ID MICB_HUMAN Reviewed; 383 AA. AC Q29980; A2AC57; A6NP85; B0UZ10; B2RAK2; O14499; O14500; O19798; O19799; AC O19800; O19801; O19802; O19803; O78099; O78100; O78101; O78102; O78103; AC O78104; P79525; P79541; Q5GR31; Q5GR37; Q5GR41; Q5GR42; Q5GR43; Q5GR44; AC Q5GR46; Q5GR48; Q5RIY6; Q5SSK1; Q5ST25; Q7JK51; Q7YQ89; Q861E6; Q9MY18; AC Q9MY19; Q9MY20; Q9UBH4; Q9UBZ8; Q9UEJ0; X6R344; DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot. DT 12-AUG-2020, sequence version 2. DT 24-JAN-2024, entry version 180. DE RecName: Full=MHC class I polypeptide-related sequence B; DE Short=MIC-B; DE Flags: Precursor; GN Name=MICB {ECO:0000312|EMBL:CAA62823.1}; GN Synonyms=PERB11.2 {ECO:0000312|EMBL:AAB51802.1}; 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] {ECO:0000305, ECO:0000312|EMBL:CAA62823.1} RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE MICB*001; ISOFORM 1). RX PubMed=8575823; DOI=10.1007/bf00587305; RA Bahram S., Spies T.; RT "Nucleotide sequence of a human MHC class I MICB cDNA."; RL Immunogenetics 43:230-233(1996). RN [2] {ECO:0000305, ECO:0000312|EMBL:AAB42011.1} RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE MICB*002; ISOFORM 1). RX PubMed=8952966; DOI=10.1007/s002510050184; RA Bahram S., Shiina T., Oka A., Tamiya G., Inoko H.; RT "Genomic structure of the human MHC class I MICB gene."; RL Immunogenetics 45:161-162(1996). RN [3] {ECO:0000305, ECO:0000312|EMBL:ABO16470.1} RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE MICB*005; ISOFORM 1), AND RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RX PubMed=17678727; DOI=10.1016/j.humimm.2007.05.003; RA Martinez-Borra J., Rodrigo L., Rodriguez-Rodero S., Fernandez-Morera J.L., RA Diaz-Pena R., Pruneda L., Lopez-Vazquez A., Lopez-Larrea C.; RT "The allele MICB*0050204, over-represented in the Caucasian population, has RT an additional exon resulting from a new splice junction sequence."; RL Hum. Immunol. 68:705-707(2007). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS GLU-39; RP GLU-80; ASN-136 AND VAL-300. 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 [5] {ECO:0000305, ECO:0000312|EMBL:BAB63307.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELE MICB*002). RA Hirakawa M., Yamaguchi H., Imai K., Shimada J., Shiina S., Tamiya G., RA Oka A., Inoko H.; RT "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region."; RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases. RN [6] {ECO:0000305, ECO:0000312|EMBL:CR753864} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELES MICB*002; MICB*003; RP MICB*004; MICB*005 AND MICB*008). RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS GLU-39; RP GLU-80 AND VAL-300. RC TISSUE=Pancreas; 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 [8] {ECO:0000305, ECO:0000312|EMBL:AAB51802.1} RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-341 (ALLELE MICB*003; ISOFORM 1). RX PubMed=8995188; DOI=10.1007/s002510050191; RA Gaudieri S., Leelayuwat C., Townend D.C., Mullberg J., Cosman D., RA Dawkins R.L.; RT "Allelic and interlocus comparison of the PERB11 multigene family in the RT MHC."; RL Immunogenetics 45:209-216(1997). RN [9] {ECO:0000305, ECO:0000312|EMBL:AAB71642.1} RP NUCLEOTIDE SEQUENCE [MRNA] OF 24-341 (ALLELES MICB*002; MICB*003; MICB*004; RP MICB*005 AND MICB*006; ISOFORM 1). RX PubMed=9271635; DOI=10.1007/s002510050299; RA Pellet P., Renaud M., Fodil N., Laloux L., Inoko H., Hauptmann G., RA Debre P., Bahram S., Theodorou I.; RT "Allelic repertoire of the human MICB gene."; RL Immunogenetics 46:434-436(1997). RN [10] {ECO:0000305, ECO:0000312|EMBL:CAD91554.1} RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 24-341 (ALLELE MICB*015; ISOFORM 1). RC TISSUE=Blood {ECO:0000312|EMBL:CAD91554.1}; RX PubMed=15191526; DOI=10.1111/j.1399-0039.2004.00242.x; RA Quiroga I., Sweeney D., Sutton P.M., Chapple S.D.J., Souto-Grando J.P., RA Barnardo M.C.N.M., Fuggle S.V.; RT "A novel major