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CRYAA_HUMAN
ID   CRYAA_HUMAN             Reviewed;         173 AA.
AC   P02489; A0A140G945; E9PHE4; Q53X53;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   03-AUG-2022, entry version 223.
DE   RecName: Full=Alpha-crystallin A chain;
DE   AltName: Full=Heat shock protein beta-4;
DE            Short=HspB4;
DE   Contains:
DE     RecName: Full=Alpha-crystallin A(1-172);
DE   Contains:
DE     RecName: Full=Alpha-crystallin A(1-168);
DE   Contains:
DE     RecName: Full=Alpha-crystallin A(1-162);
GN   Name=CRYAA; Synonyms=CRYA1, HSPB4;
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, AND ACETYLATION AT MET-1.
RX   PubMed=817940; DOI=10.1016/0014-5793(75)80286-9;
RA   de Jong W.W., Terwindt E.C., Bloemendal H.;
RT   "The amino acid sequence of the A chain of human alpha-crystallin.";
RL   FEBS Lett. 58:310-313(1975).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lens;
RX   PubMed=8587135; DOI=10.1007/bf00173170;
RA   Jaworski C.J.;
RT   "A reassessment of mammalian alpha A-crystallin sequences using DNA
RT   sequencing: implications for anthropoid affinities of tarsier.";
RL   J. Mol. Evol. 41:901-908(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lens;
RX   PubMed=8943244; DOI=10.1074/jbc.271.50.31973;
RA   Andley U.P., Mathur S., Griest T.A., Petrash J.M.;
RT   "Cloning, expression, and chaperone-like activity of human alphaA-
RT   crystallin.";
RL   J. Biol. Chem. 271:31973-31980(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lens;
RA   Rajkumar S.;
RT   "Functional candidate gene approach to study genetic polymorphisms in lens
RT   specific genes.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10830953; DOI=10.1038/35012518;
RA   Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA   Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA   Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA   Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA   Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA   Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA   Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA   Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA   Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA   Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA   Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT   "The DNA sequence of human chromosome 21.";
RL   Nature 405:311-319(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Colon;
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   [9]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-104.
RX   PubMed=2918909; DOI=10.1038/337752a0;
RA   Jaworski C.J., Piatigorsky J.;
RT   "A pseudo-exon in the functional human alpha A-crystallin gene.";
RL   Nature 337:752-754(1989).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-63 AND 166-173.
RC   TISSUE=Spleen;
RX   PubMed=3758227; DOI=10.1016/s0014-4835(86)80098-7;
RA   McDevitt D.S., Hawkins J.W., Jaworski C.J., Piatigorsky J.;
RT   "Isolation and partial characterization of the human alpha A-crystallin
RT   gene.";
RL   Exp. Eye Res. 43:285-291(1986).
RN   [11]
RP   PROTEIN SEQUENCE OF 13-21 AND 79-88.
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   STRUCTURE OF CARBOHYDRATE.
RX   PubMed=1730617; DOI=10.1016/s0021-9258(18)48530-4;
RA   Roquemore E.P., Dell A., Morris H.R., Panico M., Reason A.J., Savoy L.-A.,
RA   Wistow G.J., Zigler J.S. Jr., Earles B.J., Hart G.W.;
RT   "Vertebrate lens alpha-crystallins are modified by O-linked N-
RT   acetylglucosamine.";
RL   J. Biol. Chem. 267:555-563(1992).
RN   [13]
RP   PHOSPHORYLATION AT SER-122, DISULFIDE BOND, PROTEOLYTIC PROCESSING OF
RP   C-TERMINAL, DEAMIDATION AT ASN-101, 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   [14]
RP   PHOSPHORYLATION AT SER-122.
RX   PubMed=8759518; DOI=10.1006/exer.1996.0060;
RA   Takemoto L.J.;
RT   "Differential phosphorylation of alpha-A crystallin in human lens of
RT   different age.";
RL   Exp. Eye Res. 62:499-504(1996).
RN   [15]
RP   PROTEOLYTIC PROCESSING, SUSCEPTIBILITY TO OXIDATION, PHOSPHORYLATION AT
RP   SER-45 AND SER-122, DISULFIDE BOND, DEAMIDATION AT GLN-6; GLN-50; GLN-90;
RP   ASN-101 AND GLN-147, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=9068373; DOI=10.1006/exer.1996.0160;
RA   Lund A.L., Smith J.B., Smith D.L.;
RT   "Modifications of the water-insoluble human lens alpha-crystallins.";
RL   Exp. Eye Res. 63:661-672(1996).
RN   [16]
RP   DEAMIDATION AT ASN-101.
RX   PubMed=9543632; DOI=10.1076/ceyr.17.3.247.5218;
RA   Takemoto L.J.;
RT   "Quantitation of asparagine-101 deamidation from alpha-A crystallin during
RT   aging of the human lens.";
RL   Curr. Eye Res. 17:247-250(1998).
RN   [17]
RP   PROTEOLYTIC PROCESSING OF C-TERMINAL, ACETYLATION AT LYS-70,
RP   PHOSPHORYLATION, DEAMIDATION AT ASN-101, AND MASS SPECTROMETRY.
RX   PubMed=9655350; DOI=10.1002/pro.5560070622;
RA   Lin P.P., Barry R.C., Smith D.L., Smith J.B.;
RT   "In vivo acetylation identified at lysine 70 of human lens alphaA-
RT   crystallin.";
RL   Protein Sci. 7:1451-1457(1998).
RN   [18]
RP   PHOSPHORYLATION, SUSCEPTIBILITY TO OXIDATION, PROTEOLYTIC PROCESSING OF
RP   C-TERMINAL, AND 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   [19]
RP   REVIEW.
RX   PubMed=12369933; DOI=10.2174/1389203013381107;
RA   Ganea E.;
RT   "Chaperone-like activity of alpha-crystallin and other small heat shock
RT   proteins.";
RL   Curr. Protein Pept. Sci. 2:205-225(2001).
RN   [20]
RP   PROTEOLYTIC PROCESSING, AND TISSUE SPECIFICITY.
RX   PubMed=12356833;
RA   Thampi P., Hassan A., Smith J.B., Abraham E.C.;
RT   "Enhanced C-terminal truncation of alphaA- and alphaB-crystallins in
RT   diabetic lenses.";
RL   Invest. Ophthalmol. Vis. Sci. 43:3265-3272(2002).
RN   [21]
RP   DEAMIDATION AT ASN-123, AND MUTAGENESIS OF ASN-123.
RX   PubMed=18754677; DOI=10.1021/bi8001902;
RA   Chaves J.M., Srivastava K., Gupta R., Srivastava O.P.;
RT   "Structural and functional roles of deamidation and/or truncation of N- or
RT   C-termini in human alpha A-crystallin.";
RL   Biochemistry 47:10069-10083(2008).
RN   [22]
RP   SUBUNIT.
RX   PubMed=17909943; DOI=10.1007/s11010-007-9615-2;
RA   Kallur L.S., Aziz A., Abraham E.C.;
RT   "C-Terminal truncation affects subunit exchange of human alphaA-crystallin
RT   with alphaB-crystallin.";
RL   Mol. Cell. Biochem. 308:85-91(2008).
RN   [23]
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   [24]
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   [25]
RP   FUNCTION, AND ACETYLATION AT LYS-70 AND LYS-99.
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   [26]
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   [27]
RP   FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH BFSP1 AND BFSP2.
RX   PubMed=28935373; DOI=10.1016/j.bbrc.2017.09.088;
RA   Chaves J.M., Gupta R., Srivastava K., Srivastava O.;
RT   "Human alpha A-crystallin missing N-terminal domain poorly complexes with
RT   filensin and phakinin.";
RL   Biochem. Biophys. Res. Commun. 494:402-408(2017).
RN   [28] {ECO:0007744|PDB:6T1R}
RP   STRUCTURE BY ELECTRON MICROSCOPY (9.80 ANGSTROMS), HOMOMERIZATION,
RP   DISULFIDE BOND, AND FUNCTION.
