9BXN2; -.
DR MassIVE; Q9BXN2; -.
DR PaxDb; Q9BXN2; -.
DR PeptideAtlas; Q9BXN2; -.
DR PRIDE; Q9BXN2; -.
DR ProteomicsDB; 79462; -. [Q9BXN2-1]
DR ProteomicsDB; 79463; -. [Q9BXN2-2]
DR ProteomicsDB; 79464; -. [Q9BXN2-3]
DR ProteomicsDB; 79465; -. [Q9BXN2-4]
DR ProteomicsDB; 79466; -. [Q9BXN2-5]
DR ProteomicsDB; 79467; -. [Q9BXN2-6]
DR ProteomicsDB; 79468; -. [Q9BXN2-7]
DR ABCD; Q9BXN2; 1 sequenced antibody.
DR Antibodypedia; 23238; 745 antibodies from 37 providers.
DR DNASU; 64581; -.
DR Ensembl; ENST00000298523.9; ENSP00000298523.5; ENSG00000172243.18. [Q9BXN2-7]
DR Ensembl; ENST00000304084.13; ENSP00000302569.8; ENSG00000172243.18. [Q9BXN2-1]
DR Ensembl; ENST00000310002.4; ENSP00000312089.4; ENSG00000172243.18. [Q9BXN2-9]
DR Ensembl; ENST00000349926.9; ENSP00000344723.5; ENSG00000172243.18. [Q9BXN2-8]
DR Ensembl; ENST00000353231.9; ENSP00000266456.6; ENSG00000172243.18. [Q9BXN2-2]
DR Ensembl; ENST00000396484.6; ENSP00000379743.2; ENSG00000172243.18. [Q9BXN2-5]
DR Ensembl; ENST00000465100.5; ENSP00000436923.1; ENSG00000172243.18. [Q9BXN2-10]
DR Ensembl; ENST00000529761.5; ENSP00000432876.1; ENSG00000172243.18. [Q9BXN2-1]
DR Ensembl; ENST00000531192.5; ENSP00000434392.1; ENSG00000172243.18. [Q9BXN2-4]
DR Ensembl; ENST00000533022.5; ENSP00000431461.1; ENSG00000172243.18. [Q9BXN2-3]
DR GeneID; 64581; -.
DR KEGG; hsa:64581; -.
DR MANE-Select; ENST00000304084.13; ENSP00000302569.8; NM_197947.3; NP_922938.1.
DR UCSC; uc001qxe.5; human. [Q9BXN2-1]
DR CTD; 64581; -.
DR DisGeNET; 64581; -.
DR GeneCards; CLEC7A; -.
DR HGNC; HGNC:14558; CLEC7A.
DR HPA; ENSG00000172243; Group enriched (bone marrow, lung, lymphoid tissue).
DR MalaCards; CLEC7A; -.
DR MIM; 606264; gene.
DR MIM; 613108; phenotype.
DR MIM; 614079; phenotype.
DR neXtProt; NX_Q9BXN2; -.
DR OpenTargets; ENSG00000172243; -.
DR Orphanet; 1334; Chronic mucocutaneous candidiasis.
DR PharmGKB; PA26581; -.
DR VEuPathDB; HostDB:ENSG00000172243; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000161161; -.
DR HOGENOM; CLU_049894_8_0_1; -.
DR InParanoid; Q9BXN2; -.
DR OMA; PNWIIHE; -.
DR PhylomeDB; Q9BXN2; -.
DR TreeFam; TF336674; -.
DR PathwayCommons; Q9BXN2; -.
DR Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
DR SignaLink; Q9BXN2; -.
DR BioGRID-ORCS; 64581; 12 hits in 1061 CRISPR screens.
DR GeneWiki; CLEC7A; -.
DR GenomeRNAi; 64581; -.
DR Pharos; Q9BXN2; Tbio.
DR PRO; PR:Q9BXN2; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9BXN2; protein.
DR Bgee; ENSG00000172243; Expressed in monocyte and 168 other tissues.
DR ExpressionAtlas; Q9BXN2; baseline and differential.
DR Genevisible; Q9BXN2; HS.
DR GO; GO:0009986; C:cell surface; IDA:ARUK-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:ARUK-UCL.
DR GO; GO:0016021; C:integral component of membrane; TAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0001872; F:(1->3)-beta-D-glucan binding; IDA:ARUK-UCL.
