PIP82_DROME
ID PIP82_DROME Reviewed; 1195 AA.
AC Q9W3E2; C0HBU3; O61732;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 3.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Protein PIP82 {ECO:0000303|PubMed:9697866};
GN Name=PIP82 {ECO:0000303|PubMed:9697866, ECO:0000312|FlyBase:FBgn0024943};
GN ORFNames=CG11219 {ECO:0000312|FlyBase:FBgn0024943};
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 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|EMBL:AAC18395.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND PHOSPHORYLATION.
RC STRAIN=Canton-S {ECO:0000312|EMBL:AAC18395.1};
RX PubMed=9697866; DOI=10.1016/s0896-6273(00)80529-2;
RA Suri V., Qian Z., Hall J.C., Rosbash M.;
RT "Evidence that the TIM light response is relevant to light-induced phase
RT shifts in Drosophila melanogaster.";
RL Neuron 21:225-234(1998).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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] {ECO:0000312|EMBL:ACN12159.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-367.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RA Carlson J., Booth B., Frise E., Sandler J., Wan K., Yu C., Celniker S.;
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP SUBCELLULAR LOCATION, DOMAIN, AND PHOSPHORYLATION.
RX PubMed=26481050; DOI=10.1016/j.devcel.2015.09.016;
RA Bailey M.J., Prehoda K.E.;
RT "Establishment of Par-Polarized Cortical Domains via Phosphoregulated
RT Membrane Motifs.";
RL Dev. Cell 35:199-210(2015).
RN [6] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DOMAIN,
RP PHOSPHORYLATION, AND DISRUPTION PHENOTYPE.
RX PubMed=32579558; DOI=10.1371/journal.pgen.1008890;
RA Zelhof A.C., Mahato S., Liang X., Rylee J., Bergh E., Feder L.E.,
RA Larsen M.E., Britt S.G., Friedrich M.;
RT "The brachyceran de novo gene PIP82, a phosphorylation target of aPKC, is
RT essential for proper formation and maintenance of the rhabdomeric
RT photoreceptor apical domain in Drosophila.";
RL PLoS Genet. 16:e1008890-e1008890(2020).
CC -!- FUNCTION: Required for the morphological differentiation and
CC maintenance of the rhabdomeric photoreceptor apical domain
CC (PubMed:32579558). Acts as a downstream component of the gl and Pph13
CC transcriptional pathway which is required for photoreceptor cell
CC development (PubMed:32579558). Likely to function by regulating the
CC trafficking or retention of rhabdomeric proteins including the
CC phototransduction proteins ninaE and didum (PubMed:32579558).
CC {ECO:0000269|PubMed:32579558}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:26481050, ECO:0000269|PubMed:32579558}. Cytoplasm,
CC cytosol {ECO:0000269|PubMed:26481050, ECO:0000269|PubMed:32579558}.
CC Note=Cortical membrane protein (PubMed:26481050, PubMed:32579558). In
CC photoreceptors, restricted to the rhabdomeric portion of the apical
CC surface (PubMed:32579558). Phosphorylation appears to displace it from
CC the cortex, increasing cytosol levels (PubMed:26481050,
CC PubMed:32579558). {ECO:0000269|PubMed:26481050,
CC ECO:0000269|PubMed:32579558}.
CC -!- TISSUE SPECIFICITY: Restricted to photoreceptor cells (at protein
CC level) (PubMed:32579558). Not detected until approximately 48hrs after
CC puparium formation (APF) and then maintained in the photoreceptor cells
CC post-eclosion (at protein level) (PubMed:32579558).
CC {ECO:0000269|PubMed:32579558}.
CC -!- DOMAIN: The phospho-regulated basic and hydrophobic (PRBH) motif is
CC sufficient and important for interaction with phospholipids permitting
CC cortical localization (PubMed:26481050). Phosphorylation of the PRBH
CC motif by aPKC inhibits the association of the protein with the cortical
CC membrane (PubMed:26481050, PubMed:32579558).
CC {ECO:0000269|PubMed:26481050, ECO:0000269|PubMed:32579558}.
CC -!- PTM: Phosphorylated by aPKC which lowers lipid affinity and promotes
CC dissociation from the cell cortex (PubMed:26481050, PubMed:32579558).
CC In the photoreceptor cells, aPKC-mediated phosphorylation leads to its
CC displacement from the stalk apical cortex and thus restricts its
CC localization to the rhabdomeric apical cortex where it functions
CC (PubMed:32579558). Dephosphorylation appears to be light-dependent
CC (PubMed:9697866). {ECO:0000269|PubMed:26481050,
CC ECO:0000269|PubMed:32579558, ECO:0000269|PubMed:9697866}.
CC -!- DISRUPTION PHENOTYPE: Viable however, rhabdomeres are flat and oblong,
CC and alignment or organization of the microvillar projections along the
CC depth of the retina are not maintained (PubMed:32579558). Severity of
CC the phenotype increases with age, by seven days post-eclosion
CC rhabdomeres have become irregular, misaligned and fragmented structures
CC (PubMed:32579558). The phototransduction proteins ninaE and, to a much
CC lesser extent, didum are displaced from vesicles near the rhabdomere
CC terminal web and instead become mislocalized to the basal lateral
CC membranes (PubMed:32579558). Photoactivation of ninaE and
CC phototransduction are unaffected, and amplitudes of light response is
CC enhanced at higher light intensities (PubMed:32579558).
CC {ECO:0000269|PubMed:32579558}.
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DR EMBL; AF067153; AAC18395.1; -; mRNA.
DR EMBL; AE014298; AAF46386.3; -; Genomic_DNA.
DR EMBL; BT059799; ACN12159.1; -; mRNA.
DR PIR; T13065; T13065.
