CRBB2_HUMAN
ID CRBB2_HUMAN Reviewed; 205 AA.
AC P43320; Q9UCM8;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Beta-crystallin B2;
DE AltName: Full=Beta-B2 crystallin;
DE AltName: Full=Beta-crystallin Bp;
GN Name=CRYBB2; Synonyms=CRYB2, CRYB2A;
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].
RC TISSUE=Lens;
RX PubMed=8224918; DOI=10.1016/0378-1119(93)90655-m;
RA Chambers C., Russell P.;
RT "Sequence of the human lens beta B2-crystallin-encoding cDNA.";
RL Gene 133:295-299(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INVOLVEMENT IN CTRCT3.
RX PubMed=9158139; DOI=10.1093/hmg/6.5.665;
RA Litt M., Carrero-Valenzuela R., Lamorticella D.M., Schultz D.W.,
RA Mitchell T.N., Kramer P., Maumenee I.H.;
RT "Autosomal dominant cerulean cataract is associated with a chain
RT termination mutation in the human beta-crystallin gene CRYBB2.";
RL Hum. Mol. Genet. 6:665-668(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 PROTEIN SEQUENCE OF 2-205, CLEAVAGE OF INITIATOR METHIONINE, AND
RP ACETYLATION AT ALA-2.
RC TISSUE=Lens;
RX PubMed=8443605; DOI=10.1002/pro.5560020217;
RA Miesbauer L.R., Smith J.B., Smith D.L.;
RT "Amino acid sequence of human lens beta B2-crystallin.";
RL Protein Sci. 2:290-291(1993).
RN [7]
RP PROTEIN SEQUENCE OF 192-205, AND MASS SPECTROMETRY.
RX PubMed=8999933; DOI=10.1074/jbc.272.4.2268;
RA Lampi K.J., Ma Z., Shih M., Shearer T.R., Smith J.B., Smith D.L.,
RA David L.L.;
RT "Sequence analysis of betaA3, betaB3, and betaA4 crystallins completes the
RT identification of the major proteins in young human lens.";
RL J. Biol. Chem. 272:2268-2275(1997).
RN [8]
RP PROTEIN SEQUENCE OF 123-142.
RC TISSUE=Lens;
RX PubMed=1521468; DOI=10.3109/02713689209000740;
RA Datiles M.B., Schumer D.J., Zigler J.S. Jr., Russell P., Anderson L.,
RA Garland D.;
RT "Two-dimensional gel electrophoretic analysis of human lens proteins.";
RL Curr. Eye Res. 11:669-677(1992).
RN [9]
RP MASS SPECTROMETRY.
RX PubMed=8175657; DOI=10.1016/s0021-9258(18)99902-3;
RA Miesbauer L.R., Zhou X., Yang Z., Yang Z., Sun Y., Smith D.L., Smith J.B.;
RT "Post-translational modifications of water-soluble human lens crystallins
RT from young adults.";
RL J. Biol. Chem. 269:12494-12502(1994).
RN [10]
RP MASS SPECTROMETRY.
RX PubMed=10930324; DOI=10.1006/exer.2000.0868;
RA Hanson S.R.A., Hasan A., Smith D.L., Smith J.B.;
RT "The major in vivo modifications of the human water-insoluble lens
RT crystallins are disulfide bonds, deamidation, methionine oxidation and
RT backbone cleavage.";
RL Exp. Eye Res. 71:195-207(2000).
RN [11]
RP INVOLVEMENT IN CTRCT3.
RX PubMed=10634616;
RA Gill D., Klose R., Munier F.L., McFadden M., Priston M., Billingsley G.,
RA Ducrey N., Schorderet D.F., Heon E.;
RT "Genetic heterogeneity of the Coppock-like cataract: a mutation in CRYBB2
RT on chromosome 22q11.2.";
RL Invest. Ophthalmol. Vis. Sci. 41:159-165(2000).
RN [12]
RP VARIANTS CTRCT3 LEU-188 AND 155-GLN--ASN-205 DEL.
RX PubMed=28839118; DOI=10.1534/g3.117.300109;
RA Javadiyan S., Craig J.E., Souzeau E., Sharma S., Lower K.M., Mackey D.A.,
RA Staffieri S.E., Elder J.E., Taranath D., Straga T., Black J., Pater J.,
RA Casey T., Hewitt A.W., Burdon K.P.;
RT "High-Throughput Genetic Screening of 51 Pediatric Cataract Genes
RT Identifies Causative Mutations in Inherited Pediatric Cataract in South
RT Eastern Australia.";
RL G3 (Bethesda) 7:3257-3268(2017).
