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Integrin alpha-PS2 (Position-specific antigen subunit alpha-2) (Protein inflated) [Cleaved into: Integrin alpha-PS2 heavy chain; Integrin alpha-PS2 light chain]

 ITA2_DROME              Reviewed;        1396 AA.
P12080; E1JJN2; Q8IR07; Q8MSG3; Q9VXB6;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-DEC-2000, sequence version 2.
18-JUL-2018, entry version 192.
RecName: Full=Integrin alpha-PS2;
AltName: Full=Position-specific antigen subunit alpha-2;
AltName: Full=Protein inflated;
Contains:
RecName: Full=Integrin alpha-PS2 heavy chain;
Contains:
RecName: Full=Integrin alpha-PS2 light chain;
Flags: Precursor;
Name=if; ORFNames=CG9623;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PS2C), IDENTIFICATION BY MASS
SPECTROMETRY, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=2961459; DOI=10.1016/0092-8674(87)90580-0;
Bogaert T., Brown N.H., Wilcox M.;
"The Drosophila PS2 antigen is an invertebrate integrin that, like the
fibronectin receptor, becomes localized to muscle attachments.";
Cell 51:929-940(1987).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 213-757 (ISOFORM PS2M8).
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[5]
ALTERNATIVE SPLICING, AND DEVELOPMENTAL STAGE.
PubMed=2507168; DOI=10.1016/0092-8674(89)90880-5;
Brown N.H., King D.L., Wilcox M., Kafatos F.C.;
"Developmentally regulated alternative splicing of Drosophila integrin
PS2 alpha transcripts.";
Cell 59:185-195(1989).
[6]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
STRAIN=Oregon-R; TISSUE=Embryo, and Larva;
PubMed=8240969; DOI=10.1016/0925-4773(93)90020-X;
Wehrli M., Diantonio A., Fearnley I.M., Smith R.J., Wilcox M.;
"Cloning and characterization of alpha PS1, a novel Drosophila
melanogaster integrin.";
Mech. Dev. 43:21-36(1993).
[7]
FUNCTION.
PubMed=7924982;
Fogerty F.J., Fessler L.I., Bunch T.A., Yaron Y., Parker C.G.,
Nelson R.E., Brower D.L., Gullberg D., Fessler J.H.;
"Tiggrin, a novel Drosophila extracellular matrix protein that
functions as a ligand for Drosophila alpha PS2 beta PS integrins.";
Development 120:1747-1758(1994).
[8]
FUNCTION.
PubMed=7972082; DOI=10.1073/pnas.91.24.11447;
Gotwals P.J., Fessler L.I., Wehrli M., Hynes R.O.;
"Drosophila PS1 integrin is a laminin receptor and differs in ligand
specificity from PS2.";
Proc. Natl. Acad. Sci. U.S.A. 91:11447-11451(1994).
[9]
FUNCTION.
PubMed=9660786; DOI=10.1074/jbc.273.29.18235;
Graner M.W., Bunch T.A., Baumgartner S., Kerschen A., Brower D.L.;
"Splice variants of the Drosophila PS2 integrins differentially
interact with RGD-containing fragments of the extracellular proteins
tiggrin, ten-m, and D-laminin 2.";
J. Biol. Chem. 273:18235-18241(1998).
[10]
FUNCTION.
PubMed=10821184; DOI=10.1007/s004380051194;
Ayyub C., Rodrigues V., Hasan G., Siddiqi O.;
"Genetic analysis of olfC demonstrates a role for the position-
specific integrins in the olfactory system of Drosophila
melanogaster.";
Mol. Gen. Genet. 263:498-504(2000).
[11]
TISSUE SPECIFICITY.
PubMed=15469969; DOI=10.1242/dev.01427;
Devenport D., Brown N.H.;
"Morphogenesis in the absence of integrins: mutation of both
Drosophila beta subunits prevents midgut migration.";
Development 131:5405-5415(2004).
