ITA3_DROME
ID ITA3_DROME Reviewed; 1115 AA.
AC O44386; O44387; O46186; Q58CK3; Q6AWK3; Q9V7A3;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Integrin alpha-PS3;
DE AltName: Full=Position-specific antigen subunit alpha-3;
DE Short=Protein scab;
DE AltName: Full=Protein volado;
DE Contains:
DE RecName: Full=Integrin alpha-PS3 heavy chain;
DE Contains:
DE RecName: Full=Integrin alpha-PS3 light chain;
DE Flags: Precursor;
GN Name=scb; Synonyms=alphaPS3, Vol; ORFNames=CG8095;
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 B), FUNCTION, INTERACTION WITH MYS, AND
RP TISSUE SPECIFICITY.
RX PubMed=9409675; DOI=10.1242/dev.124.22.4583;
RA Stark K.A., Yee G.H., Roote C.E., Williams E.L., Zusman S., Hynes R.O.;
RT "A novel alpha integrin subunit associates with betaPS and functions in
RT tissue morphogenesis and movement during Drosophila development.";
RL Development 124:4583-4594(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), FUNCTION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=9461212; DOI=10.1038/35079;
RA Grotewiel M.S., Beck C.D.O., Wu K.H., Zhu X.R., Davis R.L.;
RT "Integrin-mediated short-term memory in Drosophila.";
RL Nature 391:455-460(1998).
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 B).
RC STRAIN=Berkeley; TISSUE=Larva, and Pupae;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INTERACTION WITH ITGBN, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15469969; DOI=10.1242/dev.01427;
RA Devenport D., Brown N.H.;
RT "Morphogenesis in the absence of integrins: mutation of both Drosophila
RT beta subunits prevents midgut migration.";
RL Development 131:5405-5415(2004).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-82, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Oregon-R; TISSUE=Head;
RX PubMed=17893096; DOI=10.1093/glycob/cwm097;
RA Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,
RA Panin V.;
RT "Identification of N-glycosylated proteins from the central nervous system
RT of Drosophila melanogaster.";
RL Glycobiology 17:1388-1403(2007).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=19035354; DOI=10.1002/dvdy.21802;
RA Dinkins M.B., Fratto V.M., Lemosy E.K.;
RT "Integrin alpha chains exhibit distinct temporal and spatial localization
RT patterns in epithelial cells of the Drosophila ovary.";
RL Dev. Dyn. 237:3927-3939(2008).
RN [9]
RP FUNCTION.
RX PubMed=18925939; DOI=10.1186/1749-8104-3-26;
RA Tsai P.I., Kao H.H., Grabbe C., Lee Y.T., Ghose A., Lai T.T., Peng K.P.,
RA Van Vactor D., Palmer R.H., Chen R.H., Yeh S.R., Chien C.T.;
RT "Fak56 functions downstream of integrin alphaPS3betanu and suppresses MAPK
RT activation in neuromuscular junction growth.";
RL Neural Dev. 3:26-26(2008).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-82, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [11]
RP FUNCTION, INTERACTION WITH ITGBN, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=23426364; DOI=10.1074/jbc.m113.451427;
RA Nonaka S., Nagaosa K., Mori T., Shiratsuchi A., Nakanishi Y.;
RT "Integrin alphaPS3/betanu-mediated phagocytosis of apoptotic cells and
RT bacteria in Drosophila.";
RL J. Biol. Chem. 288:10374-10380(2013).
CC -!- FUNCTION: Integrin alpha-PS3/beta-PS is a receptor for laminin. Also
CC binds to wb. Important during embryogenesis for the development of the
CC trachea, dorsal vessel and salivary gland, as well as for dorsal
CC closure. Required for short-term memory processes. Minor involvement in
CC the establishment of the oocyte anterior-posterior length. Plays a role
CC in timely border cell migration during oogenesis, probably mediated by
CC JNK signaling. Integrin alpha-PS3/Itgbn is required for effective
CC phagocytosis of apoptotic cells during embryonic development and for
CC the phagocytic elimination of S.aureus by mediating the binding of
CC S.aureus peptidoglycan to larval hemocytes, which probably activates a
CC signaling pathway involving Rac1 and Rac2. Integrin alpha-PS3/Itgbn
CC also regulates Fak activity during neuromuscular junction (NMJ) growth
CC and is required for its activation in presynapsis of NMJs. Seems to be
CC dispensable for major morphogenetic processes.