RN [13]
RP VARIANT CTRCT3 VAL-149.
RX PubMed=29386872;
RA Sun Z., Zhou Q., Li H., Yang L., Wu S., Sui R.;
RT "Mutations in crystallin genes result in congenital cataract associated
RT with other ocular abnormalities.";
RL Mol. Vis. 23:977-986(2017).
RN [14]
RP VARIANT CTRCT3 LEU-146.
RX PubMed=29259299; DOI=10.1038/s41598-017-18222-z;
RA Li L., Fan D.B., Zhao Y.T., Li Y., Kong D.Q., Cai F.F., Zheng G.Y.;
RT "Two novel mutations identified in ADCC families impair crystallin protein
RT distribution and induce apoptosis in human lens epithelial cells.";
RL Sci. Rep. 7:17848-17848(2017).
RN [15]
RP VARIANT CTRCT3 LYS-155.
RX PubMed=31523120;
RA Zhuang J., Cao Z., Zhu Y., Liu L., Tong Y., Chen X., Wang Y., Lu C., Ma X.,
RA Yang J.;
RT "Mutation screening of crystallin genes in Chinese families with congenital
RT cataracts.";
RL Mol. Vis. 25:427-437(2019).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 2-205, SUBUNIT, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RX PubMed=17327390; DOI=10.1110/ps.062659107;
RA Smith M.A., Bateman O.A., Jaenicke R., Slingsby C.;
RT "Mutation of interfaces in domain-swapped human betaB2-crystallin.";
RL Protein Sci. 16:615-625(2007).
CC -!- FUNCTION: Crystallins are the dominant structural components of the
CC vertebrate eye lens.
CC -!- SUBUNIT: Homo/heterodimer, or complexes of higher-order. The structure
CC of beta-crystallin oligomers seems to be stabilized through
CC interactions between the N-terminal arms (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC P43320; P05813: CRYBA1; NbExp=3; IntAct=EBI-974082, EBI-7043337;
CC P43320; P43320: CRYBB2; NbExp=5; IntAct=EBI-974082, EBI-974082;
CC P43320; P61968: LMO4; NbExp=3; IntAct=EBI-974082, EBI-2798728;
CC -!- DOMAIN: Has a two-domain beta-structure, folded into four very similar
CC Greek key motifs.
CC -!- MASS SPECTROMETRY: Mass=23291; Mass_error=3; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8999933};
CC -!- MASS SPECTROMETRY: Mass=23289; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8175657};
CC -!- MASS SPECTROMETRY: Mass=23290; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10930324};
CC -!- DISEASE: Cataract 3, multiple types (CTRCT3) [MIM:601547]: An
CC opacification of the crystalline lens of the eye that frequently
CC results in visual impairment or blindness. Opacities vary in
CC morphology, are often confined to a portion of the lens, and may be
CC static or progressive. CTRCT3 includes congenital cerulean and sutural
CC cataract with punctate and cerulean opacities, among others. Cerulean
CC cataract is characterized by peripheral bluish and white opacifications
CC organized in concentric layers with occasional central lesions arranged
CC radially. The opacities are observed in the superficial layers of the
CC fetal nucleus as well as the adult nucleus of the lens. Involvement is
CC usually bilateral. Visual acuity is only mildly reduced in childhood.
CC In adulthood, the opacifications may progress, making lens extraction
CC necessary. Histologically the lesions are described as fusiform
CC cavities between lens fibers which contain a deeply staining granular
CC material. Although the lesions may take on various colors, a dull blue
CC is the most common appearance and is responsible for the designation
CC cerulean cataract. Sutural cataract with punctate and cerulean
CC opacities is characterized by white opacification around the anterior
CC and posterior Y sutures, and grayish and bluish, spindle shaped, oval
CC punctate and cerulean opacities of various sizes arranged in lamellar
CC form. The spots are more concentrated towards the peripheral layers and
CC do not delineate the embryonal or fetal nucleus. Phenotypic variation
CC with respect to the size and density of the sutural opacities as well
CC as the number and position of punctate and cerulean spots is observed
CC among affected subjects. {ECO:0000269|PubMed:10634616,
CC ECO:0000269|PubMed:28839118, ECO:0000269|PubMed:29259299,
CC ECO:0000269|PubMed:29386872, ECO:0000269|PubMed:31523120,
CC ECO:0000269|PubMed:9158139}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the beta/gamma-crystallin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Eye disease Crystallin, beta-B2 (CRYBB2);
CC Note=Leiden Open Variation Database (LOVD);
CC URL="https://databases.lovd.nl/shared/genes/CRYBB2";
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DR EMBL; L10035; AAA16864.1; -; mRNA.
