CRYAB_HUMAN
ID CRYAB_HUMAN Reviewed; 175 AA.
AC P02511; B0YIX0; O43416; Q9UC37; Q9UC38; Q9UC39; Q9UC40; Q9UC41;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 2.
DT 03-AUG-2022, entry version 242.
DE RecName: Full=Alpha-crystallin B chain;
DE AltName: Full=Alpha(B)-crystallin;
DE AltName: Full=Heat shock protein beta-5;
DE Short=HspB5;
DE AltName: Full=Renal carcinoma antigen NY-REN-27;
DE AltName: Full=Rosenthal fiber component;
GN Name=CRYAB {ECO:0000312|HGNC:HGNC:2389}; Synonyms=CRYA2, HSPB5;
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 PRELIMINARY PROTEIN SEQUENCE, TISSUE SPECIFICITY, AND ACETYLATION AT MET-1.
RX PubMed=838078; DOI=10.1016/0014-5793(77)80757-6;
RA Kramps J.A., de Man B.M., de Jong W.W.;
RT "The primary structure of the B2 chain of human alpha-crystallin.";
RL FEBS Lett. 74:82-84(1977).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=2387586; DOI=10.1016/0888-7543(90)90204-8;
RA Dubin R.A., Ally A.H., Chung S., Piatigorsky J.;
RT "Human alpha B-crystallin gene and preferential promoter function in
RT lens.";
RL Genomics 7:594-601(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1407707; DOI=10.1016/0304-3940(92)90689-5;
RA Iwaki A., Iwaki T., Goldman J.E., Ogomori K., Tateishi J., Sakaki Y.;
RT "Accumulation of alpha B-crystallin in brains of patients with Alexander's
RT disease is not due to an abnormality of the 5'-flanking and coding sequence
RT of the genomic DNA.";
RL Neurosci. Lett. 140:89-92(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Yu W., Sarginson J., Gibbs R.A.;
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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 [10]
RP PROTEIN SEQUENCE OF 2-24; 35-66 AND 118-175, AND ASSOCIATION WITH HSPB1.
RC TISSUE=Pectoralis muscle;
RX PubMed=1560006; DOI=10.1016/s0021-9258(18)42574-4;
RA Kato K., Shinohara H., Goto S., Inaguma Y., Morishita R., Asano T.;
RT "Copurification of small heat shock protein with alpha B crystallin from
RT human skeletal muscle.";
RL J. Biol. Chem. 267:7718-7725(1992).
RN [11]
RP PROTEIN SEQUENCE OF 57-66.
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 [12]
RP PROTEIN SEQUENCE OF 83-89 AND 164-172.
RC TISSUE=Heart;
RX PubMed=7498159; DOI=10.1002/elps.11501601192;
RA Kovalyov L.I., Shishkin S.S., Efimochkin A.S., Kovalyova M.A.,
RA Ershova E.S., Egorov T.A., Musalyamov A.K.;
RT "The major protein expression profile and two-dimensional protein database
RT of human heart.";
RL Electrophoresis 16:1160-1169(1995).
RN [13]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 107-175.
RX PubMed=2539261; DOI=10.1016/0092-8674(89)90173-6;
RA Iwaki T., Kume-Iwaki A., Liem R.K.H., Goldman J.E.;
RT "Alpha B-crystallin is expressed in non-lenticular tissues and accumulates
RT in Alexander's disease brain.";
RL Cell 57:71-78(1989).
RN [14]
RP RACEMIZATION/ISOMERIZATION OF SPECIFIC ASP, AND ACETYLATION AT MET-1.
RX PubMed=8142454; DOI=10.1016/0167-4838(94)90003-5;
RA Fujii N., Ishibashi Y., Satoh K., Fujino M., Harada K.;
RT "Simultaneous racemization and isomerization at specific aspartic acid
RT residues in alpha B-crystallin from the aged human lens.";
RL Biochim. Biophys. Acta 1204:157-163(1994).
RN [15]
RP PHOSPHORYLATION AT SER-19; SER-45 AND SER-59, AND 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 [16]
RP IDENTIFICATION AS A RENAL CANCER ANTIGEN.
RC TISSUE=Renal cell carcinoma;
RX PubMed=10508479;
RX DOI=10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5;
RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
RA Old L.J.;
RT "Antigens recognized by autologous antibody in patients with renal-cell
RT carcinoma.";
RL Int. J. Cancer 83:456-464(1999).
RN [17]
RP MASS SPECTROMETRY, SUSCEPTIBILITY TO OXIDATION, AND PHOSPHORYLATION.
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 [18]
RP INTERACTION WITH HSPBAP1.
RX PubMed=10751411; DOI=10.1074/jbc.m001981200;
RA Liu C., Gilmont R.R., Benndorf R., Welsh M.J.;
RT "Identification and characterization of a novel protein from Sertoli cells,
RT PASS1, that associates with mammalian small stress protein hsp27.";
RL J. Biol. Chem. 275:18724-18731(2000).
RN [19]
RP INVOLVEMENT IN CTRCT16.
