CRBB3_HUMAN
ID CRBB3_HUMAN Reviewed; 211 AA.
AC P26998; Q3B7S9; Q3T1B7; Q6ISK6; Q92965; Q9UH09;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 4.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Beta-crystallin B3;
DE AltName: Full=Beta-B3 crystallin;
DE Contains:
DE RecName: Full=Beta-crystallin B3, N-terminally processed;
GN Name=CRYBB3; Synonyms=CRYB3;
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 [LARGE SCALE MRNA], AND VARIANT ASP-113.
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLN-105 AND ASP-113.
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-103, ACETYLATION AT MET-1, AND MASS
RP 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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 66-211, AND VARIANT ASP-113.
RC TISSUE=Lens;
RX PubMed=2499686; DOI=10.1007/bf02103427;
RA Aarts H.J.M., Jacobs E.H.M., van Willigen G., Lubsen N.H.,
RA Schoenmakers J.G.G.;
RT "Different evolution rates within the lens-specific beta-crystallin gene
RT family.";
RL J. Mol. Evol. 28:313-321(1989).
RN [6]
RP VARIANT CTRCT22 ARG-165.
RX PubMed=15914629; DOI=10.1167/iovs.04-1481;
RA Riazuddin S.A., Yasmeen A., Yao W., Sergeev Y.V., Zhang Q., Zulfiqar F.,
RA Riaz A., Riazuddin S., Hejtmancik J.F.;
RT "Mutations in betaB3-crystallin associated with autosomal recessive
RT cataract in two Pakistani families.";
RL Invest. Ophthalmol. Vis. Sci. 46:2100-2106(2005).
RN [7]
RP VARIANT CTRCT22 HIS-75.
RX PubMed=19182255; DOI=10.1167/iovs.08-3149;
RA Hansen L., Mikkelsen A., Nuernberg P., Nuernberg G., Anjum I., Eiberg H.,
RA Rosenberg T.;
RT "Comprehensive mutational screening in a cohort of Danish families with
RT hereditary congenital cataract.";
RL Invest. Ophthalmol. Vis. Sci. 50:3291-3303(2009).
RN [8]
RP VARIANT CTRCT22 GLU-194.
RX PubMed=23508780; DOI=10.1007/s00439-013-1289-0;
RA Reis L.M., Tyler R.C., Muheisen S., Raggio V., Salviati L., Han D.P.,
RA Costakos D., Yonath H., Hall S., Power P., Semina E.V.;
RT "Whole exome sequencing in dominant cataract identifies a new causative
RT factor, CRYBA2, and a variety of novel alleles in known genes.";
RL Hum. Genet. 132:761-770(2013).
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 P26998; P55212: CASP6; NbExp=3; IntAct=EBI-1965681, EBI-718729;
CC P26998; P02489: CRYAA; NbExp=3; IntAct=EBI-1965681, EBI-6875961;
CC P26998; P05813: CRYBA1; NbExp=6; IntAct=EBI-1965681, EBI-7043337;
CC P26998; Q6PKX4: DOK6; NbExp=3; IntAct=EBI-1965681, EBI-2880244;
CC P26998; Q14204: DYNC1H1; NbExp=3; IntAct=EBI-1965681, EBI-356015;
CC P26998; P13473-2: LAMP2; NbExp=3; IntAct=EBI-1965681, EBI-21591415;
CC P26998; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-1965681, EBI-5280197;
CC -!- DOMAIN: Has a two-domain beta-structure, folded into four very similar
CC Greek key motifs.
CC -!- MASS SPECTROMETRY: [Beta-crystallin B3]: Mass=24222; Mass_error=3;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:8999933};
CC -!- DISEASE: Cataract 22, multiple types (CTRCT22) [MIM:609741]: 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. In general, the more posteriorly located and
CC dense an opacity, the greater the impact on visual function. CTRCT22
CC includes nuclear cataract among others. Nuclear cataracts affect the
CC central nucleus of the eye, and are often not highly visually
CC significant. The density of the opacities varies greatly from fine dots
CC to a dense, white and chalk-like, central cataract. The condition is
CC usually bilateral. Nuclear cataracts are often combined with opacified
CC cortical fibers encircling the nuclear opacity, which are referred to
CC as cortical riders. {ECO:0000269|PubMed:15914629,
CC ECO:0000269|PubMed:19182255, ECO:0000269|PubMed:23508780}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the beta/gamma-crystallin family. {ECO:0000305}.
