BFSP1_HUMAN
ID BFSP1_HUMAN Reviewed; 665 AA.
AC Q12934; F5H0G1; O43595; O76034; O95676; Q8IVZ6; Q9HBX4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 3.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Filensin;
DE AltName: Full=Beaded filament structural protein 1;
DE AltName: Full=Lens fiber cell beaded-filament structural protein CP 115;
DE Short=CP115;
DE AltName: Full=Lens intermediate filament-like heavy;
DE Short=LIFL-H;
DE Contains:
DE RecName: Full=Filensin C-terminal fragment {ECO:0000303|PubMed:30790544};
DE Contains:
DE RecName: Full=Filensin N-terminal fragment {ECO:0000250|UniProtKB:Q06002};
GN Name=BFSP1;
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] (ISOFORM 1).
RX PubMed=9628810; DOI=10.1006/exer.1998.0478;
RA Hess J.F., Casselman J.T., Kong A.P., FitzGerald P.G.;
RT "Primary sequence, secondary structure, gene structure, and assembly
RT properties suggests that the lens-specific cytoskeletal protein filensin
RT represents a novel class of intermediate filament protein.";
RL Exp. Eye Res. 66:625-644(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RX PubMed=9787085; DOI=10.1006/geno.1998.5478;
RA Rendtorff N.D., Hansen C., Silahtaroglu A., Henriksen K.F., Tommerup N.;
RT "Isolation of the human beaded-filament structural protein 1 gene (BFSP1)
RT and assignment to chromosome 20p11.23-p12.1.";
RL Genomics 53:114-116(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Mammary gland;
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 [MRNA] OF 120-249, AND TISSUE SPECIFICITY.
RC TISSUE=Lens;
RX PubMed=7720401; DOI=10.3109/02713689508999909;
RA Hess J.F., Casselman J.T., FitzGerald P.G.;
RT "Chromosomal locations of the genes for the beaded filament proteins CP 115
RT and CP 47.";
RL Curr. Eye Res. 14:11-18(1995).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-178.
RX PubMed=10909854; DOI=10.1038/sj.ejhg.5200485;
RA Yamada K., Tomita H., Yoshiura K., Kondo S., Wakui K., Fukushima Y.,
RA Ikegawa S., Nakamura Y., Amemiya T., Niikawa N.;
RT "An autosomal dominant posterior polar cataract locus maps to human
RT chromosome 20p12-q12.";
RL Eur. J. Hum. Genet. 8:535-539(2000).
RN [7]
RP INVOLVEMENT IN CTRCT33.
RX PubMed=17225135; DOI=10.1007/s00439-006-0319-6;
RA Ramachandran R.D., Perumalsamy V., Hejtmancik J.F.;
RT "Autosomal recessive juvenile onset cataract associated with mutation in
RT BFSP1.";
RL Hum. Genet. 121:475-482(2007).
RN [8]
RP FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH BFSP2 AND CRYAA.
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 [9]
RP INVOLVEMENT IN CTRCT33.
RX PubMed=28450710; DOI=10.1038/s41598-017-01182-9;
RA Zhai Y., Li J., Yu W., Zhu S., Yu Y., Wu M., Sun G., Gong X., Yao K.;
RT "Targeted exome sequencing of congenital cataracts related genes:
RT broadening the mutation spectrum and genotype-phenotype correlations in 27
RT Chinese Han families.";
RL Sci. Rep. 7:1219-1219(2017).
RN [10]
RP FUNCTION, TISSUE SPECIFICITY, MYRISTOYLATION AT GLY-434, PROTEOLYTIC
RP CLEAVAGE, AND MUTAGENESIS OF ASP-433 AND GLY-434.
RX PubMed=30790544; DOI=10.1016/j.exer.2019.02.001;
RA Tapodi A., Clemens D.M., Uwineza A., Goldberg M.W., Thinon E., Heal W.P.,
RA Tate E.W., Nemeth-Cahalan K., Vorontsova I., Jarrin M., Hall J.E.,
RA Quinlan R.A.;
RT "BFSP1 C-terminal domains released by post-translational processing events
RT can alter significantly the calcium regulation of AQP0 water
RT permeability.";
RL Exp. Eye Res. 185:107585-107585(2019).
RN [11]
RP VARIANT CTRCT33 ASN-348.
RX PubMed=24379646;
RA Wang H., Zhang T., Wu D., Zhang J.;
RT "A novel beaded filament structural protein 1 (BFSP1) gene mutation
RT associated with autosomal dominant congenital cataract in a Chinese
RT family.";
RL Mol. Vis. 19:2590-2595(2013).
