ITA4_DROME
ID ITA4_DROME Reviewed; 1069 AA.
AC Q9V7A4; G2J626; Q4V4A2;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Integrin alpha-PS4;
DE AltName: Full=Position-specific antigen subunit alpha-4;
DE Flags: Precursor;
GN Name=ItgaPS4 {ECO:0000312|FlyBase:FBgn0034005};
GN Synonyms=alphaPS4, ItgalphaPS4;
GN ORFNames=CG16827 {ECO:0000312|FlyBase:FBgn0034005};
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 371-1069.
RC STRAIN=Berkeley;
RA Stapleton M., Booth B., Carlson J.W., Chavez C., Frise E., George R.A.,
RA Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, 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 [5]
RP TISSUE SPECIFICITY.
RX PubMed=20689801; DOI=10.1371/journal.pbio.1000441;
RA Makki R., Meister M., Pennetier D., Ubeda J.M., Braun A., Daburon V.,
RA Krzemien J., Bourbon H.M., Zhou R., Vincent A., Crozatier M.;
RT "A short receptor downregulates JAK/STAT signalling to control the
RT Drosophila cellular immune response.";
RL PLoS Biol. 8:E1000441-E1000441(2010).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=21124962; DOI=10.1371/journal.pone.0014051;
RA Stofanko M., Kwon S.Y., Badenhorst P.;
RT "Lineage tracing of lamellocytes demonstrates Drosophila macrophage
RT plasticity.";
RL PLoS ONE 5:E14051-E14051(2010).
RN [7]
RP FUNCTION.
RX PubMed=22438831; DOI=10.1371/journal.pgen.1002582;
RA Zhai Z., Ha N., Papagiannouli F., Hamacher-Brady A., Brady N., Sorge S.,
RA Bezdan D., Lohmann I.;
RT "Antagonistic regulation of apoptosis and differentiation by the Cut
RT transcription factor represents a tumor-suppressing mechanism in
RT Drosophila.";
RL PLoS Genet. 8:E1002582-E1002582(2012).
CC -!- FUNCTION: Possible role in cell adhesion. Minor involvement in the
CC establishment of the oocyte anterior-posterior length.
CC {ECO:0000269|PubMed:19035354, ECO:0000269|PubMed:22438831}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Alpha-PS4
CC associates with beta-PS (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in lamellocytes (at protein level). At
CC the anterior end of the oocyte, expressed in the follicle cells that
CC will form the operculum and the micropyle.
CC {ECO:0000269|PubMed:19035354, ECO:0000269|PubMed:20689801,
CC ECO:0000269|PubMed:21124962}.
CC -!- DEVELOPMENTAL STAGE: Weakly expressed during late-oogenesis.
CC {ECO:0000269|PubMed:19035354}.
CC -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAY55520.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=AEO17898.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AE013599; AAF58154.2; -; Genomic_DNA.
DR EMBL; BT023104; AAY55520.1; ALT_SEQ; mRNA.
DR EMBL; BT128883; AEO17898.1; ALT_SEQ; mRNA.
DR RefSeq; NP_611025.2; NM_137181.3.
DR AlphaFoldDB; Q9V7A4; -.
DR SMR; Q9V7A4; -.
DR STRING; 7227.FBpp0086503; -.
DR GlyGen; Q9V7A4; 12 sites.
DR PaxDb; Q9V7A4; -.
DR EnsemblMetazoa; FBtr0087371; FBpp0086503; FBgn0034005.
DR GeneID; 36693; -.
DR KEGG; dme:Dmel_CG16827; -.
DR CTD; 36693; -.
DR FlyBase; FBgn0034005; ItgaPS4.
DR VEuPathDB; VectorBase:FBgn0034005; -.
DR eggNOG; KOG3637; Eukaryota.
DR GeneTree; ENSGT00940000165133; -.
DR HOGENOM; CLU_008760_0_0_1; -.
DR InParanoid; Q9V7A4; -.
DR OMA; NNGEFAY; -.
DR OrthoDB; 189377at2759; -.
DR PhylomeDB; Q9V7A4; -.
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 BioGRID-ORCS; 36693; 0 hits in 3 CRISPR screens.
DR ChiTaRS; ItgaPS4; fly.
DR GenomeRNAi; 36693; -.
DR PRO; PR:Q9V7A4; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0034005; Expressed in centripetally migrating follicle cell and 8 other tissues.