RX PubMed=11577372; DOI=10.1086/324158;
RA Berry V., Francis P., Reddy M.A., Collyer D., Vithana E., MacKay I.,
RA Dawson G., Carey A.H., Moore A., Bhattacharya S.S., Quinlan R.A.;
RT "Alpha-B crystallin gene (CRYAB) mutation causes dominant congenital
RT posterior polar cataract in humans.";
RL Am. J. Hum. Genet. 69:1141-1145(2001).
RN [20]
RP PHOSPHORYLATION AT SER-45 AND SER-59.
RX PubMed=11158243; DOI=10.1046/j.1471-4159.2001.00038.x;
RA Kato K., Inaguma Y., Ito H., Iida K., Iwamoto I., Kamei K., Ochi N.,
RA Ohta H., Kishikawa M.;
RT "Ser-59 is the major phosphorylation site in alphaB-crystallin accumulated
RT in the brains of patients with Alexander's disease.";
RL J. Neurochem. 76:730-736(2001).
RN [21]
RP ACETYLATION AT LYS-92.
RX PubMed=11369851; DOI=10.1110/ps.40901;
RA Lapko V.N., Smith D.L., Smith J.B.;
RT "In vivo carbamylation and acetylation of water-soluble human lens alphaB-
RT crystallin lysine 92.";
RL Protein Sci. 10:1130-1136(2001).
RN [22]
RP INVOLVEMENT IN MFM2.
RX PubMed=14681890; DOI=10.1002/ana.10767;
RA Selcen D., Engel A.G.;
RT "Myofibrillar myopathy caused by novel dominant negative alpha B-crystallin
RT mutations.";
RL Ann. Neurol. 54:804-810(2003).
RN [23]
RP INTERACTION WITH TTN.
RX PubMed=14676215; DOI=10.1074/jbc.m307473200;
RA Bullard B., Ferguson C., Minajeva A., Leake M.C., Gautel M., Labeit D.,
RA Ding L., Labeit S., Horwitz J., Leonard K.R., Linke W.A.;
RT "Association of the chaperone alphaB-crystallin with titin in heart
RT muscle.";
RL J. Biol. Chem. 279:7917-7924(2004).
RN [24]
RP SUBCELLULAR LOCATION.
RX PubMed=19464326; DOI=10.1016/j.bbamcr.2009.05.005;
RA Vos M.J., Kanon B., Kampinga H.H.;
RT "HSPB7 is a SC35 speckle resident small heat shock protein.";
RL Biochim. Biophys. Acta 1793:1343-1353(2009).
RN [25]
RP SUBUNIT.
RX PubMed=20836128; DOI=10.1002/iub.373;
RA Srinivas P., Narahari A., Petrash J.M., Swamy M.J., Reddy G.B.;
RT "Importance of eye lens alpha-crystallin heteropolymer with 3:1 alphaA to
RT alphaB ratio: stability, aggregation, and modifications.";
RL IUBMB Life 62:693-702(2010).
RN [26]
RP INVOLVEMENT IN MFMFIH-CRYAB.
RX PubMed=21337604; DOI=10.1002/ana.22331;
RA Del Bigio M.R., Chudley A.E., Sarnat H.B., Campbell C., Goobie S.,
RA Chodirker B.N., Selcen D.;
RT "Infantile muscular dystrophy in Canadian aboriginals is an alphaB-
RT crystallinopathy.";
RL Ann. Neurol. 69:866-871(2011).
RN [27]
RP ACETYLATION AT LYS-92 AND LYS-166.
RX PubMed=22120592; DOI=10.1016/j.bbadis.2011.11.011;
RA Nagaraj R.H., Nahomi R.B., Shanthakumar S., Linetsky M., Padmanabha S.,
RA Pasupuleti N., Wang B., Santhoshkumar P., Panda A.K., Biswas A.;
RT "Acetylation of alphaA-crystallin in the human lens: effects on structure
RT and chaperone function.";
RL Biochim. Biophys. Acta 1822:120-129(2012).
RN [28]
RP SUBUNIT, AND ZINC-BINDING SITES.
RX PubMed=22890888; DOI=10.1007/s10930-012-9439-0;
RA Karmakar S., Das K.P.;
RT "Identification of histidine residues involved in Zn(2+) binding to
RT alphaA- and alphaB-Crystallin by chemical modification and MALDI TOF mass
RT spectrometry.";
RL Protein J. 31:623-640(2012).
RN [29]
RP INTERACTION WITH TMEM109.
RX PubMed=23542032; DOI=10.1016/j.febslet.2013.03.024;
RA Yamashita A., Taniwaki T., Kaikoi Y., Yamazaki T.;
RT "Protective role of the endoplasmic reticulum protein mitsugumin23 against
RT ultraviolet C-induced cell death.";
RL FEBS Lett. 587:1299-1303(2013).
RN [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [31]
RP INTERACTION WITH DES.
RX PubMed=28470624; DOI=10.1007/s12192-017-0788-7;
RA Sharma S., Conover G.M., Elliott J.L., Der Perng M., Herrmann H.,
RA Quinlan R.A.;
RT "alphaB-crystallin is a sensor for assembly intermediates and for the
RT subunit topology of desmin intermediate filaments.";
RL Cell Stress Chaperones 22:613-626(2017).
