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Protein

Integrin alpha-PS1

Gene

mew

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Integrin alpha-PS1/beta-PS is a receptor for laminin.1 Publication

GO - Molecular functioni

  • cell adhesion molecule binding Source: FlyBase
  • extracellular matrix binding Source: FlyBase
  • protein heterodimerization activity Source: FlyBase
  • receptor activity Source: FlyBase

GO - Biological processi

  • actin filament organization Source: FlyBase
  • apposition of dorsal and ventral imaginal disc-derived wing surfaces Source: FlyBase
  • axonal defasciculation Source: FlyBase
  • axon guidance Source: FlyBase
  • cell adhesion Source: FlyBase
  • cell adhesion mediated by integrin Source: FlyBase
  • cell differentiation Source: FlyBase
  • cell-matrix adhesion Source: FlyBase
  • cell migration Source: FlyBase
  • ectodermal digestive tract morphogenesis Source: FlyBase
  • epithelial cell migration, open tracheal system Source: FlyBase
  • heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules Source: FlyBase
  • imaginal disc-derived wing morphogenesis Source: FlyBase
  • integrin-mediated signaling pathway Source: UniProtKB-KW
  • maintenance of epithelial integrity, open tracheal system Source: FlyBase
  • midgut development Source: FlyBase
  • muscle attachment Source: FlyBase
  • open tracheal system development Source: FlyBase
  • salivary gland boundary specification Source: FlyBase
  • salivary gland development Source: FlyBase
  • salivary gland morphogenesis Source: FlyBase
  • sensory perception of smell Source: FlyBase
  • single organismal cell-cell adhesion Source: FlyBase
  • substrate adhesion-dependent cell spreading Source: FlyBase
  • tracheal outgrowth, open tracheal system Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Integrin, Receptor

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiR-DME-210991. Basigin interactions.
R-DME-216083. Integrin cell surface interactions.
R-DME-3000178. ECM proteoglycans.
R-DME-446107. Type I hemidesmosome assembly.

Names & Taxonomyi

Protein namesi
Recommended name:
Integrin alpha-PS1
Alternative name(s):
Position-specific antigen subunit alpha-1
Protein multiple edematous wings
Cleaved into the following 2 chains:
Gene namesi
Name:mew
ORF Names:CG1771
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0004456. mew.

Subcellular locationi

  • Apical cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication
  • Lateral cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication
  • Basal cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication

  • 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. Localization to lateral and basal membranes persists during dorsal appendage morphogenesis, although diminished and often absent.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini31 – 10851055ExtracellularSequence analysisAdd
BLAST
Transmembranei1086 – 110621HelicalSequence analysisAdd
BLAST
Topological domaini1107 – 114640CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • apical plasma membrane Source: UniProtKB
  • basal plasma membrane Source: FlyBase
  • focal adhesion Source: FlyBase
  • integral component of plasma membrane Source: FlyBase
  • integrin complex Source: FlyBase
  • lateral plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3030Sequence analysisAdd
BLAST
Chaini31 – 11461116Integrin alpha-PS1PRO_0000016320Add
BLAST
Chaini31 – ?960930Integrin alpha-PS1 heavy chainSequence analysisPRO_0000016321Add
BLAST
Chaini?961 – 1146186Integrin alpha-PS1 light chainSequence analysisPRO_0000016322Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi68 – 681N-linked (GlcNAc...)Sequence analysis
Glycosylationi86 – 861N-linked (GlcNAc...)Sequence analysis
Glycosylationi147 – 1471N-linked (GlcNAc...)Sequence analysis
Glycosylationi470 – 4701N-linked (GlcNAc...)Sequence analysis
Glycosylationi511 – 5111N-linked (GlcNAc...)Sequence analysis
Glycosylationi657 – 6571N-linked (GlcNAc...)1 Publication
Glycosylationi680 – 6801N-linked (GlcNAc...)Sequence analysis
Glycosylationi711 – 7111N-linked (GlcNAc...)1 Publication
Glycosylationi718 – 7181N-linked (GlcNAc...)1 Publication
Glycosylationi761 – 7611N-linked (GlcNAc...)1 Publication
Glycosylationi928 – 9281N-linked (GlcNAc...)Sequence analysis
Glycosylationi1027 – 10271N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ24247.

