ESPN_HUMAN
ID ESPN_HUMAN Reviewed; 854 AA.
AC B1AK53; Q6XYB2; Q9H0A2; Q9Y329;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Espin;
DE AltName: Full=Autosomal recessive deafness type 36 protein;
DE AltName: Full=Ectoplasmic specialization protein;
GN Name=ESPN; Synonyms=DFNB36; ORFNames=LP2654;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 663-854.
RC TISSUE=Testis;
RA Bartles J.R., Zheng L., Li A., Wang M.;
RT "Organization and chromosomal location of the espin gene in the human.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INVOLVEMENT IN DFNB36.
RX PubMed=15286153; DOI=10.1136/jmg.2004.018523;
RA Naz S., Griffith A.J., Riazuddin S., Hampton L.L., Battey J.F. Jr.,
RA Khan S.N., Riazuddin S., Wilcox E.R., Friedman T.B.;
RT "Mutations of ESPN cause autosomal recessive deafness and vestibular
RT dysfunction.";
RL J. Med. Genet. 41:591-595(2004).
RN [7]
RP VARIANTS DFNB36 ARG-719; ASN-744; GLN-774 AND LYS-848 DEL, AND
RP CHARACTERIZATION OF VARIANTS DFNB36 ARG-719; ASN-744 AND LYS-848 DEL.
RX PubMed=15930085; DOI=10.1136/jmg.2005.032086;
RA Donaudy F., Zheng L., Ficarella R., Ballana E., Carella M., Melchionda S.,
RA Estivill X., Bartles J.R., Gasparini P.;
RT "Espin gene (ESPN) mutations associated with autosomal dominant hearing
RT loss cause defects in microvillar elongation or organisation.";
RL J. Med. Genet. 43:157-161(2006).
RN [8]
RP VARIANT DFNB36 840-TRP--TYR-854 DEL.
RX PubMed=28281779; DOI=10.1089/gtmb.2016.0328;
RA Wang R., Han S., Khan A., Zhang X.;
RT "Molecular Analysis of Twelve Pakistani Families with Nonsyndromic or
RT Syndromic Hearing Loss.";
RL Genet. Test. Mol. Biomarkers 21:316-321(2017).
RN [9]
RP VARIANT USH1M 790-ARG--ARG-795 DEL, INVOLVEMENT IN USH1M, FUNCTION,
RP SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT USH1M 790-ARG--ARG-795
RP DEL, AND MUTAGENESIS OF 790-ARG--ARG-795.
RX PubMed=29572253; DOI=10.1136/jmedgenet-2017-105221;
RA Ahmed Z.M., Jaworek T.J., Sarangdhar G.N., Zheng L., Gul K., Khan S.N.,
RA Friedman T.B., Sisk R.A., Bartles J.R., Riazuddin S., Riazuddin S.;
RT "Inframe deletion of human ESPN is associated with deafness, vestibulopathy
RT and vision impairment.";
RL J. Med. Genet. 55:479-488(2018).
CC -!- FUNCTION: Multifunctional actin-bundling protein. Plays a major role in
CC regulating the organization, dimension, dynamics and signaling
CC capacities of the actin filament-rich microvilli in the mechanosensory
CC and chemosensory cells (PubMed:29572253). Required for the assembly and
CC stabilization of the stereociliary parallel actin bundles. Plays a
CC crucial role in the formation and maintenance of inner ear hair cell
CC stereocilia (By similarity). Involved in the elongation of actin in
CC stereocilia (PubMed:29572253). In extrastriolar hair cells, required
CC for targeting MYO3B to stereocilia tips, and for regulation of
CC stereocilia diameter and staircase formation.
CC {ECO:0000250|UniProtKB:Q9ET47, ECO:0000269|PubMed:29572253}.
CC -!- SUBUNIT: Monomer. Binds F-actin in a Ca(2+)-resistant fashion.
CC Interacts (via N-terminus) with BAIAP2 (via SH3-domain). Interacts with
CC PFN2. Interacts with MYO3A (via C-terminus). Interacts with MYO3B (via
CC C-terminus). {ECO:0000250|UniProtKB:Q9ET47}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q9ET47}. Cell projection, stereocilium
CC {ECO:0000269|PubMed:29572253}. Cell projection, microvillus
CC {ECO:0000269|PubMed:29572253}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=B1AK53-1; Sequence=Displayed;
CC Name=2;
CC IsoId=B1AK53-2; Sequence=VSP_033728, VSP_033729;
CC -!- DOMAIN: The WH2-domain binds actin monomer and mediates actin bundle
CC assembly. {ECO:0000250|UniProtKB:Q9ET47}.