RN [32]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INVOLVEMENT IN RESTRICTIVE
RP CARDIOMYOPATHY, VARIANT GLY-109, AND CHARACTERIZATION OF VARIANT GLY-109
RP AND GLY-120.
RX PubMed=28493373; DOI=10.1002/humu.23248;
RA Brodehl A., Gaertner-Rommel A., Klauke B., Grewe S.A., Schirmer I.,
RA Peterschroeder A., Faber L., Vorgerd M., Gummert J., Anselmetti D.,
RA Schulz U., Paluszkiewicz L., Milting H.;
RT "The novel alphaB-crystallin (CRYAB) mutation p.D109G causes restrictive
RT cardiomyopathy.";
RL Hum. Mutat. 38:947-952(2017).
RN [33]
RP FUNCTION, AND INTERACTION WITH ATP6V1A AND MTOR.
RX PubMed=31786107; DOI=10.1016/j.bbagen.2019.129496;
RA Cui X., Feng R., Wang J., Du C., Pi X., Chen D., Li J., Li H., Zhang J.,
RA Zhang J., Mu H., Zhang F., Liu M., Hu Y.;
RT "Heat shock factor 4 regulates lysosome activity by modulating the alphaB-
RT crystallin-ATP6V1A-mTOR complex in ocular lens.";
RL Biochim. Biophys. Acta 1864:129496-129496(2020).
RN [34]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH TMED10.
RX PubMed=32272059; DOI=10.1016/j.cell.2020.03.031;
RA Zhang M., Liu L., Lin X., Wang Y., Li Y., Guo Q., Li S., Sun Y., Tao X.,
RA Zhang D., Lv X., Zheng L., Ge L.;
RT "A Translocation Pathway for Vesicle-Mediated Unconventional Protein
RT Secretion.";
RL Cell 181:637-652(2020).
RN [35]
RP X-RAY CRYSTALLOGRAPHY (2.63 ANGSTROMS) OF 67-157, AND HOMODIMERIZATION.
RX PubMed=19646995; DOI=10.1016/j.jmb.2009.07.069;
RA Bagneris C., Bateman O.A., Naylor C.E., Cronin N., Boelens W.C., Keep N.H.,
RA Slingsby C.;
RT "Crystal structures of alpha-crystallin domain dimers of alphaB-crystallin
RT and Hsp20.";
RL J. Mol. Biol. 392:1242-1252(2009).
RN [36]
RP VARIANT MFM2 GLY-120.
RX PubMed=9731540; DOI=10.1038/1765;
RA Vicart P., Caron A., Guicheney P., Li Z., Prevost M.-C., Faure A.,
RA Chateau D., Chapon F., Tome F., Dupret J.-M., Paulin D., Fardeau M.;
RT "A missense mutation in the alphaB-crystallin chaperone gene causes a
RT desmin-related myopathy.";
RL Nat. Genet. 20:92-95(1998).
RN [37]
RP CHARACTERIZATION OF VARIANTS MFM2 GLY-120.
RX PubMed=12601044; DOI=10.1167/iovs.02-0950;
RA Fu L., Liang J.J.-N.;
RT "Alteration of protein-protein interactions of congenital cataract
RT crystallin mutants.";
RL Invest. Ophthalmol. Vis. Sci. 44:1155-1159(2003).
RN [38]
RP VARIANT CMD1II HIS-157.
RX PubMed=16483541; DOI=10.1016/j.bbrc.2006.01.154;
RA Inagaki N., Hayashi T., Arimura T., Koga Y., Takahashi M., Shibata H.,
RA Teraoka K., Chikamori T., Yamashina A., Kimura A.;
RT "Alpha B-crystallin mutation in dilated cardiomyopathy.";
RL Biochem. Biophys. Res. Commun. 342:379-386(2006).
RN [39]
RP VARIANT CMD1II SER-154.
RX PubMed=16793013; DOI=10.1016/j.bbrc.2006.05.203;
RA Pilotto A., Marziliano N., Pasotti M., Grasso M., Costante A.M.,
RA Arbustini E.;
RT "alphaB-crystallin mutation in dilated cardiomyopathies: low prevalence in
RT a consecutive series of 200 unrelated probands.";
RL Biochem. Biophys. Res. Commun. 346:1115-1117(2006).
RN [40]
RP VARIANT CTRCT16 THR-171.
RX PubMed=18587492;
RA Devi R.R., Yao W., Vijayalakshmi P., Sergeev Y.V., Sundaresan P.,
RA Hejtmancik J.F.;
RT "Crystallin gene mutations in Indian families with inherited pediatric
RT cataract.";
RL Mol. Vis. 14:1157-1170(2008).
RN [41]
RP VARIANT CTRCT16 CYS-69.
RX PubMed=21866213;
RA Sun W., Xiao X., Li S., Guo X., Zhang Q.;
RT "Mutation analysis of 12 genes in Chinese families with congenital
RT cataracts.";
RL Mol. Vis. 17:2197-2206(2011).