Expressioni

Tissue specificityi

Expressed in follicle cells (at protein level). At syncytial blastoderm stage, expressed in the ectoderm but not in the mesodermal precursors. At embryonic stage 7, expressed in dorsal and ventrolateral ectoderm and in some yolk nuclei. At late stage 10, expression is homogeneous in the ectoderm and is particularly abundant in the anterior and posterior midgut primordia. At stage 11, strongly expressed in a metameric pattern in the ectoderm, in the proctodeum and in the posterior midgut primordium. At stage 12, accumulates at the segment boundaries that start to become morphologically visible, similar expression pattern is observed in the central nervous system. In third larval instar wing imaginal disk, strongly expressed in the dorsal compartment, in the adepithelial cells and in patches on the peripodial membrane covering the imaginal disk to the outside.2 Publications

Developmental stagei

Expressed during mid- and late-oogenesis (at protein level). Expressed throughout embryonic and larval development with peaks of expression during mid-embryogenesis and at third larval instar.2 Publications

Gene expression databases

BgeeiQ24247.
ExpressionAtlasiQ24247. differential.
GenevisibleiQ24247. DM.

Interactioni

Subunit structurei

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-PS1 associates with beta-PS.

GO - Molecular functioni

  • cell adhesion molecule binding Source: FlyBase
  • protein heterodimerization activity Source: FlyBase

Protein-protein interaction databases

BioGridi58660. 4 interactions.
IntActiQ24247. 15 interactions.
STRINGi7227.FBpp0302767.

Structurei

3D structure databases

ProteinModelPortaliQ24247.
SMRiQ24247. Positions 32-703.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati38 – 10568FG-GAP 1PROSITE-ProRule annotationAdd
BLAST
Repeati121 – 18666FG-GAP 2PROSITE-ProRule annotationAdd
BLAST
Repeati193 – 24553FG-GAP 3PROSITE-ProRule annotationAdd
BLAST
Repeati254 – 30350FG-GAP 4PROSITE-ProRule annotationAdd
BLAST
Repeati304 – 36663FG-GAP 5PROSITE-ProRule annotationAdd
BLAST
Repeati367 – 42256FG-GAP 6PROSITE-ProRule annotationAdd
BLAST
Repeati432 – 49463FG-GAP 7PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the integrin alpha chain family.Curated
Contains 7 FG-GAP repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IPBB. Eukaryota.
ENOG410XVGZ. LUCA.
GeneTreeiENSGT00760000118782.
InParanoidiQ24247.
OMAiFGYELTT.
OrthoDBiEOG70PBWR.
PhylomeDBiQ24247.

Family and domain databases

InterProiIPR013517. FG-GAP.
IPR013519. Int_alpha_beta-p.
IPR000413. Integrin_alpha.
IPR013649. Integrin_alpha-2.
IPR018184. Integrin_alpha_C_CS.
IPR032695. Integrin_dom.
[Graphical view]
PfamiPF01839. FG-GAP. 2 hits.
PF08441. Integrin_alpha2. 1 hit.
[Graphical view]
PRINTSiPR01185. INTEGRINA.
SMARTiSM00191. Int_alpha. 5 hits.
[Graphical view]
SUPFAMiSSF69179. SSF69179. 4 hits.
PROSITEiPS51470. FG_GAP. 7 hits.
PS00242. INTEGRIN_ALPHA. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform B (identifier: Q24247-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLELPFTTIR PNCRLRQNLG ILIILQCVLT CYNFNLEQRL PIVKYGHPHS
60 70 80 90 100
HFGYSVATHT IGEANGPNKT NCVLVGAPLD QNRQPNTTHS GALWRCPMTQ
110 120 130 140 150
RFDDCEQVIT DGRRNFDSEI LSPPGNDEIK EDQWMGVTVR SNPLQANGSG
160 170 180 190 200
GKVIVCAHRY MYIVRENRYG QGLCYLLTND LQFEEVHEPC KGRPVQRQHE
210 220 230 240 250
DYGLCQAGTS AALLDDDTMV LGSPGPYTWR GSIWVTQVGG EYLQRDKTTY
260 270 280 290 300
YSDHSDLNSP VDKYSYLGMS VTGGRFFGHM SYAAGAPRSE GHGQVVIFDK
310 320 330 340 350
STDNPIPVHS ILDGEQFGSS FGYELATADI NGDHRPDLIV AAPLYFTKTE
360 370 380 390 400
GGAVYVYQNI QDTLPMKYTL KLTGPLESRF GLALANIGDL NKDNCEDLAV
410 420 430 440 450
GAPYEGNGVV YIYLGSSQGL NSKPAQKIQA SELGGTIPNG QPIRTFGISI
460 470 480 490 500
SGNTDLDDNS YPDVVIGAFN SSAAVILLAR PIISIQTSVQ RKELHNMDPN
510 520 530 540 550
TPGCLDDPAS NLTCFTFRAC CSIEPYDEKN KELRLAYSVE AETFDHLKKF
560 570 580 590 600
SRVFFFDREN KRTNVLSRVV RVHTNGRTEC QAVTGYIKAN TRDIQTPVRF
610 620 630 640 650
RLKYSLVEPP LADSALVRLN PILDQTQAHV DFEGTFQKDC GDDDLCESNL
660 670 680 690 700
IIRVEPNITE SSGNEYTLIL DETELEVRIN VSNLADSAYE AQLFIAHQAG
710 720 730 740 750
VSYVATKKPT NATCNSYNTT LVACSLGNPM LRDTTTFVTI RFQPKGLEPS
760 770 780 790 800
EKIMLFHIFA NTTSKLVGPE RPERDLRVNV VRRAKLNFRG WAIPEQSFYS
810 820 830 840 850
GSSVANSVAN TAATDIEGHG PMGMDDVGSQ VHHMFTIFNE GPSTAPKVQM
860 870 880 890 900
VIHWPYSLYS DPQSGRPVQY LLYLEQVPTV EVSQGECHVA KEYVNPLNLA
910 920 930 940 950
SGSRENPAYL SAPAQMRMFP SQSRHSFNKS LIHSQRSYYS SSHRDDHSDD
960 970 980 990 1000
TQSNRNRVRR SFLERVTRLE RLMYDPESSN AANGKKQDIV ELDCNKGATN
1010 1020 1030 1040 1050
CVRIECDILN MPALSEAQVV VKARLWNSTL VSEYPRVERV RIFSTATAQI
1060 1070 1080 1090 1100
PESYGVEVMD HNNIEVETRA YPELRNQQRD TSIPWLIIIL GIVGGLLLLA
1110 1120 1130 1140
LVTYVLWKVG FFKRIRPTDP TLSGNLEKMN EEKPFLAPSK NTHHVF
Length:1,146
Mass (Da):127,973
Last modified:February 21, 2001 - v2
Checksum:iE8AB75BC8DE6854E
GO
Isoform A (identifier: Q24247-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-97: Missing.

