CRGD_HUMAN
ID CRGD_HUMAN Reviewed; 174 AA.
AC P07320; Q17RF7; Q53R51; Q99681;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 212.
DE RecName: Full=Gamma-crystallin D;
DE AltName: Full=Gamma-D-crystallin;
DE AltName: Full=Gamma-crystallin 4;
GN Name=CRYGD; Synonyms=CRYG4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-102.
RX PubMed=4033658; DOI=10.1128/mcb.5.6.1408-1414.1985;
RA Meakin S.O., Breitman M.L., Tsui L.-C.;
RT "Structural and evolutionary relationships among five members of the human
RT gamma-crystallin gene family.";
RL Mol. Cell. Biol. 5:1408-1414(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lens;
RA Petrash J.M., Mathur S., Manoharan M., Andley U.P.;
RT "Cloning and expression of human lens crystallins.";
RL Invest. Ophthalmol. Vis. Sci. 36:S882-S882(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [5]
RP PROTEIN SEQUENCE OF 2-11.
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 [6]
RP MUTAGENESIS OF PRO-24, AND CHARACTERIZATION OF VARIANTS CTRCT4 THR-24 AND
RP SER-24.
RX PubMed=15709761; DOI=10.1021/bi0479611;
RA Pande A., Annunziata O., Asherie N., Ogun O., Benedek G.B., Pande J.;
RT "Decrease in protein solubility and cataract formation caused by the Pro23
RT to Thr mutation in human gamma D-crystallin.";
RL Biochemistry 44:2491-2500(2005).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS), AND X-RAY CRYSTALLOGRAPHY (1.15
RP ANGSTROMS) OF VARIANT HIS-59.
RX PubMed=12729747; DOI=10.1016/s0022-2836(03)00375-9;
RA Basak A., Bateman O., Slingsby C., Pande A., Asherie N., Ogun O.,
RA Benedek G.B., Pande J.;
RT "High-resolution X-ray crystal structures of human gammaD crystallin (1.25
RT A) and the R58H mutant (1.15 A) associated with aculeiform cataract.";
RL J. Mol. Biol. 328:1137-1147(2003).
RN [9]
RP 3D-STRUCTURE MODELING.
RX PubMed=12507494; DOI=10.1016/s0006-291x(02)02895-4;
RA Salim A., Zaidi Z.H.;
RT "Homology models of human gamma-crystallins: structural study of the
RT extensive charge network in gamma-crystallins.";
RL Biochem. Biophys. Res. Commun. 300:624-630(2003).
RN [10]
RP VARIANT CTRCT4 HIS-59.
RX PubMed=10521291; DOI=10.1086/302619;
RA Heon E., Priston M., Schorderet D.F., Billingsley G.D., Girard P.O.,
RA Lubsen N., Munier F.L.;
RT "The gamma-crystallins and human cataracts: a puzzle made clearer.";
RL Am. J. Hum. Genet. 65:1261-1267(1999).
RN [11]
RP VARIANT CTRCT4 CYS-15.
RX PubMed=9927684; DOI=10.1073/pnas.96.3.1008;
RA Stephan D.A., Gillanders E., Vanderveen D., Freas-Lutz D., Wistow G.,
RA Baxevanis A.D., Robbins C.M., VanAuken A., Quesenberry M.I.,
RA Bailey-Wilson J., Juo S.-H.H., Trent J.M., Smith L., Brownstein M.J.;
RT "Progressive juvenile-onset punctate cataracts caused by mutation of the
RT gamma-D-crystallin gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:1008-1012(1999).
RN [12]
RP VARIANT CTRCT4 SER-37.
RX PubMed=10915766; DOI=10.1093/hmg/9.12.1779;
RA Kmoch S., Brynda J., Asfaw B., Bezouska K., Novak P., Rezacova P.,
RA Ondrova L., Filipec M., Sedlacek J., Elleder M.;
RT "Link between a novel human gamma-D-crystallin allele and a unique cataract
RT phenotype explained by protein crystallography.";
RL Hum. Mol. Genet. 9:1779-1786(2000).