CC -!- FUNCTION: Required for the correct formation of lens intermediate
CC filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA
CC (PubMed:28935373). Involved in altering the calcium regulation of MIP
CC water permeability (PubMed:30790544). {ECO:0000269|PubMed:28935373,
CC ECO:0000269|PubMed:30790544}.
CC -!- SUBUNIT: Part of a complex required for lens intermediate filament
CC formation composed of BFSP1, BFSP2 and CRYAA (PubMed:28935373).
CC Identified in a complex that contains VIM, EZR, AHNAK, BFSP1, BFSP2,
CC ANK2, PLEC, PRX and spectrin (By similarity). Found in a complex
CC composed of PPL (via C-terminal linker domain), BFSP1 and BFSP2 in the
CC retinal lens (By similarity). Within the complex interacts with BFSP2
CC (By similarity). Interacts (via C-terminus) with MIP (via C-terminus)
CC in aged lens fiber cells (By similarity).
CC {ECO:0000250|UniProtKB:A2AMT1, ECO:0000250|UniProtKB:Q06002,
CC ECO:0000269|PubMed:28935373}.
CC -!- INTERACTION:
CC Q12934; P37198: NUP62; NbExp=3; IntAct=EBI-10227494, EBI-347978;
CC Q12934-2; Q13515: BFSP2; NbExp=5; IntAct=EBI-12123320, EBI-10229433;
CC Q12934-2; Q13895: BYSL; NbExp=3; IntAct=EBI-12123320, EBI-358049;
CC Q12934-2; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-12123320, EBI-10175300;
CC Q12934-2; Q9Y6C2-2: EMILIN1; NbExp=3; IntAct=EBI-12123320, EBI-11748557;
CC Q12934-2; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-12123320, EBI-14069005;
CC Q12934-2; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-12123320, EBI-3044087;
CC Q12934-2; P37198: NUP62; NbExp=3; IntAct=EBI-12123320, EBI-347978;
CC Q12934-2; O95295: SNAPIN; NbExp=3; IntAct=EBI-12123320, EBI-296723;
CC Q12934-2; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-12123320, EBI-739895;
CC Q12934-2; O95229: ZWINT; NbExp=3; IntAct=EBI-12123320, EBI-1001132;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q06002};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q06002}; Cytoplasmic
CC side {ECO:0000250|UniProtKB:Q06002}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q02435}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q06002}. Cytoplasm, cell cortex
CC {ECO:0000250|UniProtKB:Q06002}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q12934-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q12934-2; Sequence=VSP_024921, VSP_024922;
CC Name=3;
CC IsoId=Q12934-3; Sequence=VSP_055064;
CC -!- TISSUE SPECIFICITY: Expressed in the cortex and nucleus of the retina
CC lens (at protein level). {ECO:0000269|PubMed:30790544,
CC ECO:0000269|PubMed:7720401}.
CC -!- PTM: Proteolytically cleaved during lens cell fiber differentiation
CC with increased fragmentation as fiber cell age increases.
CC {ECO:0000250|UniProtKB:Q06002}.
CC -!- PTM: [Filensin C-terminal fragment]: Myristoylated at Gly-434 following
CC proteolytic cleavage at Asp-433. {ECO:0000269|PubMed:30790544}.
CC -!- PTM: [Filensin N-terminal fragment]: Acetylated at Ala-42 following
CC proteolytic cleavage at Leu-41. {ECO:0000250|UniProtKB:Q06002}.
CC -!- DISEASE: Cataract 33, multiple types (CTRCT33) [MIM:611391]: 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. CTRCT33
CC has juvenile-onset and the opacities are restricted to the cortex of
CC the lens, not involving the nucleus. {ECO:0000269|PubMed:17225135,
CC ECO:0000269|PubMed:24379646, ECO:0000269|PubMed:28450710}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA76349.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF039655; AAB94939.1; -; mRNA.
DR EMBL; Y16717; CAA76348.1; -; mRNA.
DR EMBL; Y16718; CAA76349.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Y16719; CAA76349.1; JOINED; Genomic_DNA.
DR EMBL; Y16720; CAA76349.1; JOINED; Genomic_DNA.
DR EMBL; Y16722; CAA76349.1; JOINED; Genomic_DNA.
DR EMBL; Y16723; CAA76349.1; JOINED; Genomic_DNA.
DR EMBL; Y16721; CAA76349.1; JOINED; Genomic_DNA.
DR EMBL; AL031664; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL132765; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC041483; AAH41483.1; -; mRNA.
DR EMBL; U12622; AAA74423.1; -; mRNA.
