ID CRBB2_HUMAN Reviewed; 205 AA. AC P43320; Q9UCM8; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 29-SEP-2021, entry version 193. DE RecName: Full=Beta-crystallin B2; DE AltName: Full=Beta-B2 crystallin; DE AltName: Full=Beta-crystallin Bp; GN Name=CRYBB2; Synonyms=CRYB2, CRYB2A; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Lens; RX PubMed=8224918; DOI=10.1016/0378-1119(93)90655-m; RA Chambers C., Russell P.; RT "Sequence of the human lens beta B2-crystallin-encoding cDNA."; RL Gene 133:295-299(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INVOLVEMENT IN CTRCT3. RX PubMed=9158139; DOI=10.1093/hmg/6.5.665; RA Litt M., Carrero-Valenzuela R., Lamorticella D.M., Schultz D.W., RA Mitchell T.N., Kramer P., Maumenee I.H.; RT "Autosomal dominant cerulean cataract is associated with a chain RT termination mutation in the human beta-crystallin gene CRYBB2."; RL Hum. Mol. Genet. 6:665-668(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84; RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., RA Beare D.M., Dunham I.; RT "A genome annotation-driven approach to cloning the human ORFeome."; RL Genome Biol. 5:R84.1-R84.11(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C., RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., RA Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP PROTEIN SEQUENCE OF 2-205, CLEAVAGE OF INITIATOR METHIONINE, AND RP ACETYLATION AT ALA-2. RC TISSUE=Lens; RX PubMed=8443605; DOI=10.1002/pro.5560020217; RA Miesbauer L.R., Smith J.B., Smith D.L.; RT "Amino acid sequence of human lens beta B2-crystallin."; RL Protein Sci. 2:290-291(1993). RN [7] RP PROTEIN SEQUENCE OF 192-205, AND MASS SPECTROMETRY. RX PubMed=8999933; DOI=10.1074/jbc.272.4.2268; RA Lampi K.J., Ma Z., Shih M., Shearer T.R., Smith J.B., Smith D.L., RA David L.L.; RT "Sequence analysis of betaA3, betaB3, and betaA4 crystallins completes the RT identification of the major proteins in young human lens."; RL J. Biol. Chem. 272:2268-2275(1997). RN [8] RP PROTEIN SEQUENCE OF 123-142. RC TISSUE=Lens; RX PubMed=1521468; DOI=10.3109/02713689209000740; RA Datiles M.B., Schumer D.J., Zigler J.S. Jr., Russell P., Anderson L., RA Garland D.; RT "Two-dimensional gel electrophoretic analysis of human lens proteins."; RL Curr. Eye Res. 11:669-677(1992). RN [9] RP MASS SPECTROMETRY. RX PubMed=8175657; RA Miesbauer L.R., Zhou X., Yang Z., Yang Z., Sun Y., Smith D.L., Smith J.B.; RT "Post-translational modifications of water-soluble human lens crystallins RT from young adults."; RL J. Biol. Chem. 269:12494-12502(1994). RN [10] RP MASS SPECTROMETRY. RX PubMed=10930324; DOI=10.1006/exer.2000.0868; RA Hanson S.R.A., Hasan A., Smith D.L., Smith J.B.; RT "The major in vivo modifications of the human water-insoluble lens RT crystallins are disulfide bonds, deamidation, methionine oxidation and RT backbone cleavage."; RL Exp. Eye Res. 71:195-207(2000). RN [11] RP INVOLVEMENT IN CTRCT3. RX PubMed=10634616; RA Gill D., Klose R., Munier F.L., McFadden M., Priston M., Billingsley G., RA Ducrey N., Schorderet D.F., Heon E.; RT "Genetic heterogeneity of the Coppock-like cataract: a mutation in CRYBB2 RT on chromosome 22q11.2."; RL Invest. Ophthalmol. Vis. Sci. 41:159-165(2000). RN [12] RP VARIANTS CTRCT3 LEU-188 AND 155-GLN--ASN-205 DEL. RX PubMed=28839118; DOI=10.1534/g3.117.300109; RA Javadiyan S., Craig J.E., Souzeau E., Sharma S., Lower K.M., Mackey D.A., RA Staffieri S.E., Elder J.E., Taranath D., Straga T., Black J., Pater J., RA Casey T., Hewitt A.W., Burdon K.P.; RT "High-Throughput Genetic Screening of 51 Pediatric Cataract Genes RT Identifies Causative Mutations in Inherited Pediatric Cataract in South RT Eastern Australia."; RL G3 (Bethesda) 7:3257-3268(2017). RN [13] RP VARIANT CTRCT3 VAL-149. RX PubMed=29386872; RA Sun Z., Zhou Q., Li H., Yang L., Wu S., Sui R.; RT "Mutations in crystallin genes result in congenital cataract associated RT with other ocular abnormalities."; RL Mol. Vis. 23:977-986(2017). RN [14] RP VARIANT CTRCT3 LEU-146. RX PubMed=29259299; DOI=10.1038/s41598-017-18222-z; RA Li L., Fan D.B., Zhao Y.T., Li Y., Kong D.Q., Cai F.F., Zheng G.Y.; RT "Two novel mutations identified in ADCC families impair crystallin protein RT distribution and induce apoptosis in human lens epithelial cells."; RL Sci. Rep. 7:17848-17848(2017). RN [15] RP VARIANT CTRCT3 LYS-155. RX PubMed=31523120; RA Zhuang J., Cao Z., Zhu Y., Liu L., Tong Y., Chen X., Wang Y., Lu C., Ma X., RA Yang J.; RT "Mutation screening of crystallin genes in Chinese families with congenital RT cataracts."; RL Mol. Vis. 25:427-437(2019). RN [16] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 2-205, SUBUNIT, AND IDENTIFICATION RP BY MASS SPECTROMETRY. RX PubMed=17327390; DOI=10.1110/ps.062659107; RA Smith M.A., Bateman O.A., Jaenicke R., Slingsby C.; RT "Mutation of interfaces in domain-swapped human betaB2-crystallin."; RL Protein Sci. 16:615-625(2007). CC -!- FUNCTION: Crystallins are the dominant structural components of the CC vertebrate eye lens. CC -!- SUBUNIT: Homo/heterodimer, or complexes of higher-order. The structure CC of beta-crystallin oligomers seems to be stabilized through CC interactions between the N-terminal arms (By similarity). CC {ECO:0000250}. CC -!- INTERACTION: CC P43320; P05813: CRYBA1; NbExp=3; IntAct=EBI-974082, EBI-7043337; CC P43320; P43320: CRYBB2; NbExp=5; IntAct=EBI-974082, EBI-974082; CC P43320; P61968: LMO4; NbExp=3; IntAct=EBI-974082, EBI-2798728; CC -!- DOMAIN: Has a two-domain beta-structure, folded into four very similar CC Greek key motifs. CC -!- MASS SPECTROMETRY: Mass=23291; Mass_error=3; Method=Electrospray; CC Evidence={ECO:0000269|PubMed:8999933}; CC -!- MASS SPECTROMETRY: Mass=23289; Method=Electrospray; CC Evidence={ECO:0000269|PubMed:8175657}; CC -!- MASS SPECTROMETRY: Mass=23290; Method=Electrospray; CC Evidence={ECO:0000269|PubMed:10930324}; CC -!- DISEASE: Cataract 3, multiple types (CTRCT3) [MIM:601547]: An CC opacification of the crystalline lens of the eye that frequently CC results in visual impairment or blindness. Opacities vary in CC morphology, are often confined to a portion of the lens, and may be CC static or progressive. CTRCT3 includes congenital cerulean and sutural CC cataract with punctate and cerulean opacities, among others. Cerulean CC cataract is characterized by peripheral bluish and white opacifications CC organized in concentric layers with occasional central lesions arranged CC radially. The opacities are observed in the superficial layers of the CC fetal nucleus as well as the adult nucleus of the lens. Involvement is CC usually bilateral. Visual acuity is only mildly reduced in childhood. CC In adulthood, the opacifications may progress, making lens extraction CC necessary. Histologically the lesions are described as fusiform CC cavities between lens fibers which contain a deeply staining granular CC material. Although the lesions may take on various colors, a dull blue CC is the most common appearance and is responsible for the designation CC cerulean cataract. Sutural cataract with punctate and cerulean CC opacities is characterized by white opacification around the anterior CC and posterior Y sutures, and grayish and bluish, spindle shaped, oval CC punctate and cerulean opacities of various sizes arranged in lamellar CC form. The spots are more concentrated towards the peripheral layers and CC do not