ITA5_DROME
ID ITA5_DROME Reviewed; 1000 AA.
AC Q9W1M8;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Integrin alpha-PS5;
DE AltName: Full=Position-specific antigen subunit alpha-5;
DE Flags: Precursor;
GN Name=ItgaPS5 {ECO:0000312|FlyBase:FBgn0034880};
GN Synonyms=alphaPS5, ItgalphaPS5;
GN ORFNames=CG5372 {ECO:0000312|FlyBase:FBgn0034880};
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 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 [4]
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).
CC -!- FUNCTION: Possible role in cell-cell interactions. Minor involvement in
CC the establishment of the oocyte anterior-posterior length.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Alpha-PS5
CC associates with beta-PS (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in all follicle cells overlying the
CC oocyte during mid-oogenesis, the strongest expression is observed in
CC the cells covering the anterior end of the oocyte and in the cells
CC forming the dorsal appendages. After completion of oocyte enlargement,
CC expression in main body follicle cells is down-regulated but persists
CC strongly in the dorsal appendage forming cells. Expressed in
CC lamellocytes. {ECO:0000269|PubMed:19035354,
CC ECO:0000269|PubMed:21124962}.
CC -!- DEVELOPMENTAL STAGE: Expressed during mid- and late-oogenesis.
CC {ECO:0000269|PubMed:19035354}.
CC -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}.
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DR EMBL; AE013599; AAF47029.1; -; Genomic_DNA.
DR RefSeq; NP_611808.1; NM_137964.2.
DR AlphaFoldDB; Q9W1M8; -.
DR SMR; Q9W1M8; -.
DR BioGRID; 63332; 3.
DR DIP; DIP-20602N; -.
DR IntAct; Q9W1M8; 2.
DR STRING; 7227.FBpp0071972; -.
DR GlyGen; Q9W1M8; 11 sites.
DR PaxDb; Q9W1M8; -.
DR PRIDE; Q9W1M8; -.
DR EnsemblMetazoa; FBtr0473618; FBpp0423081; FBgn0034880.
DR GeneID; 37732; -.
DR KEGG; dme:Dmel_CG5372; -.
DR CTD; 37732; -.
DR FlyBase; FBgn0034880; ItgaPS5.
DR VEuPathDB; VectorBase:FBgn0034880; -.
DR eggNOG; KOG3637; Eukaryota.
DR GeneTree; ENSGT00940000165133; -.
DR HOGENOM; CLU_008760_0_0_1; -.
DR InParanoid; Q9W1M8; -.
DR OMA; PGNCRVR; -.
DR OrthoDB; 189377at2759; -.
DR PhylomeDB; Q9W1M8; -.
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; 37732; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 37732; -.
DR PRO; PR:Q9W1M8; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0034880; Expressed in oocyte associated follicle cell (Drosophila) and 2 other tissues.
DR Genevisible; Q9W1M8; 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; 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; 6.
PE 2: Evidence at transcript level;
KW Cell adhesion; Glycoprotein; Integrin; Membrane; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..?
FT /evidence="ECO:0000255"
FT CHAIN ?..1000
FT /note="Integrin alpha-PS5"
FT /id="PRO_0000016330"
FT TOPO_DOM ?..929
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 930..950
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 951..1000
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 15..74
FT /note="FG-GAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 75..137
FT /note="FG-GAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 145..198
FT /note="FG-GAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 199..261
FT /note="FG-GAP 4"
FT REPEAT 262..323
FT /note="FG-GAP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 324..379
FT /note="FG-GAP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 386..448
FT /note="FG-GAP 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REGION 971..1000
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 516
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 592
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 622
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 732
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 771
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 829
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 842
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 853
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 922
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1000 AA; 110544 MW; BD1D95C924D0B71E CRC64;
MNFSPLPNRV IDAPKHLKTR MIQVRSSYFG YSLVIRPTSI FVGAPRAQST LESQGSINET
GAVYRCPLAS GSCSHYVLND KLNKQFQWLG GSMDGGTKDT DKLLVCAPRF FVPKNKNYGQ
MRGICYWVRD TVADTPPLSD VRTISLIPSQ AEEHFMLELG LSAHVTDDNS GFLIGAPGVR
SWKGSVLVHR GEDLAAQGSY AVKMLDSWDW VKNHFTYVGY ALSSGYFSSN NRTSLLYVTT
APSSVLNTGK AYIFDVVGEI VRKLHVFHGE QLGEYFGYSV VAEDLNGDGL TDVVVSAPLN
ALGDSYDVGA IYVFINKGLF KFEKKIIRLP LSSGARFGSS LSKVGDINHD GYNDLAVGAP
FAGNGAVFIF LGSEHGLRDE PSQRLDAPSR EPGPYGAHMF GQGLSRGSDI DGNGFNDLAI
GAPGAEAVYL YRAYPVVKIH ATVRSESRAI RPEQETITVT ACYRLETTSK ARQMQQQELT
FRMTIDELLQ RVSFAPMRTN EVSFQAQAGL SGSCRNFSVG VHYTGGIFTP IDLELHYELA
KKIPHSHEAF CESCAVVDPL EPKYATGTLS FMTGCAAHVC VSDLQLSSKD VNSSFIFGSL
EVLSFSYEIT NSGEPAYVAQ FNVTSSARLP FAKVPGNCRV RHEVMLCDLN GGRALARGDS
ESLTIIFDVT QLSGQSLTIE AAVSSAGMDQ NPKDNTMSTT ISLREYAEID ASGGPIDGHI
ALKEYPYSAE VNNSYEFKSH GPSIIDELTV YVDVPIAYTV TGSAGIKSIF NISSLQMQAT
HGSELVPIKL YDQTNTLAKE YPLEDSSRRA NRKRRELQQD QYAIMPDVNI SDILTKENLP
ANRTLVLDCL RGNWTICVRS QMRVQLKPEQ PIDLRISFKV DLNDFVNTFD YLVIFTNVEM
FKEGDSTSIA LKRNLKPNVI FNYSETPLPI WYIILSLIAG HLLLGAMTYI LYKLRFFKRG
KKEELKRLLE EHRSETKEPA TDCEGNQEEI NVEMHSDLEN