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DR EMBL; CR456427; CAG30313.1; -; mRNA.
DR EMBL; Z99916; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC069479; AAH69479.2; -; mRNA.
DR EMBL; BC102021; AAI02022.1; -; mRNA.
DR EMBL; BC102022; AAI02023.1; -; mRNA.
DR EMBL; BC107482; AAI07483.1; -; mRNA.
DR EMBL; U71216; AAC50972.1; -; mRNA.
DR EMBL; X15144; CAA33242.2; -; Genomic_DNA.
DR EMBL; X15145; CAA33242.2; JOINED; Genomic_DNA.
DR EMBL; X15146; CAA33242.2; JOINED; Genomic_DNA.
DR CCDS; CCDS13830.1; -.
DR PIR; S10089; S10089.
DR RefSeq; NP_004067.1; NM_004076.4.
DR PDB; 3QK3; X-ray; 1.95 A; A/B/C=21-199.
DR PDBsum; 3QK3; -.
DR AlphaFoldDB; P26998; -.
DR SMR; P26998; -.
DR BioGRID; 107807; 83.
DR IntAct; P26998; 11.
DR MINT; P26998; -.
DR STRING; 9606.ENSP00000215855; -.
DR iPTMnet; P26998; -.
DR PhosphoSitePlus; P26998; -.
DR BioMuta; CRYBB3; -.
DR DMDM; 311033476; -.
DR MassIVE; P26998; -.
DR PaxDb; P26998; -.
DR PeptideAtlas; P26998; -.
DR PRIDE; P26998; -.
DR ProteomicsDB; 54372; -.
DR Antibodypedia; 24112; 124 antibodies from 21 providers.
DR DNASU; 1417; -.
DR Ensembl; ENST00000215855.7; ENSP00000215855.2; ENSG00000100053.10.
DR GeneID; 1417; -.
DR KEGG; hsa:1417; -.
DR MANE-Select; ENST00000215855.7; ENSP00000215855.2; NM_004076.5; NP_004067.1.
DR UCSC; uc003abo.3; human.
DR CTD; 1417; -.
DR DisGeNET; 1417; -.
DR GeneCards; CRYBB3; -.
DR HGNC; HGNC:2400; CRYBB3.
DR HPA; ENSG00000100053; Low tissue specificity.
DR MalaCards; CRYBB3; -.
DR MIM; 123630; gene.
DR MIM; 609741; phenotype.
DR neXtProt; NX_P26998; -.
DR OpenTargets; ENSG00000100053; -.
DR Orphanet; 98988; Early-onset anterior polar cataract.
DR Orphanet; 98991; Early-onset nuclear cataract.
DR PharmGKB; PA26914; -.
DR VEuPathDB; HostDB:ENSG00000100053; -.
DR eggNOG; ENOG502QTNZ; Eukaryota.
DR GeneTree; ENSGT00940000158425; -.
DR HOGENOM; CLU_081883_0_1_1; -.
DR InParanoid; P26998; -.
DR OMA; NEWNASQ; -.
DR OrthoDB; 1237607at2759; -.
DR PhylomeDB; P26998; -.
DR TreeFam; TF331401; -.
DR PathwayCommons; P26998; -.
DR SignaLink; P26998; -.
DR SIGNOR; P26998; -.
DR BioGRID-ORCS; 1417; 18 hits in 1069 CRISPR screens.
DR GeneWiki; CRYBB3; -.
DR GenomeRNAi; 1417; -.
DR Pharos; P26998; Tbio.
DR PRO; PR:P26998; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; P26998; protein.
DR Bgee; ENSG00000100053; Expressed in mucosa of transverse colon and 104 other tissues.
DR ExpressionAtlas; P26998; baseline and differential.
DR Genevisible; P26998; HS.
DR GO; GO:0005212; F:structural constituent of eye lens; IBA:GO_Central.
DR GO; GO:0002088; P:lens development in camera-type eye; IBA:GO_Central.
