ID   ACTN_DROME              Reviewed;         924 AA.
AC   P18091; O46044; O46045; Q24370; Q8T024; Q9W536; Q9W537;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2001, sequence version 2.
DT   24-JAN-2024, entry version 204.
DE   RecName: Full=Alpha-actinin, sarcomeric;
DE   AltName: Full=F-actin cross-linking protein;
GN   Name=Actn; Synonyms=fliA, l(1)2Cb; ORFNames=CG4376;
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 ADULT MUSCLE), AND FUNCTION.
RC   STRAIN=Canton-S;
RX   PubMed=2112549; DOI=10.1083/jcb.110.6.1999;
RA   Fyrberg E.A., Kelly M., Ball E., Fyrberg C., Reedy M.C.;
RT   "Molecular genetics of Drosophila alpha-actinin: mutant alleles disrupt Z
RT   disc integrity and muscle insertions.";
RL   J. Cell Biol. 110:1999-2011(1990).
RN   [2]
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS LONG AND ADULT
RP   MUSCLE).
RC   STRAIN=Oregon-R;
RX   PubMed=10731137; DOI=10.1126/science.287.5461.2220;
RA   Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G.,
RA   Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Borkova D., Minana B., Kafatos F.C.,
RA   Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L.,
RA   Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P.,
RA   Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H.,
RA   Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
RA   McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
RA   Glover D.M.;
RT   "From sequence to chromosome: the tip of the X chromosome of D.
RT   melanogaster.";
RL   Science 287:2220-2222(2000).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC   STRAIN=Berkeley; TISSUE=Embryo;
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 [MRNA] OF 229-286 (ISOFORM NON-MUSCLE), ALTERNATIVE
RP   SPLICING, FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   STRAIN=Oregon-R; TISSUE=Embryo;
RX   PubMed=1734023; DOI=10.1083/jcb.116.4.911;
RA   Roulier E.M., Fyrberg C., Fyrberg E.;
RT   "Perturbations of Drosophila alpha-actinin cause muscle paralysis,
RT   weakness, and atrophy but do not confer obvious nonmuscle phenotypes.";
RL   J. Cell Biol. 116:911-922(1992).
RN   [7]
RP   INTERACTION WITH SMN, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=17353360; DOI=10.1083/jcb.200610053;
RA   Rajendra T.K., Gonsalvez G.B., Walker M.P., Shpargel K.B., Salz H.K.,
RA   Matera A.G.;
RT   "A Drosophila melanogaster model of spinal muscular atrophy reveals a
RT   function for SMN in striated muscle.";
RL   J. Cell Biol. 176:831-841(2007).
CC   -!- FUNCTION: F-actin cross-linking protein which is thought to anchor
CC       actin to a variety of intracellular structures. This is a bundling
CC       protein. {ECO:0000269|PubMed:1734023, ECO:0000269|PubMed:2112549}.
CC   -!- SUBUNIT: Homodimer; antiparallel. Interacts with Smn; the interaction
CC       occurs in adult thoracic tissues. {ECO:0000269|PubMed:17353360}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, Z line
CC       {ECO:0000269|PubMed:17353360}. Note=Colocalizes with Smn at the Z-line
CC       of indirect flight muscles.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC         Comment=Experimental confirmation may be lacking for some isoforms.;
CC       Name=Long;
CC         IsoId=P18091-1; Sequence=Displayed;
CC       Name=Non-muscle;
CC         IsoId=P18091-2; Sequence=VSP_000712, VSP_000714;
CC       Name=Larval muscle; Synonyms=C;
CC         IsoId=P18091-3; Sequence=VSP_000716;
CC       Name=Adult muscle; Synonyms=B;
CC         IsoId=P18091-4; Sequence=VSP_000715;
CC       Name=A;
CC         IsoId=P18091-5; Sequence=VSP_000713;
CC   -!- TISSUE SPECIFICITY: Larval muscle isoform is expressed in the larval
CC       body wall, adult muscles of the head and abdomen and supercontractile
CC       muscles of the larva and adult. Adult muscle isoform accumulates within
CC       adult fibrillar and tubular muscles. {ECO:0000269|PubMed:1734023,
CC       ECO:0000269|PubMed:17353360}.