[12]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=19035354; DOI=10.1002/dvdy.21802;
Dinkins M.B., Fratto V.M., Lemosy E.K.;
"Integrin alpha chains exhibit distinct temporal and spatial
localization patterns in epithelial cells of the Drosophila ovary.";
Dev. Dyn. 237:3927-3939(2008).
-!- FUNCTION: Alpha-PS2/beta-PS is a receptor for Tig, wb and Ten-m.
Involved in the function and/or development of the olfactory
system. {ECO:0000269|PubMed:10821184, ECO:0000269|PubMed:7924982,
ECO:0000269|PubMed:7972082, ECO:0000269|PubMed:9660786}.
-!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The alpha
subunit is composed of a heavy and a light chain linked by a
disulfide bond. Alpha-PS2 associates with beta-PS.
-!- SUBCELLULAR LOCATION: Apical cell membrane
{ECO:0000269|PubMed:19035354}; Single-pass type I membrane protein
{ECO:0000269|PubMed:19035354}. Lateral cell membrane
{ECO:0000269|PubMed:19035354}; Single-pass type I membrane protein
{ECO:0000269|PubMed:19035354}. Basal cell membrane
{ECO:0000269|PubMed:19035354}; Single-pass type I membrane protein
{ECO:0000269|PubMed:19035354}. Note=During mid-oogenesis,
localizes to the apical, to the lateral and to the basal membranes
of follicle cells. Apical membrane localization peaks at oogenesis
stages 9 and 10A in columnar follicle cells overlying the oocyte
while decreases in the most posterior follicle cells. During
embryogenesis, at the end of germband extension concentrates at
the basal membrane of mesodermal cells, where they adhere to the
ectoderm. Then, in visceral mesoderm localizes basally, whereas in
somatic mesoderm is homogenously distributed.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=PS2C; Synonyms=D, F;
IsoId=P12080-1; Sequence=Displayed;
Name=PS2M8; Synonyms=C;
IsoId=P12080-2; Sequence=VSP_002739;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: In ovaries, highly expressed in follicle
cells. At syncytial blastoderm stage, expressed in the embryonic
mesodermal precursors but not in the ectoderm. At embryonic stages
7 and 10, expression is restricted to the mesoderm. At stage 12,
expressed in the gonadal sheath and the interstitial cells of the
gonad. In stage 16 embryos, expressed in the somatic and visceral
muscles where localizes to sites of attachment between adjacent
muscles. In third larval instar wing imaginal disk, expressed in
the ventral compartment and in a subset of adepithelial and
peripodial cells (at protein level). {ECO:0000269|PubMed:15469969,
ECO:0000269|PubMed:19035354, ECO:0000269|PubMed:2961459,
ECO:0000269|PubMed:8240969}.
-!- DEVELOPMENTAL STAGE: Expressed throughout embryonic and larval
development with peaks of expression during mid-embryogenesis and
at third larval instar (at protein level). The relative ratio of
isoform 1/PS2C and isoform 2/PS2M8 varies widely during
development. {ECO:0000269|PubMed:2507168,
ECO:0000269|PubMed:2961459, ECO:0000269|PubMed:8240969}.
-!- PTM: The heavy-light chain cleavage site is either in 1230-1231,
or 1233-1234, or 1243-1244.
-!- SIMILARITY: Belongs to the integrin alpha chain family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAM50700.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAM50700.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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EMBL; M19059; AAC12788.1; -; mRNA.
EMBL; AE014298; AAF48661.1; -; Genomic_DNA.
EMBL; AE014298; AAN09423.2; -; Genomic_DNA.
EMBL; AE014298; ACZ95312.1; -; Genomic_DNA.
EMBL; AE014298; ACZ95313.1; -; Genomic_DNA.
EMBL; AY118840; AAM50700.1; ALT_SEQ; mRNA.
PIR; A29637; A29637.
RefSeq; NP_001162777.1; NM_001169306.2. [P12080-1]
RefSeq; NP_001162778.1; NM_001169307.1. [P12080-1]
RefSeq; NP_523378.2; NM_078654.2. [P12080-1]
RefSeq; NP_728021.2; NM_167544.2. [P12080-2]
UniGene; Dm.7766; -.
