CRBB1_HUMAN
ID CRBB1_HUMAN Reviewed; 252 AA.
AC P53674;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Beta-crystallin B1;
DE AltName: Full=Beta-B1 crystallin;
GN Name=CRYBB1;
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], PROTEIN SEQUENCE OF 2-22 AND 25-252, CLEAVAGE
RP OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND MASS SPECTROMETRY.
RC TISSUE=Lens;
RX PubMed=8626774; DOI=10.1074/jbc.271.8.4273;
RA David L.L., Lampi K.J., Lund A.L., Smith J.B.;
RT "The sequence of human betaB1-crystallin cDNA allows mass spectrometric
RT detection of betaB1 protein missing portions of its N-terminal extension.";
RL J. Biol. Chem. 271:4273-4279(1996).
RN [2]
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 200-246.
RX PubMed=8575764; DOI=10.1006/geno.1995.9947;
RA Hulsebos T.J.M., Gilbert D.J., Delattre O., Smink L.J., Dunham I.,
RA Westerveld A., Thomas G., Jenkins N.A., Copeland N.G.;
RT "Assignment of the beta B1 crystallin gene (CRYBB1) to human chromosome 22
RT and mouse chromosome 5.";
RL Genomics 29:712-718(1995).
RN [6]
RP INVOLVEMENT IN CTRCT17.
RX PubMed=12360425; DOI=10.1086/344212;
RA Mackay D.S., Boskovska O.B., Knopf H.L., Lampi K.J., Shiels A.;
RT "A nonsense mutation in CRYBB1 associated with autosomal dominant cataract
RT linked to human chromosome 22q.";
RL Am. J. Hum. Genet. 71:1216-1221(2002).
RN [7]
RP CHARACTERIZATION.
RX PubMed=15667225; DOI=10.1021/bi048419f;
RA Annunziata O., Pande A., Pande J., Ogun O., Lubsen N.H., Benedek G.B.;
RT "Oligomerization and phase transitions in aqueous solutions of native and
RT truncated human beta B1-crystallin.";
RL Biochemistry 44:1316-1328(2005).
RN [8]
RP INVOLVEMENT IN CONGENITAL CATARACT-MICROCORNEA SYNDROME.
RX PubMed=16110300;
RA Willoughby C.E., Shafiq A., Ferrini W., Chan L.L., Billingsley G.,
RA Priston M., Mok C., Chandna A., Kaye S., Heon E.;
RT "CRYBB1 mutation associated with congenital cataract and microcornea.";
RL Mol. Vis. 11:587-593(2005).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 43-252.
RX PubMed=14573871; DOI=10.1110/ps.03265903;
RA Van Montfort R.L., Bateman O.A., Lubsen N.H., Slingsby C.;
RT "Crystal structure of truncated human betaB1-crystallin.";
RL Protein Sci. 12:2606-2612(2003).
RN [10]
RP INVOLVEMENT IN CTRCT17.
RX PubMed=17460281; DOI=10.1167/iovs.06-1019;
RA Cohen D., Bar-Yosef U., Levy J., Gradstein L., Belfair N., Ofir R.,
RA Joshua S., Lifshitz T., Carmi R., Birk O.S.;
RT "Homozygous CRYBB1 deletion mutation underlies autosomal recessive
RT congenital cataract.";
RL Invest. Ophthalmol. Vis. Sci. 48:2208-2213(2007).
RN [11]
RP INVOLVEMENT IN CONGENITAL CATARACT-MICROCORNEA SYNDROME, VARIANT ARG-129,
RP AND CHARACTERIZATION OF VARIANT ARG-129.
RX PubMed=21972112; DOI=10.1002/humu.21436;
RA Wang K.J., Wang S., Cao N.-Q., Yan Y.-B., Zhu S.Q.;
RT "A novel mutation in CRYBB1 associated with congenital cataract-microcornea
RT syndrome: the p.Ser129Arg mutation destabilizes the betaB1/betaA3-
RT crystallin heteromer but not the betaB1-crystallin homomer.";
RL Hum. Mutat. 32:E2050-E2060(2011).
RN [12]
RP VARIANT CTRCT17 PHE-96.
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 [13]
RP VARIANT CTRCT17 CYS-230.
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 CTRCT17 TYR-170.
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 [15]
RP VARIANTS CTRCT17 206-TYR--LYS-252 DEL AND 219-TRP--LYS-252 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: 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.
CC -!- INTERACTION:
CC P53674; Q10567-3: AP1B1; NbExp=3; IntAct=EBI-7519424, EBI-11978055;
CC P53674; P05813: CRYBA1; NbExp=9; IntAct=EBI-7519424, EBI-7043337;
CC P53674; P53673: CRYBA4; NbExp=3; IntAct=EBI-7519424, EBI-7519711;
CC P53674; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-7519424, EBI-742054;
CC P53674; O00471: EXOC5; NbExp=3; IntAct=EBI-7519424, EBI-949824;
CC P53674; O95995: GAS8; NbExp=3; IntAct=EBI-7519424, EBI-1052570;
CC P53674; P54274: TERF1; NbExp=2; IntAct=EBI-7519424, EBI-710997;
CC -!- DOMAIN: Has a two-domain beta-structure, folded into four very similar
CC Greek key motifs.