CC -!- DISEASE: Deafness, autosomal recessive, 36, with or without vestibular
CC involvement (DFNB36) [MIM:609006]: A form of non-syndromic
CC sensorineural hearing loss. Sensorineural deafness results from damage
CC to the neural receptors of the inner ear, the nerve pathways to the
CC brain, or the area of the brain that receives sound information. DFNB36
CC is characterized by prelingual, profound hearing loss, and vestibular
CC areflexia in some patients. {ECO:0000269|PubMed:15286153,
CC ECO:0000269|PubMed:15930085, ECO:0000269|PubMed:28281779}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Usher syndrome 1M (USH1M) [MIM:618632]: A form of Usher
CC syndrome, a genetically heterogeneous condition characterized by the
CC association of retinitis pigmentosa with sensorineural deafness. Age at
CC onset and differences in auditory and vestibular function distinguish
CC Usher syndrome type 1 (USH1), Usher syndrome type 2 (USH2) and Usher
CC syndrome type 3 (USH3). USH1M is an autosomal recessive disease
CC characterized by prelingual sensorineural hearing loss, vestibular
CC dysfunction, night blindness, and progressive impairment of vision.
CC {ECO:0000269|PubMed:29572253}. Note=The disease may be caused by
CC variants affecting the gene represented in this entry.
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DR EMBL; AL136880; CAB66814.1; -; mRNA.
DR EMBL; AY203958; AAP34481.1; -; mRNA.
DR EMBL; AL031848; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL158217; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471130; EAW71537.1; -; Genomic_DNA.
DR EMBL; AF134401; AAD24480.1; -; mRNA.
DR CCDS; CCDS70.1; -. [B1AK53-1]
DR RefSeq; NP_113663.2; NM_031475.2. [B1AK53-1]
DR AlphaFoldDB; B1AK53; -.
DR SMR; B1AK53; -.
DR BioGRID; 123738; 16.
DR STRING; 9606.ENSP00000367059; -.
DR iPTMnet; B1AK53; -.
DR PhosphoSitePlus; B1AK53; -.
DR BioMuta; ESPN; -.
DR EPD; B1AK53; -.
DR jPOST; B1AK53; -.
DR MassIVE; B1AK53; -.
DR MaxQB; B1AK53; -.
DR PaxDb; B1AK53; -.
DR PeptideAtlas; B1AK53; -.
DR PRIDE; B1AK53; -.
DR ProteomicsDB; 3019; -. [B1AK53-1]
DR ProteomicsDB; 3020; -. [B1AK53-2]
DR Antibodypedia; 27332; 88 antibodies from 22 providers.
DR DNASU; 83715; -.
DR Ensembl; ENST00000461727.6; ENSP00000465308.1; ENSG00000187017.18. [B1AK53-2]
DR Ensembl; ENST00000645284.1; ENSP00000496593.1; ENSG00000187017.18. [B1AK53-1]
DR GeneID; 83715; -.
DR KEGG; hsa:83715; -.
DR MANE-Select; ENST00000645284.1; ENSP00000496593.1; NM_031475.3; NP_113663.2.
DR UCSC; uc001amy.3; human. [B1AK53-1]
DR CTD; 83715; -.
DR DisGeNET; 83715; -.
DR GeneCards; ESPN; -.
DR GeneReviews; ESPN; -.
DR HGNC; HGNC:13281; ESPN.
DR HPA; ENSG00000187017; Tissue enhanced (liver, retina, testis).
DR MalaCards; ESPN; -.
DR MIM; 606351; gene.
DR MIM; 609006; phenotype.
DR MIM; 618632; phenotype.
DR neXtProt; NX_B1AK53; -.
DR OpenTargets; ENSG00000187017; -.
DR Orphanet; 90636; Autosomal recessive non-syndromic sensorineural deafness type DFNB.
DR Orphanet; 231169; Usher syndrome type 1.
DR PharmGKB; PA27885; -.
DR VEuPathDB; HostDB:ENSG00000187017; -.
DR eggNOG; KOG0504; Eukaryota.