CC {ECO:0000269|PubMed:18925939, ECO:0000269|PubMed:19035354,
CC ECO:0000269|PubMed:23426364, ECO:0000269|PubMed:9409675,
CC ECO:0000269|PubMed:9461212}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The alpha subunit
CC is composed of a heavy and a light chain linked by a disulfide bond.
CC Interacts with mys/beta-PS and Itgbn. {ECO:0000269|PubMed:15469969,
CC ECO:0000269|PubMed:23426364, ECO:0000269|PubMed:9409675}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane; Single-pass type I membrane
CC protein. Lateral cell membrane; Single-pass type I membrane protein.
CC Cytoplasm. Note=Apical membrane localization in primordial dorsal-
CC appendage cells at oogenesis stages 10B and 11. Later, weakly expressed
CC in lateral membrane of cells surrounding the outgrowing dorsal
CC appendages.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B; Synonyms=Vol-L;
CC IsoId=O44386-1; Sequence=Displayed;
CC Name=A; Synonyms=Vol-S;
CC IsoId=O44386-2; Sequence=VSP_002740;
CC -!- TISSUE SPECIFICITY: Expressed in embryonic and larval hemocytes (at
CC protein level). Expressed in tissues undergoing invagination, tissue
CC movement and morphogenesis such as salivary gland, trachea, midgut
CC endoderm, dorsal vessel, midline of the ventral nerve cord, amnioserosa
CC and the amnioproctodeal invagination. Expressed in the mushroom body
CC neuropil, brain areas that contain mushroom body processes in synaptic
CC contact with other neurons. In egg chambers, expressed in border cells,
CC in stretch cells and in dorsal appendage primordia.
CC {ECO:0000269|PubMed:15469969, ECO:0000269|PubMed:19035354,
CC ECO:0000269|PubMed:23426364, ECO:0000269|PubMed:9409675,
CC ECO:0000269|PubMed:9461212}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development. Highest
CC expression is observed in pupae (at protein level). During oogenesis,
CC expressed from stage 10B onwards. {ECO:0000269|PubMed:19035354,
CC ECO:0000269|PubMed:23426364}.
CC -!- DISRUPTION PHENOTYPE: Flies display impaired olfactory memories within
CC 3 min of training. Mutant embryos show reduced level of phagocytosis.
CC {ECO:0000269|PubMed:23426364, ECO:0000269|PubMed:9461212}.
CC -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}.
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; U76605; AAC04505.1; -; mRNA.
DR EMBL; AF034199; AAC38853.1; -; mRNA.
DR EMBL; AF034200; AAC38854.1; -; mRNA.
DR EMBL; AE013599; AAF58155.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF58156.1; -; Genomic_DNA.
DR EMBL; BT015245; AAT94474.1; -; mRNA.
DR EMBL; BT021944; AAX51649.1; -; mRNA.
DR PIR; T09403; T09403.
DR PIR; T09433; T09433.
DR RefSeq; NP_523750.2; NM_079026.3. [O44386-1]
DR RefSeq; NP_725445.1; NM_166083.2. [O44386-2]
DR AlphaFoldDB; O44386; -.
DR SMR; O44386; -.
DR BioGRID; 62429; 11.
DR IntAct; O44386; 1.
DR STRING; 7227.FBpp0086501; -.
DR GlyGen; O44386; 8 sites.
DR iPTMnet; O44386; -.
DR PaxDb; O44386; -.
DR PRIDE; O44386; -.
DR EnsemblMetazoa; FBtr0087369; FBpp0086501; FBgn0286785. [O44386-1]
DR EnsemblMetazoa; FBtr0087370; FBpp0086502; FBgn0286785. [O44386-2]
DR GeneID; 36692; -.
DR KEGG; dme:Dmel_CG8095; -.
DR CTD; 20242; -.
DR FlyBase; FBgn0286785; scb.
DR VEuPathDB; VectorBase:FBgn0286785; -.
DR eggNOG; KOG3637; Eukaryota.
DR GeneTree; ENSGT00940000165133; -.