RX   PubMed=31792453; DOI=10.1038/s41594-019-0332-9;
RA   Kaiser C.J.O., Peters C., Schmid P.W.N., Stavropoulou M., Zou J.,
RA   Dahiya V., Mymrikov E.V., Rockel B., Asami S., Haslbeck M., Rappsilber J.,
RA   Reif B., Zacharias M., Buchner J., Weinkauf S.;
RT   "The structure and oxidation of the eye lens chaperone alphaA-crystallin.";
RL   Nat. Struct. Mol. Biol. 26:1141-1150(2019).
RN   [29]
RP   VARIANT CTRCT9 CYS-116.
RX   PubMed=9467006; DOI=10.1093/hmg/7.3.471;
RA   Litt M., Kramer P., la Morticella D.M., Murphey W., Lovrien E.W.,
RA   Weleber R.G.;
RT   "Autosomal dominant congenital cataract associated with a missense mutation
RT   in the human alpha crystallin gene CRYAA.";
RL   Hum. Mol. Genet. 7:471-474(1998).
RN   [30]
RP   CHARACTERIZATION OF VARIANT CTRCT9 CYS-116.
RX   PubMed=11123904; DOI=10.1021/bi001453j;
RA   Cobb B.A., Petrash J.M.;
RT   "Structural and functional changes in the alpha A-crystallin R116C mutant
RT   in hereditary cataracts.";
RL   Biochemistry 39:15791-15798(2000).
RN   [31]
RP   VARIANT CTRCT9 9-TRP--SER-173 DEL.
RX   PubMed=11006246;
RA   Pras E., Frydman M., Levy-Nissenbaum E., Bakhan T., Raz J., Assia E.I.,
RA   Goldman B., Pras E.;
RT   "A nonsense mutation (W9X) in CRYAA causes autosomal recessive cataract in
RT   an inbred Jewish Persian family.";
RL   Invest. Ophthalmol. Vis. Sci. 41:3511-3515(2000).
RN   [32]
RP   VARIANT CTRCT9 CYS-49, AND SUBCELLULAR LOCATION.
RX   PubMed=14512969; DOI=10.1038/sj.ejhg.5201046;
RA   Mackay D.S., Andley U.P., Shiels A.;
RT   "Cell death triggered by a novel mutation in the alphaA-crystallin gene
RT   underlies autosomal dominant cataract linked to chromosome 21q.";
RL   Eur. J. Hum. Genet. 11:784-793(2003).
RN   [33]
RP   VARIANT CTRCT9 LEU-21.
RX   PubMed=16453125; DOI=10.1007/s00417-005-0234-x;
RA   Graw J., Klopp N., Illig T., Preising M.N., Lorenz B.;
RT   "Congenital cataract and macular hypoplasia in humans associated with a de
RT   novo mutation in CRYAA and compound heterozygous mutations in P.";
RL   Graefes Arch. Clin. Exp. Ophthalmol. 244:912-919(2006).
RN   [34]
RP   VARIANT CTRCT9 CYS-116.
RX   PubMed=16735993;
RA   Vanita V., Singh J.R., Hejtmancik J.F., Nuernberg P., Hennies H.C.,
RA   Singh D., Sperling K.;
RT   "A novel fan-shaped cataract-microcornea syndrome caused by a mutation of
RT   CRYAA in an Indian family.";
RL   Mol. Vis. 12:518-522(2006).
RN   [35]
RP   VARIANT CTRCT9 ARG-98.
RX   PubMed=16862070;
RA   Santhiya S.T., Soker T., Klopp N., Illig T., Prakash M.V., Selvaraj B.,
RA   Gopinath P.M., Graw J.;
RT   "Identification of a novel, putative cataract-causing allele in CRYAA
RT   (G98R) in an Indian family.";
RL   Mol. Vis. 12:768-773(2006).
RN   [36]
RP   VARIANT [LARGE SCALE ANALYSIS] HIS-105.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
RN   [37]
RP   VARIANT CTRCT9 CYS-54.
RX   PubMed=17937925; DOI=10.1016/j.ajo.2007.08.005;
RA   Khan A.O., Aldahmesh M.A., Meyer B.;
RT   "Recessive congenital total cataract with microcornea and heterozygote
RT   carrier signs caused by a novel missense CRYAA mutation (R54C).";
RL   Am. J. Ophthalmol. 144:949-952(2007).
RN   [38]
RP   VARIANT CTRCT9 CYS-116.
RX   PubMed=17296897; DOI=10.1001/archopht.125.2.213;
RA   Beby F., Commeaux C., Bozon M., Denis P., Edery P., Morle L.;
RT   "New phenotype associated with an Arg116Cys mutation in the CRYAA gene:
RT   nuclear cataract, iris coloboma, and microphthalmia.";
RL   Arch. Ophthalmol. 125:213-216(2007).
RN   [39]
RP   VARIANTS CTRCT9 CYS-12 AND TRP-21.
RX   PubMed=17724170; DOI=10.1167/iovs.07-0013;
RA   Hansen L., Yao W., Eiberg H., Kjaer K.W., Baggesen K., Hejtmancik J.F.,
RA   Rosenberg T.;
RT   "Genetic heterogeneity in microcornea-cataract: five novel mutations in
RT   CRYAA, CRYGD, and GJA8.";
RL   Invest. Ophthalmol. Vis. Sci. 48:3937-3944(2007).
RN   [40]
RP   CHARACTERIZATION OF VARIANT CTRCT9 ARG-98, AND FUNCTION.
RX   PubMed=18199971;
RA   Murugesan R., Santhoshkumar P., Sharma K.K.;
RT   "Cataract-causing alphaAG98R mutant shows substrate-dependent chaperone
RT   activity.";
RL   Mol. Vis. 13:2301-2309(2007).
RN   [41]
RP   FUNCTION, AND VARIANT CTRCT9 HIS-116.
RX   PubMed=18302245; DOI=10.1002/ajmg.a.32236;
RA   Richter L., Flodman P., Barria von-Bischhoffshausen F., Burch D., Brown S.,
RA   Nguyen L., Turner J., Spence M.A., Bateman J.B.;
RT   "Clinical variability of autosomal dominant cataract, microcornea and
RT   corneal opacity and novel mutation in the alpha A crystallin gene
RT   (CRYAA).";
RL   Am. J. Med. Genet. A 146:833-842(2008).
RN   [42]
RP   VARIANT CTRCT9 HIS-116, AND CHARACTERIZATION OF VARIANT CTRCT9 HIS-116.
RX   PubMed=18407550; DOI=10.1002/humu.20724;
RA   Gu F., Luo W., Li X., Wang Z., Lu S., Zhang M., Zhao B., Zhu S., Feng S.,
RA   Yan Y.-B., Huang S., Ma X.;
RT   "A novel mutation in AlphaA-crystallin (CRYAA) caused autosomal dominant
RT   congenital cataract in a large Chinese family.";
RL   Hum. Mutat. 29:769-769(2008).
RN   [43]
RP   VARIANTS CTRCT9 CYS-12; TRP-21 AND CYS-54.
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   [44]
RP   VARIANT CTRCT9 LEU-71, CHARACTERIZATION OF VARIANT CTRCT9 LEU-71, AND
RP   FUNCTION.
RX   PubMed=19595763; DOI=10.1016/j.bbadis.2009.06.011;
RA   Bhagyalaxmi S.G., Srinivas P., Barton K.A., Kumar K.R., Vidyavathi M.,
RA   Petrash J.M., Bhanuprakash Reddy G., Padma T.;
RT   "A novel mutation (F71L) in alphaA-crystallin with defective chaperone-like
RT   function associated with age-related cataract.";
RL   Biochim. Biophys. Acta 1792:974-981(2009).
RN   [45]
RP   VARIANT CTRCT9 CYS-12.