histocompatibility complex class I-related chain allele."; RL Tissue Antigens 64:74-77(2004). RN [11] {ECO:0000305, ECO:0000312|EMBL:AAC39847.1} RP NUCLEOTIDE SEQUENCE [MRNA] OF 25-383 (ALLELES MICB*002; MICB*005; MICB*008; RP MICB*010; MICB*011 AND MICB*012; ISOFORM 1). RX PubMed=9694358; DOI=10.1111/j.1399-0039.1998.tb03008.x; RA Visser C.J., Tilanus M.G., Schaeffer V., Tatari Z., Tamouza R., Janin A., RA Charron D.; RT "Sequencing-based typing reveals six novel MHC class I chain-related gene B RT (MICB) alleles."; RL Tissue Antigens 51:649-652(1998). RN [12] {ECO:0000305, ECO:0000312|EMBL:BAA23479.1} RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-341 (ALLELES MICB*002; MICB*003; RP MICB*004; MICB*005; MICB*007 AND MICB*008; ISOFORM 1). RX PubMed=9321430; DOI=10.1007/s002510050311; RA Ando H., Mizuki N., Ota M., Yamazaki M., Ohno S., Goto K., Miyata Y., RA Wakisaka K., Bahram S., Inoko H.; RT "Allelic variants of the human MHC class I chain-related B gene (MICB)."; RL Immunogenetics 46:499-508(1997). RN [13] {ECO:0000305, ECO:0000312|EMBL:CAB72097.1} RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-341 (ALLELES MICB*008; MICB*013 AND RP MICB*014; ISOFORM 1). RX PubMed=10746790; DOI=10.1034/j.1399-0039.2000.550210.x; RA Fischer G., Perez-Rodriguez M., Arguello J.R., Cox S.T., McWhinnie A., RA Travers P.J., Madrigal J.A.; RT "Three novel MICB alleles."; RL Tissue Antigens 55:166-170(2000). RN [14] {ECO:0000305, ECO:0000312|EMBL:CAE54939.1} RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-297 (ALLELES MICB*005; MICB*014; RP MICB*016; MICB*018; MICB*019; MICB*020 AND MICB*022; ISOFORM 1). RX PubMed=15304008; DOI=10.1111/j.1399-0039.2004.00286.x; RA Schroeder M., Elsner H.-A., Kim T.D., Blasczyk R.; RT "Eight novel MICB alleles, including a null allele, identified in gastric RT MALT lymphoma patients."; RL Tissue Antigens 64:276-280(2004). RN [15] {ECO:0000305} RP FUNCTION, AND INDUCTION. RX PubMed=9497295; DOI=10.1126/science.279.5357.1737; RA Groh V., Steinle A., Bauer S., Spies T.; RT "Recognition of stress-induced MHC molecules by intestinal epithelial RT gammadelta T cells."; RL Science 279:1737-1740(1998). RN [16] {ECO:0000305} RP TISSUE SPECIFICITY. RX PubMed=10359807; DOI=10.1073/pnas.96.12.6879; RA Groh V., Rhinehart R., Secrist H., Bauer S., Grabstein K.H., Spies T.; RT "Broad tumor-associated expression and recognition by tumor-derived gamma RT delta T cells of MICA and MICB."; RL Proc. Natl. Acad. Sci. U.S.A. 96:6879-6884(1999). RN [17] {ECO:0000305} RP INDUCTION. RX PubMed=11287116; DOI=10.1016/s0304-4165(01)00099-x; RA Yamamoto K., Fujiyama Y., Andoh A., Bamba T., Okabe H.; RT "Oxidative stress increases MICA and MICB gene expression in the human RT colon carcinoma cell line (CaCo-2)."; RL Biochim. Biophys. Acta 1526:10-12(2001). RN [18] {ECO:0000305} RP INTERACTION WITH CYTOMEGALOVIRUS GLYCOPROTEIN UL16 (MICROBIAL INFECTION). RX PubMed=11239445; DOI=10.1016/s1074-7613(01)00095-4; RA Cosman D., Mullberg J., Sutherland C.L., Chin W., Armitage R., Fanslow W., RA Kubin M., Chalupny N.J.; RT "ULBPs, novel MHC class I-related molecules, bind to CMV glycoprotein UL16 RT and stimulate NK cytotoxicity through the NKG2D receptor."; RL Immunity 14:123-133(2001). RN [19] {ECO:0000305} RP FUNCTION, AND INTERACTION WITH KLRK1. RX PubMed=11491531; DOI=10.1007/s002510100325; RA Steinle A., Li P., Morris D.L., Groh V., Lanier L.L., Strong R.K., RA Spies T.; RT "Interactions of human NKG2D with its ligands MICA, MICB, and homologs of RT the mouse RAE-1 protein family."; RL Immunogenetics 53:279-287(2001). RN [20] {ECO:0000305} RP ALTERNATIVE SPLICING. RX PubMed=12466900; DOI=10.1007/s00251-002-0496-y; RA Zou Y., Stastny P.; RT "Alternatively spliced forms of MICA and MICB lacking exon 3 in a human RT cell line and evidence of presence of similar RNA in human peripheral blood RT mononuclear cells."; RL Immunogenetics 54:671-674(2002). RN [21] RP FUNCTION AS A LIGAND FOR KLRK1. RX PubMed=11777960; DOI=10.4049/jimmunol.168.2.671; RA Sutherland C.L., Chalupny N.J., Schooley K., VandenBos T., Kubin M., RA Cosman D.; RT "UL16-binding proteins, novel MHC class I-related proteins, bind to NKG2D RT and activate multiple signaling pathways in primary NK cells."; RL J. Immunol. 