ITA2_DROME
ID ITA2_DROME Reviewed; 1396 AA.
AC P12080; E1JJN2; Q8IR07; Q8MSG3; Q9VXB6;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=Integrin alpha-PS2;
DE AltName: Full=Position-specific antigen subunit alpha-2;
DE AltName: Full=Protein inflated;
DE Contains:
DE RecName: Full=Integrin alpha-PS2 heavy chain;
DE Contains:
DE RecName: Full=Integrin alpha-PS2 light chain;
DE Flags: Precursor;
GN Name=if; ORFNames=CG9623;
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 PS2C), IDENTIFICATION BY MASS
RP SPECTROMETRY, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=2961459; DOI=10.1016/0092-8674(87)90580-0;
RA Bogaert T., Brown N.H., Wilcox M.;
RT "The Drosophila PS2 antigen is an invertebrate integrin that, like the
RT fibronectin receptor, becomes localized to muscle attachments.";
RL Cell 51:929-940(1987).
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.
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] OF 213-757 (ISOFORM PS2M8).
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 [5]
RP ALTERNATIVE SPLICING, AND DEVELOPMENTAL STAGE.
RX PubMed=2507168; DOI=10.1016/0092-8674(89)90880-5;
RA Brown N.H., King D.L., Wilcox M., Kafatos F.C.;
RT "Developmentally regulated alternative splicing of Drosophila integrin PS2
RT alpha transcripts.";
RL Cell 59:185-195(1989).
RN [6]
RP TISSUE 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 [7]
RP FUNCTION.
RX PubMed=7924982; DOI=10.1242/dev.120.7.1747;
RA Fogerty F.J., Fessler L.I., Bunch T.A., Yaron Y., Parker C.G., Nelson R.E.,
RA Brower D.L., Gullberg D., Fessler J.H.;
RT "Tiggrin, a novel Drosophila extracellular matrix protein that functions as
RT a ligand for Drosophila alpha PS2 beta PS integrins.";
RL Development 120:1747-1758(1994).
RN [8]
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 [9]
RP FUNCTION.
RX PubMed=9660786; DOI=10.1074/jbc.273.29.18235;
RA Graner M.W., Bunch T.A., Baumgartner S., Kerschen A., Brower D.L.;
RT "Splice variants of the Drosophila PS2 integrins differentially interact
RT with RGD-containing fragments of the extracellular proteins tiggrin, ten-m,
RT and D-laminin 2.";
RL J. Biol. Chem. 273:18235-18241(1998).
RN [10]
RP FUNCTION.
RX PubMed=10821184; DOI=10.1007/s004380051194;
RA Ayyub C., Rodrigues V., Hasan G., Siddiqi O.;
RT "Genetic analysis of olfC demonstrates a role for the position-specific
RT integrins in the olfactory system of Drosophila melanogaster.";
RL Mol. Gen. Genet. 263:498-504(2000).
RN [11]
RP 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 [12]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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).
CC -!- FUNCTION: Alpha-PS2/beta-PS is a receptor for Tig, wb and Ten-m.
CC Involved in the function and/or development of the olfactory system.
CC {ECO:0000269|PubMed:10821184, ECO:0000269|PubMed:7924982,
CC ECO:0000269|PubMed:7972082, ECO:0000269|PubMed:9660786}.
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-PS2 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. During embryogenesis, at the end of
CC germband extension concentrates at the basal membrane of mesodermal
CC cells, where they adhere to the ectoderm. Then, in visceral mesoderm
CC localizes basally, whereas in somatic mesoderm is homogenously
CC distributed.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=PS2C; Synonyms=D, F;
CC IsoId=P12080-1; Sequence=Displayed;
CC Name=PS2M8; Synonyms=C;
CC IsoId=P12080-2; Sequence=VSP_002739;
CC -!- TISSUE SPECIFICITY: In ovaries, highly expressed in follicle cells. At
CC syncytial blastoderm stage, expressed in the embryonic mesodermal
CC precursors but not in the ectoderm. At embryonic stages 7 and 10,
CC expression is restricted to the mesoderm. At stage 12, expressed in the
CC gonadal sheath and the interstitial cells of the gonad. In stage 16
CC embryos, expressed in the somatic and visceral muscles where localizes
CC to sites of attachment between adjacent muscles. In third larval instar
CC wing imaginal disk, expressed in the ventral compartment and in a
CC subset of adepithelial and peripodial cells (at protein level).
CC {ECO:0000269|PubMed:15469969, ECO:0000269|PubMed:19035354,
CC ECO:0000269|PubMed:2961459, ECO:0000269|PubMed:8240969}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout embryonic and larval
CC development with peaks of expression during mid-embryogenesis and at
CC third larval instar (at protein level). The relative ratio of isoform
CC 1/PS2C and isoform 2/PS2M8 varies widely during development.
CC {ECO:0000269|PubMed:2507168, ECO:0000269|PubMed:2961459,
CC ECO:0000269|PubMed:8240969}.
CC -!- PTM: The heavy-light chain cleavage site is either in 1230-1231, or
CC 1233-1234, or 1243-1244.
CC -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM50700.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAM50700.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; M19059; AAC12788.1; -; mRNA.
DR EMBL; AE014298; AAF48661.1; -; Genomic_DNA.
DR EMBL; AE014298; AAN09423.2; -; Genomic_DNA.
DR EMBL; AE014298; ACZ95312.1; -; Genomic_DNA.
DR EMBL; AE014298; ACZ95313.1; -; Genomic_DNA.
DR EMBL; AY118840; AAM50700.1; ALT_SEQ; mRNA.
DR PIR; A29637; A29637.