RN [13]
RP SUBUNIT, AND CHARACTERIZATION OF VARIANT CTRCT4 CYS-15.
RX PubMed=10688888; DOI=10.1073/pnas.040554397;
RA Pande A., Pande J., Asherie N., Lomakin A., Ogun O., King J.A.,
RA Lubsen N.H., Walton D., Benedek G.B.;
RT "Molecular basis of a progressive juvenile-onset hereditary cataract.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:1993-1998(2000).
RN [14]
RP CHARACTERIZATION OF VARIANTS CTRCT4 SER-37 AND HIS-59.
RX PubMed=11371638; DOI=10.1073/pnas.101124798;
RA Pande A., Pande J., Asherie N., Lomakin A., Ogun O., King J., Benedek G.B.;
RT "Crystal cataracts: human genetic cataract caused by protein
RT crystallization.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:6116-6120(2001).
RN [15]
RP VARIANTS CTRCT4 THR-24 AND 157-TYP--SER-174 DEL, AND VARIANT VAL-102.
RX PubMed=12011157; DOI=10.1136/jmg.39.5.352;
RA Santhiya S.T., Shyam Manohar M., Rawlley D., Vijayalakshmi P.,
RA Namperumalsamy P., Gopinath P.M., Loester J., Graw J.;
RT "Novel mutations in the gamma-crystallin genes cause autosomal dominant
RT congenital cataracts.";
RL J. Med. Genet. 39:352-358(2002).
RN [16]
RP VARIANT CTRCT4 THR-24.
RX PubMed=12676897; DOI=10.1136/jmg.40.4.262;
RA Nandrot E., Slingsby C., Basak A., Cherif-Chefchaouni M., Benazzouz B.,
RA Hajaji Y., Boutayeb S., Gribouval O., Arbogast L., Berraho A., Abitbol M.,
RA Hilal L.;
RT "Gamma-D crystallin gene (CRYGD) mutation causes autosomal dominant
RT congenital cerulean cataracts.";
RL J. Med. Genet. 40:262-267(2003).
RN [17]
RP VARIANT CTRCT4 ALA-107.
RX PubMed=16943771;
RA Messina-Baas O.M., Gonzalez-Huerta L.M., Cuevas-Covarrubias S.A.;
RT "Two affected siblings with nuclear cataract associated with a novel
RT missense mutation in the CRYGD gene.";
RL Mol. Vis. 12:995-1000(2006).
RN [18]
RP VARIANT CTRCT4 SER-24.
RX PubMed=17564961; DOI=10.1086/518616;
RA Plotnikova O.V., Kondrashov F.A., Vlasov P.K., Grigorenko A.P.,
RA Ginter E.K., Rogaev E.I.;
RT "Conversion and compensatory evolution of the gamma-crystallin genes and
RT identification of a cataractogenic mutation that reverses the sequence of
RT the human CRYGD gene to an ancestral state.";
RL Am. J. Hum. Genet. 81:32-43(2007).
RN [19]
RP VARIANT CTRCT4 140-ARG--SER-174 DEL.
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 [20]
RP VARIANT CTRCT4 56-TYR--SER-174 DEL.
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 [21]
RP VARIANT CTRCT4 ARG-43, AND CHARACTERIZATION OF VARIANT CTRCT4 ARG-43.
RX PubMed=21031598; DOI=10.1002/humu.21386;
RA Wang B., Yu C., Xi Y.B., Cai H.C., Wang J., Zhou S., Zhou S., Wu Y.,
RA Yan Y.B., Ma X., Xie L.;
RT "A novel CRYGD mutation (p.Trp43Arg) causing autosomal dominant congenital
RT cataract in a Chinese family.";
RL Hum. Mutat. 32:E1939-E1947(2011).