DR RefSeq; NP_572487.3; NM_132259.3.
DR AlphaFoldDB; Q9W3E2; -.
DR IntAct; Q9W3E2; 3.
DR STRING; 7227.FBpp0071179; -.
DR PaxDb; Q9W3E2; -.
DR PRIDE; Q9W3E2; -.
DR EnsemblMetazoa; FBtr0071235; FBpp0071179; FBgn0024943.
DR GeneID; 31791; -.
DR KEGG; dme:Dmel_CG11219; -.
DR UCSC; CG11219-RA; d. melanogaster.
DR CTD; 31791; -.
DR FlyBase; FBgn0024943; PIP82.
DR VEuPathDB; VectorBase:FBgn0024943; -.
DR eggNOG; ENOG502T911; Eukaryota.
DR GeneTree; ENSGT00440000033589; -.
DR HOGENOM; CLU_284044_0_0_1; -.
DR InParanoid; Q9W3E2; -.
DR OMA; WPAPALY; -.
DR OrthoDB; 168474at2759; -.
DR PhylomeDB; Q9W3E2; -.
DR BioGRID-ORCS; 31791; 0 hits in 1 CRISPR screen.
DR ChiTaRS; PIP82; fly.
DR GenomeRNAi; 31791; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0024943; Expressed in head capsule and 5 other tissues.
DR ExpressionAtlas; Q9W3E2; baseline and differential.
DR Genevisible; Q9W3E2; DM.
DR GO; GO:0045179; C:apical cortex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0016028; C:rhabdomere; IDA:UniProtKB.
DR GO; GO:0071482; P:cellular response to light stimulus; IDA:FlyBase.
DR GO; GO:0046530; P:photoreceptor cell differentiation; IMP:UniProtKB.
DR GO; GO:0045494; P:photoreceptor cell maintenance; IMP:UniProtKB.
DR GO; GO:1990146; P:protein localization to rhabdomere; IMP:UniProtKB.
PE 1: Evidence at protein level;
KW Cytoplasm; Reference proteome.
FT CHAIN 1..1195
FT /note="Protein PIP82"
FT /id="PRO_0000451416"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..450
FT /note="Phospho-regulated basic and hydrophobic (PRBH)
FT motif"
FT /evidence="ECO:0000269|PubMed:26481050,
FT ECO:0000269|PubMed:32579558"
FT REGION 493..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 612..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 833..977
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1060..1195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..26
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..373
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..435
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..458
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..716
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 852..868
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 877..892
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..943
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 944..965
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1083
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1084..1098
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1099..1156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1174..1189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 108
FT /note="G -> A (in Ref. 1; AAC18395)"
FT /evidence="ECO:0000305"
FT CONFLICT 928
FT /note="P -> S (in Ref. 1; AAC18395)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1195 AA; 132341 MW; E25DAA951839481C CRC64;
MSHQEQQFQH YPHHQHHHHH HHHHIHQVQS ETQLEQRSSD LEPNRSRNTD RIGSSMDFRN
LCQRIDVDGL KAKLPQLKLP KSLPKLRGRK IFRSSKSGSN AAGGGTAGGS AKDGAGAAQQ
THLQVAGQSQ QFINRTPQRI STISSLMYEG EQEEIRANLG QSQPGTYRSA GSLDDDYYAP
GSGDRASRPI SPIKIPVVGA LDDSSPSENG NVRTTFTQRL QRGYKSLSEL RIKHIFAKQT
TVRRDNIEVD RYVEQYEREL KSEKLARERR DREIAENYDI KIKTLAGTRQ NTFDDDDVEH
EQFERGKISH ETDESGMEAT PPLPSRRKPG IAATRFAKVR KPPLEMEEEQ QQAAAEESPQ
ANPPPPPPPR PSSYKQLLIN KLPHLPSLPN LPQFSRTKEE TTKTAENADE NNASRKLSIR
QNIKRLRKSI KRPSKIKSKA AAPVPDSDEE EATPDGQKTK DAPTRSSTAN LRARLSRFAS
TEQLQQRWRK SFKVAKEPEE LETKAEGSAT GGASGVLGGL LVGSQLEKTL AKLNEKVHQL
KFFQRNANNQ NATTSKQPKP NTVGHEPIEI DDDELEATYH RSDSLEAENG NGNENDDSGE
DISAEEAFGQ IQEEDNEEDH SQDQTKRGQS SVSGIATAHA ARQMAKLAEI QAASKSGAAA
WSSESLEEIA DEDYPRVLIH QEHSDAYEST LIIAVASKGS SMSPVVRSSG LKSSPAAGPK
TSPHPEIRIS ASGPQKSMSY SPGNPRGEPV TKRSPSPEFK TPAGGNKIVP KSETSAWLPN
EQIIAGFKEQ TSWPAPALYK PKSIDIFEAS AGGSAAFADF DEALRNAPVL RISAGSSIDT
SGEEADDSCS RVTRIRVQSP QIGNSRESLM AQEEEDKEAE RDSEEEEEER DPSERPPSES
PPPPPLPQRR PPTKRPATPP IYDAVPPPLP VSKPPPPPSV ETIPSVASLP SPAPVTRSMA
QRSASMSRPA KPLVKTSSLR LTYNEQVRPG DVGKVNKLIS RFEGGRPRLC PRRMHSEEYE
RCAQPEDEEP EMEQILELQI IERRAVDSVT PTNRAVVIPQ ITVNNNNNNE RQLEQSDQSD
QSAHQEITDT RKTKSMELAL DRQNSNCSRS EYGSPLSFPS SRRSSTPTNL NANSNSNPNP
STNPNQNPSQ ILQHQRRSRR SMTRDDDNFY SFDSDEENSY YSISPSGSSR YVVEI
