ITA1_DROME
ID ITA1_DROME Reviewed; 1146 AA.
AC Q24247; M9PEG3; M9PHG7; M9PJL8; Q8SY51; Q9VYF6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2001, sequence version 2.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Integrin alpha-PS1;
DE AltName: Full=Position-specific antigen subunit alpha-1;
DE AltName: Full=Protein multiple edematous wings;
DE Contains:
DE RecName: Full=Integrin alpha-PS1 heavy chain;
DE Contains:
DE RecName: Full=Integrin alpha-PS1 light chain;
DE Flags: Precursor;
GN Name=mew; ORFNames=CG1771;
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), PARTIAL PROTEIN SEQUENCE, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Oregon-R; TISSUE=Embryo, and Larva;
RX PubMed=8240969; DOI=10.1016/0925-4773(93)90020-x;
RA Wehrli M., Diantonio A., Fearnley I.M., Smith R.J., Wilcox M.;
RT "Cloning and characterization of alpha PS1, a novel Drosophila melanogaster
RT integrin.";
RL Mech. Dev. 43:21-36(1993).
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 MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Head;
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 [5]
RP FUNCTION.
RX PubMed=7972082; DOI=10.1073/pnas.91.24.11447;
RA Gotwals P.J., Fessler L.I., Wehrli M., Hynes R.O.;
RT "Drosophila PS1 integrin is a laminin receptor and differs in ligand
RT specificity from PS2.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:11447-11451(1994).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-657 AND ASN-1027, AND
RP IDENTIFICATION BY MASS 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 [7]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL 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 [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-711; ASN-718 AND ASN-761, AND
RP IDENTIFICATION BY MASS 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).
CC -!- FUNCTION: Integrin alpha-PS1/beta-PS is a receptor for laminin.
CC {ECO:0000269|PubMed:7972082}.
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 Alpha-PS1 associates with beta-PS.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:19035354}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:19035354}. Lateral cell membrane
CC {ECO:0000269|PubMed:19035354}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:19035354}. Basal cell membrane
CC {ECO:0000269|PubMed:19035354}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:19035354}. Note=During mid-oogenesis, localizes to
CC the apical, to the lateral and to the basal membranes of follicle
CC cells. Apical membrane localization peaks at oogenesis stages 9 and 10A
CC in columnar follicle cells overlying the oocyte while decreases in the
CC most posterior follicle cells. Localization to lateral and basal
CC membranes persists during dorsal appendage morphogenesis, although
CC diminished and often absent.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=B;
CC IsoId=Q24247-1; Sequence=Displayed;
CC Name=A;
CC IsoId=Q24247-2; Sequence=VSP_009270;
CC Name=C;
CC IsoId=Q24247-3; Sequence=VSP_053396;
CC Name=D;
CC IsoId=Q24247-4; Sequence=VSP_009270, VSP_053396;
CC Name=E;
CC IsoId=Q24247-5; Sequence=VSP_009270, VSP_053397;
CC -!- TISSUE SPECIFICITY: Expressed in follicle cells (at protein level). At
CC syncytial blastoderm stage, expressed in the ectoderm but not in the
CC mesodermal precursors. At embryonic stage 7, expressed in dorsal and
CC ventrolateral ectoderm and in some yolk nuclei. At late stage 10,
CC expression is homogeneous in the ectoderm and is particularly abundant
CC in the anterior and posterior midgut primordia. At stage 11, strongly
CC expressed in a metameric pattern in the ectoderm, in the proctodeum and
CC in the posterior midgut primordium. At stage 12, accumulates at the
CC segment boundaries that start to become morphologically visible,
CC similar expression pattern is observed in the central nervous system.
CC In third larval instar wing imaginal disk, strongly expressed in the
CC dorsal compartment, in the adepithelial cells and in patches on the
CC peripodial membrane covering the imaginal disk to the outside.
CC {ECO:0000269|PubMed:19035354, ECO:0000269|PubMed:8240969}.
CC -!- DEVELOPMENTAL STAGE: Expressed during mid- and late-oogenesis (at
CC protein level). Expressed throughout embryonic and larval development
CC with peaks of expression during mid-embryogenesis and at third larval
CC instar. {ECO:0000269|PubMed:19035354, ECO:0000269|PubMed:8240969}.
CC -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}.
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DR EMBL; X73975; CAA52155.1; -; mRNA.
DR EMBL; AE014298; AAF48242.2; -; Genomic_DNA.
DR EMBL; AE014298; AAN09652.1; -; Genomic_DNA.
DR EMBL; AE014298; AGB95345.1; -; Genomic_DNA.
DR EMBL; AE014298; AGB95346.1; -; Genomic_DNA.