168:671-679(2002). RN [22] {ECO:0000305} RP TISSUE SPECIFICITY, AND INDUCTION. RX PubMed=12569559; DOI=10.1002/ijc.10966; RA Jinushi M., Takehara T., Tatsumi T., Kanto T., Groh V., Spies T., RA Kimura R., Miyagi T., Mochizuki K., Sasaki Y., Hayashi N.; RT "Expression and role of MICA and MICB in human hepatocellular carcinomas RT and their regulation by retinoic acid."; RL Int. J. Cancer 104:354-361(2003). RN [23] {ECO:0000305} RP INTERACTION WITH CYTOMEGALOVIRUS GLYCOPROTEIN UL16, AND SUBCELLULAR RP LOCATION. RX PubMed=12782710; DOI=10.1084/jem.20022059; RA Dunn C., Chalupny N.J., Sutherland C.L., Dosch S., Sivakumar P.V., RA Johnson D.C., Cosman D.; RT "Human cytomegalovirus glycoprotein UL16 causes intracellular sequestration RT of NKG2D ligands, protecting against natural killer cell cytotoxicity."; RL J. Exp. Med. 197:1427-1439(2003). RN [24] {ECO:0000305} RP INDUCTION. RX PubMed=12538683; DOI=10.4049/jimmunol.170.3.1249; RA Jinushi M., Takehara T., Kanto T., Tatsumi T., Groh V., Spies T., RA Miyagi T., Suzuki T., Sasaki Y., Hayashi N.; RT "Critical role of MHC class I-related chain A and B expression on IFN- RT alpha-stimulated dendritic cells in NK cell activation: impairment in RT chronic hepatitis C virus infection."; RL J. Immunol. 170:1249-1256(2003). RN [25] {ECO:0000305} RP PROTEOLYTIC CLEAVAGE ON TUMOR CELLS. RX PubMed=16698441; DOI=10.1016/j.humimm.2006.02.008; RA Salih H.R., Goehlsdorf D., Steinle A.; RT "Release of MICB molecules by tumor cells: mechanism and soluble MICB in RT sera of cancer patients."; RL Hum. Immunol. 67:188-195(2006). RN [26] {ECO:0000305} RP INTERACTION WITH KLRK1. RX PubMed=16849432; DOI=10.1073/pnas.0600721103; RA Roda-Navarro P., Vales-Gomez M., Chisholm S.E., Reyburn H.T.; RT "Transfer of NKG2D and MICB at the cytotoxic NK cell immune synapse RT correlates with a reduction in NK cell cytotoxic function."; RL Proc. Natl. Acad. Sci. U.S.A. 103:11258-11263(2006). RN [27] {ECO:0000305} RP TISSUE SPECIFICITY. RX PubMed=17565371; DOI=10.1371/journal.pone.0000518; RA Schrambach S., Ardizzone M., Leymarie V., Sibilia J., Bahram S.; RT "In vivo expression pattern of MICA and MICB and its relevance to auto- RT immunity and cancer."; RL PLoS ONE 2:E518-E518(2007). RN [28] {ECO:0000305} RP INVOLVEMENT IN RHEUMATOID ARTHRITIS. RX PubMed=17003176; DOI=10.1093/rheumatology/kel331; RA Lopez-Arbesu R., Ballina-Garcia F.J., Alperi-Lopez M., Lopez-Soto A., RA Rodriguez-Rodero S., Martinez-Borra J., Lopez-Vazquez A., RA Fernandez-Morera J.L., Riestra-Noriega J.L., Queiro-Silva R., RA Quinones-Lombrana A., Lopez-Larrea C., Gonzalez S.; RT "MHC class I chain-related gene B (MICB) is associated with rheumatoid RT arthritis susceptibility."; RL Rheumatology 46:426-430(2007). RN [29] {ECO:0000305} RP INVOLVEMENT IN SCHIZOPHRENIA. RX PubMed=17561376; DOI=10.1016/j.schres.2007.04.021; RA Shirts B.H., Kim J.J., Reich S., Dickerson F.B., Yolken R.H., Devlin B., RA Nimgaonkar V.L.; RT "Polymorphisms in MICB are associated with human herpes virus RT seropositivity and schizophrenia risk."; RL Schizophr. Res. 94:342-353(2007). RN [30] {ECO:0000305} RP INDUCTION. RX PubMed=17641203; DOI=10.1126/science.1140956; RA Stern-Ginossar N., Elefant N., Zimmermann A., Wolf D.G., Saleh N., RA Biton M., Horwitz E., Prokocimer Z., Prichard M., Hahn G., Goldman-Wohl D., RA Greenfield C., Yagel S., Hengel H., Altuvia Y., Margalit H., Mandelboim O.; RT "Host immune system gene targeting by a viral miRNA."; RL Science 317:376-381(2007). RN [31] {ECO:0000305} RP INDUCTION. RX PubMed=18395517; DOI=10.1016/j.bbrc.2008.03.131; RA Tang K.