RN [22]
RP VARIANT CTRCT4 PRO-36.
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 [23]
RP VARIANTS CTRCT4 THR-24; PRO-45 AND 140-ARG--SER-174 DEL.
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 [24]
RP VARIANT CTRCT4 THR-24.
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 [25]
RP VARIANTS CTRCT4 131-TYP--SER-174 DEL; 140-ARG--SER-174 DEL AND
RP 157-TYP--SER-174 DEL.
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: Crystallins are the dominant structural components of the
CC vertebrate eye lens.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10688888}.
CC -!- INTERACTION:
CC P07320; P24623: Cryaa; Xeno; NbExp=2; IntAct=EBI-7673124, EBI-7673244;
CC P07320; P23927: Cryab; Xeno; NbExp=2; IntAct=EBI-7673124, EBI-299046;
CC -!- DOMAIN: Has a two-domain beta-structure, folded into four very similar
CC Greek key motifs.
CC -!- DISEASE: Cataract 4, multiple types (CTRCT4) [MIM:115700]: 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. CTRCT4 includes crystalline aculeiform,
CC congenital cerulean and non-nuclear polymorphic cataracts, among
CC others. Crystalline aculeiform cataract is characterized by fiberglass-
CC like or needle-like crystals projecting in different directions,
CC through or close to the axial region of the lens. Non-nuclear
CC polymorphic cataract is a partial opacity with variable location
CC between the fetal nucleus of the lens and the equator. The fetal
CC nucleus is normal. The opacities are irregular and look similar to a
CC bunch of grapes and may be present simultaneously in different lens
CC layers. Congenital cerulean cataract is characterized by peripheral
CC bluish and white opacifications organized in concentric layers with
CC occasional central lesions arranged radially. The opacities are
CC observed in the superficial layers of the fetal nucleus as well as the
CC adult nucleus of the lens. Involvement is usually bilateral. Visual
CC acuity is only mildly reduced in childhood. In adulthood, the
CC opacifications may progress, making lens extraction necessary.
CC Histologically the lesions are described as fusiform cavities between
CC lens fibers which contain a deeply staining granular material. Although
CC the lesions may take on various colors, a dull blue is the most common
CC appearance and is responsible for the designation cerulean cataract.
CC {ECO:0000269|PubMed:10521291, ECO:0000269|PubMed:10688888,
CC ECO:0000269|PubMed:10915766, ECO:0000269|PubMed:11371638,
CC ECO:0000269|PubMed:12011157, ECO:0000269|PubMed:12676897,
CC ECO:0000269|PubMed:15709761, ECO:0000269|PubMed:16943771,
CC ECO:0000269|PubMed:17564961, ECO:0000269|PubMed:18587492,
CC ECO:0000269|PubMed:19390652, ECO:0000269|PubMed:21031598,
CC ECO:0000269|PubMed:21866213, ECO:0000269|PubMed:29914532,
CC ECO:0000269|PubMed:31523120, ECO:0000269|PubMed:33243271,
CC ECO:0000269|PubMed:9927684}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the beta/gamma-crystallin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Eye disease Crystallin, gamma-D (CRYGD); Note=Leiden
CC Open Variation Database (LOVD);
CC URL="https://databases.lovd.nl/shared/genes/CRYGD";
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DR EMBL; K03006; AAA52112.1; -; Genomic_DNA.
DR EMBL; K03005; AAA52112.1; JOINED; Genomic_DNA.
DR EMBL; U66583; AAB38686.1; -; mRNA.
DR EMBL; AC093698; AAY24041.1; -; Genomic_DNA.
DR EMBL; BC117338; AAI17339.1; -; mRNA.
DR EMBL; BC117340; AAI17341.1; -; mRNA.
DR CCDS; CCDS2378.1; -.
DR PIR; I77413; I77413.
DR RefSeq; NP_008822.2; NM_006891.3.
DR PDB; 1H4A; X-ray; 1.15 A; X=2-174.