RN [42]
RP VARIANT MFM2 HIS-109.
RX PubMed=21920752; DOI=10.1016/j.nmd.2011.07.004;
RA Sacconi S., Feasson L., Antoine J.C., Pecheux C., Bernard R., Cobo A.M.,
RA Casarin A., Salviati L., Desnuelle C., Urtizberea A.;
RT "A novel CRYAB mutation resulting in multisystemic disease.";
RL Neuromuscul. Disord. 22:66-72(2012).
CC -!- FUNCTION: May contribute to the transparency and refractive index of
CC the lens. Has chaperone-like activity, preventing aggregation of
CC various proteins under a wide range of stress conditions. In lens
CC epithelial cells, stabilizes the ATP6V1A protein, preventing its
CC degradation by the proteasome (By similarity).
CC {ECO:0000250|UniProtKB:P23927}.
CC -!- SUBUNIT: Heteromer composed of three CRYAA and one CRYAB subunits
CC (PubMed:20836128). Aggregates with homologous proteins, including the
CC small heat shock protein HSPB1, to form large heteromeric complexes
CC (PubMed:10751411). Inter-subunit bridging via zinc ions enhances
CC stability, which is crucial as there is no protein turn over in the
CC lens (PubMed:22890888). Interacts with HSPBAP1 and TTN/titin
CC (PubMed:14676215). Interacts with TMEM109 (PubMed:23542032). Interacts
CC with DES; binds rapidly during early stages of DES filament assembly
CC and a reduced binding seen in the later stages (PubMed:28470624).
CC Interacts with TMED10; the interaction mediates the translocation from
CC the cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate
CC compartment) and thereby secretion (PubMed:32272059). Interacts with
CC ATP6V1A and with MTOR, forming a ternary complex (PubMed:31786107).
CC {ECO:0000269|PubMed:10751411, ECO:0000269|PubMed:14676215,
CC ECO:0000269|PubMed:20836128, ECO:0000269|PubMed:22890888,
CC ECO:0000269|PubMed:23542032, ECO:0000269|PubMed:28470624,
CC ECO:0000269|PubMed:31786107, ECO:0000269|PubMed:32272059}.
CC -!- INTERACTION:
CC P02511; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-739060, EBI-10173507;
CC P02511; Q6LES2: ANXA4; NbExp=3; IntAct=EBI-739060, EBI-10250835;
CC P02511; P05067: APP; NbExp=7; IntAct=EBI-739060, EBI-77613;
CC P02511; Q6QEF8-4: CORO6; NbExp=3; IntAct=EBI-739060, EBI-10699285;
CC P02511; Q14194: CRMP1; NbExp=3; IntAct=EBI-739060, EBI-473101;
CC P02511; P02489: CRYAA; NbExp=18; IntAct=EBI-739060, EBI-6875961;
CC P02511; P02511: CRYAB; NbExp=30; IntAct=EBI-739060, EBI-739060;
CC P02511; P05813: CRYBA1; NbExp=2; IntAct=EBI-739060, EBI-7043337;
CC P02511; P07315: CRYGC; NbExp=3; IntAct=EBI-739060, EBI-6875941;
CC P02511; P22914: CRYGS; NbExp=2; IntAct=EBI-739060, EBI-11308647;
CC P02511; P35222: CTNNB1; NbExp=6; IntAct=EBI-739060, EBI-491549;
CC P02511; O00471: EXOC5; NbExp=3; IntAct=EBI-739060, EBI-949824;
CC P02511; Q9H8Y8: GORASP2; NbExp=3; IntAct=EBI-739060, EBI-739467;
CC P02511; Q96LI6-3: HSFY2; NbExp=3; IntAct=EBI-739060, EBI-25830912;
CC P02511; P04792: HSPB1; NbExp=6; IntAct=EBI-739060, EBI-352682;
CC P02511; Q16082: HSPB2; NbExp=3; IntAct=EBI-739060, EBI-739395;
CC P02511; Q3LI64: KRTAP6-1; NbExp=3; IntAct=EBI-739060, EBI-12111050;
CC P02511; P60891: PRPS1; NbExp=3; IntAct=EBI-739060, EBI-749195;
CC P02511; A0A0C4DFM3: PRUNE2; NbExp=3; IntAct=EBI-739060, EBI-25830870;
CC P02511; Q3UBX0: Tmem109; Xeno; NbExp=2; IntAct=EBI-739060, EBI-2366300;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19464326,
CC ECO:0000269|PubMed:28493373}. Nucleus {ECO:0000269|PubMed:19464326}.
CC Secreted {ECO:0000269|PubMed:32272059}. Lysosome
CC {ECO:0000250|UniProtKB:P23927}. Note=Translocates to the nucleus during
CC heat shock and resides in sub-nuclear structures known as SC35 speckles
CC or nuclear splicing speckles (PubMed:19464326). Localizes at the Z-
CC bands and the intercalated disk in cardiomyocytes (PubMed:28493373).