ProteinModelPortal; P12080; -.
SMR; P12080; -.
BioGrid; 58994; 29.
DIP; DIP-23111N; -.
IntAct; P12080; 6.
STRING; 7227.FBpp0074131; -.
PaxDb; P12080; -.
PRIDE; P12080; -.
EnsemblMetazoa; FBtr0074357; FBpp0074131; FBgn0001250. [P12080-1]
EnsemblMetazoa; FBtr0301352; FBpp0290566; FBgn0001250. [P12080-2]
EnsemblMetazoa; FBtr0301353; FBpp0290567; FBgn0001250. [P12080-1]
EnsemblMetazoa; FBtr0301354; FBpp0290568; FBgn0001250. [P12080-1]
GeneID; 32661; -.
KEGG; dme:Dmel_CG9623; -.
UCSC; CG9623-RA; d. melanogaster.
CTD; 32661; -.
FlyBase; FBgn0001250; if.
eggNOG; KOG3637; Eukaryota.
eggNOG; ENOG410XPVZ; LUCA.
GeneTree; ENSGT00760000118782; -.
InParanoid; P12080; -.
OMA; ESNPREV; -.
OrthoDB; EOG091G02JI; -.
PhylomeDB; P12080; -.
Reactome; R-DME-114608; Platelet degranulation.
Reactome; R-DME-1236973; Cross-presentation of particulate exogenous antigens (phagosomes).
Reactome; R-DME-1566948; Elastic fibre formation.
Reactome; R-DME-1566977; Fibronectin matrix formation.
Reactome; R-DME-202733; Cell surface interactions at the vascular wall.
Reactome; R-DME-2129379; Molecules associated with elastic fibres.
Reactome; R-DME-216083; Integrin cell surface interactions.
Reactome; R-DME-3000170; Syndecan interactions.
Reactome; R-DME-3000178; ECM proteoglycans.
Reactome; R-DME-354192; Integrin alphaIIb beta3 signaling.
Reactome; R-DME-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
Reactome; R-DME-372708; p130Cas linkage to MAPK signaling for integrins.
Reactome; R-DME-445144; Signal transduction by L1.
Reactome; R-DME-5674135; MAP2K and MAPK activation.
Reactome; R-DME-6798695; Neutrophil degranulation.
ChiTaRS; if; fly.
GenomeRNAi; 32661; -.
PRO; PR:P12080; -.
Proteomes; UP000000803; Chromosome X.
Bgee; FBgn0001250; -.
ExpressionAtlas; P12080; differential.
Genevisible; P12080; DM.
GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0009925; C:basal plasma membrane; IDA:FlyBase.
GO; GO:0005925; C:focal adhesion; IDA:FlyBase.
GO; GO:0005887; C:integral component of plasma membrane; IDA:FlyBase.
GO; GO:0008305; C:integrin complex; IDA:FlyBase.
GO; GO:0016328; C:lateral plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
GO; GO:0042383; C:sarcolemma; IDA:FlyBase.
GO; GO:0050840; F:extracellular matrix binding; IDA:FlyBase.
GO; GO:0046982; F:protein heterodimerization activity; IPI:FlyBase.
GO; GO:0007475; P:apposition of dorsal and ventral imaginal disc-derived wing surfaces; NAS:FlyBase.
GO; GO:0007411; P:axon guidance; IMP:FlyBase.
GO; GO:0007414; P:axonal defasciculation; IMP:FlyBase.
GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
GO; GO:0033627; P:cell adhesion mediated by integrin; IDA:FlyBase.
GO; GO:0016477; P:cell migration; TAS:FlyBase.
GO; GO:0098609; P:cell-cell adhesion; TAS:FlyBase.
GO; GO:0007160; P:cell-matrix adhesion; ISS:FlyBase.
GO; GO:0021551; P:central nervous system morphogenesis; IMP:FlyBase.
GO; GO:0007427; P:epithelial cell migration, open tracheal system; TAS:FlyBase.