DR EMBL; U72404; AAB39700.1; -; Genomic_DNA.
DR EMBL; U72400; AAB39700.1; JOINED; Genomic_DNA.
DR EMBL; U72401; AAB39700.1; JOINED; Genomic_DNA.
DR EMBL; U72402; AAB39700.1; JOINED; Genomic_DNA.
DR EMBL; U72403; AAB39700.1; JOINED; Genomic_DNA.
DR EMBL; CR456426; CAG30312.1; -; mRNA.
DR EMBL; Z99916; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC069535; AAH69535.1; -; mRNA.
DR CCDS; CCDS13831.1; -.
DR PIR; JC2009; JC2009.
DR RefSeq; NP_000487.1; NM_000496.2.
DR RefSeq; XP_006724204.1; XM_006724141.3.
DR RefSeq; XP_011528202.1; XM_011529900.2.
DR PDB; 1YTQ; X-ray; 1.70 A; A=2-205.
DR PDB; 7K7U; X-ray; 3.03 A; A/B/C/D/E/F/G/H/I/J/K/L=1-205.
DR PDBsum; 1YTQ; -.
DR PDBsum; 7K7U; -.
DR AlphaFoldDB; P43320; -.
DR PCDDB; P43320; -.
DR SASBDB; P43320; -.
DR SMR; P43320; -.
DR BioGRID; 107805; 8.
DR IntAct; P43320; 7.
DR MINT; P43320; -.
DR STRING; 9606.ENSP00000381273; -.
DR ChEMBL; CHEMBL4296284; -.
DR iPTMnet; P43320; -.
DR PhosphoSitePlus; P43320; -.
DR BioMuta; CRYBB2; -.
DR DMDM; 1169091; -.
DR MassIVE; P43320; -.
DR PaxDb; P43320; -.
DR PeptideAtlas; P43320; -.
DR PRIDE; P43320; -.
DR ProteomicsDB; 55612; -.
DR Antibodypedia; 35320; 127 antibodies from 24 providers.
DR DNASU; 1415; -.
DR Ensembl; ENST00000398215.3; ENSP00000381273.2; ENSG00000244752.3.
DR Ensembl; ENST00000651629.1; ENSP00000498905.1; ENSG00000244752.3.
DR GeneID; 1415; -.
DR KEGG; hsa:1415; -.
DR MANE-Select; ENST00000398215.3; ENSP00000381273.2; NM_000496.3; NP_000487.1.
DR CTD; 1415; -.
DR DisGeNET; 1415; -.
DR GeneCards; CRYBB2; -.
DR HGNC; HGNC:2398; CRYBB2.
DR HPA; ENSG00000244752; Tissue enhanced (brain).
DR MalaCards; CRYBB2; -.
DR MIM; 123620; gene.
DR MIM; 601547; phenotype.
DR neXtProt; NX_P43320; -.
DR OpenTargets; ENSG00000244752; -.
DR Orphanet; 1377; Cataract-microcornea syndrome.
DR Orphanet; 98989; Cerulean cataract.
DR Orphanet; 98991; Early-onset nuclear cataract.
DR Orphanet; 441447; Early-onset posterior subcapsular cataract.
DR Orphanet; 98985; Early-onset sutural cataract.
DR Orphanet; 98984; Pulverulent cataract.
DR Orphanet; 98994; Total early-onset cataract.
DR PharmGKB; PA26912; -.
DR VEuPathDB; HostDB:ENSG00000244752; -.
DR eggNOG; ENOG502QVM6; Eukaryota.
DR GeneTree; ENSGT00940000160048; -.
DR HOGENOM; CLU_081883_0_1_1; -.
DR InParanoid; P43320; -.
DR OMA; TWVAYQY; -.
DR OrthoDB; 1237607at2759; -.
DR PhylomeDB; P43320; -.
DR TreeFam; TF331401; -.
DR PathwayCommons; P43320; -.
DR SignaLink; P43320; -.
DR SIGNOR; P43320; -.
DR BioGRID-ORCS; 1415; 9 hits in 1074 CRISPR screens.
DR ChiTaRS; CRYBB2; human.