RX   PubMed=19390652;
RA   Santana A., Waiswol M., Arcieri E.S., Cabral de Vasconcellos J.P.,
RA   Barbosa de Melo M.;
RT   "Mutation analysis of CRYAA, CRYGC, and CRYGD associated with autosomal
RT   dominant congenital cataract in Brazilian families.";
RL   Mol. Vis. 15:793-800(2009).
RN   [46]
RP   CHARACTERIZATION OF VARIANT CTRCT9 CYS-12, AND SUBCELLULAR LOCATION.
RX   PubMed=19503744;
RA   Zhang L.Y., Yam G.H., Tam P.O., Lai R.Y., Lam D.S., Pang C.P., Fan D.S.;
RT   "An alphaA-crystallin gene mutation, Arg12Cys, causing inherited cataract-
RT   microcornea exhibits an altered heat-shock response.";
RL   Mol. Vis. 15:1127-1138(2009).
RN   [47]
RP   VARIANTS CTRCT9 TRP-21 AND CYS-49.
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   [48]
RP   VARIANT CTRCT9 CYS-116.
RX   PubMed=20465443; DOI=10.3109/02713681003624901;
RA   Li F.F., Yang M., Ma X., Zhang Q., Zhang M., Wang S.Z., Zhu S.Q.;
RT   "Autosomal dominant congenital nuclear cataracts caused by a CRYAA gene
RT   mutation.";
RL   Curr. Eye Res. 35:492-498(2010).
RN   [49]
RP   VARIANT CTRCT9 CYS-12.
RX   PubMed=21686328;
RA   Sun W., Xiao X., Li S., Guo X., Zhang Q.;
RT   "Mutational screening of six genes in Chinese patients with congenital
RT   cataract and microcornea.";
RL   Mol. Vis. 17:1508-1513(2011).
RN   [50]
RP   VARIANTS CTRCT9 ARG-98 AND 117-ARG-TYR-118 DELINS HIS.
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   [51]
RP   VARIANT CTRCT9 HIS-116.
RX   PubMed=22065922;
RA   Zhang L., Zhang Y., Liu P., Cao W., Tang X., Su S.;
RT   "Congenital anterior polar cataract associated with a missense mutation in
RT   the human alpha crystallin gene CRYAA.";
RL   Mol. Vis. 17:2693-2697(2011).
RN   [52]
RP   VARIANT CTRCT9 PRO-54.
RX   PubMed=23288997;
RA   Su D., Guo Y., Li Q., Guan L., Zhu S., Ma X.;
RT   "A novel mutation in CRYAA is associated with autosomal dominant suture
RT   cataracts in a Chinese family.";
RL   Mol. Vis. 18:3057-3063(2012).
RN   [53]
RP   VARIANT CTRCT9 HIS-116.
RX   PubMed=22216983; DOI=10.3109/13816810.2011.642451;
RA   Wang B., Wang K.J., Zhu S.Q., Wang J., Ma X.;
RT   "Identification of the p. R116H mutation in a Chinese family with novel
RT   variable cataract phenotype: evidence for a mutational hot spot in alphaA-
RT   crystallin gene.";
RL   Ophthalmic Genet. 33:134-138(2012).
RN   [54]
RP   VARIANT CTRCT9 LEU-54.
RX   PubMed=24074001; DOI=10.3109/02713683.2013.811260;
RA   Yang Z., Su D., Li Q., Ma Z., Yang F., Zhu S., Ma X.;
RT   "A R54L mutation of CRYAA associated with autosomal dominant nuclear
RT   cataracts in a Chinese family.";
RL   Curr. Eye Res. 38:1221-1228(2013).
RN   [55]
RP   VARIANT CTRCT9 CYS-12.
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).
RN   [56]
RP   CHARACTERIZATION OF VARIANT CTRCT9 GLN-21, SUBUNIT, AND TISSUE SPECIFICITY.
RX   PubMed=23255486; DOI=10.1002/humu.22260;
RA   Laurie K.J., Dave A., Straga T., Souzeau E., Chataway T., Sykes M.J.,
RA   Casey T., Teo T., Pater J., Craig J.E., Sharma S., Burdon K.P.;
RT   "Identification of a novel oligomerization disrupting mutation in CRYAlphaA
RT   associated with congenital cataract in a South Australian family.";
RL   Hum. Mutat. 34:435-438(2013).
RN   [57]
RP   VARIANT CTRCT9 TRP-21.
RX   PubMed=23441109;
RA   Kondo Y., Saitsu H., Miyamoto T., Lee B.J., Nishiyama K., Nakashima M.,
RA   Tsurusaki Y., Doi H., Miyake N., Kim J.H., Yu Y.S., Matsumoto N.;
RT   "Pathogenic mutations in two families with congenital cataract identified
RT   with whole-exome sequencing.";
RL   Mol. Vis. 19:384-389(2013).
RN   [58]
RP   VARIANT CTRCT9 ARG-117 DEL.
RX   PubMed=25729975; DOI=10.4238/2015.january.23.16;
RA   Kong X.D., Liu N., Shi H.R., Dong J.M., Zhao Z.H., Liu J., Li-Ling J.,
RA   Yang Y.X.;
RT   "A novel 3-base pair deletion of the CRYAA gene identified in a large
RT   Chinese pedigree featuring autosomal dominant congenital perinuclear
RT   cataract.";
RL   Genet. Mol. Res. 14:426-432(2015).
RN   [59]
RP   VARIANT CTRCT9 PRO-139, AND SUBCELLULAR LOCATION.
RX   PubMed=26004348; DOI=10.3892/mmr.2015.3819;
RA   Liang C., Liang H., Yang Y., Ping L., Jie Q.;
RT   "Mutation analysis of two families with inherited congenital cataracts.";
RL   Mol. Med. Report. 12:3469-3475(2015).
RN   [60]
RP   VARIANT CTRCT9 GLN-21.
RX   PubMed=26867756; DOI=10.1186/s13104-016-1890-0;
RA   Javadiyan S., Craig J.E., Souzeau E., Sharma S., Lower K.M., Pater J.,
RA   Casey T., Hodson T., Burdon K.P.;
RT   "Recurrent mutation in the crystallin alpha A gene associated with
RT   inherited paediatric cataract.";
RL   BMC Res. Notes 9:83-83(2016).
RN   [61]
RP   VARIANT CTRCT9 CYS-54.
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   [62]
RP   VARIANTS CTRCT9 GLN-65 AND HIS-119.
RX   PubMed=28690483; DOI=10.1159/000471992;
RA   Patel R., Zenith R.K., Chandra A., Ali A.;
RT   "Novel Mutations in the Crystallin Gene in Age-Related Cataract Patients
RT   from a North Indian Population.";
RL   Mol. Syndromol. 8:179-186(2017).
RN   [63]
RP   VARIANT CTRCT9 TRP-21.
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   [64]
RP   VARIANT CTRCT9 LEU-12, CHARACTERIZATION OF VARIANT CTRCT9 LEU-12, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=30340470; DOI=10.1186/s12881-018-0695-5;
RA   Song Z., Si N., Xiao W.;
RT   "A novel mutation in the CRYAA gene associated with congenital cataract and
RT   microphthalmia in a Chinese family.";
RL   BMC Med. Genet. 19:190-190(2018).
RN   [65]
RP   VARIANT CTRCT9 TRP-21.
RX   PubMed=29914532; DOI=10.1186/s13023-018-0828-0;
RA   Li J., Leng Y., Han S., Yan L., Lu C., Luo Y., Zhang X., Cao L.;
RT   "Clinical and genetic characteristics of Chinese patients with familial or
RT   sporadic pediatric cataract.";
RL   Orphanet J. Rare Dis. 13:94-94(2018).
RN   [66]
RP   VARIANTS CTRCT9 LEU-12; TRP-21 AND CYS-116.
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   [67]
RP   VARIANT CTRCT9 CYS-12.