CC   -!- DEVELOPMENTAL STAGE: Larval muscle isoform is found in the larvae and
CC       adults, the adult muscle isoform in adults only.
CC       {ECO:0000269|PubMed:1734023}.
CC   -!- SIMILARITY: Belongs to the alpha-actinin family. {ECO:0000305}.
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DR   EMBL; X51753; CAA36042.1; -; mRNA.
DR   EMBL; AE014298; AAF45705.2; -; Genomic_DNA.
DR   EMBL; AE014298; AAF45706.2; -; Genomic_DNA.
DR   EMBL; AE014298; AAN09068.1; -; Genomic_DNA.
DR   EMBL; AL009192; CAA15688.1; -; Genomic_DNA.
DR   EMBL; AL031765; CAA15688.1; JOINED; Genomic_DNA.
DR   EMBL; AL009192; CAA15689.1; -; Genomic_DNA.
DR   EMBL; AL031765; CAA15689.1; JOINED; Genomic_DNA.
DR   EMBL; AL031765; CAA21120.1; -; Genomic_DNA.
DR   EMBL; AL009192; CAA21120.1; JOINED; Genomic_DNA.
DR   EMBL; AL031765; CAA21121.1; -; Genomic_DNA.
DR   EMBL; AL009192; CAA21121.1; JOINED; Genomic_DNA.
DR   EMBL; AY069615; AAL39760.1; -; mRNA.
DR   EMBL; X64419; CAA45764.1; -; mRNA.
DR   PIR; A35598; FAFFAA.
DR   PIR; T13413; T13413.
DR   PIR; T13414; T13414.
DR   RefSeq; NP_001188532.1; NM_001201603.2. [P18091-4]
DR   RefSeq; NP_001188533.1; NM_001201604.2. [P18091-4]
DR   RefSeq; NP_001259165.1; NM_001272236.1. [P18091-3]
DR   RefSeq; NP_001259166.1; NM_001272237.1. [P18091-3]
DR   RefSeq; NP_001259167.1; NM_001272238.1. [P18091-3]
DR   RefSeq; NP_477484.2; NM_058136.4. [P18091-5]
DR   RefSeq; NP_477485.1; NM_058137.6. [P18091-3]
DR   RefSeq; NP_726784.1; NM_166920.2. [P18091-4]
DR   AlphaFoldDB; P18091; -.
DR   SMR; P18091; -.
DR   BioGRID; 57710; 45.
DR   DIP; DIP-22313N; -.
DR   IntAct; P18091; 12.
DR   STRING; 7227.FBpp0070331; -.
DR   PaxDb; 7227-FBpp0070331; -.
DR   EnsemblMetazoa; FBtr0070343; FBpp0070329; FBgn0000667. [P18091-4]
DR   EnsemblMetazoa; FBtr0070344; FBpp0070330; FBgn0000667. [P18091-5]
DR   EnsemblMetazoa; FBtr0070345; FBpp0070331; FBgn0000667. [P18091-3]
DR   EnsemblMetazoa; FBtr0303048; FBpp0292167; FBgn0000667. [P18091-4]
DR   EnsemblMetazoa; FBtr0310658; FBpp0302778; FBgn0000667. [P18091-3]
DR   EnsemblMetazoa; FBtr0310659; FBpp0302779; FBgn0000667. [P18091-3]
DR   EnsemblMetazoa; FBtr0333801; FBpp0305935; FBgn0000667. [P18091-4]
DR   EnsemblMetazoa; FBtr0333802; FBpp0305936; FBgn0000667. [P18091-3]
DR   GeneID; 31166; -.
DR   KEGG; dme:Dmel_CG4376; -.
DR   AGR; FB:FBgn0000667; -.
DR   CTD; 31166; -.
DR   FlyBase; FBgn0000667; Actn.
DR   VEuPathDB; VectorBase:FBgn0000667; -.
DR   eggNOG; KOG0035; Eukaryota.
DR   GeneTree; ENSGT00940000155548; -.
DR   InParanoid; P18091; -.
DR   OMA; CYEGVEV; -.
DR   OrthoDB; 2872403at2759; -.
DR   PhylomeDB; P18091; -.