-F., He C.-X., Zeng G.-L., Wu J., Song G.-B., Shi Y.-S., RA Zhang W.-G., Huang A.-L., Steinle A., Ren H.; RT "Induction of MHC class I-related chain B (MICB) by 5-aza-2'- RT deoxycytidine."; RL Biochem. Biophys. Res. Commun. 370:578-583(2008). RN [32] RP POLYMORPHISM. RX PubMed=32153595; DOI=10.3389/fimmu.2020.00314; RA Klussmeier A., Massalski C., Putke K., Schaefer G., Sauter J., Schefzyk D., RA Pruschke J., Hofmann J., Fuerst D., Carapito R., Bahram S., Schmidt A.H., RA Lange V.; RT "High-Throughput MICA/B Genotyping of Over Two Million Samples: Workflow RT and Allele Frequencies."; RL Front. Immunol. 11:314-314(2020). RN [33] {ECO:0000305} RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 24-297, AND DISULFIDE BONDS. RX PubMed=12133964; DOI=10.4049/jimmunol.169.3.1395; RA Holmes M.A., Li P., Petersdorf E.W., Strong R.K.; RT "Structural studies of allelic diversity of the MHC class I homolog MIC-B, RT a stress-inducible ligand for the activating immunoreceptor NKG2D."; RL J. Immunol. 169:1395-1400(2002). CC -!- FUNCTION: Seems to have no role in antigen presentation. Acts as a CC stress-induced self-antigen that is recognized by gamma delta T cells. CC Ligand for the KLRK1/NKG2D receptor. Binding to KLRK1 leads to cell CC lysis. {ECO:0000269|PubMed:11491531, ECO:0000269|PubMed:11777960, CC ECO:0000269|PubMed:9497295}. CC -!- SUBUNIT: Unlike classical MHC class I molecules, does not form a CC heterodimer with beta-2-microglobulin. Binds as a monomer to a CC KLRK1/NKG2D homodimer. KLRK1 forms a complex with HCST/DAP10 in which CC KLRK1 binds MICB while HCST acts as an adapter molecule which enables CC signal transduction. Receptor-ligand interaction induces clustering of CC both proteins in ordered structures called immune synapses and also CC leads to their intercellular transfer. This is associated with a CC reduction in the cytotoxicity of KLRK1-expressing cells. CC {ECO:0000250|UniProtKB:Q29983, ECO:0000269|PubMed:11239445, CC ECO:0000269|PubMed:11491531, ECO:0000269|PubMed:12782710, CC ECO:0000269|PubMed:16849432}. CC -!- SUBUNIT: (Microbial infection) Interacts with human CC cytomegalovirus/HHV-5 glycoprotein UL16; this interaction causes CC sequestration of MICB in the endoplasmic reticulum and increases CC resistance to KLRK1-mediated cytotoxicity. CC {ECO:0000269|PubMed:11239445}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q29983}; CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q29983}. CC Note=Binding to human cytomegalovirus glycoprotein UL16 causes CC sequestration in the endoplasmic reticulum. CC {ECO:0000250|UniProtKB:Q29983, ECO:0000269|PubMed:12782710}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1 {ECO:0000269|PubMed:12466900}; Synonyms=MICB1 CC {ECO:0000269|PubMed:12466900}; CC IsoId=Q29980-1; Sequence=Displayed; CC Name=2 {ECO:0000269|PubMed:12466900}; Synonyms=MICB2 CC {ECO:0000269|PubMed:12466900}, ex3-del; CC IsoId=Q29980-2; Sequence=VSP_055246; CC Name=3 {ECO:0000269|PubMed:17678727}; CC IsoId=Q29980-3; Sequence=VSP_052801, VSP_052802; CC -!- TISSUE SPECIFICITY: Widely expressed with the exception of the central CC nervous system where it is absent. Expressed in many, but not all, CC epithelial tumors of lung, breast, kidney, ovary, prostate and colon. CC In hepatocellular carcinomas, expressed in tumor cells but not in CC surrounding non-cancerous tissue. {ECO:0000269|PubMed:10359807, CC ECO:0000269|PubMed:12569559, ECO:0000269|PubMed:17565371}. CC -!- INDUCTION: By heat shock, oxidative stress, retinoic acid, IFN-alpha CC and the DNA methyltransferase inhibitor 5-aza-2'-deoxycytidine. CC Induction by IFN-alpha is impaired in patients with chronic hepatitis C CC virus infection. Down-regulated by human cytomegalovirus UL112 microRNA CC during viral infection which leads to decreased binding of KLRK1/NKG2D CC and reduced killing by natural killer cells. CC {ECO:0000269|PubMed:11287116, ECO:0000269|PubMed:12538683, CC ECO:0000269|PubMed:12569559, ECO:0000269|PubMed:17641203, CC ECO:0000269|PubMed:18395517, ECO:0000269|PubMed:9497295}. CC -!