Note: No experimental confirmation available.
Show »
Length:1,049
Mass (Da):117,097
Checksum:i49304E861063716F
GO
Isoform C (identifier: Q24247-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     114-115: RN → RTNGAYEINKH

Note: No experimental confirmation available.
Show »
Length:1,155
Mass (Da):128,987
Checksum:i0E1C9A43562D9DF1
GO
Isoform D (identifier: Q24247-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-97: Missing.
     114-115: RN → RTNGAYEINKH

Note: No experimental confirmation available.
Show »
Length:1,058
Mass (Da):118,111
Checksum:i9316E6312504B21E
GO
Isoform E (identifier: Q24247-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-97: Missing.
     1146-1146: F → FXQEGTVGWD...ASAAWWGHHM

Note: No experimental confirmation available.
Show »
Length:1,146
Mass (Da):128,348
Checksum:i38098E971537C1C7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti730 – 7312ML → IV in CAA52155 (PubMed:8240969).Curated
Sequence conflicti815 – 8151D → E in CAA52155 (PubMed:8240969).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 9797Missing in isoform A, isoform D and isoform E. 1 PublicationVSP_009270Add
BLAST
Alternative sequencei114 – 1152RN → RTNGAYEINKH in isoform C and isoform D. CuratedVSP_053396
Alternative sequencei1146 – 11461F → FXQEGTVGWDLVRRRRRRRR LKLRLPVTAQPRHGWRKTTD KSINNNNNNNHNNNSSNSRN DSDVDVLSLTPPPPPLSIFS WGNDGYYQASAAWWGHHM in isoform E. CuratedVSP_053397

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X73975 mRNA. Translation: CAA52155.1.
AE014298 Genomic DNA. Translation: AAF48242.2.
AE014298 Genomic DNA. Translation: AAN09652.1.
AE014298 Genomic DNA. Translation: AGB95345.1.
AE014298 Genomic DNA. Translation: AGB95346.1.
AE014298 Genomic DNA. Translation: AGB95347.1.
AY075338 mRNA. Translation: AAL68203.1.
PIRiS40311.
RefSeqiNP_001259503.1. NM_001272574.1. [Q24247-5]
NP_001259504.1. NM_001272575.2. [Q24247-3]
NP_001259505.1. NM_001272576.2. [Q24247-4]
NP_511145.2. NM_078590.3. [Q24247-1]
NP_727679.1. NM_167354.2. [Q24247-2]
UniGeneiDm.152.