RX   PubMed=32010934; DOI=10.1042/bsr20191349;
RA   Liu Q., Zhu S.;
RT   "Clinical characteristics of congenital lamellar cataract and myopia in a
RT   Chinese family.";
RL   Biosci. Rep. 40:0-0(2020).
RN   [68]
RP   VARIANT CTRCT9 CYS-49.
RX   PubMed=33243271; DOI=10.1186/s13023-020-01613-3;
RA   Berry V., Ionides A., Pontikos N., Georgiou M., Yu J., Ocaka L.A.,
RA   Moore A.T., Quinlan R.A., Michaelides M.;
RT   "The genetic landscape of crystallins in congenital cataract.";
RL   Orphanet J. Rare Dis. 15:333-333(2020).
CC   -!- FUNCTION: Contributes to the transparency and refractive index of the
CC       lens (PubMed:18302245). In its oxidized form (absence of intramolecular
CC       disulfide bond), acts as a chaperone, preventing aggregation of various
CC       proteins under a wide range of stress conditions (PubMed:22120592,
CC       PubMed:31792453, PubMed:18199971, PubMed:19595763). Required for the
CC       correct formation of lens intermediate filaments as part of a complex
CC       composed of BFSP1, BFSP2 and CRYAA (PubMed:28935373).
CC       {ECO:0000269|PubMed:18199971, ECO:0000269|PubMed:19595763,
CC       ECO:0000269|PubMed:22120592, ECO:0000269|PubMed:28935373,
CC       ECO:0000269|PubMed:31792453, ECO:0000303|PubMed:18302245}.
CC   -!- SUBUNIT: Heteropolymer composed of three CRYAA and one CRYAB subunits
CC       (PubMed:20836128). 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). Can also form homodimers and homotetramers
CC       (dimers of dimers) which serve as the building blocks of homooligomers
CC       (PubMed:17909943, PubMed:31792453, PubMed:23255486). Within
CC       homooligomers, the zinc-binding motif is created from residues of 3
CC       different molecules. His-100 and Glu-102 from one molecule are ligands
CC       of the zinc ion, and His-107 and His-154 residues from additional
CC       molecules complete the site with tetrahedral coordination geometry (By
CC       similarity). Part of a complex required for lens intermediate filament
CC       formation composed of BFSP1, BFSP2 and CRYAA (PubMed:28935373).
CC       {ECO:0000250|UniProtKB:P02470, ECO:0000269|PubMed:17909943,
CC       ECO:0000269|PubMed:20836128, ECO:0000269|PubMed:22890888,
CC       ECO:0000269|PubMed:23255486, ECO:0000269|PubMed:28935373,
CC       ECO:0000269|PubMed:31792453}.
CC   -!- INTERACTION:
CC       P02489; Q8NC06-3: ACBD4; NbExp=3; IntAct=EBI-6875961, EBI-12811089;
CC       P02489; P35611: ADD1; NbExp=3; IntAct=EBI-6875961, EBI-2809187;
CC       P02489; Q9NP61: ARFGAP3; NbExp=3; IntAct=EBI-6875961, EBI-2875816;
CC       P02489; O95817: BAG3; NbExp=3; IntAct=EBI-6875961, EBI-747185;
CC       P02489; Q8TBE0: BAHD1; NbExp=3; IntAct=EBI-6875961, EBI-742750;
CC       P02489; Q9UQB8-6: BAIAP2; NbExp=3; IntAct=EBI-6875961, EBI-9092016;
CC       P02489; Q9H0W9-3: C11orf54; NbExp=3; IntAct=EBI-6875961, EBI-12108466;
CC       P02489; Q9NNX6-10: CD209; NbExp=3; IntAct=EBI-6875961, EBI-12300031;
CC       P02489; Q9BXL8: CDCA4; NbExp=3; IntAct=EBI-6875961, EBI-1773949;
CC       P02489; P49336-2: CDK8; NbExp=3; IntAct=EBI-6875961, EBI-11039720;
CC       P02489; P20849: COL9A1; NbExp=3; IntAct=EBI-6875961, EBI-2528238;
CC       P02489; Q86WV2: COX4I1; NbExp=3; IntAct=EBI-6875961, EBI-10260134;
CC       P02489; P02489: CRYAA; NbExp=12; IntAct=EBI-6875961, EBI-6875961;
CC       P02489; P02511: CRYAB; NbExp=18; IntAct=EBI-6875961, EBI-739060;
CC       P02489; P26998: CRYBB3; NbExp=3; IntAct=EBI-6875961, EBI-1965681;
CC       P02489; P07315: CRYGC; NbExp=3; IntAct=EBI-6875961, EBI-6875941;
CC       P02489; Q9Y6W6: DUSP10; NbExp=3; IntAct=EBI-6875961, EBI-3443946;
CC       P02489; Q99944: EGFL8; NbExp=4; IntAct=EBI-6875961, EBI-3924130;
CC       P02489; P60228: EIF3E; NbExp=3; IntAct=EBI-6875961, EBI-347740;
CC       P02489; P23588: EIF4B; NbExp=3; IntAct=EBI-6875961, EBI-970310;
CC       P02489; Q6NXG1: ESRP1; NbExp=3; IntAct=EBI-6875961, EBI-10213520;
CC       P02489; Q6NXG1-3: ESRP1; NbExp=3; IntAct=EBI-6875961, EBI-21567429;
CC       P02489; Q6NZ36-4: FAAP20; NbExp=3; IntAct=EBI-6875961, EBI-12013806;
CC       P02489; Q96GL9: FAM163A; NbExp=3; IntAct=EBI-6875961, EBI-11793142;
CC       P02489; Q06547-2: GABPB1; NbExp=3; IntAct=EBI-6875961, EBI-618189;
CC       P02489; P15976-2: GATA1; NbExp=3; IntAct=EBI-6875961, EBI-9090198;
CC       P02489; Q9NXC2: GFOD1; NbExp=3; IntAct=EBI-6875961, EBI-8799578;
CC       P02489; Q9H8Y8: GORASP2; NbExp=12; IntAct=EBI-6875961, EBI-739467;
CC       P02489; Q13322-4: GRB10; NbExp=3; IntAct=EBI-6875961, EBI-12353035;
CC       P02489; V9HW27: HEL-S-101; NbExp=3; IntAct=EBI-6875961, EBI-10178933;
CC       P02489; Q9P0W2: HMG20B; NbExp=3; IntAct=EBI-6875961, EBI-713401;
CC       P02489; Q4VB01: HOXB1; NbExp=3; IntAct=EBI-6875961, EBI-17494170;
CC       P02489; P04792: HSPB1; NbExp=4; IntAct=EBI-6875961, EBI-352682;
CC       P02489; O43464: HTRA2; NbExp=3; IntAct=EBI-6875961, EBI-517086;
CC       P02489; P42858: HTT; NbExp=3; IntAct=EBI-6875961, EBI-466029;
CC       P02489; Q14005-2: IL16; NbExp=3; IntAct=EBI-6875961, EBI-17178971;
CC       P02489; Q0VD86: INCA1; NbExp=3; IntAct=EBI-6875961, EBI-6509505;
CC       P02489; O60333-2: KIF1B; NbExp=3; IntAct=EBI-6875961, EBI-10975473;
CC       P02489; P57682: KLF3; NbExp=3; IntAct=EBI-6875961, EBI-8472267;
CC       P02489; Q9Y2M5: KLHL20; NbExp=3; IntAct=EBI-6875961, EBI-714379;
CC       P02489; Q14533: KRT81; NbExp=3; IntAct=EBI-6875961, EBI-739648;
