LVA_DROME
ID LVA_DROME Reviewed; 2779 AA.
AC Q8MSS1; Q9W4N7;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 09-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Protein lava lamp;
GN Name=lva; ORFNames=CG6450;
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|EMBL:AAM50007.1};
RN [1] {ECO:0000305}
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 980-2779.
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 [4] {ECO:0000305}
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=11076973; DOI=10.1083/jcb.151.4.905;
RA Sisson J.C., Field C., Ventura R., Royou A., Sullivan W.;
RT "Lava lamp, a novel peripheral Golgi protein, is required for Drosophila
RT melanogaster cellularization.";
RL J. Cell Biol. 151:905-918(2000).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-35; SER-95; SER-98;
RP SER-122; SER-133; SER-186; SER-352 AND SER-354, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22493244; DOI=10.1073/pnas.1120320109;
RA Kim S., Naylor S.A., DiAntonio A.;
RT "Drosophila Golgi membrane protein Ema promotes autophagosomal growth and
RT function.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:E1072-E1081(2012).
CC -!- FUNCTION: Lva and spectrin may form a Golgi-based scaffold that
CC mediates interaction of Golgi bodies with microtubules and facilitates
CC Golgi-derived membrane secretion required for the formation of furrows
CC during cellularization (PubMed:11076973). Under starvation conditions
CC recruited by ema to developing autophagsosomes where it may function in
CC autophagosome growth (PubMed:22493244). {ECO:0000269|PubMed:11076973,
CC ECO:0000269|PubMed:22493244}.
CC -!- SUBUNIT: Interacts with CLIP-190 and spectrin separately.
CC {ECO:0000269|PubMed:11076973}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:11076973,
CC ECO:0000269|PubMed:18327897}. Cytoplasmic vesicle, autophagosome
CC {ECO:0000269|PubMed:22493244}. Note=Lva-alpha-spectrin and Lva-CLIP-190
CC complexes are found at the Golgi (PubMed:11076973). Upon autophagosome
CC induction by starvation, also detected in small vesicle structures
CC (PubMed:22493244). {ECO:0000269|PubMed:11076973,
CC ECO:0000269|PubMed:22493244}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM50007.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE014298; AAF45910.1; -; Genomic_DNA.
DR EMBL; AY118638; AAM50007.1; ALT_INIT; mRNA.
DR RefSeq; NP_001284849.1; NM_001297920.1.
DR RefSeq; NP_525064.1; NM_080325.4.
DR SMR; Q8MSS1; -.
DR BioGRID; 57868; 30.
DR DIP; DIP-17967N; -.
DR IntAct; Q8MSS1; 4.
DR MINT; Q8MSS1; -.
DR STRING; 7227.FBpp0070596; -.
DR iPTMnet; Q8MSS1; -.
DR PaxDb; Q8MSS1; -.
DR PRIDE; Q8MSS1; -.
DR EnsemblMetazoa; FBtr0070626; FBpp0070596; FBgn0029688.
DR EnsemblMetazoa; FBtr0342740; FBpp0309608; FBgn0029688.
DR GeneID; 31350; -.
DR KEGG; dme:Dmel_CG6450; -.
DR CTD; 31350; -.
DR FlyBase; FBgn0029688; lva.
DR VEuPathDB; VectorBase:FBgn0029688; -.
DR eggNOG; ENOG502S5D8; Eukaryota.
DR HOGENOM; CLU_226592_0_0_1; -.
DR InParanoid; Q8MSS1; -.
DR OMA; AINQQWE; -.
DR OrthoDB; 342745at2759; -.
DR PhylomeDB; Q8MSS1; -.
DR SignaLink; Q8MSS1; -.
DR BioGRID-ORCS; 31350; 0 hits in 1 CRISPR screen.
DR ChiTaRS; lva; fly.
DR GenomeRNAi; 31350; -.
DR PRO; PR:Q8MSS1; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0029688; Expressed in adult Malpighian tubule (Drosophila) and 29 other tissues.
DR ExpressionAtlas; Q8MSS1; baseline and differential.
DR Genevisible; Q8MSS1; DM.
DR GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000137; C:Golgi cis cisterna; IDA:FlyBase.
DR GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0030507; F:spectrin binding; TAS:FlyBase.
DR GO; GO:0007349; P:cellularization; IMP:UniProtKB.
