SRR55_DROME
ID SRR55_DROME Reviewed; 376 AA.
AC P26686; A4V2U2; E1JIK1; E1JIK2; E1JIK3; E4NKI6; Q24252; Q26277; Q8IH12;
AC Q8ING7; Q8ING8; Q8ING9; Q8MZ66; Q8T0I0; Q9VFT0; Q9VFT1;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Serine-arginine protein 55;
DE Short=SRP55;
DE AltName: Full=52 kDa bracketing protein;
DE AltName: Full=B52 protein;
DE AltName: Full=Protein enhancer of deformed;
GN Name=B52; Synonyms=E(Dfd), RS55, SR55; ORFNames=CG10851;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), PROTEIN SEQUENCE OF 2-15; 126-132
RP AND 137-148, FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RC STRAIN=CL; TISSUE=Embryo;
RX PubMed=1717489; DOI=10.1083/jcb.115.3.587;
RA Roth M.B., Zahler A.M., Stolk J.A.;
RT "A conserved family of nuclear phosphoproteins localized to sites of
RT polymerase II transcription.";
RL J. Cell Biol. 115:587-596(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), AND SUBCELLULAR LOCATION.
RC TISSUE=Embryo;
RX PubMed=1885003; DOI=10.1101/gad.5.9.1611;
RA Champlin D.T., Frasch M., Saumweber H., Lis J.T.;
RT "Characterization of a Drosophila protein associated with boundaries of
RT transcriptionally active chromatin.";
RL Genes Dev. 5:1611-1621(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND G).
RC STRAIN=Berkeley; TISSUE=Embryo, Head, and Testis;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A; E AND G).
RC STRAIN=Berkeley; TISSUE=Head, and Ovary;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Booth B.,
RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E.,
RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G.,
RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S.,
RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M.,
RA Celniker S.E.;
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 7-42.
RX PubMed=8417324; DOI=10.1128/mcb.13.1.174-183.1993;
RA Kim Y.-J., Baker B.S.;
RT "Isolation of RRM-type RNA-binding protein genes and the analysis of their
RT relatedness by using a numerical approach.";
RL Mol. Cell. Biol. 13:174-183(1993).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=1741384; DOI=10.1073/pnas.89.4.1301;
RA Mayeda A., Zahler A.M., Krainer A.R., Roth M.B.;
RT "Two members of a conserved family of nuclear phosphoproteins are involved
RT in pre-mRNA splicing.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:1301-1304(1992).
RN [9]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=7935465; DOI=10.1128/mcb.14.11.7499-7506.1994;
RA Ring H.Z., Lis J.T.;
RT "The SR protein B52/SRp55 is essential for Drosophila development.";
RL Mol. Cell. Biol. 14:7499-7506(1994).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Essential for development. May have a critical role in
CC splicing or in controlling alternative splice site use of at least some
CC pre-mRNA in vivo. Not required for all splicing. May play a general
CC role in the condensation or decondensation of chromatin.
CC {ECO:0000269|PubMed:1717489, ECO:0000269|PubMed:1741384,
CC ECO:0000269|PubMed:7935465}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:1717489,
CC ECO:0000269|PubMed:1741384, ECO:0000269|PubMed:1885003}.
CC Note=Associated with boundaries of transcriptionally active chromatin.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=Long;
CC IsoId=P26686-1; Sequence=Displayed;
CC Name=A; Synonyms=C;
CC IsoId=P26686-2; Sequence=VSP_015926, VSP_005878;
CC Name=B;
CC IsoId=P26686-3; Sequence=VSP_015932;
CC Name=D {ECO:0000312|FlyBase:FBgn0004587}; Synonyms=I
CC {ECO:0000312|FlyBase:FBgn0004587};
CC IsoId=P26686-4; Sequence=VSP_015926, VSP_015929, VSP_015930;
CC Name=E;
CC IsoId=P26686-5; Sequence=VSP_005878;
CC Name=F; Synonyms=K;
CC IsoId=P26686-6; Sequence=VSP_015926, VSP_015928, VSP_015931;
CC Name=G; Synonyms=H;
CC IsoId=P26686-7; Sequence=VSP_015924, VSP_005878;
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development.
CC {ECO:0000269|PubMed:7935465}.
CC -!- PTM: Extensively phosphorylated on serine residues in the RS domain.
CC {ECO:0000269|PubMed:1717489, ECO:0000269|PubMed:18327897}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN71237.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X58720; CAA41556.1; -; mRNA.
DR EMBL; X62599; CAA44483.1; -; mRNA.
DR EMBL; AE014297; AAF54968.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF54969.2; -; Genomic_DNA.