DR GeneTree; ENSGT00940000160408; -.
DR HOGENOM; CLU_017441_0_0_1; -.
DR InParanoid; B1AK53; -.
DR OMA; QTAHFDI; -.
DR OrthoDB; 280300at2759; -.
DR PhylomeDB; B1AK53; -.
DR TreeFam; TF326392; -.
DR PathwayCommons; B1AK53; -.
DR Reactome; R-HSA-9662360; Sensory processing of sound by inner hair cells of the cochlea.
DR Reactome; R-HSA-9662361; Sensory processing of sound by outer hair cells of the cochlea.
DR SignaLink; B1AK53; -.
DR BioGRID-ORCS; 83715; 96 hits in 1077 CRISPR screens.
DR ChiTaRS; ESPN; human.
DR GeneWiki; Espin_(protein); -.
DR GenomeRNAi; 83715; -.
DR Pharos; B1AK53; Tbio.
DR PRO; PR:B1AK53; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; B1AK53; protein.
DR Bgee; ENSG00000187017; Expressed in right testis and 137 other tissues.
DR ExpressionAtlas; B1AK53; baseline and differential.
DR Genevisible; B1AK53; HS.
DR GO; GO:0005903; C:brush border; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031941; C:filamentous actin; ISS:UniProtKB.
DR GO; GO:0005902; C:microvillus; IDA:UniProtKB.
DR GO; GO:0032420; C:stereocilium; IDA:UniProtKB.
DR GO; GO:0032426; C:stereocilium tip; ISS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0017124; F:SH3 domain binding; ISS:UniProtKB.
DR GO; GO:0051017; P:actin filament bundle assembly; IBA:GO_Central.
DR GO; GO:0030034; P:microvillar actin bundle assembly; IMP:UniProtKB.
DR GO; GO:0007605; P:sensory perception of sound; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR030233; Espn.
DR InterPro; IPR003124; WH2_dom.
DR PANTHER; PTHR24153:SF14; PTHR24153:SF14; 1.
DR Pfam; PF12796; Ank_2; 3.
DR Pfam; PF02205; WH2; 1.
DR SMART; SM00248; ANK; 8.
DR SMART; SM00246; WH2; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 6.
DR PROSITE; PS51082; WH2; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; ANK repeat; Cell projection;
KW Coiled coil; Cytoplasm; Cytoskeleton; Deafness; Disease variant; Hearing;
KW Non-syndromic deafness; Phosphoprotein; Reference proteome; Repeat;
KW Retinitis pigmentosa; Usher syndrome.
FT CHAIN 1..854
FT /note="Espin"
FT /id="PRO_0000334666"
FT REPEAT 1..31
FT /note="ANK 1"
FT REPEAT 35..64
FT /note="ANK 2"
FT REPEAT 69..99
FT /note="ANK 3"
FT REPEAT 103..133
FT /note="ANK 4"
FT REPEAT 137..167
FT /note="ANK 5"
FT REPEAT 171..201
FT /note="ANK 6"
FT REPEAT 205..235
FT /note="ANK 7"
FT REPEAT 239..268
FT /note="ANK 8"
FT REPEAT 271..300
FT /note="ANK 9"
FT DOMAIN 651..668
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 338..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 765..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 800..832
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 756..830
FT /evidence="ECO:0000255"
FT COMPBIAS 349..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..463
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..507
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..622
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..683
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..708
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63618"
FT MOD_RES 342
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ET47"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63618"
FT MOD_RES 647
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ET47"
FT MOD_RES 690
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ET47"
FT MOD_RES 696
