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 24-JAN-2024, entry version 202. 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, 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"; 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; 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.ENSP00000497249; -. DR iPTMnet; P53674; -. DR PhosphoSitePlus; P53674; -. DR BioMuta; CRYBB1; -. DR DMDM; 1706116; -. DR EPD; P53674; -. DR MassIVE; P53674; -. DR PaxDb; 9606-ENSP00000215939; -. DR PeptideAtlas; P53674; -. DR ProteomicsDB; 56607; -. DR Antibodypedia; 24283; 183 antibodies from 27 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 AGR; HGNC:2397; -. 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; 3998747at2759; -. DR PhylomeDB; P53674; -. DR TreeFam; TF331401; -. DR PathwayCommons; P53674; -. DR SignaLink; P53674; -. DR SIGNOR; P53674; -. DR BioGRID-ORCS; 1414; 17 hits in 1155 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 primordial germ cell in gonad and 99 other cell types or tissues. 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 Gene3D; 2.60.20.10; Crystallins; 2. DR InterPro; IPR001064; Beta/gamma_crystallin. DR InterPro; IPR011024; G_crystallin-like. DR PANTHER; PTHR11818:SF12; BETA-CRYSTALLIN B1; 1. DR PANTHER; PTHR11818; BETA/GAMMA CRYSTALLIN; 1. DR Pfam; PF00030; Crystall; 2. DR PRINTS; PR01367; BGCRYSTALLIN. DR SMART; SM00247; XTALbg; 2. DR SUPFAM; SSF49695; gamma-Crystallin-like; 1. DR PROSITE; PS50915; CRYSTALLIN_BETA_GAMMA; 4. DR Genevisible; P53674; HS. 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 (found in a family with autosomal dominant FT congenital cataract and microcornea; likely pathogenic; FT significantly decreased thermal stability of FT CRYBB1/CRYBA1-crystallin heteromer but not FT CRYBB1-crystallin homomer; dbSNP:rs1114167433)" FT /evidence="ECO:0000269|PubMed:21972112" FT /id="VAR_065296" FT VARIANT 170 FT /note="D -> Y (in CTRCT17; uncertain significance)" FT /evidence="ECO:0000269|PubMed:29914532" FT /id="VAR_084783" FT VARIANT 206..252 FT /note="Missing (in CTRCT17; uncertain significance)" FT /evidence="ECO:0000269|PubMed:33243271" FT /id="VAR_084784" FT VARIANT 219..252 FT /note="Missing (in CTRCT17; uncertain significance)" FT /evidence="ECO:0000269|PubMed:33243271" FT /id="VAR_084785" FT VARIANT 230 FT /note="R -> C (in CTRCT17; uncertain significance; FT 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 //