CC -!- PTM: Specific cleavages in the N-terminal arm occur during lens
CC maturation and give rise to truncated forms, leading to impaired
CC oligomerization and protein insolubilization.
CC -!- MASS SPECTROMETRY: Mass=27941; Mass_error=6; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8626774};
CC -!- DISEASE: Cataract 17, multiple types (CTRCT17) [MIM:611544]: 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. CTRCT17
CC includes nuclear and pulverulent cataracts, among others. Nuclear
CC cataracts affect the central nucleus of the eye, are often not highly
CC visually significant. The density of the opacities varies greatly from
CC fine dots to a dense, white and chalk-like, central cataract. The
CC condition is usually bilateral. Nuclear cataracts are often combined
CC with opacified cortical fibers encircling the nuclear opacity, which
CC are referred to as cortical riders. Pulverulent cataracts are
CC characterized by a dust-like, 'pulverised' appearance of the opacities
CC which can be found in any part of the lens.
CC {ECO:0000269|PubMed:12360425, ECO:0000269|PubMed:17460281,
CC ECO:0000269|PubMed:23508780, ECO:0000269|PubMed:29386872,
CC ECO:0000269|PubMed:29914532, ECO:0000269|PubMed:33243271}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Note=CRYBB1 mutations may be a cause of congenital cataract
CC and microcornea syndrome, a disease characterized by the association of
CC congenital cataract and microcornea without any other systemic anomaly
CC or dysmorphism. Clinical findings include a corneal diameter inferior
CC to 10 mm in both meridians in an otherwise normal eye, and an inherited
CC cataract, which is most often bilateral posterior polar with
CC opacification in the lens periphery. The cataract progresses to form a
CC total cataract after visual maturity has been achieved, requiring
CC cataract extraction in the first to third decade of life
CC (PubMed:16110300 and PubMed:21972112). {ECO:0000305|PubMed:16110300,
CC ECO:0000305|PubMed:21972112}.
CC -!- SIMILARITY: Belongs to the beta/gamma-crystallin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Eye disease Crystallin, beta-B1 (CRYBB1);
CC Note=Leiden Open Variation Database (LOVD);
CC URL="https://databases.lovd.nl/shared/genes/CRYBB1";
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DR EMBL; U35340; AAC50383.1; -; mRNA.
DR EMBL; CR456425; CAG30311.1; -; mRNA.
DR EMBL; Z95115; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC036790; AAH36790.1; -; mRNA.
DR EMBL; X86398; CAA60150.1; -; Genomic_DNA.
DR CCDS; CCDS13840.1; -.
DR PIR; S55441; S55441.
DR RefSeq; NP_001878.1; NM_001887.3.
DR RefSeq; XP_011528201.1; XM_011529899.2.
DR PDB; 1OKI; X-ray; 1.40 A; A/B=43-252.
DR PDBsum; 1OKI; -.
DR AlphaFoldDB; P53674; -.
DR PCDDB; P53674; -.
DR SMR; P53674; -.
DR BioGRID; 107804; 18.
DR IntAct; P53674; 11.
DR MINT; P53674; -.
DR STRING; 9606.ENSP00000215939; -.
DR iPTMnet; P53674; -.
DR PhosphoSitePlus; P53674; -.
DR BioMuta; CRYBB1; -.
DR DMDM; 1706116; -.
DR EPD; P53674; -.
DR MassIVE; P53674; -.
DR PaxDb; P53674; -.
DR PeptideAtlas; P53674; -.
DR PRIDE; P53674; -.
DR ProteomicsDB; 56607; -.
DR Antibodypedia; 24283; 171 antibodies from 26 providers.
DR DNASU; 1414; -.
DR Ensembl; ENST00000647684.1; ENSP00000497249.1; ENSG00000100122.7.
DR GeneID; 1414; -.
DR KEGG; hsa:1414; -.
DR MANE-Select; ENST00000647684.1; ENSP00000497249.1; NM_001887.4; NP_001878.1.
DR UCSC; uc003acy.2; human.
DR CTD; 1414; -.
DR DisGeNET; 1414; -.
DR GeneCards; CRYBB1; -.
DR HGNC; HGNC:2397; CRYBB1.
DR HPA; ENSG00000100122; Tissue enhanced (epididymis).
DR MalaCards; CRYBB1; -.
DR MIM; 600929; gene.
DR MIM; 611544; phenotype.
DR neXtProt; NX_P53674; -.
DR OpenTargets; ENSG00000100122; -.
DR Orphanet; 1377; Cataract-microcornea syndrome.
DR Orphanet; 98991; Early-onset nuclear cataract.
DR Orphanet; 98984; Pulverulent cataract.
DR PharmGKB; PA26911; -.
DR VEuPathDB; HostDB:ENSG00000100122; -.
DR eggNOG; ENOG502QTJT; Eukaryota.
DR GeneTree; ENSGT00940000160516; -.
DR HOGENOM; CLU_081883_0_1_1; -.