- PTM: Proteolytically cleaved and released from the cell surface of CC tumor cells. {ECO:0000269|PubMed:16698441}. CC -!- POLYMORPHISM: The following alleles of MICB are known: MICB*001, CC MICB*002, MICB*003, MICB*004, MICB*005, MICB*006, MICB*007, MICB*008, CC MICB*009N, MICB*010, MICB*011, MICB*012, MICB*013, MICB*014, MICB*015, CC MICB*016, MICB*018, MICB*019, MICB*020, MICB*021N and MICB*022. CC MICB*009N and MICB*021N are null alleles which are not expressed. The CC three most common MICB alleles in the human population could be CC MICB*005, MICB*004, and MICB*002. The sequence shown is that of CC MICB*004. {ECO:0000305|PubMed:32153595}. CC -!- DISEASE: Rheumatoid arthritis (RA) [MIM:180300]: An inflammatory CC disease with autoimmune features and a complex genetic component. It CC primarily affects the joints and is characterized by inflammatory CC changes in the synovial membranes and articular structures, widespread CC fibrinoid degeneration of the collagen fibers in mesenchymal tissues, CC and by atrophy and rarefaction of bony structures. CC {ECO:0000269|PubMed:17003176}. Note=Disease susceptibility is CC associated with variants affecting the gene represented in this entry. CC The MICB*004 allele is associated with rheumatoid arthritis. CC -!- DISEASE: Note=Genetic variation in MICB is associated with CC cytomegalovirus and herpes simplex virus I seropositivity and this may CC be associated with schizophrenia risk. CC -!- MISCELLANEOUS: [Isoform 3]: A GC to AG nucleotide substitution in CC intron 1 generates a splice junction which gives rise to an additional CC exon between exons 1 and 2. May be produced at very low levels due to a CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA CC decay. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the MHC class I family. MIC subfamily. CC {ECO:0000255}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X91625; CAA62823.1; -; mRNA. DR EMBL; U65416; AAB42011.1; -; Genomic_DNA. DR EMBL; AY885251; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; EF051579; ABO16470.1; -; Genomic_DNA. DR EMBL; EF051580; ABO16471.1; -; Genomic_DNA. DR EMBL; AK314228; BAG36899.1; -; mRNA. DR EMBL; BA000025; BAB63307.1; -; Genomic_DNA. DR EMBL; AL662866; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL663061; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX001040; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX005439; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR753820; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR753864; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR788288; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC044218; AAH44218.1; -; mRNA. DR EMBL; U69978; AAB51802.1; -; Genomic_DNA. DR EMBL; U95729; AAB71642.1; -; mRNA. DR EMBL; U95730; AAB71643.1; -; mRNA. DR EMBL; U95731; AAB71644.1; -; mRNA. DR EMBL; U95732; AAB71645.1; -; mRNA. DR EMBL; U95733; AAB71646.1; -; mRNA. DR EMBL; U95734; AAB71647.1; -; mRNA. DR EMBL; AJ563706; CAD91554.1; -; Genomic_DNA. DR EMBL; AF021221; AAC39846.1; -; mRNA. DR EMBL; AF021222; AAC39847.1; -; mRNA. DR EMBL; AF021223; AAC39848.1; -; mRNA. DR EMBL; AF021224; AAC39849.1; -; mRNA. DR EMBL; AF021225; AAC39850.1; -; mRNA. DR EMBL; AF021226; AAC39851.1; -; mRNA. DR EMBL; AB003609; BAA23476.1; -; Genomic_DNA. DR EMBL; AB003610; BAA23477.1; -; Genomic_DNA. DR EMBL; AB003611; BAA23478.1; -; Genomic_DNA. DR EMBL; AB003612; BAA23479.1; -; Genomic_DNA. DR EMBL; AB003613; BAA23480.1; -; Genomic_DNA. DR EMBL; AB003614; BAA23481.1; -; Genomic_DNA. DR EMBL; AB003615; BAA23482.1; -; Genomic_DNA. DR EMBL; AB003616; BAA23483.1; -; Genomic_DNA. DR EMBL; AB003617; BAA23484.1; -; Genomic_DNA. DR EMBL; AJ251156; CAB72101.1; -; Genomic_DNA. DR EMBL; AJ251157; CAB72101.1; JOINED; Genomic_DNA. DR