DR EMBL; AE014297; AAN13575.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13577.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13578.1; -; Genomic_DNA.
DR EMBL; AE014297; ACZ94900.1; -; Genomic_DNA.
DR EMBL; AE014297; ACZ94901.1; -; Genomic_DNA.
DR EMBL; AY069302; AAL39447.1; -; mRNA.
DR EMBL; AY113327; AAM29332.1; -; mRNA.
DR EMBL; BT001417; AAN71172.1; -; mRNA.
DR EMBL; BT001482; AAN71237.1; ALT_FRAME; mRNA.
DR EMBL; BT001495; AAN71250.1; -; mRNA.
DR EMBL; BT001750; AAN71505.1; -; mRNA.
DR EMBL; BT003286; AAO25044.1; -; mRNA.
DR EMBL; BT004500; AAO42664.1; -; mRNA.
DR EMBL; BT125783; ADQ89797.1; -; mRNA.
DR EMBL; S51722; AAB24629.1; -; mRNA.
DR PIR; A37282; A37282.
DR PIR; A40459; A40459.
DR PIR; H48110; H48110.
DR RefSeq; NP_001014619.2; NM_001014619.3. [P26686-5]
DR RefSeq; NP_001163603.1; NM_001170132.2. [P26686-4]
DR RefSeq; NP_001163604.1; NM_001170133.2. [P26686-6]
DR RefSeq; NP_788665.1; NM_176488.3. [P26686-2]
DR RefSeq; NP_788666.1; NM_176489.3. [P26686-2]
DR RefSeq; NP_788667.2; NM_176490.3. [P26686-2]
DR RefSeq; NP_788668.1; NM_176491.3. [P26686-3]
DR RefSeq; NP_788669.1; NM_176492.4. [P26686-4]
DR RefSeq; NP_788670.1; NM_176493.4. [P26686-6]
DR RefSeq; NP_788671.2; NM_176494.4. [P26686-5]
DR AlphaFoldDB; P26686; -.
DR SMR; P26686; -.
DR BioGRID; 66750; 36.
DR IntAct; P26686; 12.
DR STRING; 7227.FBpp0300515; -.
DR iPTMnet; P26686; -.
DR PRIDE; P26686; -.
DR DNASU; 41670; -.
DR EnsemblMetazoa; FBtr0082801; FBpp0082269; FBgn0004587. [P26686-2]
DR EnsemblMetazoa; FBtr0082802; FBpp0082270; FBgn0004587. [P26686-3]
DR EnsemblMetazoa; FBtr0082803; FBpp0082271; FBgn0004587. [P26686-4]
DR EnsemblMetazoa; FBtr0082804; FBpp0082272; FBgn0004587. [P26686-6]
DR EnsemblMetazoa; FBtr0082806; FBpp0082274; FBgn0004587. [P26686-2]
DR EnsemblMetazoa; FBtr0300586; FBpp0289813; FBgn0004587. [P26686-4]
DR EnsemblMetazoa; FBtr0300588; FBpp0289815; FBgn0004587. [P26686-6]
DR EnsemblMetazoa; FBtr0308195; FBpp0300515; FBgn0004587. [P26686-5]
DR EnsemblMetazoa; FBtr0308196; FBpp0300516; FBgn0004587. [P26686-2]
DR EnsemblMetazoa; FBtr0308197; FBpp0300517; FBgn0004587. [P26686-5]
DR GeneID; 41670; -.
DR KEGG; dme:Dmel_CG10851; -.
DR UCSC; CG10851-RC; d. melanogaster.
DR CTD; 41670; -.
DR FlyBase; FBgn0004587; B52.
DR VEuPathDB; VectorBase:FBgn0004587; -.
DR eggNOG; KOG0106; Eukaryota.
DR GeneTree; ENSGT00940000156213; -.
DR InParanoid; P26686; -.
DR OMA; EAYSDHE; -.
DR PhylomeDB; P26686; -.
DR Reactome; R-DME-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-DME-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-DME-72165; mRNA Splicing - Minor Pathway.
DR Reactome; R-DME-72187; mRNA 3'-end processing.
DR Reactome; R-DME-73856; RNA Polymerase II Transcription Termination.
DR SignaLink; P26686; -.
DR BioGRID-ORCS; 41670; 2 hits in 3 CRISPR screens.
DR ChiTaRS; B52; fly.
DR GenomeRNAi; 41670; -.
DR PRO; PR:P26686; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0004587; Expressed in wing disc and 30 other tissues.
DR ExpressionAtlas; P26686; baseline and differential.
DR Genevisible; P26686; DM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; HDA:FlyBase.