DR EMBL; AE014298; AGB95347.1; -; Genomic_DNA.
DR EMBL; AY075338; AAL68203.1; -; mRNA.
DR PIR; S40311; S40311.
DR RefSeq; NP_001259503.1; NM_001272574.1. [Q24247-5]
DR RefSeq; NP_001259504.1; NM_001272575.2. [Q24247-3]
DR RefSeq; NP_001259505.1; NM_001272576.2. [Q24247-4]
DR RefSeq; NP_511145.2; NM_078590.3. [Q24247-1]
DR RefSeq; NP_727679.1; NM_167354.2. [Q24247-2]
DR AlphaFoldDB; Q24247; -.
DR SMR; Q24247; -.
DR BioGRID; 58660; 12.
DR IntAct; Q24247; 23.
DR STRING; 7227.FBpp0302767; -.
DR GlyGen; Q24247; 12 sites.
DR iPTMnet; Q24247; -.
DR PaxDb; Q24247; -.
DR DNASU; 32275; -.
DR EnsemblMetazoa; FBtr0073731; FBpp0073562; FBgn0004456. [Q24247-2]
DR EnsemblMetazoa; FBtr0073732; FBpp0073563; FBgn0004456. [Q24247-1]
DR EnsemblMetazoa; FBtr0310647; FBpp0302767; FBgn0004456. [Q24247-3]
DR EnsemblMetazoa; FBtr0310648; FBpp0302768; FBgn0004456. [Q24247-4]
DR EnsemblMetazoa; FBtr0330398; FBpp0303424; FBgn0004456. [Q24247-5]
DR GeneID; 32275; -.
DR KEGG; dme:Dmel_CG1771; -.
DR CTD; 32275; -.
DR FlyBase; FBgn0004456; mew.
DR VEuPathDB; VectorBase:FBgn0004456; -.
DR eggNOG; KOG3637; Eukaryota.
DR GeneTree; ENSGT00940000167229; -.
DR HOGENOM; CLU_004111_1_0_1; -.
DR InParanoid; Q24247; -.
DR OMA; CERVDFD; -.
DR PhylomeDB; Q24247; -.
DR Reactome; R-DME-210991; Basigin interactions.
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-446107; Type I hemidesmosome assembly.
DR BioGRID-ORCS; 32275; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 32275; -.
DR PRO; PR:Q24247; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0004456; Expressed in spermathecum and 74 other tissues.
DR ExpressionAtlas; Q24247; baseline and differential.
DR Genevisible; Q24247; DM.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0009925; C:basal plasma membrane; IDA:FlyBase.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; IDA:FlyBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:FlyBase.
DR GO; GO:0008305; C:integrin complex; IDA:FlyBase.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0050839; F:cell adhesion molecule binding; IMP:FlyBase.
DR GO; GO:0050840; F:extracellular matrix binding; IDA:FlyBase.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:FlyBase.
DR GO; GO:0007015; P:actin filament organization; IMP:FlyBase.
DR GO; GO:0007475; P:apposition of dorsal and ventral imaginal disc-derived wing surfaces; NAS:FlyBase.
DR GO; GO:0007411; P:axon guidance; IMP:FlyBase.
DR GO; GO:0007414; P:axonal defasciculation; IMP:FlyBase.
DR GO; GO:0007155; P:cell adhesion; IMP:FlyBase.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IDA:FlyBase.
DR GO; GO:0030154; P:cell differentiation; TAS:FlyBase.
DR GO; GO:0016477; P:cell migration; TAS:FlyBase.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central.
DR GO; GO:0048567; P:ectodermal digestive tract morphogenesis; TAS:FlyBase.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; TAS:FlyBase.
DR GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0035160; P:maintenance of epithelial integrity, open tracheal system; IGI:FlyBase.
DR GO; GO:0007494; P:midgut development; TAS:FlyBase.
DR GO; GO:0016203; P:muscle attachment; IGI:FlyBase.
DR GO; GO:0007432; P:salivary gland boundary specification; IMP:FlyBase.
DR GO; GO:0007431; P:salivary gland development; TAS:FlyBase.
DR GO; GO:0007435; P:salivary gland morphogenesis; IGI:FlyBase.
DR GO; GO:0007608; P:sensory perception of smell; IGI:FlyBase.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IDA: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; 2.
DR Pfam; PF08441; Integrin_alpha2; 1.
DR PRINTS; PR01185; INTEGRINA.
DR SMART; SM00191; Int_alpha; 5.
DR SUPFAM; SSF69179; SSF69179; 3.