DR InParanoid; P53674; -.
DR OMA; AQEHKIC; -.
DR OrthoDB; 1237607at2759; -.
DR PhylomeDB; P53674; -.
DR TreeFam; TF331401; -.
DR PathwayCommons; P53674; -.
DR SignaLink; P53674; -.
DR SIGNOR; P53674; -.
DR BioGRID-ORCS; 1414; 17 hits in 1077 CRISPR screens.
DR ChiTaRS; CRYBB1; human.
DR EvolutionaryTrace; P53674; -.
DR GeneWiki; CRYBB1; -.
DR GenomeRNAi; 1414; -.
DR Pharos; P53674; Tbio.
DR PRO; PR:P53674; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; P53674; protein.
DR Bgee; ENSG00000100122; Expressed in prefrontal cortex and 98 other tissues.
DR Genevisible; P53674; HS.
DR GO; GO:0005212; F:structural constituent of eye lens; IBA:GO_Central.
DR GO; GO:0002088; P:lens development in camera-type eye; IBA:GO_Central.
DR GO; GO:0007601; P:visual perception; IBA:GO_Central.
DR InterPro; IPR001064; Beta/gamma_crystallin.
DR InterPro; IPR033059; CRYBB1.
DR InterPro; IPR011024; G_crystallin-like.
DR PANTHER; PTHR11818:SF12; PTHR11818:SF12; 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.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8626774"
FT CHAIN 2..252
FT /note="Beta-crystallin B1"
FT /id="PRO_0000057550"
FT DOMAIN 59..98
FT /note="Beta/gamma crystallin 'Greek key' 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 99..143
FT /note="Beta/gamma crystallin 'Greek key' 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 149..190
FT /note="Beta/gamma crystallin 'Greek key' 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 191..233
FT /note="Beta/gamma crystallin 'Greek key' 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..58
FT /note="N-terminal arm"
FT REGION 144..148
FT /note="Connecting peptide"
FT REGION 235..252
FT /note="C-terminal arm"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:8626774"
FT VARIANT 96
FT /note="V -> F (in CTRCT17)"
FT /evidence="ECO:0000269|PubMed:23508780"
FT /id="VAR_070030"
FT VARIANT 129
FT /note="S -> R (probable disease-associated variant found in
FT a family with autosomal dominant congenital cataract and
FT microcornea; significantly decreased thermal stability of
FT CRYBB1/CRYBA1-crystallin heteromer but not CRYBB1-
FT crystallin homomer; dbSNP:rs1114167433)"
FT /evidence="ECO:0000269|PubMed:21972112"
FT /id="VAR_065296"
FT VARIANT 170
FT /note="D -> Y (in CTRCT17; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:29914532"
FT /id="VAR_084783"
FT VARIANT 206..252
FT /note="Missing (in CTRCT17; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33243271"
FT /id="VAR_084784"
FT VARIANT 219..252
FT /note="Missing (in CTRCT17; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33243271"
FT /id="VAR_084785"
FT VARIANT 230
FT /note="R -> C (in CTRCT17; unknown pathological
FT significance; dbSNP:rs762942964)"
FT /evidence="ECO:0000269|PubMed:29386872"
FT /id="VAR_084786"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:1OKI"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:1OKI"
FT STRAND 70..78
FT /evidence="ECO:0007829|PDB:1OKI"
FT TURN 83..87
FT /evidence="ECO:0007829|PDB:1OKI"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:1OKI"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:1OKI"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:1OKI"
FT STRAND 110..116
FT /evidence="ECO:0007829|PDB:1OKI"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:1OKI"
FT HELIX 124..127
FT /evidence="ECO:0007829|PDB:1OKI"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:1OKI"
FT STRAND 150..156
FT /evidence="ECO:0007829|PDB:1OKI"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:1OKI"
FT STRAND 160..169
FT /evidence="ECO:0007829|PDB:1OKI"
FT HELIX 174..177
FT /evidence="ECO:0007829|PDB:1OKI"
FT STRAND 185..198
FT /evidence="ECO:0007829|PDB:1OKI"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:1OKI"
FT STRAND 202..208
FT /evidence="ECO:0007829|PDB:1OKI"
FT STRAND 210..215
FT /evidence="ECO:0007829|PDB:1OKI"
FT HELIX 216..219
FT /evidence="ECO:0007829|PDB:1OKI"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:1OKI"
SQ SEQUENCE 252 AA; 28023 MW; 93D81A9C95A86F7F CRC64;
MSQAAKASAS ATVAVNPGPD TKGKGAPPAG TSPSPGTTLA PTTVPITSAK AAELPPGNYR
LVVFELENFQ GRRAEFSGEC SNLADRGFDR VRSIIVSAGP WVAFEQSNFR GEMFILEKGE
YPRWNTWSSS YRSDRLMSFR PIKMDAQEHK ISLFEGANFK GNTIEIQGDD APSLWVYGFS
DRVGSVKVSS GTWVGYQYPG YRGYQYLLEP GDFRHWNEWG AFQPQMQSLR RLRDKQWHLE
GSFPVLATEP PK