DR PDB; 1HK0; X-ray; 1.25 A; X=2-174.
DR PDB; 2G98; X-ray; 2.20 A; A/B=2-174.
DR PDB; 2KFB; NMR; -; A=2-174.
DR PDB; 2KLJ; Other; -; A=2-174.
DR PDB; 4GR7; X-ray; 1.70 A; A/X=2-174.
DR PDB; 4JGF; X-ray; 2.50 A; A/B=2-172.
DR PDB; 6ETA; X-ray; 2.20 A; A/B=1-174.
DR PDB; 6ETC; X-ray; 1.20 A; X=1-174.
DR PDB; 6W5B; X-ray; 1.15 A; A=2-174.
DR PDB; 6WCY; X-ray; 1.20 A; A/B=2-174.
DR PDB; 7P53; X-ray; 1.57 A; X=2-174.
DR PDBsum; 1H4A; -.
DR PDBsum; 1HK0; -.
DR PDBsum; 2G98; -.
DR PDBsum; 2KFB; -.
DR PDBsum; 2KLJ; -.
DR PDBsum; 4GR7; -.
DR PDBsum; 4JGF; -.
DR PDBsum; 6ETA; -.
DR PDBsum; 6ETC; -.
DR PDBsum; 6W5B; -.
DR PDBsum; 6WCY; -.
DR PDBsum; 7P53; -.
DR AlphaFoldDB; P07320; -.
DR BMRB; P07320; -.
DR PCDDB; P07320; -.
DR SMR; P07320; -.
DR BioGRID; 107811; 17.
DR DIP; DIP-46208N; -.
DR IntAct; P07320; 2.
DR MINT; P07320; -.
DR STRING; 9606.ENSP00000264376; -.
DR ChEMBL; CHEMBL4296286; -.
DR iPTMnet; P07320; -.
DR PhosphoSitePlus; P07320; -.
DR BioMuta; CRYGD; -.
DR DMDM; 2506321; -.
DR EPD; P07320; -.
DR jPOST; P07320; -.
DR MassIVE; P07320; -.
DR MaxQB; P07320; -.
DR PaxDb; P07320; -.
DR PeptideAtlas; P07320; -.
DR PRIDE; P07320; -.
DR ProteomicsDB; 51987; -.
DR Antibodypedia; 34193; 217 antibodies from 23 providers.
DR DNASU; 1421; -.
DR Ensembl; ENST00000264376.5; ENSP00000264376.4; ENSG00000118231.5.
DR Ensembl; ENST00000644920.2; ENSP00000496652.1; ENSG00000285434.2.
DR GeneID; 1421; -.
DR KEGG; hsa:1421; -.
DR MANE-Select; ENST00000264376.5; ENSP00000264376.4; NM_006891.4; NP_008822.2.
DR UCSC; uc002vcn.5; human.
DR CTD; 1421; -.
DR DisGeNET; 1421; -.
DR GeneCards; CRYGD; -.
DR HGNC; HGNC:2411; CRYGD.
DR HPA; ENSG00000118231; Tissue enriched (ovary).
DR MalaCards; CRYGD; -.
DR MIM; 115700; phenotype.
DR MIM; 123690; gene.
DR neXtProt; NX_P07320; -.
DR OpenTargets; ENSG00000118231; -.
DR Orphanet; 1377; Cataract-microcornea syndrome.
DR Orphanet; 98989; Cerulean cataract.
DR Orphanet; 98990; Coralliform cataract.
DR Orphanet; 441452; Early-onset lamellar cataract.
DR Orphanet; 98991; Early-onset nuclear cataract.
DR Orphanet; 98984; Pulverulent cataract.
DR PharmGKB; PA26918; -.
DR VEuPathDB; HostDB:ENSG00000118231; -.
DR eggNOG; ENOG502RXJY; Eukaryota.
DR GeneTree; ENSGT00940000158720; -.