DR   Reactome; R-DME-114608; Platelet degranulation.
DR   Reactome; R-DME-438066; Unblocking of NMDA receptors, glutamate binding and activation.
DR   Reactome; R-DME-446388; Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.
DR   Reactome; R-DME-9013405; RHOD GTPase cycle.
DR   Reactome; R-DME-9013418; RHOBTB2 GTPase cycle.
DR   Reactome; R-DME-9035034; RHOF GTPase cycle.
DR   SignaLink; P18091; -.
DR   BioGRID-ORCS; 31166; 0 hits in 3 CRISPR screens.
DR   ChiTaRS; Actn; fly.
DR   GenomeRNAi; 31166; -.
DR   PRO; PR:P18091; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0000667; Expressed in crop (Drosophila) and 36 other cell types or tissues.
DR   ExpressionAtlas; P18091; baseline and differential.
DR   GO; GO:0030054; C:cell junction; IBA:GO_Central.
DR   GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR   GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR   GO; GO:0005925; C:focal adhesion; ISS:FlyBase.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0030018; C:Z disc; IDA:FlyBase.
DR   GO; GO:0003779; F:actin binding; IPI:UniProtKB.
DR   GO; GO:0051015; F:actin filament binding; IMP:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IMP:FlyBase.
DR   GO; GO:0051017; P:actin filament bundle assembly; IMP:UniProtKB.
DR   GO; GO:0055001; P:muscle cell development; IBA:GO_Central.
DR   GO; GO:0045214; P:sarcomere organization; IDA:FlyBase.
DR   CDD; cd21214; CH_ACTN_rpt1; 1.
DR   CDD; cd21216; CH_ACTN_rpt2; 1.
DR   CDD; cd00051; EFh; 1.
DR   CDD; cd00176; SPEC; 3.
DR   Gene3D; 1.20.58.60; -; 4.
DR   Gene3D; 1.10.418.10; Calponin-like domain; 2.
DR   Gene3D; 1.10.238.10; EF-hand; 2.
DR   InterPro; IPR001589; Actinin_actin-bd_CS.
DR   InterPro; IPR001715; CH_dom.
DR   InterPro; IPR036872; CH_dom_sf.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR014837; EF-hand_Ca_insen.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   PANTHER; PTHR11915:SF442; ALPHA-ACTININ, SARCOMERIC-RELATED; 1.
DR   PANTHER; PTHR11915; SPECTRIN/FILAMIN RELATED CYTOSKELETAL PROTEIN; 1.
DR   Pfam; PF00307; CH; 2.
DR   Pfam; PF13405; EF-hand_6; 1.
DR   Pfam; PF08726; EFhand_Ca_insen; 1.
DR   Pfam; PF00435; Spectrin; 4.
DR   SMART; SM00033; CH; 2.
DR   SMART; SM00054; EFh; 2.
DR   SMART; SM01184; efhand_Ca_insen; 1.
DR   SMART; SM00150; SPEC; 4.
DR   SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF46966; Spectrin repeat; 4.
DR   PROSITE; PS00019; ACTININ_1; 1.
DR   PROSITE; PS00020; ACTININ_2; 1.
DR   PROSITE; PS50021; CH; 2.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 2.
DR   Genevisible; P18091; DM.
PE   1: Evidence at protein level;
KW   Actin-binding; Alternative splicing; Calcium; Cytoplasm; Metal-binding;
KW   Reference proteome; Repeat.