DR InParanoid; O44386; -.
DR OMA; HNQVKFG; -.
DR PhylomeDB; O44386; -.
DR Reactome; R-DME-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-DME-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-DME-216083; Integrin cell surface interactions.
DR Reactome; R-DME-3000157; Laminin interactions.
DR Reactome; R-DME-3000170; Syndecan interactions.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR SignaLink; O44386; -.
DR BioGRID-ORCS; 36692; 0 hits in 3 CRISPR screens.
DR ChiTaRS; scb; fly.
DR GenomeRNAi; 36692; -.
DR PRO; PR:O44386; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0286785; Expressed in seminal fluid secreting gland and 54 other tissues.
DR Genevisible; O44386; DM.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0009925; C:basal plasma membrane; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; ISS:FlyBase.
DR GO; GO:0016021; C:integral component of membrane; IDA:FlyBase.
DR GO; GO:0008305; C:integrin complex; IDA:FlyBase.
DR GO; GO:0016328; C:lateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:FlyBase.
DR GO; GO:0043277; P:apoptotic cell clearance; IMP:FlyBase.
DR GO; GO:0007411; P:axon guidance; IMP:FlyBase.
DR GO; GO:0048149; P:behavioral response to ethanol; IMP:FlyBase.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; ISS:FlyBase.
DR GO; GO:0016477; P:cell migration; TAS:FlyBase.
DR GO; GO:0007160; P:cell-matrix adhesion; TAS:FlyBase.
DR GO; GO:0007391; P:dorsal closure; IMP:FlyBase.
DR GO; GO:0035001; P:dorsal trunk growth, open tracheal system; IMP:FlyBase.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; TAS:FlyBase.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0007508; P:larval heart development; IMP:FlyBase.
DR GO; GO:0007613; P:memory; TAS:FlyBase.
DR GO; GO:0007494; P:midgut development; TAS:FlyBase.
DR GO; GO:0030336; P:negative regulation of cell migration; IMP:UniProtKB.
DR GO; GO:0045886; P:negative regulation of synaptic assembly at neuromuscular junction; IGI:FlyBase.
DR GO; GO:0001555; P:oocyte growth; IMP:UniProtKB.
DR GO; GO:0003344; P:pericardium morphogenesis; IMP:FlyBase.
DR GO; GO:0006909; P:phagocytosis; IMP:FlyBase.
DR GO; GO:0007431; P:salivary gland development; IMP:FlyBase.
DR GO; GO:0007614; P:short-term memory; TAS:FlyBase.
DR GO; GO:0042060; P:wound healing; HMP:FlyBase.
DR Gene3D; 2.130.10.130; -; 1.
DR InterPro; IPR013517; FG-GAP.
DR InterPro; IPR013519; Int_alpha_beta-p.
DR InterPro; IPR000413; Integrin_alpha.
DR InterPro; IPR013649; Integrin_alpha-2.
DR InterPro; IPR018184; Integrin_alpha_C_CS.
DR InterPro; IPR028994; Integrin_alpha_N.
DR InterPro; IPR032695; Integrin_dom_sf.
DR Pfam; PF01839; FG-GAP; 3.
DR Pfam; PF08441; Integrin_alpha2; 1.
DR PRINTS; PR01185; INTEGRINA.
DR SMART; SM00191; Int_alpha; 7.
DR SUPFAM; SSF69179; SSF69179; 2.
DR SUPFAM; SSF69318; SSF69318; 1.
DR PROSITE; PS51470; FG_GAP; 7.