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; Cell adhesion; Cell membrane;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Integrin; Membrane; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..1146
FT /note="Integrin alpha-PS1"
FT /id="PRO_0000016320"
FT CHAIN 31..?960
FT /note="Integrin alpha-PS1 heavy chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000016321"
FT CHAIN ?961..1146
FT /note="Integrin alpha-PS1 light chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000016322"
FT TOPO_DOM 31..1085
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1086..1106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1107..1146
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 38..105
FT /note="FG-GAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 121..186
FT /note="FG-GAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 193..245
FT /note="FG-GAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 254..303
FT /note="FG-GAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 304..366
FT /note="FG-GAP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 367..422
FT /note="FG-GAP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 432..494
FT /note="FG-GAP 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REGION 938..958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..958
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 470
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 511
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 657
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17893096"
FT CARBOHYD 680
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 711
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 718
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 761
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 928
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1027
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17893096"
FT VAR_SEQ 1..97
FT /note="Missing (in isoform A, isoform D and isoform E)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_009270"
FT VAR_SEQ 114..115
FT /note="RN -> RTNGAYEINKH (in isoform C and isoform D)"
FT /evidence="ECO:0000305"
FT /id="VSP_053396"
FT VAR_SEQ 1146
FT /note="F -> FXQEGTVGWDLVRRRRRRRRLKLRLPVTAQPRHGWRKTTDKSINNNN
FT NNNHNNNSSNSRNDSDVDVLSLTPPPPPLSIFSWGNDGYYQASAAWWGHHM (in
FT isoform E)"
FT /evidence="ECO:0000305"
FT /id="VSP_053397"
FT CONFLICT 730..731
FT /note="ML -> IV (in Ref. 1; CAA52155)"
FT /evidence="ECO:0000305"
FT CONFLICT 815
FT /note="D -> E (in Ref. 1; CAA52155)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1146 AA; 127973 MW; E8AB75BC8DE6854E CRC64;
MLELPFTTIR PNCRLRQNLG ILIILQCVLT CYNFNLEQRL PIVKYGHPHS HFGYSVATHT
IGEANGPNKT NCVLVGAPLD QNRQPNTTHS GALWRCPMTQ RFDDCEQVIT DGRRNFDSEI
LSPPGNDEIK EDQWMGVTVR SNPLQANGSG GKVIVCAHRY MYIVRENRYG QGLCYLLTND
LQFEEVHEPC KGRPVQRQHE DYGLCQAGTS AALLDDDTMV LGSPGPYTWR GSIWVTQVGG
EYLQRDKTTY YSDHSDLNSP VDKYSYLGMS VTGGRFFGHM SYAAGAPRSE GHGQVVIFDK
STDNPIPVHS ILDGEQFGSS FGYELATADI NGDHRPDLIV AAPLYFTKTE GGAVYVYQNI
QDTLPMKYTL KLTGPLESRF GLALANIGDL NKDNCEDLAV GAPYEGNGVV YIYLGSSQGL
NSKPAQKIQA SELGGTIPNG QPIRTFGISI SGNTDLDDNS YPDVVIGAFN SSAAVILLAR
PIISIQTSVQ RKELHNMDPN TPGCLDDPAS NLTCFTFRAC CSIEPYDEKN KELRLAYSVE
AETFDHLKKF SRVFFFDREN KRTNVLSRVV RVHTNGRTEC QAVTGYIKAN TRDIQTPVRF
RLKYSLVEPP LADSALVRLN PILDQTQAHV DFEGTFQKDC GDDDLCESNL IIRVEPNITE
SSGNEYTLIL DETELEVRIN VSNLADSAYE AQLFIAHQAG VSYVATKKPT NATCNSYNTT
LVACSLGNPM LRDTTTFVTI RFQPKGLEPS EKIMLFHIFA NTTSKLVGPE RPERDLRVNV
VRRAKLNFRG WAIPEQSFYS GSSVANSVAN TAATDIEGHG PMGMDDVGSQ VHHMFTIFNE
GPSTAPKVQM VIHWPYSLYS DPQSGRPVQY LLYLEQVPTV EVSQGECHVA KEYVNPLNLA
SGSRENPAYL SAPAQMRMFP SQSRHSFNKS LIHSQRSYYS SSHRDDHSDD TQSNRNRVRR
SFLERVTRLE RLMYDPESSN AANGKKQDIV ELDCNKGATN CVRIECDILN MPALSEAQVV
VKARLWNSTL VSEYPRVERV RIFSTATAQI PESYGVEVMD HNNIEVETRA YPELRNQQRD
TSIPWLIIIL GIVGGLLLLA LVTYVLWKVG FFKRIRPTDP TLSGNLEKMN EEKPFLAPSK
NTHHVF