GO; GO:0035099; P:hemocyte migration; IMP:FlyBase.
GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; TAS:FlyBase.
GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0035160; P:maintenance of epithelial integrity, open tracheal system; IGI:FlyBase.
GO; GO:0045185; P:maintenance of protein location; IMP:FlyBase.
GO; GO:0007494; P:midgut development; TAS:FlyBase.
GO; GO:0016203; P:muscle attachment; IMP:FlyBase.
GO; GO:0030239; P:myofibril assembly; IMP:FlyBase.
GO; GO:0051492; P:regulation of stress fiber assembly; IMP:FlyBase.
GO; GO:0007431; P:salivary gland development; TAS:FlyBase.
GO; GO:0007435; P:salivary gland morphogenesis; IGI:FlyBase.
GO; GO:0045214; P:sarcomere organization; IMP:FlyBase.
GO; GO:0007608; P:sensory perception of smell; IGI:FlyBase.
GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IDA:FlyBase.
GO; GO:0007426; P:tracheal outgrowth, open tracheal system; TAS:FlyBase.
GO; GO:0007419; P:ventral cord development; IMP:FlyBase.
Gene3D; 2.130.10.130; -; 1.
InterPro; IPR013517; FG-GAP.
InterPro; IPR013519; Int_alpha_beta-p.
InterPro; IPR000413; Integrin_alpha.
InterPro; IPR013649; Integrin_alpha-2.
InterPro; IPR018184; Integrin_alpha_C_CS.
InterPro; IPR028994; Integrin_alpha_N.
InterPro; IPR032695; Integrin_dom_sf.
Pfam; PF01839; FG-GAP; 2.
Pfam; PF00357; Integrin_alpha; 1.
Pfam; PF08441; Integrin_alpha2; 1.
PRINTS; PR01185; INTEGRINA.
SMART; SM00191; Int_alpha; 5.
SUPFAM; SSF69179; SSF69179; 4.
PROSITE; PS51470; FG_GAP; 7.
PROSITE; PS00242; INTEGRIN_ALPHA; 1.
1: Evidence at protein level;
Alternative splicing; Cell adhesion; Cell membrane; Complete proteome;
Disulfide bond; Glycoprotein; Integrin; Membrane; Olfaction; Receptor;
Reference proteome; Repeat; Sensory transduction; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 31 {ECO:0000255}.
CHAIN 32 1396 Integrin alpha-PS2.
/FTId=PRO_0000016323.
CHAIN 32 ?1243 Integrin alpha-PS2 heavy chain.
/FTId=PRO_0000016324.
CHAIN ?1244 1396 Integrin alpha-PS2 light chain.
/FTId=PRO_0000016325.
TOPO_DOM 32 1341 Extracellular. {ECO:0000255}.
TRANSMEM 1342 1366 Helical. {ECO:0000255}.
TOPO_DOM 1367 1396 Cytoplasmic. {ECO:0000255}.
REPEAT 36 106 FG-GAP 1. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 117 174 FG-GAP 2. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 186 239 FG-GAP 3. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 266 317 FG-GAP 4. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 318 383 FG-GAP 5. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 386 445 FG-GAP 6. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 452 514 FG-GAP 7. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
COMPBIAS 932 938 Ser-rich.
COMPBIAS 1015 1023 Ser-rich.
COMPBIAS 1049 1054 Ser-rich.
COMPBIAS 1217 1226 Ser-rich.
CARBOHYD 69 69 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 209 209 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 322 322 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 584 584 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 598 598 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 741 741 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 783 783 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 833 833 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 959 959 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1005 1005 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1299 1299 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1307 1307 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 225 249 Missing (in isoform PS2M8).
{ECO:0000303|PubMed:12537569}.
/FTId=VSP_002739.
CONFLICT 29 29 A -> G (in Ref. 1; AAC12788).
{ECO:0000305}.
CONFLICT 968 976 SPKQVEQRR -> RSQASGATA (in Ref. 1;
AAC12788). {ECO:0000305}.