DR EMBL; AH009849; AAG17186.1; -; Genomic_DNA.
DR CCDS; CCDS13126.1; -. [Q12934-1]
DR CCDS; CCDS54448.1; -. [Q12934-2]
DR CCDS; CCDS63229.1; -. [Q12934-3]
DR PIR; I38730; I38730.
DR RefSeq; NP_001155177.1; NM_001161705.1. [Q12934-2]
DR RefSeq; NP_001186.1; NM_001195.4. [Q12934-1]
DR RefSeq; NP_001265535.1; NM_001278606.1. [Q12934-3]
DR RefSeq; NP_001265536.1; NM_001278607.1.
DR RefSeq; NP_001265537.1; NM_001278608.1. [Q12934-3]
DR AlphaFoldDB; Q12934; -.
DR SMR; Q12934; -.
DR BioGRID; 107100; 46.
DR IntAct; Q12934; 15.
DR STRING; 9606.ENSP00000367104; -.
DR iPTMnet; Q12934; -.
DR PhosphoSitePlus; Q12934; -.
DR BioMuta; BFSP1; -.
DR DMDM; 17372543; -.
DR jPOST; Q12934; -.
DR MassIVE; Q12934; -.
DR PaxDb; Q12934; -.
DR PeptideAtlas; Q12934; -.
DR PRIDE; Q12934; -.
DR ProteomicsDB; 25331; -.
DR ProteomicsDB; 59039; -. [Q12934-1]
DR ProteomicsDB; 59040; -. [Q12934-2]
DR Antibodypedia; 9222; 287 antibodies from 29 providers.
DR DNASU; 631; -.
DR Ensembl; ENST00000377868.6; ENSP00000367099.2; ENSG00000125864.14. [Q12934-2]
DR Ensembl; ENST00000377873.8; ENSP00000367104.3; ENSG00000125864.14. [Q12934-1]
DR Ensembl; ENST00000536626.7; ENSP00000442522.1; ENSG00000125864.14. [Q12934-3]
DR GeneID; 631; -.
DR KEGG; hsa:631; -.
DR MANE-Select; ENST00000377873.8; ENSP00000367104.3; NM_001195.5; NP_001186.1.
DR UCSC; uc002wpo.4; human. [Q12934-1]
DR CTD; 631; -.
DR DisGeNET; 631; -.
DR GeneCards; BFSP1; -.
DR HGNC; HGNC:1040; BFSP1.
DR HPA; ENSG00000125864; Low tissue specificity.
DR MalaCards; BFSP1; -.
DR MIM; 603307; gene.
DR MIM; 611391; phenotype.
DR neXtProt; NX_Q12934; -.
DR OpenTargets; ENSG00000125864; -.
DR Orphanet; 98991; Early-onset nuclear cataract.
DR PharmGKB; PA25343; -.
DR VEuPathDB; HostDB:ENSG00000125864; -.
DR eggNOG; ENOG502QRCH; Eukaryota.
DR GeneTree; ENSGT00390000016976; -.
DR HOGENOM; CLU_028949_0_0_1; -.
DR InParanoid; Q12934; -.
DR OMA; MIVETMI; -.
DR OrthoDB; 677568at2759; -.
DR PhylomeDB; Q12934; -.
DR TreeFam; TF331671; -.
DR PathwayCommons; Q12934; -.
DR SignaLink; Q12934; -.
DR BioGRID-ORCS; 631; 14 hits in 1073 CRISPR screens.
DR ChiTaRS; BFSP1; human.
DR GeneWiki; BFSP1; -.
DR GenomeRNAi; 631; -.
DR Pharos; Q12934; Tbio.
DR PRO; PR:Q12934; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q12934; protein.
DR Bgee; ENSG00000125864; Expressed in tendon of biceps brachii and 117 other tissues.
DR Genevisible; Q12934; HS.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005882; C:intermediate filament; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc.
DR GO; GO:0005212; F:structural constituent of eye lens; IBA:GO_Central.
DR GO; GO:0048469; P:cell maturation; IEA:Ensembl.
DR GO; GO:0045109; P:intermediate filament organization; ISS:UniProtKB.
DR GO; GO:0070307; P:lens fiber cell development; IBA:GO_Central.
DR InterPro; IPR042358; BFSP1.
DR InterPro; IPR039008; IF_rod_dom.
DR PANTHER; PTHR14069; PTHR14069; 1.
DR Pfam; PF00038; Filament; 1.