DR HOGENOM; CLU_081883_1_1_1; -.
DR InParanoid; P07320; -.
DR OMA; YRGQMME; -.
DR OrthoDB; 1220704at2759; -.
DR PhylomeDB; P07320; -.
DR PathwayCommons; P07320; -.
DR SignaLink; P07320; -.
DR SIGNOR; P07320; -.
DR BioGRID-ORCS; 1421; 18 hits in 1072 CRISPR screens.
DR EvolutionaryTrace; P07320; -.
DR GeneWiki; Crystallin,_gamma_D; -.
DR GenomeRNAi; 1421; -.
DR Pharos; P07320; Tbio.
DR PRO; PR:P07320; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P07320; protein.
DR Bgee; ENSG00000118231; Expressed in ventricular zone and 42 other tissues.
DR ExpressionAtlas; P07320; baseline and differential.
DR Genevisible; P07320; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005212; F:structural constituent of eye lens; IBA:GO_Central.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; IDA:UniProtKB.
DR GO; GO:0002088; P:lens development in camera-type eye; ISS:UniProtKB.
DR GO; GO:0070306; P:lens fiber cell differentiation; ISS:UniProtKB.
DR GO; GO:0007601; P:visual perception; IMP:UniProtKB.
DR InterPro; IPR001064; Beta/gamma_crystallin.
DR InterPro; IPR011024; G_crystallin-like.
DR Pfam; PF00030; Crystall; 2.
DR PRINTS; PR01367; BGCRYSTALLIN.
DR SMART; SM00247; XTALbg; 2.
DR SUPFAM; SSF49695; SSF49695; 1.
DR PROSITE; PS50915; CRYSTALLIN_BETA_GAMMA; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Cataract; Direct protein sequencing; Disease variant;
KW Eye lens protein; Reference proteome; Repeat; Sensory transduction; Vision.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8999933"
FT CHAIN 2..174
FT /note="Gamma-crystallin D"
FT /id="PRO_0000057588"
FT DOMAIN 2..40
FT /note="Beta/gamma crystallin 'Greek key' 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 41..83
FT /note="Beta/gamma crystallin 'Greek key' 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 88..128
FT /note="Beta/gamma crystallin 'Greek key' 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 129..171
FT /note="Beta/gamma crystallin 'Greek key' 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT REGION 84..87
FT /note="Connecting peptide"
FT VARIANT 15
FT /note="R -> C (in CTRCT4; progressive punctate cataract
FT with early onset; causes disulfide-linked oligomers
FT formation with consequent protein aggregation and
FT precipitation; dbSNP:rs121909595)"
FT /evidence="ECO:0000269|PubMed:10688888,
FT ECO:0000269|PubMed:9927684"
FT /id="VAR_010733"
FT VARIANT 24
FT /note="P -> S (in CTRCT4; reduces solubility;
FT dbSNP:rs28931605)"
FT /evidence="ECO:0000269|PubMed:15709761,
FT ECO:0000269|PubMed:17564961"
FT /id="VAR_034955"
FT VARIANT 24
FT /note="P -> T (in CTRCT4; unknown pathological
FT significance; reduces solubility; dbSNP:rs28931605)"
FT /evidence="ECO:0000269|PubMed:12011157,
FT ECO:0000269|PubMed:12676897, ECO:0000269|PubMed:15709761,
FT ECO:0000269|PubMed:29914532, ECO:0000269|PubMed:31523120"
FT /id="VAR_021145"
FT VARIANT 36
FT /note="A -> P (in CTRCT4; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:21866213"
FT /id="VAR_084800"
FT VARIANT 37
FT /note="R -> S (in CTRCT4; very low solubility; crystallizes
FT spontaneously; dbSNP:rs121909597)"
FT /evidence="ECO:0000269|PubMed:10915766,
FT ECO:0000269|PubMed:11371638"
FT /id="VAR_010734"
FT VARIANT 43
FT /note="W -> R (in CTRCT4; much less stable than the wild-