DR GO; GO:0051683; P:establishment of Golgi localization; IMP:FlyBase.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; IMP:FlyBase.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasmic vesicle; Developmental protein; Golgi apparatus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..2779
FT /note="Protein lava lamp"
FT /id="PRO_0000084526"
FT REGION 31..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 110..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 622..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1716..1753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2348..2367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2484..2507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2552..2578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2633..2665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 52..85
FT /evidence="ECO:0000255"
FT COILED 141..175
FT /evidence="ECO:0000255"
FT COILED 220..607
FT /evidence="ECO:0000255"
FT COILED 659..716
FT /evidence="ECO:0000255"
FT COILED 751..1733
FT /evidence="ECO:0000255"
FT COILED 1785..1863
FT /evidence="ECO:0000255"
FT COILED 1941..2433
FT /evidence="ECO:0000255"
FT COILED 2504..2544
FT /evidence="ECO:0000255"
FT COILED 2600..2641
FT /evidence="ECO:0000255"
FT COMPBIAS 33..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1716..1744
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2556..2572
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2640..2665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 1211
FT /note="E -> K (in Ref. 3; AAM50007)"
FT /evidence="ECO:0000305"
FT CONFLICT 1424
FT /note="A -> S (in Ref. 3; AAM50007)"
FT /evidence="ECO:0000305"
FT CONFLICT 1506
FT /note="E -> D (in Ref. 3; AAM50007)"
FT /evidence="ECO:0000305"
FT CONFLICT 2034
FT /note="A -> V (in Ref. 3; AAM50007)"
FT /evidence="ECO:0000305"
FT CONFLICT 2069
FT /note="Q -> H (in Ref. 3; AAM50007)"
FT /evidence="ECO:0000305"
FT CONFLICT 2133
FT /note="G -> E (in Ref. 3; AAM50007)"
FT /evidence="ECO:0000305"
FT CONFLICT 2154
FT /note="Q -> E (in Ref. 3; AAM50007)"
FT /evidence="ECO:0000305"
FT CONFLICT 2160
FT /note="E -> V (in Ref. 3; AAM50007)"
FT /evidence="ECO:0000305"
FT CONFLICT 2200
FT /note="L -> P (in Ref. 3; AAM50007)"
FT /evidence="ECO:0000305"
FT CONFLICT 2217
FT /note="A -> T (in Ref. 3; AAM50007)"
FT /evidence="ECO:0000305"
FT CONFLICT 2271
FT /note="E -> D (in Ref. 3; AAM50007)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2779 AA; 315900 MW; 1CB3965102018AEE CRC64;
MAEDSGALES SYDFSIVQPD DHEYGEADIR LAGSSNDLSS LQNVSASTTR GTKGKGRLDS
LKENLYKQQE RLTALKERAL RKSQDERHKS SMSDSMESLK TLGQKLTVLK TRSGDSSTPL
VSPTKDSDPG DVSLLQTSGS EKLLMLTQRT EQNRALLEQR KRDLAKSLLS VKSNIGHQTT
AELGSSMTDL RHAASVSNPP VSRHRSALDL EAQGQEAVDE SRVKLLRSRM KLTELKQGRQ