CC       P02489; Q3LI72: KRTAP19-5; NbExp=3; IntAct=EBI-6875961, EBI-1048945;
CC       P02489; Q3SYF9: KRTAP19-7; NbExp=3; IntAct=EBI-6875961, EBI-10241353;
CC       P02489; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-6875961, EBI-10261141;
CC       P02489; Q92615: LARP4B; NbExp=3; IntAct=EBI-6875961, EBI-1052558;
CC       P02489; Q14847-2: LASP1; NbExp=3; IntAct=EBI-6875961, EBI-9088686;
CC       P02489; Q6DKI2: LGALS9C; NbExp=3; IntAct=EBI-6875961, EBI-9088829;
CC       P02489; Q96JB6: LOXL4; NbExp=3; IntAct=EBI-6875961, EBI-749562;
CC       P02489; Q99683: MAP3K5; NbExp=3; IntAct=EBI-6875961, EBI-476263;
CC       P02489; Q15759: MAPK11; NbExp=3; IntAct=EBI-6875961, EBI-298304;
CC       P02489; Q8N6R0: METTL13; NbExp=3; IntAct=EBI-6875961, EBI-1053295;
CC       P02489; Q92886: NEUROG1; NbExp=3; IntAct=EBI-6875961, EBI-10279647;
CC       P02489; Q9Y239: NOD1; NbExp=3; IntAct=EBI-6875961, EBI-1051262;
CC       P02489; Q96HA8: NTAQ1; NbExp=7; IntAct=EBI-6875961, EBI-741158;
CC       P02489; Q9Y266: NUDC; NbExp=3; IntAct=EBI-6875961, EBI-357298;
CC       P02489; Q6P4D5-2: PABIR3; NbExp=3; IntAct=EBI-6875961, EBI-9091052;
CC       P02489; Q495U3: PANX2; NbExp=3; IntAct=EBI-6875961, EBI-17242559;
CC       P02489; O15160: POLR1C; NbExp=3; IntAct=EBI-6875961, EBI-1055079;
CC       P02489; P19388: POLR2E; NbExp=3; IntAct=EBI-6875961, EBI-395189;
CC       P02489; Q6ZMI0-5: PPP1R21; NbExp=3; IntAct=EBI-6875961, EBI-25835994;
CC       P02489; Q96QH2: PRAM1; NbExp=3; IntAct=EBI-6875961, EBI-2860740;
CC       P02489; P41219: PRPH; NbExp=3; IntAct=EBI-6875961, EBI-752074;
CC       P02489; P60891: PRPS1; NbExp=3; IntAct=EBI-6875961, EBI-749195;
CC       P02489; P61289: PSME3; NbExp=3; IntAct=EBI-6875961, EBI-355546;
CC       P02489; P53801: PTTG1IP; NbExp=3; IntAct=EBI-6875961, EBI-3906138;
CC       P02489; Q9NWB1-5: RBFOX1; NbExp=3; IntAct=EBI-6875961, EBI-12123390;
CC       P02489; Q9BWF3: RBM4; NbExp=3; IntAct=EBI-6875961, EBI-2856454;
CC       P02489; Q8WZ73-3: RFFL; NbExp=3; IntAct=EBI-6875961, EBI-25839575;
CC       P02489; P47804-3: RGR; NbExp=3; IntAct=EBI-6875961, EBI-25834767;
CC       P02489; Q9H4E5: RHOJ; NbExp=3; IntAct=EBI-6875961, EBI-6285694;
CC       P02489; Q969K3: RNF34; NbExp=3; IntAct=EBI-6875961, EBI-2340642;
CC       P02489; P08865: RPSA; NbExp=3; IntAct=EBI-6875961, EBI-354112;
CC       P02489; P48443: RXRG; NbExp=3; IntAct=EBI-6875961, EBI-712405;
CC       P02489; Q8N488: RYBP; NbExp=3; IntAct=EBI-6875961, EBI-752324;
CC       P02489; Q9BY12-3: SCAPER; NbExp=3; IntAct=EBI-6875961, EBI-25837959;
CC       P02489; O00560: SDCBP; NbExp=7; IntAct=EBI-6875961, EBI-727004;
CC       P02489; Q86SQ7-2: SDCCAG8; NbExp=3; IntAct=EBI-6875961, EBI-10696955;
CC       P02489; Q9NTN9-3: SEMA4G; NbExp=3; IntAct=EBI-6875961, EBI-9089805;
CC       P02489; Q2NKQ1-4: SGSM1; NbExp=3; IntAct=EBI-6875961, EBI-10182463;
CC       P02489; Q5T0L3: SPATA46; NbExp=3; IntAct=EBI-6875961, EBI-750105;
CC       P02489; Q496A3: SPATS1; NbExp=3; IntAct=EBI-6875961, EBI-3923692;
CC       P02489; Q9NZD8: SPG21; NbExp=7; IntAct=EBI-6875961, EBI-742688;
CC       P02489; Q9C004: SPRY4; NbExp=3; IntAct=EBI-6875961, EBI-354861;
CC       P02489; Q96BD6: SPSB1; NbExp=3; IntAct=EBI-6875961, EBI-2659201;
CC       P02489; O75558: STX11; NbExp=3; IntAct=EBI-6875961, EBI-714135;
CC       P02489; O60506-4: SYNCRIP; NbExp=3; IntAct=EBI-6875961, EBI-11123832;
CC       P02489; O15273: TCAP; NbExp=3; IntAct=EBI-6875961, EBI-954089;
CC       P02489; Q8TDR4: TCP10L; NbExp=3; IntAct=EBI-6875961, EBI-3923210;
CC       P02489; Q96A09: TENT5B; NbExp=3; IntAct=EBI-6875961, EBI-752030;
CC       P02489; Q9BXU0: TEX12; NbExp=3; IntAct=EBI-6875961, EBI-12090309;
CC       P02489; O60830: TIMM17B; NbExp=3; IntAct=EBI-6875961, EBI-2372529;
CC       P02489; Q8IU80-2: TMPRSS6; NbExp=3; IntAct=EBI-6875961, EBI-25839648;
CC       P02489; Q8IUR5-4: TMTC1; NbExp=3; IntAct=EBI-6875961, EBI-9089156;
CC       P02489; Q96KP6: TNIP3; NbExp=3; IntAct=EBI-6875961, EBI-2509913;
CC       P02489; Q96A04: TSACC; NbExp=3; IntAct=EBI-6875961, EBI-740411;
CC       P02489; O60636: TSPAN2; NbExp=3; IntAct=EBI-6875961, EBI-3914288;
CC       P02489; Q5VYS8-5: TUT7; NbExp=3; IntAct=EBI-6875961, EBI-9088812;
CC       P02489; Q13404: UBE2V1; NbExp=3; IntAct=EBI-6875961, EBI-1050671;
CC       P02489; Q9H9P5-5: UNKL; NbExp=3; IntAct=EBI-6875961, EBI-12817837;
CC       P02489; Q9NVA1: UQCC1; NbExp=3; IntAct=EBI-6875961, EBI-11911675;
CC       P02489; Q9NX94: WBP1L; NbExp=3; IntAct=EBI-6875961, EBI-10316321;
CC       P02489; Q9NZC7-5: WWOX; NbExp=3; IntAct=EBI-6875961, EBI-12040603;
CC       P02489; Q96EF9: ZHX1-C8orf76; NbExp=3; IntAct=EBI-6875961, EBI-25830993;
CC       P02489; Q8WUU4: ZNF296; NbExp=3; IntAct=EBI-6875961, EBI-8834821;
CC       P02489; Q8N0Y2-2: ZNF444; NbExp=3; IntAct=EBI-6875961, EBI-12010736;
CC       P02489; Q7Z783; NbExp=3; IntAct=EBI-6875961, EBI-9088990;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14512969,
CC       ECO:0000269|PubMed:19464326, ECO:0000269|PubMed:19503744,
CC       ECO:0000269|PubMed:26004348, ECO:0000269|PubMed:30340470}. Nucleus
CC       {ECO:0000269|PubMed:19464326}. Note=Translocates to the nucleus during
CC       heat shock and resides in sub-nuclear structures known as SC35 speckles
CC       or nuclear splicing speckles.
CC   -!- TISSUE SPECIFICITY: Expressed in the eye lens (at protein level).
CC       {ECO:0000269|PubMed:12356833, ECO:0000269|PubMed:23255486}.