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63618"
FT VAR_SEQ 1..536
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15498874"
FT /id="VSP_033728"
FT VAR_SEQ 543..572
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15498874"
FT /id="VSP_033729"
FT VARIANT 322
FT /note="R -> H (in dbSNP:rs3817911)"
FT /id="VAR_043451"
FT VARIANT 323
FT /note="Y -> C (in dbSNP:rs3817910)"
FT /id="VAR_043452"
FT VARIANT 719
FT /note="S -> R (in DFNB36; irregular microvillar
FT organization; dbSNP:rs121908134)"
FT /evidence="ECO:0000269|PubMed:15930085"
FT /id="VAR_043453"
FT VARIANT 744
FT /note="D -> N (in DFNB36; irregular microvillar
FT organization; dbSNP:rs121908135)"
FT /evidence="ECO:0000269|PubMed:15930085"
FT /id="VAR_043454"
FT VARIANT 774
FT /note="R -> Q (in DFNB36; sporadic case with mild
FT phenotype; unknown pathological significance;
FT dbSNP:rs121908136)"
FT /evidence="ECO:0000269|PubMed:15930085"
FT /id="VAR_043455"
FT VARIANT 790..795
FT /note="Missing (in USH1M; results in impaired elongation of
FT microvilli and stereocilia consistent with a loss of
FT function in parallel actin filament bundle assembly;
FT retains localization to microvilli and stereocilia)"
FT /evidence="ECO:0000269|PubMed:29572253"
FT /id="VAR_083335"
FT VARIANT 840..854
FT /note="Missing (in DFNB36)"
FT /evidence="ECO:0000269|PubMed:28281779"
FT /id="VAR_079505"
FT VARIANT 848
FT /note="Missing (in DFNB36; severe phenotype; severe
FT impairment of microvillar elongation; espin is less
FT efficiently targeted to the microvilli and accumulates in
FT the nucleus; dbSNP:rs1569771486)"
FT /evidence="ECO:0000269|PubMed:15930085"
FT /id="VAR_043456"
FT MUTAGEN 790..795
FT /note="RRDLLR->KKEIIK: No effect on localization to
FT microvilli. No effect on microvillar elongation."
FT /evidence="ECO:0000269|PubMed:29572253"
FT MUTAGEN 790..795
FT /note="RRDLLR->SQSTTS: Loss of targeting to microvilli.
FT Impaired microvillar elongation."
FT /evidence="ECO:0000269|PubMed:29572253"
FT CONFLICT 593
FT /note="R -> G (in Ref. 2; AAP34481)"
FT /evidence="ECO:0000305"
FT CONFLICT 597
FT /note="P -> L (in Ref. 1; CAB66814)"
FT /evidence="ECO:0000305"
FT CONFLICT 678
FT /note="F -> L (in Ref. 5; AAD24480)"
FT /evidence="ECO:0000305"
FT CONFLICT 773..774
FT /note="RR -> SW (in Ref. 5; AAD24480)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 854 AA; 91733 MW; 34B771071F733B62 CRC64;
MALEQALQAA RQGELDVLRS LHAAGLLGPS LRDPLDALPV HHAARAGKLH CLRFLVEEAA
LPAAARARNG ATPAHDASAT GHLACLQWLL SQGGCRVQDK DNSGATVLHL AARFGHPEVV
NWLLHHGGGD PTAATDMGAL PIHYAAAKGD FPSLRLLVEH YPEGVNAQTK NGATPLYLAC
QEGHLEVTQY LVQECGADPH ARAHDGMTPL HAAAQMGHSP VIVWLVSCTD VSLSEQDKDG
ATAMHFAASR GHTKVLSWLL LHGGEISADL WGGTPLHDAA ENGELECCQI LVVNGAELDV
RDRDGYTAAD LSDFNGHSHC TRYLRTVENL SVEHRVLSRD PSAELEAKQP DSGMSSPNTT
VSVQPLNFDL SSPTSTLSNY DSCSSSHSSI KGQHPPCGLS SARAADIQSY MDMLNPELGL
PRGTIGKPTP PPPPPSFPPP PPPPGTQLPP PPPGYPAPKP PVGPQAADIY MQTKNKLRHV
ETEALKKELS SCDGHDGLRR QDSSRKPRAF SKQPSTGDYY RQLGRCPGET LAARPGMAHS
EEVRARQPAR AGCPRLGPAA RGSLEGPSAP PQAALLPGNH VPNGCAADPK ASRELPPPPP
PPPPPLPEAA SSPPPAPPLP LESAGPGCGQ RRSSSSTGST KSFNMMSPTG DNSELLAEIK
AGKSLKPTPQ SKGLTTVFSG IGQPAFQPDS PLPSVSPALS PVRSPTPPAA GFQPLLNGSL
VPVPPTTPAP GVQLDVEALI PTHDEQGRPI PEWKRQVMVR KMQLKMQEEE EQRRKEEEEE
ARLASMPAWR RDLLRKKLEE EREQKRKEEE RQKQEELRRE KEQSEKLRTL GYDESKLAPW
QRQVILKKGD IAKY