CC Can be secreted; the secretion is dependent on protein unfolding and
CC facilitated by the cargo receptor TMED10; it results in protein
CC translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-
CC Golgi intermediate compartment) followed by vesicle entry and secretion
CC (PubMed:32272059). {ECO:0000269|PubMed:19464326,
CC ECO:0000269|PubMed:28493373, ECO:0000269|PubMed:32272059}.
CC -!- TISSUE SPECIFICITY: Lens as well as other tissues (PubMed:838078,
CC PubMed:2387586). Expressed in myocardial tissue (PubMed:28493373).
CC {ECO:0000269|PubMed:2387586, ECO:0000269|PubMed:28493373,
CC ECO:0000269|PubMed:838078}.
CC -!- MASS SPECTROMETRY: Mass=20201; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10930324, ECO:0000269|PubMed:8175657};
CC -!- MASS SPECTROMETRY: Mass=20281; Method=Electrospray; Note=With 1
CC phosphate group.; Evidence={ECO:0000269|PubMed:10930324,
CC ECO:0000269|PubMed:8175657};
CC -!- MASS SPECTROMETRY: Mass=20360; Method=Electrospray; Note=With 2
CC phosphate groups.; Evidence={ECO:0000269|PubMed:8175657};
CC -!- MASS SPECTROMETRY: Mass=20199; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10930324, ECO:0000269|PubMed:8175657};
CC -!- MASS SPECTROMETRY: Mass=20278; Method=Electrospray; Note=With 1
CC phosphate group.; Evidence={ECO:0000269|PubMed:10930324,
CC ECO:0000269|PubMed:8175657};
CC -!- DISEASE: Myopathy, myofibrillar, 2 (MFM2) [MIM:608810]: A form of
CC myofibrillar myopathy, a group of chronic neuromuscular disorders
CC characterized at ultrastructural level by disintegration of the
CC sarcomeric Z disk and myofibrils, and replacement of the normal
CC myofibrillar markings by small dense granules, or larger hyaline
CC masses, or amorphous material. MFM2 is characterized by weakness of the
CC proximal and distal limb muscles, weakness of the neck, velopharynx and
CC trunk muscles, hypertrophic cardiomyopathy, and cataract in a subset of
CC patients. {ECO:0000269|PubMed:12601044, ECO:0000269|PubMed:14681890,
CC ECO:0000269|PubMed:21920752, ECO:0000269|PubMed:9731540}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Cataract 16, multiple types (CTRCT16) [MIM:613763]: 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. CTRCT16
CC includes posterior polar cataract, among others. Posterior polar
CC cataract is a subcapsular opacity, usually disk-shaped, located at the
CC back of the lens. {ECO:0000269|PubMed:11577372,
CC ECO:0000269|PubMed:18587492, ECO:0000269|PubMed:21866213}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Note=CRYAB mutations may be involved in restrictive
CC cardiomyopathy (RCM), a rare non-ischemic myocardial disease. RCM is
CC characterized by restrictive ventricular-filling physiology in the
CC presence of normal or reduced diastolic and/or systolic volumes (of 1
CC or both ventricles), biatrial enlargement, and normal ventricular wall
CC thickness. {ECO:0000269|PubMed:28493373}.
CC -!- DISEASE: Myopathy, myofibrillar, fatal infantile hypertonic, alpha-B
CC crystallin-related (MFMFIH-CRYAB) [MIM:613869]: A form of myofibrillar
CC myopathy, a group of chronic neuromuscular disorders characterized at
CC ultrastructural level by disintegration of the sarcomeric Z disk and
CC myofibrils, and replacement of the normal myofibrillar markings by
CC small dense granules, or larger hyaline masses, or amorphous material.
CC MFMFIH-CRYAB has onset in the first weeks of life after a normal
CC neonatal period. Affected infants show rapidly progressive muscular
CC rigidity of the trunk and limbs associated with increasing respiratory
CC difficulty resulting in death before age 3 years.
CC {ECO:0000269|PubMed:21337604}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Cardiomyopathy, dilated 1II (CMD1II) [MIM:615184]: A disorder
CC characterized by ventricular dilation and impaired systolic function,
CC resulting in congestive heart failure and arrhythmia. Patients are at
CC risk of premature death. {ECO:0000269|PubMed:16483541,
CC ECO:0000269|PubMed:16793013}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC {ECO:0000255|PROSITE-ProRule:PRU00285}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/CRYABID40156ch11q23.html";
CC ---------------------------------------------------------------------------
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DR EMBL; M28638; AAA52104.1; -; Genomic_DNA.
DR EMBL; S45630; AAB23453.1; -; mRNA.
DR EMBL; AF007162; AAC19161.1; -; mRNA.
DR EMBL; AK314029; BAG36739.1; -; mRNA.
DR EMBL; BT006770; AAP35416.1; -; mRNA.
DR EMBL; EF444955; ACA05949.1; -; Genomic_DNA.
DR EMBL; CH471065; EAW67162.1; -; Genomic_DNA.
DR EMBL; BC007008; AAH07008.1; -; mRNA.
DR EMBL; M24906; AAA60267.1; -; mRNA.
DR CCDS; CCDS8351.1; -.
DR PIR; A35332; CYHUAB.
DR RefSeq; NP_001276736.1; NM_001289807.1.