CC   -!- PTM: O-glycosylated; contains N-acetylglucosamine side chains.
CC   -!- PTM: Deamidation of Asn-101 in lens occurs mostly during the first 30
CC       years of age, followed by a small additional amount of deamidation
CC       (approximately 5%) during the next approximately 38 years, resulting in
CC       a maximum of approximately 50% deamidation during the lifetime of the
CC       individual. {ECO:0000269|PubMed:18754677, ECO:0000269|PubMed:8175657,
CC       ECO:0000269|PubMed:9068373, ECO:0000269|PubMed:9543632,
CC       ECO:0000269|PubMed:9655350}.
CC   -!- PTM: Phosphorylation on Ser-122 seems to be developmentally regulated.
CC       Absent in the first months of life, it appears during the first 12
CC       years of human lifetime. The relative amount of phosphorylated form
CC       versus unphosphorylated form does not change over the lifetime of the
CC       individual. {ECO:0000269|PubMed:10930324, ECO:0000269|PubMed:8175657,
CC       ECO:0000269|PubMed:8759518, ECO:0000269|PubMed:9068373,
CC       ECO:0000269|PubMed:9655350}.
CC   -!- PTM: Acetylation at Lys-70 may increase chaperone activity.
CC       {ECO:0000269|PubMed:22120592, ECO:0000269|PubMed:817940,
CC       ECO:0000269|PubMed:9655350}.
CC   -!- PTM: Undergoes age-dependent proteolytical cleavage at the C-terminus.
CC       Alpha-crystallin A(1-172) is the most predominant form produced most
CC       rapidly during the first 12 years of age and after this age is present
CC       in approximately 50% of the lens molecules.
CC       {ECO:0000269|PubMed:10930324, ECO:0000269|PubMed:12356833,
CC       ECO:0000269|PubMed:8175657, ECO:0000269|PubMed:9068373,
CC       ECO:0000269|PubMed:9655350}.
CC   -!- PTM: In young individuals and during the first approximately 30 years
CC       of life, less than half molecules contain an intramolecular disulfide
CC       bond (oxidized form), while in the remaining fraction the cysteines are
CC       in the free sulfhydryl form (reduced form). With aging, the amount of
CC       oxidized form increases up to 90% and it becomes a major constituent of
CC       high molecular weight aggregates, concomitant with an age-dependent
CC       loss of its chaperone activity. The reduced form is undetectable in
CC       cataractous lenses. {ECO:0000305|PubMed:31792453}.
CC   -!- MASS SPECTROMETRY: [Alpha-crystallin A chain]: Mass=19950;
CC       Method=Electrospray; Evidence={ECO:0000269|PubMed:8175657};
CC   -!- MASS SPECTROMETRY: [Alpha-crystallin A(1-172)]: Mass=19863;
CC       Method=Electrospray; Evidence={ECO:0000269|PubMed:8175657};
CC   -!- MASS SPECTROMETRY: [Alpha-crystallin A chain]: Mass=20029;
CC       Method=Electrospray; Note=With 1 phosphate group.;
CC       Evidence={ECO:0000269|PubMed:8175657};
CC   -!- MASS SPECTROMETRY: [Alpha-crystallin A chain]: Mass=19951;
CC       Method=Electrospray; Evidence={ECO:0000269|PubMed:9655350};
CC   -!- MASS SPECTROMETRY: [Alpha-crystallin A(1-172)]: Mass=19864;
CC       Method=Electrospray; Evidence={ECO:0000269|PubMed:9655350};
CC   -!- MASS SPECTROMETRY: [Alpha-crystallin A chain]: Mass=19947;
CC       Method=Electrospray; Evidence={ECO:0000269|PubMed:10930324};
CC   -!- MASS SPECTROMETRY: [Alpha-crystallin A(1-172)]: Mass=19851;
CC       Method=Electrospray; Evidence={ECO:0000269|PubMed:10930324};
CC   -!- DISEASE: Note=Alpha-crystallin A 1-172 is found at nearly twofold
CC       higher levels in diabetic lenses than in age-matched control lenses.
CC       {ECO:0000269|PubMed:12356833}.
CC   -!- DISEASE: Cataract 9, multiple types (CTRCT9) [MIM:604219]: 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. CTRCT9
CC       includes nuclear, zonular central nuclear, anterior polar, cortical,
CC       embryonal, anterior subcapsular, fan-shaped, and total cataracts, among
CC       others. In some cases cataract is associated with microcornea without
CC       any other systemic anomaly or dysmorphism. Microcornea is defined by a
CC       corneal diameter inferior to 10 mm in both meridians in an otherwise
CC       normal eye. {ECO:0000269|PubMed:11006246, ECO:0000269|PubMed:11123904,
CC       ECO:0000269|PubMed:14512969, ECO:0000269|PubMed:16453125,
CC       ECO:0000269|PubMed:16735993, ECO:0000269|PubMed:16862070,
CC       ECO:0000269|PubMed:17296897, ECO:0000269|PubMed:17724170,
CC       ECO:0000269|PubMed:17937925, ECO:0000269|PubMed:18199971,
CC       ECO:0000269|PubMed:18302245, ECO:0000269|PubMed:18407550,
CC       ECO:0000269|PubMed:18587492, ECO:0000269|PubMed:19182255,
CC       ECO:0000269|PubMed:19390652, ECO:0000269|PubMed:19503744,
CC       ECO:0000269|PubMed:19595763, ECO:0000269|PubMed:20465443,
CC       ECO:0000269|PubMed:21686328, ECO:0000269|PubMed:21866213,
CC       ECO:0000269|PubMed:22065922, ECO:0000269|PubMed:22216983,
CC       ECO:0000269|PubMed:23255486, ECO:0000269|PubMed:23288997,
CC       ECO:0000269|PubMed:23441109, ECO:0000269|PubMed:23508780,
CC       ECO:0000269|PubMed:24074001, ECO:0000269|PubMed:25729975,
CC       ECO:0000269|PubMed:26004348, ECO:0000269|PubMed:26867756,
CC       ECO:0000269|PubMed:28690483, ECO:0000269|PubMed:28839118,
CC       ECO:0000269|PubMed:29386872, ECO:0000269|PubMed:29914532,
CC       ECO:0000269|PubMed:30340470, ECO:0000269|PubMed:31523120,
CC       ECO:0000269|PubMed:32010934, ECO:0000269|PubMed:33243271,
CC       ECO:0000269|PubMed:9467006}. 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}.
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DR   EMBL; U05569; AAA97523.1; -; mRNA.
DR   EMBL; U66584; AAC50900.1; -; mRNA.
DR   EMBL; X14789; CAA32891.1; -; mRNA.
DR   EMBL; KM220588; AMM63583.1; -; mRNA.
DR   EMBL; KM220592; AMM63587.1; -; mRNA.
DR   EMBL; KM220591; AMM63586.1; -; mRNA.
DR   EMBL; KM220590; AMM63585.1; -; mRNA.
DR   EMBL; KM220589; AMM63584.1; -; mRNA.
DR   EMBL; CR407691; CAG28619.1; -; mRNA.
DR   EMBL; AP001631; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP001748; BAA95535.1; -; Genomic_DNA.
DR   EMBL; CH471079; EAX09497.1; -; Genomic_DNA.
DR   EMBL; CH471079; EAX09498.1; -; Genomic_DNA.
DR   EMBL; BC069528; AAH69528.1; -; mRNA.
DR   EMBL; BC113598; AAI13599.1; -; mRNA.
DR   EMBL; M35628; AAA52106.1; -; Genomic_DNA.
DR   EMBL; M35629; AAA52105.1; -; Genomic_DNA.
DR   CCDS; CCDS13695.1; -.
DR   PIR; S03344; CYHUAA.
DR   RefSeq; NP_000385.1; NM_000394.3.
DR   RefSeq; NP_001300979.1; NM_001314050.2.
DR   PDB; 6T1R; EM; 9.80 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1-173.
