CLC2B_HUMAN
ID CLC2B_HUMAN Reviewed; 149 AA.
AC Q92478; B2R9U1; Q8IZE9; Q9BS74; Q9UQB4;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 15-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=C-type lectin domain family 2 member B;
DE AltName: Full=Activation-induced C-type lectin;
DE AltName: Full=C-type lectin superfamily member 2;
DE AltName: Full=IFN-alpha-2b-inducing-related protein 1;
GN Name=CLEC2B; Synonyms=AICL, CLECSF2, IFNRG1;
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].
RX PubMed=9038101; DOI=10.1007/s002510050208;
RA Hamann J., Montgomery K.T., Lau S., Kucherlapati R., van Lier R.A.W.;
RT "AICL, a new activation induced antigen encoded by the human NK gene
RT complex.";
RL Immunogenetics 45:295-300(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10072769; DOI=10.1016/s0378-1119(99)00004-9;
RA Yokoyama-Kobayashi M., Yamaguchi T., Sekine S., Kato S.;
RT "Selection of cDNAs encoding putative type II membrane proteins on the cell
RT surface from a human full-length cDNA bank.";
RL Gene 228:161-167(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-137.
RA Li Q., Zhao H., Wang L., Liu L., Dong C., Dong S., Wang J.;
RT "Study on gene response of IFN inducing.";
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- INTERACTION:
CC Q92478; P01023: A2M; NbExp=3; IntAct=EBI-13350535, EBI-640741;
CC Q92478; Q92478: CLEC2B; NbExp=2; IntAct=EBI-13350535, EBI-13350535;
CC Q92478; P50570-2: DNM2; NbExp=3; IntAct=EBI-13350535, EBI-10968534;
CC Q92478; P42858: HTT; NbExp=9; IntAct=EBI-13350535, EBI-466029;
CC Q92478; O14656-2: TOR1A; NbExp=3; IntAct=EBI-13350535, EBI-25847109;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed preferentially in lymphoid tissues, and
CC in most hematopoietic cell types.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=CD69 homolog;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_236";
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DR EMBL; X96719; CAA65480.1; -; mRNA.
DR EMBL; AB015628; BAA76495.1; -; mRNA.
DR EMBL; AK313916; BAG36638.1; -; mRNA.
DR EMBL; CH471094; EAW96127.1; -; Genomic_DNA.
DR EMBL; BC005254; AAH05254.1; -; mRNA.
DR EMBL; AY142147; AAN46677.1; -; mRNA.
DR CCDS; CCDS8605.1; -.
DR RefSeq; NP_005118.2; NM_005127.2.
DR AlphaFoldDB; Q92478; -.
DR SMR; Q92478; -.
DR BioGRID; 115300; 176.
DR DIP; DIP-58612N; -.
DR IntAct; Q92478; 4.
DR STRING; 9606.ENSP00000228438; -.
DR GlyGen; Q92478; 3 sites.
DR iPTMnet; Q92478; -.
DR PhosphoSitePlus; Q92478; -.
DR BioMuta; CLEC2B; -.
DR DMDM; 33860149; -.
DR EPD; Q92478; -.
DR jPOST; Q92478; -.
DR MassIVE; Q92478; -.
DR MaxQB; Q92478; -.
DR PaxDb; Q92478; -.
DR PeptideAtlas; Q92478; -.
DR PRIDE; Q92478; -.
DR ProteomicsDB; 75260; -.
DR Antibodypedia; 1470; 115 antibodies from 18 providers.
DR DNASU; 9976; -.
DR Ensembl; ENST00000228438.3; ENSP00000228438.2; ENSG00000110852.5.
DR GeneID; 9976; -.
DR KEGG; hsa:9976; -.
DR MANE-Select; ENST00000228438.3; ENSP00000228438.2; NM_005127.3; NP_005118.2.
DR UCSC; uc001qwn.4; human.
DR CTD; 9976; -.
DR DisGeNET; 9976; -.
DR GeneCards; CLEC2B; -.
DR HGNC; HGNC:2053; CLEC2B.
DR HPA; ENSG00000110852; Tissue enhanced (bone).
DR MIM; 603242; gene.
DR neXtProt; NX_Q92478; -.
DR OpenTargets; ENSG00000110852; -.
DR PharmGKB; PA26582; -.
DR VEuPathDB; HostDB:ENSG00000110852; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000163321; -.
DR HOGENOM; CLU_049894_8_4_1; -.
DR InParanoid; Q92478; -.
DR OMA; DDWIGFQ; -.
DR OrthoDB; 1289964at2759; -.
DR PhylomeDB; Q92478; -.
DR TreeFam; TF351467; -.
DR PathwayCommons; Q92478; -.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR SignaLink; Q92478; -.
DR BioGRID-ORCS; 9976; 11 hits in 1053 CRISPR screens.
DR ChiTaRS; CLEC2B; human.
DR GeneWiki; CLEC2B; -.
DR GenomeRNAi; 9976; -.
DR Pharos; Q92478; Tbio.
DR PRO; PR:Q92478; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q92478; protein.
DR Bgee; ENSG00000110852; Expressed in upper leg skin and 193 other tissues.
DR ExpressionAtlas; Q92478; baseline and differential.
DR Genevisible; Q92478; HS.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0030246; F:carbohydrate binding; TAS:ProtInc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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; IPR016187; CTDL_fold.
DR InterPro; IPR033992; NKR-like_CTLD.
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 Disulfide bond; Glycoprotein; Lectin; Membrane; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..149
FT /note="C-type lectin domain family 2 member B"
FT /id="PRO_0000046611"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..25
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..149
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 42..145
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 35..46
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 63..144
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 123..136
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT CONFLICT 79
FT /note="M -> T (in Ref. 5; AAH05254)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="D -> H (in Ref. 1; CAA65480)"
FT /evidence="ECO:0000305"
FT CONFLICT 132..137
FT /note="ATARCY -> TTAQIQ (in Ref. 6)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 149 AA; 17307 MW; 0B4FED23424F6C55 CRC64;
MMTKHKKCFI IVGVLITTNI ITLIVKLTRD SQSLCPYDWI GFQNKCYYFS KEEGDWNSSK
YNCSTQHADL TIIDNIEEMN FLRRYKCSSD HWIGLKMAKN RTGQWVDGAT FTKSFGMRGS
EGCAYLSDDG AATARCYTER KWICRKRIH