DR Genevisible; Q9V7A4; DM.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; ISS:FlyBase.
DR GO; GO:0008305; C:integrin complex; ISS:FlyBase.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:FlyBase.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; ISS: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:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; TAS:FlyBase.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0001555; P:oocyte growth; IMP:UniProtKB.
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; 5.
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 Cell adhesion; Glycoprotein; Integrin; Membrane; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..1069
FT /note="Integrin alpha-PS4"
FT /id="PRO_0000016329"
FT TOPO_DOM 19..985
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 986..1006
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1007..1069
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 29..89
FT /note="FG-GAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 104..165
FT /note="FG-GAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 184..237
FT /note="FG-GAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 255..310
FT /note="FG-GAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 312..374
FT /note="FG-GAP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 375..430
FT /note="FG-GAP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 437..499
FT /note="FG-GAP 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 415
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 509
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 643
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 661
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 800
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 875
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 896
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 907
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 931
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 545
FT /note="K -> E (in Ref. 3; AAY55520)"
FT /evidence="ECO:0000305"
FT CONFLICT 694
FT /note="N -> T (in Ref. 3; AAY55520)"
FT /evidence="ECO:0000305"
FT CONFLICT 737
FT /note="L -> F (in Ref. 3; AAY55520)"
FT /evidence="ECO:0000305"
FT CONFLICT 820
FT /note="K -> I (in Ref. 3; AAY55520)"
FT /evidence="ECO:0000305"
FT CONFLICT 932
FT /note="M -> L (in Ref. 3; AAY55520)"
FT /evidence="ECO:0000305"
FT CONFLICT 1004
FT /note="A -> V (in Ref. 3; AAY55520)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1069 AA; 118911 MW; B2AD69CF6EDA6FCC CRC64;
MFCLLVIVLL ALQSEINAYN ISPYPNSVLN FPELEGNRRS SYFGFSLVIR EKSIMVAAPR
ANSSLEAQRN ISEPGVIFRC YFESGNNCSP YNIDTKGNYK GMPNDGLLTA KNKDFRWLGG
AMDGGTRDSD KFLVCAPRFY SINNENDYNN GMCYWLSDTP KNIDSTEVME KWPLRIEKKQ
VLKLADTNLI PYYSMGELGL SAHVSDDNSK LLMGAPGIDQ WKGSVHLKQE VPSIKTSSGR
QRRGMNTNRK CNECNPEPKN FGQEEFSYFG YAVSSGYFDS SNLSTVLYVA TAPRGNNQFG
EAYIFDIYED SIYKYHEFRG NHFGEYFGYS VLAEDLNGDG KTDVIISAPL YALRNSYDDG
AIYVFINKGS FTFEERIIRS PAGSGGRFGT TLSRIGDINK DGYNDVAVGA PFAGNGSVFI
YLGSENGLRD PPSQCLDAPS QQPSKYGSYM FGHGLSRGSD IDGNGFNDFA IGAPNAEAVY
LYRAYPVVKI HAIIKPKLQN VNPEEERVNI TVCYRLSSKS DSKAKALMEQ ELVIRIDIDT
KSKIKLAVFD EEHGSQMSFK AKAFHEEICS EFQIEMDKRA KFTPIALEMQ YELSKKIPNS
GDFCEDCAVV DPAEPKFVTE YITFNTGCAT DVCVADLKIS CINASSTLVL GTTAVLRLTY
NITNNGEFAY HPKFSVTNSA GLSLAQVPGN CKVNEAVMVC DLNHGQRMAK GDTDSLTISF
DVRQLRGRSL EIQAEVLSAR DESNPENNKL TNVLSLREKA DIYVSGVQTN DHVVLKESPY
TAEVVNYYEI KSHGPSTLEN LTVSLYIPVA YKTPDSTNVK HIVTSSPKIQ SKYAHKIMPI
NFIDQNNALA NNFAIDHDQS TLLFSATPQH ENVGNLSGIV EQNPSISLLN EDLPVNNTLV
LNCQDTNVTL CVPVEIRLEN GLQLKPEELM NMTVSFTVNL KDADDIWEYF VIQTDLKVHK
IGDPTLSSFT IEKKIESNVI CKHAEIAIWK IIVSVIVGIL VFSAATYALY KRGFFKRAIK
DDLKQLIRDS FEDGIIRTEM EENAQSQGDA DLDEKLDAYA DTTGKCTHV