DR SMART; SM01391; Filament; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cataract; Cell membrane; Coiled coil;
KW Cytoplasm; Cytoskeleton; Eye lens protein; Intermediate filament;
KW Lipoprotein; Membrane; Myristate; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..665
FT /note="Filensin"
FT /id="PRO_0000063847"
FT CHAIN 42..433
FT /note="Filensin N-terminal fragment"
FT /evidence="ECO:0000250|UniProtKB:Q06002"
FT /id="PRO_0000448670"
FT CHAIN 434..665
FT /note="Filensin C-terminal fragment"
FT /evidence="ECO:0000269|PubMed:30790544"
FT /id="PRO_0000448671"
FT DOMAIN 40..320
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..40
FT /note="Head"
FT REGION 41..75
FT /note="Coil 1A"
FT REGION 76..84
FT /note="Linker 1"
FT REGION 85..184
FT /note="Coil 1B"
FT REGION 185..201
FT /note="Linker 12"
FT REGION 202..320
FT /note="Coil 2"
FT REGION 321..665
FT /note="Tail"
FT REGION 410..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..572
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 41..42
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:Q06002"
FT SITE 433..434
FT /note="Cleavage (by CASP2, CASP3, and CASP7)"
FT /evidence="ECO:0000269|PubMed:30790544"
FT SITE 457
FT /note="Interaction with MIP"
FT /evidence="ECO:0000250|UniProtKB:Q06002"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06002"
FT MOD_RES 42
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q06002"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06002"
FT MOD_RES 420
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06002"
FT MOD_RES 513
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06002"
FT MOD_RES 665
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06002"
FT LIPID 434
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:30790544"
FT VAR_SEQ 1..139
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_055064"
FT VAR_SEQ 1..125
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024921"
FT VAR_SEQ 126
FT /note="K -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024922"
FT VARIANT 345
FT /note="G -> S (in dbSNP:rs6080719)"
FT /id="VAR_024492"
FT VARIANT 348
FT /note="D -> N (in CTRCT33; dbSNP:rs1085307126)"
FT /evidence="ECO:0000269|PubMed:24379646"
FT /id="VAR_078861"
FT VARIANT 656
FT /note="D -> E (in dbSNP:rs16999317)"
FT /id="VAR_036683"
FT MUTAGEN 433
FT /note="D->A: Abolishes cleavage by CASP2."
FT /evidence="ECO:0000269|PubMed:30790544"
FT MUTAGEN 434
FT /note="G->A: No effect on cleavage."
FT /evidence="ECO:0000269|PubMed:30790544"
FT CONFLICT 96
FT /note="R -> P (in Ref. 6; AAG17186)"
FT /evidence="ECO:0000305"
FT CONFLICT 176..177
FT /note="HK -> TR (in Ref. 5; AAA74423)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="T -> A (in Ref. 5; AAA74423)"
FT /evidence="ECO:0000305"
FT CONFLICT 398
FT /note="K -> R (in Ref. 1; AAB94939)"
FT /evidence="ECO:0000305"
FT CONFLICT 568
FT /note="E -> G (in Ref. 1; AAB94939)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 665 AA; 74544 MW; A99FE174A8B63E9C CRC64;
MYRRSYVFQT RKEQYEHADE ASRAAEPERP ADEGWAGATS LAALQGLGER VAAHVQRARA
LEQRHAGLRR QLDAFQRLGE LAGPEDALAR QVESNRQRVR DLEAERARLE RQGTEAQRAL
DEFRSKYENE CECQLLLKEM LERLNKEADE ALLHNLRLQL EAQFLQDDIS AAKDRHKKNL
LEVQTYISIL QQIIHTTPPA SIVTSGMREE KLLTEREVAA LRSQLEEGRE VLSHLQAQRV
ELQAQTTTLE QAIKSAHECY DDEIQLYNEQ IETLRKEIEE TERVLEKSSY DCRQLAVAQQ
TLKNELDRYH RIIEIEGNRL TSAFIETPIP LFTQSHGVSL STGSGGKDLT RALQDITAAK
PRQKALPKNV PRRKEIITKD KTNGALEDAP LKGLEDTKLV QVVLKEESES KFESESKEVS
PLTQEGAPED VPDGGQISKG FGKLYRKVKE KVRSPKEPET PTELYTKERH VLVTGDANYV
DPRFYVSSIT AKGGVAVSVA EDSVLYDGQV EPSPESPKPP LENGQVGLQE KEDGQPIDQQ
PIDKEIEPDG AELEGPEEKR EGEERDEESR RPCAMVTPGA EEPSIPEPPK PAADQDGAEV
LGTRSRSLPE KGPPKALAYK TVEVVESIEK ISTESIQTYE ETAVIVETMI GKTKSDKKKS
GEKSS