DR PROSITE; PS00242; INTEGRIN_ALPHA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Behavior; Cell adhesion; Cell membrane;
KW Cleavage on pair of basic residues; Cytoplasm; Differentiation;
KW Disulfide bond; Glycoprotein; Integrin; Membrane; Oogenesis; Phagocytosis;
KW Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1115
FT /note="Integrin alpha-PS3"
FT /id="PRO_0000016326"
FT CHAIN 25..?929
FT /note="Integrin alpha-PS3 heavy chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000016327"
FT CHAIN ?930..1115
FT /note="Integrin alpha-PS3 light chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000016328"
FT TOPO_DOM 25..1054
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1055..1075
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1076..1115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 39..99
FT /note="FG-GAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 113..174
FT /note="FG-GAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 193..246
FT /note="FG-GAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 278..335
FT /note="FG-GAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 336..397
FT /note="FG-GAP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 398..453
FT /note="FG-GAP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 460..522
FT /note="FG-GAP 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17893096,
FT ECO:0000269|PubMed:19349973"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 438
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 696
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 845
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 868
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 964
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..63
FT /note="MNAESTMFPHIFLALLALISHIEAFNFMPRPSRVINSPKHLKFHINQTRSSY
FT FGYTLVIRQTS -> MVGQDRDFWALLVLGLWCLSSHCNAFNLSPLPNRQILDPQFATN
FT VPKVRASYFGFTMSLRPNG (in isoform A)"
FT /evidence="ECO:0000303|PubMed:9461212, ECO:0000303|Ref.5"
FT /id="VSP_002740"
FT CONFLICT 630
FT /note="I -> V (in Ref. 2; AAC38853/AAC38854)"
FT /evidence="ECO:0000305"
FT CONFLICT 664
FT /note="D -> N (in Ref. 2; AAC38853/AAC38854)"
FT /evidence="ECO:0000305"
FT CONFLICT 753
FT /note="I -> S (in Ref. 2; AAC38853/AAC38854)"
FT /evidence="ECO:0000305"
FT CONFLICT 792
FT /note="S -> R (in Ref. 2; AAC38853/AAC38854)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1115 AA; 124545 MW; B3DFB52212E84185 CRC64;
MNAESTMFPH IFLALLALIS HIEAFNFMPR PSRVINSPKH LKFHINQTRS SYFGYTLVIR
QTSIIVGAPR AQSTLESQRT INETGAIYRC SLTNGVCSPY VLDSRGNVDA PYSEYTFDSE
RKDFQWLGGS MDGGTKDTDK LLVCAPRFYA PSSRDNHLHG VCYWVNNTVA STPQHVTRIS
PLRLKSEQVK EEDNGNKASF FYIMGELGLS AHVADDNTKF LIGAPGINTW RGSVILYRQV
DPVDNPTASR RDTSKALRRT YRDVDSNDYT PEHYAPEIPT PGLWGQEEDS YFGYAVSSGF
FDSSNPTKLL YVATAPQANK QSGEAYIFDV RGKSIHKYHV FRGEQFGEYF GYSVLAEDLN
GDGKTDVIVS APQHALEDSH DNGAIYVFIN KGFFNFERQI LRSPVETMAR FGTALSRLGD
INHDGYNDVA VGAPFAGNGT VFIYLGSENG LRDQPSQRLD APSQQPSKYG SHMFGHGLSR
GSDIDGNGFN DFAIGAPNAE AVYLYRAYPV VKVHATVKSE SREIKPEQEK VKITACYRLS
TTSTDKLVQE QELAIRIAMD KQLKRVKFTQ TQTNEISFKV NANFGEQCRD FETQVRYSEK
DIFTPIDLEM HYELTKKVPD SEEFCETCAI VDPTEPKVST QNIIFSTGCA TDVCTADLQL
RSKDVSPTYI LGSADTLRLN YEITNIGETA YLPQFNVTST SRLAFAQVPG NCKVVDAVMV
CDLNRGRPLA KGDTDSVTIS FDVSQLSGQS LIIHAEVFST GYEQNPTDNR QTNVIGLKEF
TEIDASGGQT NSQIDLEHYS NSAEIVNNYE IKSNGPSVIE QLTVSFYIPI AYKVAGSTAI
IPIINVTSLK MQASYDSQLL SIDLYDQNNT MLVVDPVEVT TTLSGGLERT VITQNRQSYD
IHTSGHVHQT MEVLDTSMVA TASMSRKRRD LKALTANREQ YARISNVKAH DLLSDDFKGK
LPVNRTIVFN CRDPEMTICV RAEMRVHFRP EKSINLNMRY SVDLNEVNAI LVDPWEYFVI
LTDLKLQKKG DPTSTSFSIN RRIEPNIISK HQETGLPIWI IIVSVIGGLL LLSAISYLLY
KFGFFNRTKK DELDRLVQQN PVEPEAENLN SGGNN