DR RefSeq; NP_001162777.1; NM_001169306.2. [P12080-1]
DR RefSeq; NP_001162778.1; NM_001169307.1. [P12080-1]
DR RefSeq; NP_523378.2; NM_078654.2. [P12080-1]
DR RefSeq; NP_728021.2; NM_167544.2. [P12080-2]
DR AlphaFoldDB; P12080; -.
DR SMR; P12080; -.
DR BioGRID; 58994; 29.
DR DIP; DIP-23111N; -.
DR IntAct; P12080; 2.
DR STRING; 7227.FBpp0074131; -.
DR GlyGen; P12080; 12 sites.
DR PaxDb; P12080; -.
DR PRIDE; P12080; -.
DR EnsemblMetazoa; FBtr0074357; FBpp0074131; FBgn0001250. [P12080-1]
DR EnsemblMetazoa; FBtr0301352; FBpp0290566; FBgn0001250. [P12080-2]
DR EnsemblMetazoa; FBtr0301353; FBpp0290567; FBgn0001250. [P12080-1]
DR EnsemblMetazoa; FBtr0301354; FBpp0290568; FBgn0001250. [P12080-1]
DR GeneID; 32661; -.
DR KEGG; dme:Dmel_CG9623; -.
DR UCSC; CG9623-RA; d. melanogaster.
DR CTD; 32661; -.
DR FlyBase; FBgn0001250; if.
DR VEuPathDB; VectorBase:FBgn0001250; -.
DR eggNOG; KOG3637; Eukaryota.
DR GeneTree; ENSGT00940000169118; -.
DR HOGENOM; CLU_004111_4_0_1; -.
DR InParanoid; P12080; -.
DR OMA; KPPLYQP; -.
DR PhylomeDB; P12080; -.
DR Reactome; R-DME-114608; Platelet degranulation.
DR Reactome; R-DME-1236973; Cross-presentation of particulate exogenous antigens (phagosomes).
DR Reactome; R-DME-1566977; Fibronectin matrix formation.
DR Reactome; R-DME-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-DME-2129379; Molecules associated with elastic fibres.
DR Reactome; R-DME-216083; Integrin cell surface interactions.
DR Reactome; R-DME-2173789; TGF-beta receptor signaling activates SMADs.
DR Reactome; R-DME-3000170; Syndecan interactions.
DR Reactome; R-DME-3000178; ECM proteoglycans.
DR Reactome; R-DME-354192; Integrin signaling.
DR Reactome; R-DME-5674135; MAP2K and MAPK activation.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR Reactome; R-DME-9634597; GPER1 signaling.
DR SignaLink; P12080; -.
DR BioGRID-ORCS; 32661; 0 hits in 3 CRISPR screens.
DR ChiTaRS; if; fly.
DR GenomeRNAi; 32661; -.
DR PRO; PR:P12080; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0001250; Expressed in thoracico-abdominal ganglion (Drosophila) and 18 other tissues.
DR ExpressionAtlas; P12080; baseline and differential.
DR Genevisible; P12080; DM.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0042383; C:sarcolemma; IDA: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: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:0007298; P:border follicle cell migration; IMP:FlyBase.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IDA: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; ISS:FlyBase.
DR GO; GO:0021551; P:central nervous system morphogenesis; IMP:FlyBase.
DR GO; GO:0035099; P:hemocyte migration; IMP: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:0045185; P:maintenance of protein location; IMP:FlyBase.
DR GO; GO:0007494; P:midgut development; TAS:FlyBase.
DR GO; GO:0016203; P:muscle attachment; IMP:FlyBase.
DR GO; GO:0030239; P:myofibril assembly; IMP:FlyBase.
DR GO; GO:0051492; P:regulation of stress fiber assembly; 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:0045214; P:sarcomere organization; IMP: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 GO; GO:0007419; P:ventral cord development; IMP: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; PF00357; Integrin_alpha; 1.
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; Disulfide bond;
KW Glycoprotein; Integrin; Membrane; Olfaction; Receptor; Reference proteome;
KW Repeat; Sensory transduction; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..1396
FT /note="Integrin alpha-PS2"
FT /id="PRO_0000016323"
FT CHAIN 32..?1243
FT /note="Integrin alpha-PS2 heavy chain"
FT /id="PRO_0000016324"
FT CHAIN ?1244..1396
FT /note="Integrin alpha-PS2 light chain"
FT /id="PRO_0000016325"
FT TOPO_DOM 32..1341
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1342..1366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1367..1396
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 36..106
FT /note="FG-GAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 117..174
FT /note="FG-GAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 186..239
FT /note="FG-GAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 266..317
FT /note="FG-GAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 318..383
FT /note="FG-GAP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 386..445
FT /note="FG-GAP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 452..514
FT /note="FG-GAP 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REGION 960..1107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1159..1246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1377..1396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 968..989
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 998..1107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1159..1193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1210..1229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 584
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 598
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 741
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 783
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 833
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 959
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1005
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 225..249
FT /note="Missing (in isoform PS2M8)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_002739"
FT CONFLICT 29
FT /note="A -> G (in Ref. 1; AAC12788)"
FT /evidence="ECO:0000305"
FT CONFLICT 968..976
FT /note="SPKQVEQRR -> RSQASGATA (in Ref. 1; AAC12788)"
FT /evidence="ECO:0000305"
FT CONFLICT 1063..1064
FT /note="Missing (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 1235
FT /note="N -> D (in Ref. 1; AAC12788)"
FT /evidence="ECO:0000305"
FT CONFLICT 1242
FT /note="E -> K (in Ref. 1; AAC12788)"
FT /evidence="ECO:0000305"
FT CONFLICT 1245
FT /note="L -> Q (in Ref. 1; AAC12788)"
FT /evidence="ECO:0000305"
SQ 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