EMBL; AJ251158; CAB72097.1; -; Genomic_DNA. DR EMBL; AJ251159; CAB72097.1; JOINED; Genomic_DNA. DR EMBL; AJ251160; CAB72098.1; -; Genomic_DNA. DR EMBL; AJ251161; CAB72098.1; JOINED; Genomic_DNA. DR EMBL; AJ606906; CAE54932.1; -; Genomic_DNA. DR EMBL; AJ606907; CAE54933.1; -; Genomic_DNA. DR EMBL; AJ606908; CAE54934.1; -; Genomic_DNA. DR EMBL; AJ606909; CAE54935.1; -; Genomic_DNA. DR EMBL; AJ606910; CAE54936.1; -; Genomic_DNA. DR EMBL; AJ606911; CAE54937.1; -; Genomic_DNA. DR EMBL; AJ606912; CAE54938.1; -; Genomic_DNA. DR EMBL; AJ606913; CAE54939.1; -; Genomic_DNA. DR EMBL; AJ606914; CAE54940.1; -; Genomic_DNA. DR EMBL; AJ606915; CAE54941.1; -; Genomic_DNA. DR EMBL; AJ606916; CAE54942.1; -; Genomic_DNA. DR EMBL; AJ606917; CAE54943.1; -; Genomic_DNA. DR EMBL; AJ606918; CAE54944.1; -; Genomic_DNA. DR EMBL; AJ606919; CAE54945.1; -; Genomic_DNA. DR EMBL; AJ606920; CAE54946.1; -; Genomic_DNA. DR EMBL; AJ606921; CAE54947.1; -; Genomic_DNA. DR EMBL; AJ606922; CAE54948.1; -; Genomic_DNA. DR EMBL; AJ606923; CAE54949.1; -; Genomic_DNA. DR EMBL; AJ606929; CAE54955.1; -; Genomic_DNA. DR EMBL; AJ606930; CAE54956.1; -; Genomic_DNA. DR EMBL; AJ606931; CAE54957.1; -; Genomic_DNA. DR CCDS; CCDS43449.1; -. [Q29980-1] DR CCDS; CCDS75422.1; -. [Q29980-2] DR RefSeq; NP_001276089.1; NM_001289160.1. DR RefSeq; NP_001276090.1; NM_001289161.1. [Q29980-2] DR RefSeq; NP_005922.2; NM_005931.4. [Q29980-1] DR PDB; 1JE6; X-ray; 2.50 A; A=24-297. DR PDB; 2WY3; X-ray; 1.80 A; A/C=24-341. DR PDBsum; 1JE6; -. DR PDBsum; 2WY3; -. DR AlphaFoldDB; Q29980; -. DR SMR; Q29980; -. DR BioGRID; 110424; 157. DR CORUM; Q29980; -. DR STRING; 9606.ENSP00000252229; -. DR GlyCosmos; Q29980; 4 sites, No reported glycans. DR GlyGen; Q29980; 4 sites. DR iPTMnet; Q29980; -. DR PhosphoSitePlus; Q29980; -. DR SwissPalm; Q29980; -. DR BioMuta; MICB; -. DR DMDM; 74706857; -. DR EPD; Q29980; -. DR jPOST; Q29980; -. DR MassIVE; Q29980; -. DR MaxQB; Q29980; -. DR PaxDb; 9606-ENSP00000252229; -. DR PeptideAtlas; Q29980; -. DR ProteomicsDB; 3419; -. DR ProteomicsDB; 389; -. DR ProteomicsDB; 61282; -. [Q29980-1] DR ProteomicsDB; 69573; -. DR Pumba; Q29980; -. DR Antibodypedia; 27039; 372 antibodies from 29 providers. DR DNASU; 4277; -. DR Ensembl; ENST00000252229.7; ENSP00000252229.6; ENSG00000204516.10. [Q29980-1] DR Ensembl; ENST00000399150.7; ENSP00000382103.3; ENSG00000204516.10. [Q29980-2] DR Ensembl; ENST00000428416.2; ENSP00000398412.2; ENSG00000206449.11. DR Ensembl; ENST00000436531.6; ENSP00000409414.2; ENSG00000238289.9. DR Ensembl; ENST00000436655.2; ENSP00000402484.2; ENSG00000238289.9. DR Ensembl; ENST00000438954.6; ENSP00000398212.2; ENSG00000234218.9. DR Ensembl; ENST00000442104.6; ENSP00000387401.2; ENSG00000231179.9. [Q29980-2] DR Ensembl; ENST00000443156.2; ENSP00000393355.2; ENSG00000227772.8. DR Ensembl; ENST00000451603.6; ENSP00000407561.2; ENSG00000231179.9. [Q29980-1] DR GeneID; 4277; -. DR KEGG; hsa:4277; -. DR MANE-Select; ENST00000252229.7; ENSP00000252229.6; NM_005931.5; NP_005922.2. DR UCSC; uc003ntn.6; human. DR UCSC; uc003nto.6; human. [Q29980-1] DR AGR; HGNC:7091; -. DR CTD; 4277; -. DR DisGeNET; 4277; -. DR GeneCards; MICB; -. DR HGNC; HGNC:7091; MICB. DR HPA; ENSG00000204516; Tissue enhanced (lymphoid). DR MIM; 180300; phenotype. DR MIM; 602436; gene. DR neXtProt; NX_Q29980; -. DR OpenTargets; ENSG00000204516; -. DR PharmGKB; PA30812; -. DR VEuPathDB; HostDB:ENSG00000204516; -. DR eggNOG; ENOG502RU00; Eukaryota. DR GeneTree; ENSGT01100000263517; -. DR InParanoid; Q29980; -. DR OMA; NISVVWF; -. DR OrthoDB; 3840485at2759; -. DR PhylomeDB; Q29980; -. DR TreeFam; TF342166; -. DR PathwayCommons; Q29980; -. DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell. DR SignaLink; Q29980; -. DR BioGRID-ORCS; 4277; 23 hits in 1120 CRISPR screens. DR ChiTaRS; MICB; human. DR EvolutionaryTrace; Q29980; -. DR GenomeRNAi; 4277; -. DR Pharos; Q29980; Tbio. DR