DR GO; GO:0007601; P:visual perception; IBA:GO_Central.
DR InterPro; IPR001064; Beta/gamma_crystallin.
DR InterPro; IPR033115; CRYBB3.
DR InterPro; IPR011024; G_crystallin-like.
DR PANTHER; PTHR11818:SF13; PTHR11818:SF13; 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; Disease variant; Eye lens protein;
KW Reference proteome; Repeat.
FT CHAIN 1..211
FT /note="Beta-crystallin B3"
FT /id="PRO_0000057560"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P02524"
FT CHAIN 2..211
FT /note="Beta-crystallin B3, N-terminally processed"
FT /id="PRO_0000421774"
FT DOMAIN 24..63
FT /note="Beta/gamma crystallin 'Greek key' 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 64..108
FT /note="Beta/gamma crystallin 'Greek key' 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 114..155
FT /note="Beta/gamma crystallin 'Greek key' 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 156..198
FT /note="Beta/gamma crystallin 'Greek key' 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT REGION 2..23
FT /note="N-terminal arm"
FT REGION 109..113
FT /note="Connecting peptide"
FT REGION 200..211
FT /note="C-terminal arm"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:8999933"
FT MOD_RES 2
FT /note="N-acetylalanine; in Beta-crystallin B3, N-terminally
FT processed"
FT /evidence="ECO:0000250|UniProtKB:P02524"
FT VARIANT 75
FT /note="R -> H (in CTRCT22; unknown pathological
FT significance; dbSNP:rs183587921)"
FT /evidence="ECO:0000269|PubMed:19182255"
FT /id="VAR_084792"
FT VARIANT 105
FT /note="R -> Q (in dbSNP:rs17670506)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_025277"
FT VARIANT 113
FT /note="H -> D (in dbSNP:rs9608378)"
FT /evidence="ECO:0000269|PubMed:15461802,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:2499686"
FT /id="VAR_025278"
FT VARIANT 159
FT /note="V -> I (in dbSNP:rs4455261)"
FT /id="VAR_025279"
FT VARIANT 165
FT /note="G -> R (in CTRCT22; dbSNP:rs74315490)"
FT /evidence="ECO:0000269|PubMed:15914629"
FT /id="VAR_025280"
FT VARIANT 194
FT /note="V -> E (in CTRCT22; dbSNP:rs587777601)"
FT /evidence="ECO:0000269|PubMed:23508780"
FT /id="VAR_070031"
FT CONFLICT 130
FT /note="E -> D (in Ref. 5; CAA33242)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="F -> L (in Ref. 5; CAA33242)"
FT /evidence="ECO:0000305"
FT STRAND 25..31
FT /evidence="ECO:0007829|PDB:3QK3"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:3QK3"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:3QK3"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:3QK3"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:3QK3"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:3QK3"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:3QK3"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:3QK3"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:3QK3"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:3QK3"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:3QK3"
FT STRAND 115..121
FT /evidence="ECO:0007829|PDB:3QK3"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:3QK3"
FT STRAND 125..133
FT /evidence="ECO:0007829|PDB:3QK3"
FT HELIX 139..142
FT /evidence="ECO:0007829|PDB:3QK3"
FT STRAND 150..156
FT /evidence="ECO:0007829|PDB:3QK3"
FT STRAND 158..163
FT /evidence="ECO:0007829|PDB:3QK3"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:3QK3"
FT STRAND 167..173
FT /evidence="ECO:0007829|PDB:3QK3"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:3QK3"
FT HELIX 181..184
FT /evidence="ECO:0007829|PDB:3QK3"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:3QK3"
SQ SEQUENCE 211 AA; 24252 MW; E5ABA1165C7B45BA CRC64;
MAEQHGAPEQ AAAGKSHGDL GGSYKVILYE LENFQGKRCE LSAECPSLTD SLLEKVGSIQ
VESGPWLAFE SRAFRGEQFV LEKGDYPRWD AWSNSRDSDS LLSLRPLNID SPHHKLHLFE
NPAFSGRKME IVDDDVPSLW AHGFQDRVAS VRAINGTWVG YEFPGYRGRQ YVFERGEYRH
WNEWDASQPQ LQSVRRIRDQ KWHKRGRFPS S