DR GO; GO:0030246; F:carbohydrate binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042287; F:MHC protein binding; NAS:UniProtKB.
DR GO; GO:0038187; F:pattern recognition receptor activity; IDA:UniProtKB.
DR GO; GO:0061760; P:antifungal innate immune response; ISS:UniProtKB.
DR GO; GO:0009756; P:carbohydrate mediated signaling; TAS:UniProtKB.
DR GO; GO:0001775; P:cell activation; ISS:ARUK-UCL.
DR GO; GO:0008037; P:cell recognition; IDA:UniProtKB.
DR GO; GO:0071226; P:cellular response to molecule of fungal origin; IDA:ARUK-UCL.
DR GO; GO:0042832; P:defense response to protozoan; NAS:UniProtKB.
DR GO; GO:0016046; P:detection of fungus; IDA:ARUK-UCL.
DR GO; GO:0032491; P:detection of molecule of fungal origin; IDA:ARUK-UCL.
DR GO; GO:0001879; P:detection of yeast; ISS:ARUK-UCL.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0006910; P:phagocytosis, recognition; IDA:UniProtKB.
DR GO; GO:0050850; P:positive regulation of calcium-mediated signaling; ISS:ARUK-UCL.
DR GO; GO:1903431; P:positive regulation of cell maturation; IDA:ARUK-UCL.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:ARUK-UCL.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:ARUK-UCL.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:ARUK-UCL.
DR GO; GO:1900017; P:positive regulation of cytokine production involved in inflammatory response; IDA:ARUK-UCL.
DR GO; GO:0002732; P:positive regulation of dendritic cell cytokine production; ISS:ARUK-UCL.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISS:ARUK-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:ARUK-UCL.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IDA:ARUK-UCL.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IDA:ARUK-UCL.
DR GO; GO:0032733; P:positive regulation of interleukin-10 production; IDA:ARUK-UCL.
DR GO; GO:0032735; P:positive regulation of interleukin-12 production; IDA:ARUK-UCL.
DR GO; GO:0032743; P:positive regulation of interleukin-2 production; IDA:ARUK-UCL.
DR GO; GO:0032747; P:positive regulation of interleukin-23 production; ISS:ARUK-UCL.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IDA:ARUK-UCL.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IMP:ARUK-UCL.
DR GO; GO:0051712; P:positive regulation of killing of cells of another organism; IDA:ARUK-UCL.
DR GO; GO:0051251; P:positive regulation of lymphocyte activation; IDA:ARUK-UCL.
DR GO; GO:0071639; P:positive regulation of monocyte chemotactic protein-1 production; IMP:ARUK-UCL.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:ARUK-UCL.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IDA:ARUK-UCL.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IDA:ARUK-UCL.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; IMP:ARUK-UCL.
DR GO; GO:0060267; P:positive regulation of respiratory burst; IDA:ARUK-UCL.
DR GO; GO:0032930; P:positive regulation of superoxide anion generation; IDA:ARUK-UCL.
DR GO; GO:2000318; P:positive regulation of T-helper 17 type immune response; ISS:UniProtKB.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:ARUK-UCL.
DR GO; GO:0090303; P:positive regulation of wound healing; IMP:ARUK-UCL.
DR GO; GO:0070884; P:regulation of calcineurin-NFAT signaling cascade; ISS:ARUK-UCL.
DR GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; ISS:ARUK-UCL.
DR GO; GO:0001878; P:response to yeast; ISS:ARUK-UCL.
DR GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; ISS:ARUK-UCL.
DR GO; GO:0042110; P:T cell activation; TAS:UniProtKB.
DR CDD; cd03593; CLECT_NK_receptors_like; 1.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR042808; CLEC7A.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR033992; NKR-like_CTLD.