delineate the embryonal or fetal nucleus. Phenotypic variation CC with respect to the size and density of the sutural opacities as well CC as the number and position of punctate and cerulean spots is observed CC among affected subjects. {ECO:0000269|PubMed:10634616, CC ECO:0000269|PubMed:28839118, ECO:0000269|PubMed:29259299, CC ECO:0000269|PubMed:29386872, ECO:0000269|PubMed:31523120, CC ECO:0000269|PubMed:9158139}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the beta/gamma-crystallin family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Eye disease Crystallin, beta-B2 (CRYBB2); CC Note=Leiden Open Variation Database (LOVD); CC URL="https://databases.lovd.nl/shared/genes/CRYBB2"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L10035; AAA16864.1; -; mRNA. DR EMBL; U72404; AAB39700.1; -; Genomic_DNA. DR EMBL; U72400; AAB39700.1; JOINED; Genomic_DNA. DR EMBL; U72401; AAB39700.1; JOINED; Genomic_DNA. DR EMBL; U72402; AAB39700.1; JOINED; Genomic_DNA. DR EMBL; U72403; AAB39700.1; JOINED; Genomic_DNA. DR EMBL; CR456426; CAG30312.1; -; mRNA. DR EMBL; Z99916; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC069535; AAH69535.1; -; mRNA. DR CCDS; CCDS13831.1; -. DR PIR; JC2009; JC2009. DR RefSeq; NP_000487.1; NM_000496.2. DR RefSeq; XP_006724204.1; XM_006724141.3. DR RefSeq; XP_011528202.1; XM_011529900.2. DR PDB; 1YTQ; X-ray; 1.70 A; A=2-205. DR PDBsum; 1YTQ; -. DR PCDDB; P43320; -. DR SASBDB; P43320; -. DR SMR; P43320; -. DR BioGRID; 107805; 8. DR IntAct; P43320; 7. DR MINT; P43320; -. DR STRING; 9606.ENSP00000381273; -. DR ChEMBL; CHEMBL4296284; -. DR iPTMnet; P43320; -. DR PhosphoSitePlus; P43320; -. DR BioMuta; CRYBB2; -. DR DMDM; 1169091; -. DR MassIVE; P43320; -. DR PaxDb; P43320; -. DR PeptideAtlas; P43320; -. DR PRIDE; P43320; -. DR ProteomicsDB; 55612; -. DR Antibodypedia; 35320; 125 antibodies. DR DNASU; 1415; -. DR Ensembl; ENST00000398215; ENSP00000381273; ENSG00000244752. DR Ensembl; ENST00000651629; ENSP00000498905; ENSG00000244752. DR GeneID; 1415; -. DR KEGG; hsa:1415; -. DR CTD; 1415; -. DR DisGeNET; 1415; -. DR GeneCards; CRYBB2; -. DR HGNC; HGNC:2398; CRYBB2. DR HPA; ENSG00000244752; Tissue enriched (retina). DR MalaCards; CRYBB2; -. DR MIM; 123620; gene. DR MIM; 601547; phenotype. DR neXtProt; NX_P43320; -. DR OpenTargets; ENSG00000244752; -. DR Orphanet; 1377; Cataract-microcornea syndrome. DR Orphanet; 98989; Cerulean cataract. DR Orphanet; 98991; Early-onset nuclear cataract. DR Orphanet; 441447; Early-onset posterior subcapsular cataract. DR Orphanet; 98985; Early-onset sutural cataract. DR Orphanet; 98984; Pulverulent cataract. DR Orphanet; 98994; Total early-onset cataract. DR PharmGKB; PA26912; -. DR VEuPathDB; HostDB:ENSG00000244752; -. DR eggNOG; ENOG502QVM6; Eukaryota. DR GeneTree; ENSGT00940000160048; -. DR HOGENOM; CLU_081883_0_1_1; -. DR InParanoid; P43320; -. DR OMA; YKDSTEF; -. DR OrthoDB; 1237607at2759; -. DR PhylomeDB; P43320; -. DR TreeFam; TF331401; -. DR PathwayCommons; P43320; -. DR SIGNOR; P43320; -. DR BioGRID-ORCS; 1415; 4 hits in 1013 CRISPR screens. DR ChiTaRS; CRYBB2; human. DR EvolutionaryTrace; P43320; -. DR GeneWiki; CRYBB2; -. DR GenomeRNAi; 1415; -. DR Pharos; P43320; Tbio. DR PRO; PR:P43320; -. DR Proteomes; UP000005640; Chromosome 22. DR RNAct; P43320; protein. DR Bgee; ENSG00000244752; Expressed in muscle tissue and 109 other tissues. DR ExpressionAtlas; P43320; baseline and differential. DR Genevisible; P43320; HS. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0005212; F:structural constituent of eye lens; IBA:GO_Central. DR GO; GO:0005198; F:structural molecule activity; NAS:ProtInc. DR GO; GO:0002088; P:lens development in camera-type eye; IBA:GO_Central. DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW. DR GO; GO:0007601; P:visual perception; IBA:GO_Central. DR InterPro; IPR001064; Beta/gamma_crystallin. DR InterPro; IPR033058; CRYBB2. DR InterPro; IPR011024; G_crystallin-like. DR PANTHER; PTHR11818:SF11; PTHR11818:SF11; 1. DR Pfam; PF00030; Crystall; 2. DR PRINTS; PR01367; BGCRYSTALLIN. DR SMART; SM00247; XTALbg; 2. DR SUPFAM; SSF49695; SSF49695; 1. DR PROSITE; PS50915; CRYSTALLIN_BETA_GAMMA; 4. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cataract; Direct protein sequencing; KW Disease variant; Eye lens protein; Reference proteome; Repeat; KW Sensory transduction; Vision. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:8443605" FT CHAIN 2..205 FT /note="Beta-crystallin B2" FT /id="PRO_0000057553" FT DOMAIN 17..56 FT /note="Beta/gamma crystallin 'Greek key' 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028" FT DOMAIN 57..101 FT /note="Beta/gamma crystallin 'Greek key' 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028" FT DOMAIN 107..148 FT /note="Beta/gamma crystallin 'Greek key' 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028" FT DOMAIN 149..191 FT /note="Beta/gamma crystallin 'Greek key' 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028" FT REGION 2..16 FT /note="N-terminal arm" FT REGION 102..106 FT /note="Connecting peptide" FT REGION 193..205 FT /note="C-terminal arm" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|PubMed:8443605" FT VARIANT 65 FT /note="A -> S (in dbSNP:rs16986560)" FT /id="VAR_038431" FT VARIANT 146 FT /note="V -> L (in CTRCT3; unknown pathological FT significance)" FT /evidence="ECO:0000269|PubMed:29259299" FT /id="VAR_084787" FT VARIANT 149 FT /note="G -> V (in CTRCT3; unknown pathological FT significance)" FT /evidence="ECO:0000269|PubMed:29386872" FT /id="VAR_084788" FT VARIANT 155..205 FT /note="Missing (in CTRCT3)" FT /evidence="ECO:0000269|PubMed:28839118" FT /id="VAR_084789" FT VARIANT 155 FT /note="Q -> K (in CTRCT3; unknown pathological FT significance)" FT /evidence="ECO:0000269|PubMed:31523120" FT /id="VAR_084790" FT VARIANT 188 FT /note="R -> L (in CTRCT3; unknown pathological FT significance)" FT /evidence="ECO:0000269|PubMed:28839118" FT /id="VAR_084791" FT STRAND 18..24 FT /evidence="ECO:0007829|PDB:1YTQ" FT STRAND 31..36 FT /evidence="ECO:0007829|PDB:1YTQ" FT HELIX 41..44 FT /evidence="ECO:0007829|PDB:1YTQ" FT STRAND 50..56 FT /evidence="ECO:0007829|PDB:1YTQ" FT STRAND 59..64 FT /evidence="ECO:0007829|PDB:1YTQ" FT TURN 65..67 FT /evidence="ECO:0007829|PDB:1YTQ" FT STRAND 68..74 FT /evidence="ECO:0007829|PDB:1YTQ" FT STRAND 76..79 FT /evidence="ECO:0007829|PDB:1YTQ" FT HELIX 82..84 FT /evidence="ECO:0007829|PDB:1YTQ" FT STRAND 96..99 FT /evidence="ECO:0007829|PDB:1YTQ" FT STRAND 108..114 FT /evidence="ECO:0007829|PDB:1YTQ" FT TURN 115..117 FT /evidence="ECO:0007829|PDB:1YTQ" FT STRAND 118..127 FT /evidence="ECO:0007829|PDB:1YTQ" FT HELIX 133..135 FT /evidence="ECO:0007829|PDB:1YTQ" FT STRAND 143..146 FT /evidence="ECO:0007829|PDB:1YTQ" FT STRAND 151..156 FT /evidence="ECO:0007829|PDB:1YTQ" FT TURN 157..159 FT /evidence="ECO:0007829|PDB:1YTQ" FT STRAND 160..166 FT /evidence="ECO:0007829|PDB:1YTQ" FT STRAND 168..171 FT /evidence="ECO:0007829|PDB:1YTQ" FT HELIX 174..177 FT /evidence="ECO:0007829|PDB:1YTQ" FT STRAND 180..182 FT /evidence="ECO:0007829|PDB:1YTQ" FT STRAND 186..189 FT /evidence="ECO:0007829|PDB:1YTQ" SQ SEQUENCE 205 AA; 23380 MW; FD95C354724A67D0 CRC64; MASDHQTQAG KPQSLNPKII IFEQENFQGH SHELNGPCPN LKETGVEKAG SVLVQAGPWV GYEQANCKGE QFVFEKGEYP RWDSWTSSRR TDSLSSLRPI KVDSQEHKII LYENPNFTGK KMEIIDDDVP SFHAHGYQEK VSSVRVQSGT WVGYQYPGYR GLQYLLEKGD YKDSSDFGAP HPQVQSVRRI RDMQWHQRGA FHPSN //