DR GO; GO:0000791; C:euchromatin; IDA:FlyBase.
DR GO; GO:0016607; C:nuclear speck; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0071011; C:precatalytic spliceosome; HDA:FlyBase.
DR GO; GO:0003729; F:mRNA binding; IDA:FlyBase.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0051607; P:defense response to virus; IMP:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; HMP:FlyBase.
DR GO; GO:0044819; P:mitotic G1/S transition checkpoint signaling; IMP:FlyBase.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:FlyBase.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IMP:FlyBase.
DR GO; GO:0010468; P:regulation of gene expression; IMP:FlyBase.
DR GO; GO:0031440; P:regulation of mRNA 3'-end processing; IMP:FlyBase.
DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; IMP:FlyBase.
DR GO; GO:0001178; P:regulation of transcriptional start site selection at RNA polymerase II promoter; IMP:FlyBase.
DR GO; GO:0008380; P:RNA splicing; IMP:FlyBase.
DR CDD; cd12337; RRM1_SRSF4_like; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR035585; RRM1_SRSF4-like.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Direct protein sequencing; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1717489"
FT CHAIN 2..376
FT /note="Serine-arginine protein 55"
FT /id="PRO_0000081961"
FT DOMAIN 4..74
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 120..193
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 73..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..260
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 1..139
FT /note="Missing (in isoform G)"
FT /evidence="ECO:0000303|PubMed:12537569, ECO:0000303|Ref.6"
FT /id="VSP_015924"
FT VAR_SEQ 103..107
FT /note="Missing (in isoform A, isoform D and isoform F)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:1717489, ECO:0000303|Ref.6"
FT /id="VSP_015926"
FT VAR_SEQ 135..152
FT /note="DLKDYMRQAGEVTYADAH -> VSEHGSMYRALGVVYTVA (in isoform
FT F)"
FT /evidence="ECO:0000305"
FT /id="VSP_015928"
FT VAR_SEQ 135..140
FT /note="DLKDYM -> SLMCFD (in isoform D)"
FT /evidence="ECO:0000305"
FT /id="VSP_015929"
FT VAR_SEQ 141..376
FT /note="Missing (in isoform D)"
FT /evidence="ECO:0000305"
FT /id="VSP_015930"
FT VAR_SEQ 153..376
FT /note="Missing (in isoform F)"
FT /evidence="ECO:0000305"
FT /id="VSP_015931"
FT VAR_SEQ 319..339
FT /note="Missing (in isoform A, isoform E and isoform G)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:1717489, ECO:0000303|Ref.6"
FT /id="VSP_005878"
FT VAR_SEQ 323..376
FT /note="SFKSSFYKFTTMPFFCSDRSASAENKSRSRSRSRSASPKNGNASPDRNNESM
FT DD -> VVQKLVL (in isoform B)"
FT /evidence="ECO:0000305"
FT /id="VSP_015932"
FT CONFLICT 7
FT /note="Y -> F (in Ref. 7; AAB24629)"
FT /evidence="ECO:0000305"
FT CONFLICT 17..18
FT /note="ER -> AA (in Ref. 7; AAB24629)"
FT /evidence="ECO:0000305"
FT CONFLICT 40..42
FT /note="GFV -> AFM (in Ref. 7; AAB24629)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="T -> S (in Ref. 1; CAA41556)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="R -> A (in Ref. 2; CAA44483)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="S -> T (in Ref. 2; CAA44483)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="R -> A (in Ref. 2; CAA44483)"
FT /evidence="ECO:0000305"
FT CONFLICT 280..282
FT /note="RSR -> APV (in Ref. 2; CAA44483)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="S -> T (in Ref. 1; CAA41556)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 376 AA; 42813 MW; B35CEDA034933019 CRC64;
MVGSRVYVGG LPYGVRERDL ERFFKGYGRT RDILIKNGYG FVEFEDYRDA DDAVYELNGK
ELLGERVVVE PARGTARGSN RDRYDDRYGG RRGGGGGRYN EKNKNSRSSS RYGPPLRTEY
RLIVENLSSR VSWQDLKDYM RQAGEVTYAD AHKQRRNEGV VEFASLSDMK TAIEKLDDTE
LNGRRIHLVE DRRGGRSGGG GGSGRGRSRS SSSRSRSRSR RRSRSRRSSH SRSKSRSRSK
SRGGRSKSKS PVKSRSRSRS RSNKSRDVSK SKSKSHSRTR SRSPKRERDS RSRSRSVSKR
ESRSRSRSKS IHRDSRSRPP TVSFKSSFYK FTTMPFFCSD RSASAENKSR SRSRSRSASP
KNGNASPDRN NESMDD