DR RefSeq; NP_001276737.1; NM_001289808.1.
DR RefSeq; NP_001876.1; NM_001885.2.
DR RefSeq; XP_011540910.1; XM_011542608.1.
DR PDB; 2KLR; NMR; -; A/B=1-175.
DR PDB; 2N0K; NMR; -; A/B=64-152.
DR PDB; 2WJ7; X-ray; 2.63 A; A/B/C/D/E=67-157.
DR PDB; 2Y1Y; X-ray; 2.00 A; A=71-157.
DR PDB; 2Y1Z; X-ray; 2.50 A; A/B=67-157.
DR PDB; 2Y22; X-ray; 3.70 A; A/B/C/D/E/F=67-157.
DR PDB; 2YGD; EM; 9.40 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-175.
DR PDB; 3J07; Other; -; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-175.
DR PDB; 3L1G; X-ray; 3.32 A; A=68-162.
DR PDB; 3SGM; X-ray; 1.70 A; A/B/C/D=90-100.
DR PDB; 3SGN; X-ray; 2.81 A; A/B=90-100.
DR PDB; 3SGO; X-ray; 2.56 A; A=90-100.
DR PDB; 3SGP; X-ray; 1.40 A; A/B/C/D=90-100.
DR PDB; 3SGR; X-ray; 2.17 A; A/B/C/D/E/F=90-100.
DR PDB; 3SGS; X-ray; 1.70 A; A=95-100.
DR PDB; 4M5S; X-ray; 1.37 A; A=68-153, B=156-164.
DR PDB; 4M5T; X-ray; 2.00 A; A/C/E/G=68-153, B/D/F/H=156-164.
DR PDB; 5VVV; X-ray; 2.80 A; B/D=38-50.
DR PDB; 6BP9; NMR; -; A/B=64-152.
DR PDB; 7ROJ; X-ray; 1.60 A; A/B/C/D/E/F/G/H/I/J/K/L=90-100.
DR PDBsum; 2KLR; -.
DR PDBsum; 2N0K; -.
DR PDBsum; 2WJ7; -.
DR PDBsum; 2Y1Y; -.
DR PDBsum; 2Y1Z; -.
DR PDBsum; 2Y22; -.
DR PDBsum; 2YGD; -.
DR PDBsum; 3J07; -.
DR PDBsum; 3L1G; -.
DR PDBsum; 3SGM; -.
DR PDBsum; 3SGN; -.
DR PDBsum; 3SGO; -.
DR PDBsum; 3SGP; -.
DR PDBsum; 3SGR; -.
DR PDBsum; 3SGS; -.
DR PDBsum; 4M5S; -.
DR PDBsum; 4M5T; -.
DR PDBsum; 5VVV; -.
DR PDBsum; 6BP9; -.
DR PDBsum; 7ROJ; -.
DR AlphaFoldDB; P02511; -.
DR BMRB; P02511; -.
DR SMR; P02511; -.
DR BioGRID; 107800; 213.
DR CORUM; P02511; -.
DR DIP; DIP-35017N; -.
DR IntAct; P02511; 62.
DR MINT; P02511; -.
DR STRING; 9606.ENSP00000433560; -.
DR BindingDB; P02511; -.
DR ChEMBL; CHEMBL3621022; -.
DR MoonDB; P02511; Curated.
DR TCDB; 8.A.172.1.1; the Alpha-crystallin chaperone (crya) family.
DR GlyConnect; 33; 1 O-Linked glycan.
DR GlyGen; P02511; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; P02511; -.
DR MetOSite; P02511; -.
DR PhosphoSitePlus; P02511; -.
DR BioMuta; CRYAB; -.
DR DMDM; 117385; -.
DR REPRODUCTION-2DPAGE; IPI00021369; -.
DR SWISS-2DPAGE; P02511; -.
DR UCD-2DPAGE; P02511; -.
DR EPD; P02511; -.
DR jPOST; P02511; -.
DR MassIVE; P02511; -.
DR PaxDb; P02511; -.
DR PeptideAtlas; P02511; -.
DR PRIDE; P02511; -.
DR ProteomicsDB; 51527; -.
DR Antibodypedia; 3674; 1725 antibodies from 48 providers.
DR CPTC; P02511; 3 antibodies.
DR DNASU; 1410; -.
DR Ensembl; ENST00000227251.7; ENSP00000227251.3; ENSG00000109846.9.
DR Ensembl; ENST00000526180.6; ENSP00000436051.1; ENSG00000109846.9.
DR Ensembl; ENST00000527899.6; ENSP00000436089.2; ENSG00000109846.9.
DR Ensembl; ENST00000527950.5; ENSP00000437149.1; ENSG00000109846.9.
DR Ensembl; ENST00000531198.5; ENSP00000434247.1; ENSG00000109846.9.
DR Ensembl; ENST00000533475.6; ENSP00000433560.1; ENSG00000109846.9.
DR Ensembl; ENST00000533879.2; ENSP00000435931.2; ENSG00000109846.9.
DR Ensembl; ENST00000616970.5; ENSP00000483554.1; ENSG00000109846.9.