DR   PDBsum; 6T1R; -.
DR   AlphaFoldDB; P02489; -.
DR   SMR; P02489; -.
DR   BioGRID; 107799; 78.
DR   BioGRID; 3195755; 7.
DR   DIP; DIP-41265N; -.
DR   IntAct; P02489; 107.
DR   MINT; P02489; -.
DR   STRING; 9606.ENSP00000291554; -.
DR   BindingDB; P02489; -.
DR   ChEMBL; CHEMBL4296283; -.
DR   MoonDB; P02489; Curated.
DR   TCDB; 8.A.172.1.2; the Alpha-crystallin chaperone (crya) family.
DR   GlyConnect; 33; 1 O-Linked glycan.
DR   GlyGen; P02489; 2 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; P02489; -.
DR   PhosphoSitePlus; P02489; -.
DR   BioMuta; CRYAA; -.
DR   DMDM; 1706112; -.
DR   SWISS-2DPAGE; P02489; -.
DR   MassIVE; P02489; -.
DR   PaxDb; P02489; -.
DR   PeptideAtlas; P02489; -.
DR   PRIDE; P02489; -.
DR   ProteomicsDB; 20516; -.
DR   ProteomicsDB; 51526; -.
DR   Antibodypedia; 23982; 461 antibodies from 30 providers.
DR   Antibodypedia; 78327; 2 antibodies from 1 providers.
DR   DNASU; 1409; -.
DR   Ensembl; ENST00000291554.6; ENSP00000291554.2; ENSG00000160202.7.
DR   GeneID; 102724652; -.
DR   GeneID; 1409; -.
DR   KEGG; hsa:102724652; -.
DR   KEGG; hsa:1409; -.
DR   MANE-Select; ENST00000291554.6; ENSP00000291554.2; NM_000394.4; NP_000385.1.
DR   UCSC; uc002zdd.3; human.
DR   CTD; 1409; -.
DR   DisGeNET; 102724652; -.
DR   DisGeNET; 1409; -.
DR   GeneCards; CRYAA; -.
DR   GeneCards; CRYAA2; -.
DR   HGNC; HGNC:2388; CRYAA.
DR   HPA; ENSG00000160202; Group enriched (kidney, retina).
DR   MalaCards; CRYAA; -.
DR   MIM; 123580; gene.
DR   MIM; 604219; phenotype.
DR   neXtProt; NX_P02489; -.
DR   OpenTargets; ENSG00000160202; -.
DR   Orphanet; 1377; Cataract-microcornea syndrome.
DR   Orphanet; 98988; Early-onset anterior polar cataract.
DR   Orphanet; 441452; Early-onset lamellar cataract.
DR   Orphanet; 98991; Early-onset nuclear cataract.
DR   Orphanet; 98994; Total early-onset cataract.
DR   PharmGKB; PA26906; -.
DR   VEuPathDB; HostDB:ENSG00000160202; -.
DR   VEuPathDB; HostDB:ENSG00000276076; -.
DR   eggNOG; KOG3591; Eukaryota.
DR   GeneTree; ENSGT00940000160159; -.
DR   HOGENOM; CLU_095001_2_0_1; -.
DR   InParanoid; P02489; -.
DR   OMA; FRDWWED; -.
DR   OrthoDB; 1187096at2759; -.
DR   PhylomeDB; P02489; -.
DR   TreeFam; TF105049; -.
DR   PathwayCommons; P02489; -.
DR   SignaLink; P02489; -.
DR   SIGNOR; P02489; -.
DR   BioGRID-ORCS; 102724652; 0 hits in 4 CRISPR screens.
DR   BioGRID-ORCS; 1409; 6 hits in 1067 CRISPR screens.
DR   GeneWiki; CRYAA; -.
DR   Pharos; P02489; Tchem.
DR   PRO; PR:P02489; -.
DR   Proteomes; UP000005640; Chromosome 21.
DR   RNAct; P02489; protein.
DR   Bgee; ENSG00000160202; Expressed in adult mammalian kidney and 31 other tissues.
DR   ExpressionAtlas; P02489; baseline and differential.
DR   Genevisible; P02489; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IMP:UniProtKB.
DR   GO; GO:0002088; P:lens development in camera-type eye; IBA:GO_Central.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IDA:HGNC-UCL.
DR   GO; GO:0032387; P:negative regulation of intracellular transport; IDA:HGNC-UCL.
DR   GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR   GO; GO:0050821; P:protein stabilization; IMP:CAFA.
DR   GO; GO:0009408; P:response to heat; IBA:GO_Central.
DR   GO; GO:0007601; P:visual perception; IMP:UniProtKB.
DR   Gene3D; 2.60.40.790; -; 1.
DR   InterPro; IPR002068; A-crystallin/Hsp20_dom.
DR   InterPro; IPR001436; Alpha-crystallin/sHSP_animal.
DR   InterPro; IPR012274; Alpha-crystallin_A.
DR   InterPro; IPR003090; Alpha-crystallin_N.
DR   InterPro; IPR008978; HSP20-like_chaperone.
DR   PANTHER; PTHR45640; PTHR45640; 1.
DR   PANTHER; PTHR45640:SF14; PTHR45640:SF14; 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; Cataract; Chaperone; Cytoplasm;
KW   Direct protein sequencing; Disease variant; Disulfide bond;
KW   Eye lens protein; Glycoprotein; Metal-binding; Nucleus; Oxidation;
KW   Phosphoprotein; Reference proteome; Sensory transduction; Vision; Zinc.
FT   CHAIN           1..173
FT                   /note="Alpha-crystallin A chain"
FT                   /id="PRO_0000125865"
FT   CHAIN           1..172
FT                   /note="Alpha-crystallin A(1-172)"
FT                   /id="PRO_0000226639"
FT   CHAIN           1..168
FT                   /note="Alpha-crystallin A(1-168)"
FT                   /id="PRO_0000423503"
FT   CHAIN           1..162
FT                   /note="Alpha-crystallin A(1-162)"
FT                   /id="PRO_0000423504"
FT   DOMAIN          52..164
FT                   /note="sHSP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT   REGION          1..63
FT                   /note="Required for complex formation with BFSP1 and BFSP2;
FT                   during homooligomerization, mediates the association of 2
FT                   dimers to form a tetramer"
FT                   /evidence="ECO:0000269|PubMed:28935373,
FT                   ECO:0000269|PubMed:31792453"
FT   BINDING         100
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P02470"
FT   BINDING         102
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P02470"
FT   BINDING         107
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:22890888"
FT   BINDING         154
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:P02470"
FT   SITE            1
FT                   /note="Susceptible to oxidation"
FT   SITE            18
FT                   /note="Susceptible to oxidation"
FT   SITE            34
FT                   /note="Susceptible to oxidation"
FT   SITE            138
FT                   /note="Susceptible to oxidation"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000269|PubMed:817940"
FT   MOD_RES         6
FT                   /note="Deamidated glutamine; partial"
FT                   /evidence="ECO:0000269|PubMed:9068373"
FT   MOD_RES         45
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:9068373"
FT   MOD_RES         50
FT                   /note="Deamidated glutamine; partial"
FT                   /evidence="ECO:0000269|PubMed:9068373"
FT   MOD_RES         70
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:22120592,
FT                   ECO:0000269|PubMed:9655350"
FT   MOD_RES         90
FT                   /note="Deamidated glutamine; partial"
FT                   /evidence="ECO:0000269|PubMed:9068373"
FT   MOD_RES         99
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:22120592"
FT   MOD_RES         101
FT                   /note="Deamidated asparagine; partial"
FT                   /evidence="ECO:0000269|PubMed:8175657,
FT                   ECO:0000269|PubMed:9068373, ECO:0000269|PubMed:9543632,
FT                   ECO:0000269|PubMed:9655350"
FT   MOD_RES         122
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:8175657,
FT                   ECO:0000269|PubMed:8759518, ECO:0000269|PubMed:9068373"
FT   MOD_RES         123
FT                   /note="Deamidated asparagine; partial"
FT                   /evidence="ECO:0000269|PubMed:18754677"
FT   MOD_RES         147
FT                   /note="Deamidated glutamine; partial"
FT                   /evidence="ECO:0000269|PubMed:9068373"
FT   CARBOHYD        162
FT                   /note="O-linked (GlcNAc) serine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        131..142
FT                   /evidence="ECO:0000269|PubMed:31792453,