PRO; PR:Q29980; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; Q29980; Protein. DR Bgee; ENSG00000204516; Expressed in granulocyte and 96 other cell types or tissues. DR ExpressionAtlas; Q29980; baseline and differential. DR GO; GO:0009986; C:cell surface; ISS:UniProtKB. DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0046703; F:natural killer cell lectin-like receptor binding; IDA:UniProtKB. DR GO; GO:0042605; F:peptide antigen binding; IBA:GO_Central. DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central. DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW. DR GO; GO:0002486; P:antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent; IBA:GO_Central. DR GO; GO:0002476; P:antigen processing and presentation of endogenous peptide antigen via MHC class Ib; IBA:GO_Central. DR GO; GO:0046629; P:gamma-delta T cell activation; IDA:UniProtKB. DR GO; GO:0006955; P:immune response; IBA:GO_Central. DR GO; GO:0002429; P:immune response-activating cell surface receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW. DR GO; GO:0050689; P:negative regulation of defense response to virus by host; IDA:UniProtKB. DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IBA:GO_Central. DR GO; GO:0009408; P:response to heat; IDA:UniProtKB. DR GO; GO:0006979; P:response to oxidative stress; IDA:UniProtKB. DR GO; GO:0032526; P:response to retinoic acid; IDA:UniProtKB. DR CDD; cd21017; IgC1_MHC_Ia_MIC-A_MIC-B; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 1. DR Gene3D; 3.30.500.10; MHC class I-like antigen recognition-like; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011161; MHC_I-like_Ag-recog. DR InterPro; IPR037055; MHC_I-like_Ag-recog_sf. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR PANTHER; PTHR16675:SF154; MHC CLASS I POLYPEPTIDE-RELATED SEQUENCE A-RELATED; 1. DR PANTHER; PTHR16675; MHC CLASS I-RELATED; 1. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR SUPFAM; SSF48726; Immunoglobulin; 1. DR SUPFAM; SSF54452; MHC antigen-recognition domain; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR Genevisible; Q29980; HS. PE 1: Evidence at protein level; KW 3D-structure; Adaptive immunity; Alternative splicing; Cell membrane; KW Cytolysis; Disulfide bond; Glycoprotein; Host-virus interaction; Immunity; KW Immunoglobulin domain; Membrane; Reference proteome; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1..22 FT /evidence="ECO:0000255" FT CHAIN 23..383 FT /note="MHC class I polypeptide-related sequence B" FT /evidence="ECO:0000255" FT /id="PRO_0000341418" FT TOPO_DOM 23..309 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 310..330 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 331..383 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 207..298 FT /note="Ig-like C1-type" FT /evidence="ECO:0000255" FT CARBOHYD 164 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 210 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 220 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 261 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 119..187 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:12133964" FT DISULFID 225..282 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:12133964" FT VAR_SEQ 24..41 FT /note="EPHSLRYNLMVLSQDGSV -> VEMGFHRVSQDGLDLLTS (in isoform FT 3)" FT /evidence="ECO:0000303|PubMed:17678727" FT /id="VSP_052801" FT VAR_SEQ 42..383 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:17678727" FT /id="VSP_052802" FT VAR_SEQ 109..151 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_055246" FT VARIANT 39 FT /note="G -> E (in allele MICB*001; dbSNP:rs45578846)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334" FT /id="VAR_044068" FT VARIANT 68 FT /note="P -> H (in allele MICB*011; dbSNP:rs45583740)" FT /id="VAR_044069" FT VARIANT 75 FT /note="N -> D (in allele MICB*001, allele MICB*002, allele FT MICB*003, allele MICB*005, allele MICB*006, allele FT MICB*007, allele MICB*008, allele