DR Ensembl; ENST00000650687.2; ENSP00000499082.1; ENSG00000109846.9.
DR Ensembl; ENST00000651164.1; ENSP00000498735.1; ENSG00000109846.9.
DR GeneID; 1410; -.
DR KEGG; hsa:1410; -.
DR MANE-Select; ENST00000650687.2; ENSP00000499082.1; NM_001289808.2; NP_001276737.1.
DR CTD; 1410; -.
DR DisGeNET; 1410; -.
DR GeneCards; CRYAB; -.
DR HGNC; HGNC:2389; CRYAB.
DR HPA; ENSG00000109846; Tissue enhanced (heart muscle, skeletal muscle, tongue).
DR MalaCards; CRYAB; -.
DR MIM; 123590; gene.
DR MIM; 608810; phenotype.
DR MIM; 613763; phenotype.
DR MIM; 613869; phenotype.
DR MIM; 615184; phenotype.
DR neXtProt; NX_P02511; -.
DR OpenTargets; ENSG00000109846; -.
DR Orphanet; 399058; Alpha-B crystallin-related late-onset myopathy.
DR Orphanet; 441452; Early-onset lamellar cataract.
DR Orphanet; 98991; Early-onset nuclear cataract.
DR Orphanet; 98993; Early-onset posterior polar cataract.
DR Orphanet; 154; Familial isolated dilated cardiomyopathy.
DR Orphanet; 280553; Fatal infantile hypertonic myofibrillar myopathy.
DR PharmGKB; PA26907; -.
DR VEuPathDB; HostDB:ENSG00000109846; -.
DR eggNOG; KOG3591; Eukaryota.
DR GeneTree; ENSGT00940000157434; -.
DR InParanoid; P02511; -.
DR OMA; RDEHGWI; -.
DR OrthoDB; 1187096at2759; -.
DR PhylomeDB; P02511; -.
DR TreeFam; TF105049; -.
DR PathwayCommons; P02511; -.
DR Reactome; R-HSA-3371571; HSF1-dependent transactivation.
DR SignaLink; P02511; -.
DR SIGNOR; P02511; -.
DR BioGRID-ORCS; 1410; 23 hits in 1079 CRISPR screens.
DR ChiTaRS; CRYAB; human.
DR EvolutionaryTrace; P02511; -.
DR GeneWiki; CRYAB; -.
DR GenomeRNAi; 1410; -.
DR Pharos; P02511; Tchem.
DR PRO; PR:P02511; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P02511; protein.
DR Bgee; ENSG00000109846; Expressed in left ventricle myocardium and 204 other tissues.
DR ExpressionAtlas; P02511; baseline and differential.
DR Genevisible; P02511; HS.
DR GO; GO:0032432; C:actin filament bundle; IEA:Ensembl.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0097512; C:cardiac myofibril; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0031430; C:M band; IEA:Ensembl.
DR GO; GO:0015630; C:microtubule cytoskeleton; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:Ensembl.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0097060; C:synaptic membrane; IEA:Ensembl.
DR GO; GO:0030018; C:Z disc; IEA:Ensembl.
DR GO; GO:0001540; F:amyloid-beta binding; IPI:ARUK-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:ARUK-UCL.
DR GO; GO:0005212; F:structural constituent of eye lens; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IDA:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; IPI:UniProtKB.
DR GO; GO:0060561; P:apoptotic process involved in morphogenesis; IEA:Ensembl.
DR GO; GO:0071480; P:cellular response to gamma radiation; IMP:MGI.
DR GO; GO:0002088; P:lens development in camera-type eye; IEA:Ensembl.
DR GO; GO:0031109; P:microtubule polymerization or depolymerization; IEA:Ensembl.
DR GO; GO:0010259; P:multicellular organism aging; IEA:Ensembl.
DR GO; GO:0006936; P:muscle contraction; TAS:ProtInc.
DR GO; GO:0007517; P:muscle organ development; IEA:Ensembl.
DR GO; GO:1905907; P:negative regulation of amyloid fibril formation; IDA:ARUK-UCL.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:HGNC-UCL.
DR GO; GO:0030308; P:negative regulation of cell growth; IEA:Ensembl.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:0032387; P:negative regulation of intracellular transport; IDA:HGNC-UCL.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; IDA:ARUK-UCL.
DR GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006457; P:protein folding; NAS:ProtInc.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0050821; P:protein stabilization; IMP:CAFA.
DR GO; GO:0010941; P:regulation of cell death; IMP:MGI.
DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR GO; GO:0009408; P:response to heat; IBA:GO_Central.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0051403; P:stress-activated MAPK cascade; IEA:Ensembl.
DR GO; GO:0007021; P:tubulin complex assembly; IEA:Ensembl.
DR CDD; cd06498; ACD_alphaB-crystallin_HspB5; 1.
DR DisProt; DP00445; -.
DR Gene3D; 2.60.40.790; -; 1.
DR InterPro; IPR002068; A-crystallin/Hsp20_dom.
DR InterPro; IPR037882; ACD_alphaB-crystallin.
DR InterPro; IPR001436; Alpha-crystallin/sHSP_animal.