Genome annotation databases

EnsemblMetazoaiFBtr0073732; FBpp0073563; FBgn0004456. [Q24247-1]
GeneIDi32275.
KEGGidme:Dmel_CG1771.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X73975 mRNA. Translation: CAA52155.1.
AE014298 Genomic DNA. Translation: AAF48242.2.
AE014298 Genomic DNA. Translation: AAN09652.1.
AE014298 Genomic DNA. Translation: AGB95345.1.
AE014298 Genomic DNA. Translation: AGB95346.1.
AE014298 Genomic DNA. Translation: AGB95347.1.
AY075338 mRNA. Translation: AAL68203.1.
PIRiS40311.
RefSeqiNP_001259503.1. NM_001272574.1. [Q24247-5]
NP_001259504.1. NM_001272575.2. [Q24247-3]
NP_001259505.1. NM_001272576.2. [Q24247-4]
NP_511145.2. NM_078590.3. [Q24247-1]
NP_727679.1. NM_167354.2. [Q24247-2]
UniGeneiDm.152.

3D structure databases

ProteinModelPortaliQ24247.
SMRiQ24247. Positions 32-703.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi58660. 4 interactions.
IntActiQ24247. 15 interactions.
STRINGi7227.FBpp0302767.

Proteomic databases

PaxDbiQ24247.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0073732; FBpp0073563; FBgn0004456. [Q24247-1]
GeneIDi32275.
KEGGidme:Dmel_CG1771.

Organism-specific databases

CTDi32275.
FlyBaseiFBgn0004456. mew.

Phylogenomic databases

eggNOGiENOG410IPBB. Eukaryota.
ENOG410XVGZ. LUCA.
GeneTreeiENSGT00760000118782.
InParanoidiQ24247.
OMAiFGYELTT.
OrthoDBiEOG70PBWR.
PhylomeDBiQ24247.

Enzyme and pathway databases

ReactomeiR-DME-210991. Basigin interactions.
R-DME-216083. Integrin cell surface interactions.
R-DME-3000178. ECM proteoglycans.
R-DME-446107. Type I hemidesmosome assembly.

Miscellaneous databases

GenomeRNAii32275.
PROiQ24247.

Gene expression databases

BgeeiQ24247.
ExpressionAtlasiQ24247. differential.
GenevisibleiQ24247. DM.

Family and domain databases

InterProiIPR013517. FG-GAP.
IPR013519. Int_alpha_beta-p.
IPR000413. Integrin_alpha.
IPR013649. Integrin_alpha-2.
IPR018184. Integrin_alpha_C_CS.
IPR032695. Integrin_dom.
[Graphical view]
PfamiPF01839. FG-GAP. 2 hits.
PF08441. Integrin_alpha2. 1 hit.
[Graphical view]
PRINTSiPR01185. INTEGRINA.
SMARTiSM00191. Int_alpha. 5 hits.
[Graphical view]
SUPFAMiSSF69179. SSF69179. 4 hits.
PROSITEiPS51470. FG_GAP. 7 hits.
PS00242. INTEGRIN_ALPHA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of alpha PS1, a novel Drosophila melanogaster integrin."
    Wehrli M., Diantonio A., Fearnley I.M., Smith R.J., Wilcox M.
    Mech. Dev. 43:21-36(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), PARTIAL PROTEIN SEQUENCE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: Oregon-R.
    Tissue: Embryo and Larva.
  2. "The genome sequence of Drosophila melanogaster."
    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.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  4. "A Drosophila full-length cDNA resource."
    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.
    Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
    Strain: Berkeley.
    Tissue: Head.
  5. "Drosophila PS1 integrin is a laminin receptor and differs in ligand specificity from PS2."
    Gotwals P.J., Fessler L.I., Wehrli M., Hynes R.O.
    Proc. Natl. Acad. Sci. U.S.A. 91:11447-11451(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Identification of N-glycosylated proteins from the central nervous system of Drosophila melanogaster."
    Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L., Panin V.
    Glycobiology 17:1388-1403(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-657 AND ASN-1027, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Oregon-R.
    Tissue: Head.
  7. "Integrin alpha chains exhibit distinct temporal and spatial localization patterns in epithelial cells of the Drosophila ovary."
    Dinkins M.B., Fratto V.M., Lemosy E.K.
    Dev. Dyn. 237:3927-3939(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  8. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
    Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
    Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-711; ASN-718 AND ASN-761, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiITA1_DROME
AccessioniPrimary (citable) accession number: Q24247
Secondary accession number(s): M9PEG3
, M9PHG7, M9PJL8, Q8SY51, Q9VYF6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 21, 2001
Last modified: June 8, 2016
This is version 155 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.