FT   CHAIN           1..924
FT                   /note="Alpha-actinin, sarcomeric"
FT                   /id="PRO_0000073447"
FT   DOMAIN          34..138
FT                   /note="Calponin-homology (CH) 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT   DOMAIN          147..253
FT                   /note="Calponin-homology (CH) 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT   REPEAT          251..395
FT                   /note="Spectrin 1"
FT   REPEAT          396..510
FT                   /note="Spectrin 2"
FT   REPEAT          511..631
FT                   /note="Spectrin 3"
FT   REPEAT          632..744
FT                   /note="Spectrin 4"
FT   DOMAIN          778..813
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          819..854
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   REGION          1..250
FT                   /note="Actin-binding"
FT   BINDING         791
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         793
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         795
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         797
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         802
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   VAR_SEQ         229..260
FT                   /note="Missing (in isoform Non-muscle)"
FT                   /evidence="ECO:0000303|PubMed:1734023"
FT                   /id="VSP_000712"
FT   VAR_SEQ         231..260
FT                   /note="INTPKPDERAIMTYVSCYYHAFQGAQQVGN -> Q (in isoform A)"
FT                   /evidence="ECO:0000303|PubMed:12537569"
FT                   /id="VSP_000713"
FT   VAR_SEQ         258..286
FT                   /note="Missing (in isoform Adult muscle)"
FT                   /evidence="ECO:0000303|PubMed:2112549"
FT                   /id="VSP_000715"
FT   VAR_SEQ         261..286
FT                   /note="NTALPDERAVMTYVSSYYHCFSGAQK -> VTHVPEPTRQYTYVPNNYN
FT                   (in isoform Larval muscle)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_000716"
FT   VAR_SEQ         261
FT                   /note="N -> Q (in isoform Non-muscle)"
FT                   /evidence="ECO:0000303|PubMed:1734023"
FT                   /id="VSP_000714"
FT   CONFLICT        409
FT                   /note="A -> G (in Ref. 1; CAA36042)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        457
FT                   /note="C -> Y (in Ref. 1; CAA36042)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        474
FT                   /note="S -> C (in Ref. 1; CAA36042)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        503
FT                   /note="S -> C (in Ref. 1; CAA36042)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        574
FT                   /note="E -> V (in Ref. 1; CAA36042)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        654
FT                   /note="L -> R (in Ref. 1; CAA36042)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        684..691
FT                   /note="AVTAIGMG -> VVTPLVWD (in Ref. 1; CAA36042)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        711
FT                   /note="Y -> H (in Ref. 1; CAA36042)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        817
FT                   /note="D -> E (in Ref. 1; CAA36042)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   924 AA;  107019 MW;  08F8961520328ACE CRC64;
     MMMENGLSME YGDGYMEQEE EWEREGLLDP AWEKQQKKTF TAWCNSHLRK AGTAIDNIEE
     DFRNGLKLML LLEVISGETL PKPDRGKMRF HKIANVNKAL DFIASKGVHL VSIGAEEIVD
     GNLKMTLGMI WTIILRFAIQ DISVEEMTAK EGLLLWCQRK TAPYKNVNVQ NFHLSFKDGL
     AFCALIHRHR PDLIDYAKLS KDNPLENLNT AFDVAEKYLD IPRMLDPDDL INTPKPDERA
     IMTYVSCYYH AFQGAQQVGN NTALPDERAV MTYVSSYYHC FSGAQKAETA ANRICKVLKV
     NQENERLMEE YERLASDLLE WIRRTMPWLN SRQADNSLAG VQKKLEEYRT YRRKHKPPRV
     EQKAKLETNF NTLQTKLRLS NRPAYLPTEG KTVSDISNSW KGLELAEKAF EEWLLAETMR
     LERLEHLAQK FKHKADAHED WTRGKEEMLQ SQDFRQCKLN ELKALKKKHE AFESDLAAHQ
     DRVEQIAAIA QELNTLEYHD CVSVNARCQR ICDQWDRLGA LTQRRRTALD EAERILEKID
     ILHLEFAKRA APFNNWLDGT REDLVDMFIV HTMEEIQGLI QAHDQFKATL GEADKEFNLI
     VNLVREVESI VKQHQIPGGL ENPYTTLTAN DMTRKWSDVR QLVPQRDQTL ANELRKQQNN
     EMLRRQFAEK ANIVGPWIER QMDAVTAIGM GLQGSLEDQL HRLKEYEQAV YAYKPNIEEL
     EKIHQAVQES MIFENRYTNY TMETLRVGWE QLLTSINRNI NEVENQILTR DSKGISQEQL
     NEFRSSFNHF DKNRTGRLSP EEFKSCLVSL GYSIGKDRQG DLDFQRILAV VDPNNTGYVH
     FDAFLDFMTR ESTDTDTAEQ VIDSFRILAA DKPYILPDEL RRELPPDQAE YCIQRMPPYK
     GPNGVPGALD YMSFSTALYG ETDL
//