FT                   ECO:0000269|PubMed:8175657, ECO:0000269|PubMed:9068373"
FT   VARIANT         9..173
FT                   /note="Missing (in CTRCT9; unknown pathological
FT                   significance; dbSNP:rs74315440)"
FT                   /evidence="ECO:0000269|PubMed:11006246"
FT                   /id="VAR_084768"
FT   VARIANT         12
FT                   /note="R -> C (in CTRCT9; delays HSP70 expression increase
FT                   in response to heat shock; dbSNP:rs397515624)"
FT                   /evidence="ECO:0000269|PubMed:17724170,
FT                   ECO:0000269|PubMed:18587492, ECO:0000269|PubMed:19390652,
FT                   ECO:0000269|PubMed:19503744, ECO:0000269|PubMed:21686328,
FT                   ECO:0000269|PubMed:23508780, ECO:0000269|PubMed:32010934"
FT                   /id="VAR_070032"
FT   VARIANT         12
FT                   /note="R -> L (in CTRCT9; reduces protein solubility)"
FT                   /evidence="ECO:0000269|PubMed:30340470,
FT                   ECO:0000269|PubMed:31523120"
FT                   /id="VAR_084769"
FT   VARIANT         21
FT                   /note="R -> L (in CTRCT9; associated with macular
FT                   hypoplasia and a generally hypopigmented fundus)"
FT                   /evidence="ECO:0000269|PubMed:16453125"
FT                   /id="VAR_046892"
FT   VARIANT         21
FT                   /note="R -> Q (in CTRCT9; decreases oligomer formation;
FT                   dbSNP:rs397515626)"
FT                   /evidence="ECO:0000269|PubMed:23255486,
FT                   ECO:0000269|PubMed:26867756"
FT                   /id="VAR_084770"
FT   VARIANT         21
FT                   /note="R -> W (in CTRCT9; dbSNP:rs397515625)"
FT                   /evidence="ECO:0000269|PubMed:17724170,
FT                   ECO:0000269|PubMed:18587492, ECO:0000269|PubMed:19182255,
FT                   ECO:0000269|PubMed:23441109, ECO:0000269|PubMed:29386872,
FT                   ECO:0000269|PubMed:29914532, ECO:0000269|PubMed:31523120"
FT                   /id="VAR_084771"
FT   VARIANT         49
FT                   /note="R -> C (in CTRCT9; dbSNP:rs74315441)"
FT                   /evidence="ECO:0000269|PubMed:14512969,
FT                   ECO:0000269|PubMed:19182255, ECO:0000269|PubMed:33243271"
FT                   /id="VAR_038375"
FT   VARIANT         54
FT                   /note="R -> C (in CTRCT9; unknown pathological
FT                   significance; dbSNP:rs397515623)"
FT                   /evidence="ECO:0000269|PubMed:17937925,
FT                   ECO:0000269|PubMed:18587492, ECO:0000269|PubMed:28839118"
FT                   /id="VAR_084772"
FT   VARIANT         54
FT                   /note="R -> L (in CTRCT9; unknown pathological
FT                   significance)"
FT                   /evidence="ECO:0000269|PubMed:24074001"
FT                   /id="VAR_084773"
FT   VARIANT         54
FT                   /note="R -> P (in CTRCT9; unknown pathological
FT                   significance)"
FT                   /evidence="ECO:0000269|PubMed:23288997"
FT                   /id="VAR_084774"
FT   VARIANT         65
FT                   /note="R -> Q (in CTRCT9; unknown pathological
FT                   significance; dbSNP:rs199640007)"
FT                   /evidence="ECO:0000269|PubMed:28690483"
FT                   /id="VAR_084775"
FT   VARIANT         71
FT                   /note="F -> L (in CTRCT9; unknown pathological
FT                   significance; reduced chaperone-like activity in vitro)"
FT                   /evidence="ECO:0000269|PubMed:19595763"
FT                   /id="VAR_084776"
FT   VARIANT         98
FT                   /note="G -> R (in CTRCT9; forms inclusion bodies, decreases
FT                   chaperone activity, decreases protein stability at 45
FT                   degrees Celsius and increases protein aggregate formation
FT                   in response to DTT in vitro; dbSNP:rs398122947)"
FT                   /evidence="ECO:0000269|PubMed:16862070,
FT                   ECO:0000269|PubMed:18199971, ECO:0000269|PubMed:21866213"
FT                   /id="VAR_084777"
FT   VARIANT         105
FT                   /note="D -> H (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036564"
FT   VARIANT         116
FT                   /note="R -> C (in CTRCT9; zonular central nuclear cataract;
FT                   reduced chaperone-like activity and increased membrane-
FT                   binding capacity; dbSNP:rs74315439)"
FT                   /evidence="ECO:0000269|PubMed:11123904,
FT                   ECO:0000269|PubMed:16735993, ECO:0000269|PubMed:17296897,
FT                   ECO:0000269|PubMed:20465443, ECO:0000269|PubMed:31523120,
FT                   ECO:0000269|PubMed:9467006"
FT                   /id="VAR_003819"
FT   VARIANT         116
FT                   /note="R -> H (in CTRCT9; reverse phase-high-performance
FT                   liquid chromatography suggests an increased hydrophobicity
FT                   of the mutant protein; loss of chaperone activity of the
FT                   mutant is seen in DL-dithiothreitol-induced insulin
FT                   aggregation assay; fast protein liquid chromatography
FT                   purification shows that the mutant protein has increased
FT                   binding affinity to lysozyme; dbSNP:rs121912973)"
FT                   /evidence="ECO:0000269|PubMed:18302245,
FT                   ECO:0000269|PubMed:18407550, ECO:0000269|PubMed:22065922,
FT                   ECO:0000269|PubMed:22216983"
FT                   /id="VAR_046893"
FT   VARIANT         117..118
FT                   /note="RY -> H (in CTRCT9; unknown pathological
FT                   significance; dbSNP:rs367826363)"
FT                   /evidence="ECO:0000269|PubMed:21866213"
FT                   /id="VAR_084779"
FT   VARIANT         117
FT                   /note="Missing (in CTRCT9)"
FT                   /evidence="ECO:0000269|PubMed:25729975"
FT                   /id="VAR_084778"
FT   VARIANT         119
FT                   /note="R -> H (in CTRCT9; unknown pathological
FT                   significance; dbSNP:rs760170206)"
FT                   /evidence="ECO:0000269|PubMed:28690483"
FT                   /id="VAR_084780"
FT   VARIANT         139
FT                   /note="L -> P (in CTRCT9; results in protein aggregation in
FT                   the cytoplasm)"
FT                   /evidence="ECO:0000269|PubMed:26004348"
FT                   /id="VAR_084781"
FT   MUTAGEN         123
FT                   /note="N->D: Impairs chaperone activity."
FT                   /evidence="ECO:0000269|PubMed:18754677"
FT   CONFLICT        45
FT                   /note="S -> T (in Ref. 10; AAA52105)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        153..155
FT                   /note="THA -> HT (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   173 AA;  19909 MW;  81804A8439837D50 CRC64;
     MDVTIQHPWF KRTLGPFYPS RLFDQFFGEG LFEYDLLPFL SSTISPYYRQ SLFRTVLDSG
     ISEVRSDRDK FVIFLDVKHF SPEDLTVKVQ DDFVEIHGKH NERQDDHGYI SREFHRRYRL
     PSNVDQSALS CSLSADGMLT FCGPKIQTGL DATHAERAIP VSREEKPTSA PSS
 
 
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