DR PANTHER; PTHR47218; PTHR47218; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cytoplasm; Disulfide bond;
KW Glycoprotein; Immunity; Inflammatory response; Innate immunity; Lectin;
KW Membrane; Metal-binding; Phosphoprotein; Receptor; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..247
FT /note="C-type lectin domain family 7 member A"
FT /id="PRO_0000269491"
FT TOPO_DOM 1..44
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..65
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 66..247
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 127..242
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT MOTIF 15..18
FT /note="ITAM-like"
FT BINDING 146..153
FT /ligand="(1,3-beta-D-glucosyl)n"
FT /ligand_id="ChEBI:CHEBI:37671"
FT /evidence="ECO:0000250|UniProtKB:Q6QLQ4"
FT BINDING 157
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:Q6QLQ4"
FT BINDING 159
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:Q6QLQ4"
FT BINDING 163
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:Q6QLQ4"
FT BINDING 195
FT /ligand="(1,3-beta-D-glucosyl)n"
FT /ligand_id="ChEBI:CHEBI:37671"
FT /evidence="ECO:0000250|UniProtKB:Q6QLQ4"
FT BINDING 242
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:Q6QLQ4"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 120..131
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 148..241
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 220..233
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT VAR_SEQ 36..114
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:11567029,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_022048"
FT VAR_SEQ 36..45
FT /note="SCAASPPWRL -> IYSKTSVFPT (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:11567029"
FT /id="VSP_022049"
FT VAR_SEQ 46..247
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:11567029"
FT /id="VSP_022050"
FT VAR_SEQ 68..116
FT /note="AIWRSNSGSNTLENGYFLSRNKENHSQPTQSSLEDSVTPTKAVKTTGVL ->
FT GTGQFLKDLSFLNNRRKLFGDPIQEATHWRMATFYQEIKRTTVNPHNHL (in
FT isoform 10)"
FT /evidence="ECO:0000303|PubMed:11567029"
FT /id="VSP_047589"
FT VAR_SEQ 68..113
FT /note="Missing (in isoform 2, isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:11470510,
FT ECO:0000303|PubMed:11491532, ECO:0000303|PubMed:11567029,
FT ECO:0000303|PubMed:11745369, ECO:0000303|PubMed:12423684,
FT ECO:0000303|PubMed:12975309, ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_022051"
FT VAR_SEQ 69..77
FT /note="IWRSNSGSN -> GFKAVEFKG (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043298"
FT VAR_SEQ 78..247
FT /note="Missing (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043299"
FT VAR_SEQ 117..247
FT /note="Missing (in isoform 10)"
FT /evidence="ECO:0000303|PubMed:11567029"
FT /id="VSP_047590"
FT VAR_SEQ 165..196
FT /note="GFIVKQVSSQPDNSFWIGLSRPQTEVPWLWED -> SLTLLPKLECSEAATS
FT QAQVILPPQLPE (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11567029"
FT /id="VSP_022052"
FT VAR_SEQ 165..189
FT /note="GFIVKQVSSQPDNSFWIGLSRPQTE -> ISDQNHSYPRKPISKLCMDSRVS
FT HL (in isoform 3 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:11491532,
FT ECO:0000303|PubMed:11567029, ECO:0000303|PubMed:14702039"
FT /id="VSP_022053"
FT VAR_SEQ 165..178
FT /note="GFIVKQVSSQPDNS -> VSVDFCYDYLWCVS (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022054"
FT VAR_SEQ 179..247
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022055"
FT VAR_SEQ 190..247
FT /note="Missing (in isoform 3 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:11491532,
FT ECO:0000303|PubMed:11567029, ECO:0000303|PubMed:14702039"
FT /id="VSP_022056"
FT VAR_SEQ 197..247
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11567029"
FT /id="VSP_022057"
FT VARIANT 223
FT /note="I -> S (in dbSNP:rs16910527)"
FT /id="VAR_050111"
FT VARIANT 238..247
FT /note="Missing (may be associated with invasive
FT aspergillosis)"
FT /evidence="ECO:0000269|PubMed:20807886"
FT /id="VAR_084643"
FT CONFLICT 31
FT /note="V -> I (in Ref. 4; AAL11714)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 247 AA; 27627 MW; 98393E36976111B9 CRC64;
MEYHPDLENL DEDGYTQLHF DSQSNTRIAV VSEKGSCAAS PPWRLIAVIL GILCLVILVI
AVVLGTMAIW RSNSGSNTLE NGYFLSRNKE NHSQPTQSSL EDSVTPTKAV KTTGVLSSPC
PPNWIIYEKS CYLFSMSLNS WDGSKRQCWQ LGSNLLKIDS SNELGFIVKQ VSSQPDNSFW
IGLSRPQTEV PWLWEDGSTF SSNLFQIRTT ATQENPSPNC VWIHVSVIYD QLCSVPSYSI
CEKKFSM