FT type protein; more prone to aggregate when subjected to
FT environmental stresses such as heat and UV irradiation)"
FT /evidence="ECO:0000269|PubMed:21031598"
FT /id="VAR_064829"
FT VARIANT 45
FT /note="L -> P (in CTRCT4; unknown pathological
FT significance; dbSNP:rs28931605)"
FT /evidence="ECO:0000269|PubMed:29914532"
FT /id="VAR_084801"
FT VARIANT 56..174
FT /note="Missing (in CTRCT4; unknown pathological
FT significance; dbSNP:rs202233735)"
FT /evidence="ECO:0000269|PubMed:19390652"
FT /id="VAR_084802"
FT VARIANT 59
FT /note="R -> H (in CTRCT4; lowered solubility; crystallizes
FT easily; dbSNP:rs121909596)"
FT /evidence="ECO:0000269|PubMed:10521291,
FT ECO:0000269|PubMed:11371638, ECO:0000269|PubMed:12729747"
FT /id="VAR_010735"
FT VARIANT 102
FT /note="M -> V"
FT /evidence="ECO:0000269|PubMed:12011157,
FT ECO:0000269|PubMed:4033658"
FT /id="VAR_021146"
FT VARIANT 107
FT /note="E -> A (in CTRCT4)"
FT /evidence="ECO:0000269|PubMed:16943771"
FT /id="VAR_034956"
FT VARIANT 131..174
FT /note="Missing (in CTRCT4; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33243271"
FT /id="VAR_084803"
FT VARIANT 140..174
FT /note="Missing (in CTRCT4)"
FT /evidence="ECO:0000269|PubMed:18587492,
FT ECO:0000269|PubMed:29914532, ECO:0000269|PubMed:33243271"
FT /id="VAR_084804"
FT VARIANT 157..174
FT /note="Missing (in CTRCT4; dbSNP:rs121909598)"
FT /evidence="ECO:0000269|PubMed:12011157,
FT ECO:0000269|PubMed:33243271"
FT /id="VAR_084805"
FT MUTAGEN 24..25
FT /note="PN->TK: No effect on solubility."
FT MUTAGEN 24
FT /note="P->TP: No effect on solubility."
FT /evidence="ECO:0000269|PubMed:15709761"
FT MUTAGEN 24
FT /note="P->V: Slightly reduces solubility."
FT /evidence="ECO:0000269|PubMed:15709761"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:1H4A"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:1H4A"
FT STRAND 13..21
FT /evidence="ECO:0007829|PDB:1H4A"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:1H4A"
FT STRAND 34..48
FT /evidence="ECO:0007829|PDB:1H4A"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:1H4A"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:1H4A"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:1H4A"
FT HELIX 66..69
FT /evidence="ECO:0007829|PDB:1H4A"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:1H4A"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:1H4A"
FT STRAND 89..95
FT /evidence="ECO:0007829|PDB:1H4A"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:1H4A"
FT STRAND 99..107
FT /evidence="ECO:0007829|PDB:1H4A"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:1H4A"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:6WCY"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:1H4A"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:1H4A"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:1H4A"
FT STRAND 140..146
FT /evidence="ECO:0007829|PDB:1H4A"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:1H4A"
FT HELIX 154..157
FT /evidence="ECO:0007829|PDB:1H4A"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:1H4A"
SQ SEQUENCE 174 AA; 20738 MW; 437EC83FD79F12E4 CRC64;
MGKITLYEDR GFQGRHYECS SDHPNLQPYL SRCNSARVDS GCWMLYEQPN YSGLQYFLRR
GDYADHQQWM GLSDSVRSCR LIPHSGSHRI RLYEREDYRG QMIEFTEDCS CLQDRFRFNE
IHSLNVLEGS WVLYELSNYR GRQYLLMPGD YRRYQDWGAT NARVGSLRRV IDFS