CONFLICT 1063 1064 Missing (in Ref. 1). {ECO:0000305}.
CONFLICT 1235 1235 N -> D (in Ref. 1; AAC12788).
{ECO:0000305}.
CONFLICT 1242 1242 E -> K (in Ref. 1; AAC12788).
{ECO:0000305}.
CONFLICT 1245 1245 L -> Q (in Ref. 1; AAC12788).
{ECO:0000305}.
SEQUENCE 1396 AA; 154322 MW; 2384B07DDBA28372 CRC64;
MSGDSIHRRR MALHCPITSL ILLLIAMSAH GYNIDLPSYV RFRQSSNSMF GFSIAMHKGR
SGFYGNQNNV SLIVGAPKFD TSRYQQGVTE AGGVFKCSLN DDDCKLVPFD SKGNNRNVDK
EVVDRKSYQW LGATVATGRD SDLVVACAPR YVFHTMTPSR AFRIDPVGTC FTSHNFEEFY
EVSPCRTNNW GYHRQGSCQA GFSAAINGNG SRLFIGAPGS WYWQGQTYSI PPDAKFPFKP
PLYQPFGTGG MASSHDVTRP ENQVFSTSES ASVNDDSYLG YSMVTGDFDG DRSEDVAIGM
PRGGNLVGRI VVNRWNMANI FNITGRQIGE YFGYSLATSD VDGDGLDDLL IGAPMYTDPD
NVEGKYDVGR VYILLQGGPT EEKRWTTEHI RDGYHSKGRF GLALTTLGDV NGDGYGDFAV
GAPYDGPEGR GVVYIFHGSP MGPLAKPSQI IKSEQLVEGA PYPRTFGFAL SGGLDMDGNT
YPDLAVGAYS SDQVFIFKSR PVAAVNAETS FASNSKLISL DDRSCQLVRD HKKVPCMLLT
TCWSYTGRYL PEQLDFDVSW LLDAKKLLNP RMFFLRDEGK NIRNQTIRLN YGQKYCLNET
VYLLDKVQDK LTPLEVEARY NLRSSRPLDP MVRHRRSILE PVIDQNREIV LRDAINIQKN
CGPDNICEPD LKLKVSTVDK YLFGSPEPLV IEVFISNTNE DAFEAAFYMV TPPDLQFRKL
QQLGEKKDTP ITCSPPTPEN NHTLKCDIGN PLESGKIAHF KISLVPEEKY GSSSSYDFYW
EANSTNLEKP GSEYDNKIRQ SVGIWVDTDL DIKGTSLPDY QLYKADDYKE LENATKEDDI
GPQVVHIYEI RNNRPSIIEE AEVFIHLPYE TIVGDPLMYL LNQPETGGKI QCDDVAFNEY
NLLLDEKLVK KSYLQAQGAI WNSAQVSGQS SSSSSSGGAS VHIEKARGEG FVRGVLVSNS
TDAGDKLSPK QVEQRRQEDT LEALGDASFV HRDRASQAVQ EPQVNQTSFT TYSTSSSSSG
SGAPSAQLRG HSTQGHIQMA GPVQHTSSSS SSNYRSWPAQ QQQQHQQLLL AGSGGSGLGS
PVTFNDKSQF GGRNNNFHTG TLDLGTLNRG NVDNELYRSQ GQYQNPSQSL GQSQGQFQAN
ANQGHYQGQN QAQFQARNPG FQGQTSYQGQ TQYSGQPGGY QTHHVTYSSG SKPYYGRENE
DFYDEDNLQQ ATPGHWSSSS SSSSSSGTRR LRRSNDKDGA TEKPLQIDLN SPCQSARCKS
IRCVVTNLGT EDGDAAFVAI RARMVAKTME KLASNVPLNV STLAVANVTL LPFIGAPKDA
IVKTHEIFYK AEPEPLQVPD VVPLWVVVLA ACAGALIFLL LVWLLYKCGF FNRNRPTDHS
QERQPLRNGY HGDEHL


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