MICB*010, allele FT MICB*011, allele MICB*012, allele MICB*013, allele FT MICB*014, allele MICB*015, allele MICB*016, allele FT MICB*018, allele MICB*019 and allele MICB*022; FT dbSNP:rs3131639)" FT /id="VAR_044070" FT VARIANT 80 FT /note="K -> E (in allele MICB*002, allele MICB*007, allele FT MICB*008, allele MICB*014, allele MICB*015, allele FT MICB*016, allele MICB*019 and allele MICB*022; FT dbSNP:rs1065075)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334" FT /id="VAR_044071" FT VARIANT 88 FT /note="D -> G (in allele MICB*022; dbSNP:rs45486091)" FT /id="VAR_044072" FT VARIANT 105 FT /note="D -> G (in allele MICB*012; dbSNP:rs45502297)" FT /id="VAR_044073" FT VARIANT 121 FT /note="I -> M (in allele MICB*008; dbSNP:rs3134900)" FT /id="VAR_044074" FT VARIANT 136 FT /note="D -> H (in dbSNP:rs1051788)" FT /id="VAR_059527" FT VARIANT 136 FT /note="D -> N (in allele MICB*002, allele MICB*007, allele FT MICB*008, allele MICB*014, allele MICB*015, allele FT MICB*018, allele MICB*020 and allele MICB*022; FT dbSNP:rs1051788)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_044075" FT VARIANT 212 FT /note="T -> I (in allele MICB*003; dbSNP:rs41293883)" FT /id="VAR_044076" FT VARIANT 215 FT /note="E -> K (in allele MICB*006 and allele MICB*015; FT dbSNP:rs45624537)" FT /id="VAR_044077" FT VARIANT 279 FT /note="R -> K (in allele MICB*007; dbSNP:rs45587032)" FT /id="VAR_044078" FT VARIANT 291 FT /note="G -> S (in allele MICB*013, allele MICB*014, allele FT MICB*015 and allele MICB*016; dbSNP:rs41273040)" FT /id="VAR_044079" FT VARIANT 300 FT /note="A -> V (in allele MICB*001, allele MICB*016, allele FT MICB*018, allele MICB*019, allele MICB*020 and allele FT MICB*022; dbSNP:rs45470602)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334" FT /id="VAR_044080" FT VARIANT 383 FT /note="T -> A (in allele MICB*001, allele MICB*002, allele FT MICB*005, allele MICB*006, allele MICB*007, allele FT MICB*008, allele MICB*012, allele MICB*013, allele FT MICB*014, allele MICB*015, allele MICB*016, allele FT MICB*018, allele MICB*019, allele MICB*020 and allele FT MICB*022; dbSNP:rs1065076)" FT /id="VAR_044081" FT STRAND 26..37 FT /evidence="ECO:0007829|PDB:2WY3" FT STRAND 46..51 FT /evidence="ECO:0007829|PDB:2WY3" FT STRAND 54..60 FT /evidence="ECO:0007829|PDB:2WY3" FT TURN 61..64 FT /evidence="ECO:0007829|PDB:2WY3" FT STRAND 65..68 FT /evidence="ECO:0007829|PDB:2WY3" FT HELIX 71..75 FT /evidence="ECO:0007829|PDB:2WY3" FT HELIX 80..101 FT /evidence="ECO:0007829|PDB:2WY3" FT STRAND 104..106 FT /evidence="ECO:0007829|PDB:1JE6" FT STRAND 109..121 FT /evidence="ECO:0007829|PDB:2WY3" FT STRAND 123..125 FT /evidence="ECO:0007829|PDB:1JE6" FT STRAND 127..135 FT /evidence="ECO:0007829|PDB:2WY3" FT STRAND 138..144 FT /evidence="ECO:0007829|PDB:2WY3" FT TURN 145..147 FT /evidence="ECO:0007829|PDB:2WY3" FT HELIX 156..170 FT /evidence="ECO:0007829|PDB:2WY3" FT HELIX 176..197 FT /evidence="ECO:0007829|PDB:2WY3" FT HELIX 201..203 FT /evidence="ECO:0007829|PDB:1JE6" FT STRAND 208..214 FT /evidence="ECO:0007829|PDB:1JE6" FT STRAND 218..233 FT /evidence="ECO:0007829|PDB:1JE6" FT STRAND 236..241 FT /evidence="ECO:0007829|PDB:1JE6" FT STRAND 250..253 FT /evidence="ECO:0007829|PDB:1JE6" FT STRAND 264..273 FT /evidence="ECO:0007829|PDB:1JE6" FT HELIX 277..279 FT /evidence="ECO:0007829|PDB:1JE6" FT STRAND 280..286 FT /evidence="ECO:0007829|PDB:1JE6" FT STRAND 289..294 FT /evidence="ECO:0007829|PDB:1JE6" SQ SEQUENCE 383 AA; 42575 MW; 1309E571B48CDF9C CRC64; MGLGRVLLFL AVAFPFAPPA AAAEPHSLRY NLMVLSQDGS VQSGFLAEGH LDGQPFLRYD RQKRRAKPQG QWAENVLGAK TWDTETEDLT ENGQDLRRTL THIKDQKGGL HSLQEIRVCE IHEDSSTRGS RHFYYDGELF LSQNLETQES TVPQSSRAQT LAMNVTNFWK EDAMKTKTHY RAMQADCLQK LQRYLKSGVA IRRTVPPMVN VTCSEVSEGN ITVTCRASSF YPRNITLTWR QDGVSLSHNT QQWGDVLPDG NGTYQTWVAT RIRQGEEQRF TCYMEHSGNH GTHPVPSGKA LVLQSQRTDF PYVSAAMPCF VIIIILCVPC CKKKTSAAEG PELVSLQVLD QHPVGTGDHR DAAQLGFQPL MSATGSTGST EGT //