DR EvolutionaryTrace; P43320; -.
DR GeneWiki; CRYBB2; -.
DR GenomeRNAi; 1415; -.
DR Pharos; P43320; Tbio.
DR PRO; PR:P43320; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; P43320; protein.
DR Bgee; ENSG00000244752; Expressed in stromal cell of endometrium and 114 other tissues.
DR ExpressionAtlas; P43320; baseline and differential.
DR Genevisible; P43320; HS.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005212; F:structural constituent of eye lens; IBA:GO_Central.
DR GO; GO:0005198; F:structural molecule activity; NAS:ProtInc.
DR GO; GO:0002088; P:lens development in camera-type eye; IBA:GO_Central.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0007601; P:visual perception; IBA:GO_Central.
DR InterPro; IPR001064; Beta/gamma_crystallin.
DR InterPro; IPR033058; CRYBB2.
DR InterPro; IPR011024; G_crystallin-like.
DR PANTHER; PTHR11818:SF11; PTHR11818:SF11; 1.
DR Pfam; PF00030; Crystall; 2.
DR PRINTS; PR01367; BGCRYSTALLIN.
DR SMART; SM00247; XTALbg; 2.
DR SUPFAM; SSF49695; SSF49695; 1.
DR PROSITE; PS50915; CRYSTALLIN_BETA_GAMMA; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cataract; Direct protein sequencing;
KW Disease variant; Eye lens protein; Reference proteome; Repeat;
KW Sensory transduction; Vision.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8443605"
FT CHAIN 2..205
FT /note="Beta-crystallin B2"
FT /id="PRO_0000057553"
FT DOMAIN 17..56
FT /note="Beta/gamma crystallin 'Greek key' 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 57..101
FT /note="Beta/gamma crystallin 'Greek key' 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 107..148
FT /note="Beta/gamma crystallin 'Greek key' 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 149..191
FT /note="Beta/gamma crystallin 'Greek key' 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT REGION 2..16
FT /note="N-terminal arm"
FT REGION 102..106
FT /note="Connecting peptide"
FT REGION 193..205
FT /note="C-terminal arm"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:8443605"
FT VARIANT 65
FT /note="A -> S (in dbSNP:rs16986560)"
FT /id="VAR_038431"
FT VARIANT 146
FT /note="V -> L (in CTRCT3; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:29259299"
FT /id="VAR_084787"
FT VARIANT 149
FT /note="G -> V (in CTRCT3; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:29386872"
FT /id="VAR_084788"
FT VARIANT 155..205
FT /note="Missing (in CTRCT3)"
FT /evidence="ECO:0000269|PubMed:28839118"
FT /id="VAR_084789"
FT VARIANT 155
FT /note="Q -> K (in CTRCT3; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31523120"
FT /id="VAR_084790"
FT VARIANT 188
FT /note="R -> L (in CTRCT3; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:28839118"
FT /id="VAR_084791"
FT STRAND 18..24
FT /evidence="ECO:0007829|PDB:1YTQ"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:1YTQ"
FT HELIX 41..44
FT /evidence="ECO:0007829|PDB:1YTQ"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:1YTQ"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:1YTQ"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:1YTQ"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:1YTQ"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:1YTQ"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:1YTQ"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:1YTQ"
FT STRAND 108..114
FT /evidence="ECO:0007829|PDB:1YTQ"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:1YTQ"
FT STRAND 118..127
FT /evidence="ECO:0007829|PDB:1YTQ"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:1YTQ"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:1YTQ"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:1YTQ"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:1YTQ"
FT STRAND 160..166
FT /evidence="ECO:0007829|PDB:1YTQ"
FT STRAND 168..171
FT /evidence="ECO:0007829|PDB:1YTQ"
FT HELIX 174..177
FT /evidence="ECO:0007829|PDB:1YTQ"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:1YTQ"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:1YTQ"
SQ SEQUENCE 205 AA; 23380 MW; FD95C354724A67D0 CRC64;
MASDHQTQAG KPQSLNPKII IFEQENFQGH SHELNGPCPN LKETGVEKAG SVLVQAGPWV
GYEQANCKGE QFVFEKGEYP RWDSWTSSRR TDSLSSLRPI KVDSQEHKII LYENPNFTGK
KMEIIDDDVP SFHAHGYQEK VSSVRVQSGT WVGYQYPGYR GLQYLLEKGD YKDSSDFGAP
HPQVQSVRRI RDMQWHQRGA FHPSN
