MICB_HUMAN
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 03-AUG-2022, entry version 172.
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 ---------------------------------------------------------------------------
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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; 156.
DR CORUM; Q29980; -.
DR STRING; 9606.ENSP00000252229; -.
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; Q29980; -.
DR PeptideAtlas; Q29980; -.
DR PRIDE; Q29980; -.
DR ProteomicsDB; 3419; -.
DR ProteomicsDB; 389; -.
DR ProteomicsDB; 61282; -. [Q29980-1]
DR ProteomicsDB; 69573; -.
DR Antibodypedia; 27039; 313 antibodies from 28 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 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; ENSGT01040000240396; -.
DR InParanoid; Q29980; -.
DR OMA; WVATRIS; -.
DR OrthoDB; 1276422at2759; -.
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 1040 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 94 other tissues.
DR ExpressionAtlas; Q29980; baseline and differential.
DR Genevisible; Q29980; HS.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0046629; P:gamma-delta T cell activation; IDA:UniProtKB.
DR GO; GO:0002429; P:immune response-activating cell surface receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0050689; P:negative regulation of defense response to virus by host; IDA:UniProtKB.
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 Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.30.500.10; -; 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 Pfam; PF07654; C1-set; 1.
DR Pfam; PF00129; MHC_I; 1.
DR SMART; SM00407; IGc1; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF54452; SSF54452; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
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