DR InterPro; IPR003090; Alpha-crystallin_N.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR PANTHER; PTHR45640; PTHR45640; 1.
DR Pfam; PF00525; Crystallin; 1.
DR Pfam; PF00011; HSP20; 1.
DR PIRSF; PIRSF036514; Sm_HSP_B1; 1.
DR PRINTS; PR00299; ACRYSTALLIN.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS01031; SHSP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cardiomyopathy; Cataract; Chaperone; Cytoplasm;
KW Direct protein sequencing; Disease variant; Eye lens protein; Glycoprotein;
KW Lysosome; Metal-binding; Myofibrillar myopathy; Nucleus; Oxidation;
KW Phosphoprotein; Reference proteome; Secreted; Zinc.
FT CHAIN 1..175
FT /note="Alpha-crystallin B chain"
FT /id="PRO_0000125907"
FT DOMAIN 56..164
FT /note="sHSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT REGION 146..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT SITE 48
FT /note="Susceptible to oxidation"
FT SITE 60
FT /note="Susceptible to oxidation"
FT SITE 68
FT /note="Susceptible to oxidation"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:8142454,
FT ECO:0000269|PubMed:838078"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8175657"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11158243,
FT ECO:0000269|PubMed:8175657"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11158243,
FT ECO:0000269|PubMed:8175657, ECO:0007744|PubMed:24275569"
FT MOD_RES 92
FT /note="N6-acetyllysine; partial"
FT /evidence="ECO:0000269|PubMed:11369851,
FT ECO:0000269|PubMed:22120592"
FT MOD_RES 166
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:22120592"
FT CARBOHYD 170
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250"
FT VARIANT 41
FT /note="S -> Y (in dbSNP:rs2234703)"
FT /id="VAR_014607"
FT VARIANT 51
FT /note="P -> L (in dbSNP:rs2234704)"
FT /id="VAR_014608"
FT VARIANT 69
FT /note="R -> C (in CTRCT16; unknown pathological
FT significance; dbSNP:rs139750142)"
FT /evidence="ECO:0000269|PubMed:21866213"
FT /id="VAR_084806"
FT VARIANT 109
FT /note="D -> G (probable disease-associated variant found in
FT patients with restrictive cardiomyopathy; reduces CRYAB and
FT DES localization at the Z-bands and the intercalated disk
FT in the myocardium; cytoplasmic aggregations of CRYAB and
FT DES; dbSNP:rs1114167341)"
FT /evidence="ECO:0000269|PubMed:28493373"
FT /id="VAR_079841"
FT VARIANT 109
FT /note="D -> H (in MFM2; dbSNP:rs387907339)"
FT /evidence="ECO:0000269|PubMed:21920752"
FT /id="VAR_069528"
FT VARIANT 120
FT /note="R -> G (in MFM2; decreased interactions with wild-
FT type CRYAA and CRYAB but increased interactions with wild-
FT type CRYBB2 and CRYGC; cytoplasmic aggregation;
FT dbSNP:rs104894201)"
FT /evidence="ECO:0000269|PubMed:12601044,
FT ECO:0000269|PubMed:28493373, ECO:0000269|PubMed:9731540"
FT /id="VAR_007899"
FT VARIANT 154
FT /note="G -> S (in CMD1II; dbSNP:rs150516929)"
FT /evidence="ECO:0000269|PubMed:16793013"
FT /id="VAR_070035"
FT VARIANT 157
FT /note="R -> H (in CMD1II; dbSNP:rs141638421)"
FT /evidence="ECO:0000269|PubMed:16483541"
FT /id="VAR_070036"
FT VARIANT 171
FT /note="A -> T (in CTRCT16; unknown pathological
FT significance; dbSNP:rs370803064)"
FT /evidence="ECO:0000269|PubMed:18587492"
FT /id="VAR_084807"
FT CONFLICT 165
FT /note="E -> K (in Ref. 4; AAC19161)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="K -> KKMPFLELHFLKQESFPTSE (in Ref. 4; AAC19161)"
FT /evidence="ECO:0000305"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:4M5S"
FT STRAND 72..80
FT /evidence="ECO:0007829|PDB:4M5S"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:2N0K"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:4M5S"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:4M5S"
FT STRAND 97..109
FT /evidence="ECO:0007829|PDB:4M5S"
FT STRAND 112..123
FT /evidence="ECO:0007829|PDB:4M5S"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:2KLR"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:4M5S"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:4M5S"
FT STRAND 141..148
FT /evidence="ECO:0007829|PDB:4M5S"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:4M5T"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:4M5T"
SQ SEQUENCE 175 AA; 20159 MW; AE08BED46B7849CB CRC64;
MDIAIHHPWI RRPFFPFHSP SRLFDQFFGE HLLESDLFPT STSLSPFYLR PPSFLRAPSW
FDTGLSEMRL EKDRFSVNLD VKHFSPEELK VKVLGDVIEV HGKHEERQDE HGFISREFHR
KYRIPADVDP LTITSSLSSD GVLTVNGPRK QVSGPERTIP ITREEKPAVT AAPKK