EQELNELRTE LAKRAKLIER LELSGAELQR TLTQRNEELE QLRVVQAEED SLKVQENSRL
QGEVLVLRER LAELENVNDL LETTRCELQE ELTTARERQR NLELEQEQEK ASRSPQSEAA
HTDAQVSAEL AKQLQELTNQ LADLQATNEE LRQQVAAQAK LQVTDEIVSQ RLEELEATIA
AQLLELQEQK SAMAAQNEEL AEKTTELNVL NVNLRLLEEK LAQSSRSKPL FLEDHSEDSA
ASKQMQEDLQ QLKLKLDETN KANIKLKLKC KQAEKKLQKF QSQDGQQQLA SLLADNEELQ
QRIAVLEDEK GQWQLANMQE DDRQPEQSTE SNNPLQLETI RLLEEQKLEL QQALEALLSS
SSSAESIEIV ERHHLECLGQ RRPASEGDAQ EQKQVHPPGP SHVSELTQTE QTEEEDSSGE
TLSQLRERLE LFTQERGEVL DKLEQLSAEN LQLQARLEES SSSLQLLQRE REKDLISSTS
TSSNLSQELS SMQRSSEVVA TLDAGEGGPV LFEKCEKSLS KLNSELEAYR KANDRQAKFN
VSKKLAKEAK NCHTQLSELL HKVKEASTAV ETVTVVETVV AVTAPNGKAL AEYEQLNAQN
AELKAVISRL RQELDELRES YPETEAPLAI VGSDSQREDE ILQLQSQLED ARSLQAEQRQ
QIEEQVDQIK ELRQTEAEQL QLVARQSAEI TQLQLQSEQF DQLLNSKEMS HEKQLEQQTR
IRRELEARAE SLEGELSILQ TLVAEQKQQL IESVSESEHA LNLKMLELQS AQEELRELRA
KEDPDQLREA LRVSKSLVAQ QVRELTSSQE TVDALNQQIQ EYQGLEHAHK EEQFKNRELR
EKLKKYALNL KKRTQDNADL EQKVQELTSQ LQEQQELVKQ KEEVEREPIV DNHRVEQLQQ
QVSKLNEDLK AKIHLNLENR DALRQLKQQI QEQEQLIQER DAELQDANLV SKELRRERQE
ADQEVFQLGQ ENSRLREEIS KLQEEIHNLG QRVNEEPTAV EDLRRQLEAK SKKFEKSKEL
IKLRNATIQS LQRELQQLQQ DQDSEVEHVR NARAAHEQLR LEKDAEITAL RQEILKLERS
RAAGEGDDTI TKTSHQLLES QSQQQAESLQ VAERELQQLR VQLTAAQEQH ALLAQQYASD
KANFEMTIAR LETLHEGIQA KLQEDASYIE SLEAQNTELQ ARSAALEEQA ASQANQQAAS
QDKVQILEQQ LKEQREQEEQ KRQQDQQLQE RFYELGQREQ AQSRQLELLT SEAEESRQQL
AGLRTEYESL LAKHSQLTAT AQAEREQMSS HSQEELAELR QQLDVKEADL HRQRQVYDAK
LAAKATELDE LECDLNSHVE RAAAETRELC QQLERSQELV AQRTEELQRL NEEFQEVERE
RSTLSREVTL LRLQHDSAEQ DVLELQELRM QAMQDKTEMD NLRTQIDALC ANHSQELQAL
QQRIAELDTL GQNQTDDQVY IETENKRLAE QLSELQAQLA RQQHQQQQQQ HHHPAVQSQQ
HPPPASLFFG GDALAAPSPF DEIAQPLRVS SLAASAPPPI SPPPTIEDLQ RNVSDLEKHA
QDLETKLLAR NQNLAEQEER RLQLEQRLSE VERLLSERTQ QLADIQTANE ERDRLAALEK
LIQPAAAPTL DMFFGGQAEE TVPDAVSHHL DLGLPQTEPV VEPLIQPKKA YLCQPKQEIQ
EQTAQTIDWG VDEDPWASAA NEAPQTDVEH LHTRIAQLEL QLSNAEQQKT ELQTKAAKLM
KRLKEYKTKA TTTATPTVTV DNDLDSTIIE ELKHQLQLQE SRLSKAEEIS QQHALEKEKL
AKRIDVLTAG NDRMAEMKER QDMDVQMYQA RIRELQEKLS QLDQWGEPAA TVSSSLDGDE
AARIESLQQE IQQLRQQVSE LEDERTRDQA ELGALRQSSQ GYDEAEDNQK LELQQLRQQE
SELEALRTRD QSELEALRQS CQGHDETVRI ATLQQDNQQL ELQQLRQAII ELETLRARDQ
TELEALRQSS QGHDEAARIA IEQRDNQQLE LQQLRQQLIE LEALRARDQA ELEALRQSCQ
GQQLSVDMAS RNDEQMAQLQ EKESEIVHLK QRIEELMRED QTEKLVFEIL TKNQELQLLR
MQVKQLEEDK EDQQVSAAPP KDDGETVEKL KSLCQQLQQE KSDMEEELRV LNNHVLSSLE
LEDRMKQTLL QLDTKNIEIT ELRRSLEILQ SQNLGQNSAA EQIPDLSAIN QQWEQLVEQK
CGEVASIWQE HLSQREAAFK AQLEEVTQQQ QRELPQSQQS TQGEATSDIM QKMQKALETQ
EMEIVTLKEQ LAIRSAEYAR LAAQYDPFRL QNRGGASGGN PASTTVSAGG PPSLTANEPL
PEYVLKADLD YALMMLHQRD MRVEEMIVEL VQLLEERDHL QLKLSDTLRQ LETERSRVSD
EPSATASSSA ASSSSPSKIS SAGSNSELLG TTSAAGSDLK QKLAELQTVK HSKDKVIVDE
REQRLQQMLQ LQKDMAKQGS GSQSGAGAVA AVAAPTSAAP TAIGVDLSQS GLRSPSMMLM
DWILGNNNKE EEAGHQTTG
