TIG_DROME
ID TIG_DROME Reviewed; 2188 AA.
AC Q9VMD9; Q23984; Q6NR23;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Tiggrin {ECO:0000312|EMBL:AAF52380.2};
DE Flags: Precursor;
GN Name=Tig {ECO:0000312|EMBL:AAF52380.2, ECO:0000312|FlyBase:FBgn0011722};
GN ORFNames=CG11527;
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] {ECO:0000305, ECO:0000312|EMBL:AAA56998.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-25 AND 1476-1483,
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=7924982; DOI=10.1242/dev.120.7.1747;
RA Fogerty F.J., Fessler L.I., Bunch T.A., Yaron Y., Parker C.G., Nelson R.E.,
RA Brower D.L., Gullberg D., Fessler J.H.;
RT "Tiggrin, a novel Drosophila extracellular matrix protein that functions as
RT a ligand for Drosophila alpha PS2 beta PS integrins.";
RL Development 120:1747-1758(1994).
RN [2] {ECO:0000312|EMBL:AAF52380.2}
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 [3] {ECO:0000312|EMBL:AAF52380.2}
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 [4] {ECO:0000312|EMBL:AAQ23578.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAQ23578.1}; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP 1889-ARG--ASP-1991.
RX PubMed=9521906; DOI=10.1242/dev.125.9.1679;
RA Bunch T.A., Graner M.W., Fessler L.I., Fessler J.H., Schneider K.D.,
RA Kerschen A., Choy L.P., Burgess B.W., Brower D.L.;
RT "The PS2 integrin ligand tiggrin is required for proper muscle function in
RT Drosophila.";
RL Development 125:1679-1689(1998).
RN [6] {ECO:0000305}
RP FUNCTION.
RX PubMed=9660786; DOI=10.1074/jbc.273.29.18235;
RA Graner M.W., Bunch T.A., Baumgartner S., Kerschen A., Brower D.L.;
RT "Splice variants of the Drosophila PS2 integrins differentially interact
RT with RGD-containing fragments of the extracellular proteins tiggrin, ten-m,
RT and D-laminin 2.";
RL J. Biol. Chem. 273:18235-18241(1998).
RN [7] {ECO:0000305}
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=11034900; DOI=10.1242/jcs.113.21.3715;
RA Martin-Bermudo M.D., Brown N.H.;
RT "The localized assembly of extracellular matrix integrin ligands requires
RT cell-cell contact.";
RL J. Cell Sci. 113:3715-3723(2000).
RN [8] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND GLYCOSYLATION BY PGANT3.
RX PubMed=18835818; DOI=10.1074/jbc.m804267200;
RA Zhang L., Zhang Y., Hagen K.G.;
RT "A mucin-type O-glycosyltransferase modulates cell adhesion during
RT Drosophila development.";
RL J. Biol. Chem. 283:34076-34086(2008).
RN [9] {ECO:0000305}
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP GLYCOSYLATION BY PGANT3.
RX PubMed=20371600; DOI=10.1074/jbc.m109.098145;
RA Zhang L., Tran D.T., Ten Hagen K.G.;
RT "An O-glycosyltransferase promotes cell adhesion during development by
RT influencing secretion of an extracellular matrix integrin ligand.";
RL J. Biol. Chem. 285:19491-19501(2010).
CC -!- FUNCTION: Functions as a ligand for integrin alpha-PS2/beta-PS.
CC Required in larvae for proper muscle structure and function. Involved
CC in the regulation of cell adhesion during wing development.
CC {ECO:0000269|PubMed:18835818, ECO:0000269|PubMed:7924982,
CC ECO:0000269|PubMed:9521906, ECO:0000269|PubMed:9660786}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:20371600, ECO:0000269|PubMed:7924982}.
CC Note=Localizes to the basal surface of the dorsoventral cell layer
CC interface during pupal wing development. {ECO:0000269|PubMed:20371600,
CC ECO:0000269|PubMed:7924982}.
CC -!- TISSUE SPECIFICITY: In embryos, expressed in the apodemes (muscle
CC attachment sites) of the major longitudinal muscles 4, 6, 7, 12 and 13
CC and the wide dorsal oblique muscles 9 and 10, in hemocytes, in fat body
CC cells, in basement membranes surrounding the gut and in the commissures
CC of the ventral nerve cord. Expressed in larval imaginal wing disk and
CC in pupal wing. In adult flies, expressed in the jump muscle (at protein
CC level). {ECO:0000269|PubMed:11034900, ECO:0000269|PubMed:18835818,
CC ECO:0000269|PubMed:20371600, ECO:0000269|PubMed:7924982,
CC ECO:0000269|PubMed:9521906}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout embryogenesis; first appears
CC at 8-10 hours. Detected in larval and pupal stages (at protein level).
CC Transcripts are first detected at 6-8 hours of development, expression
CC peaks at 12-14 hours and then declines by the end of embryogenesis.
CC {ECO:0000269|PubMed:20371600, ECO:0000269|PubMed:7924982}.
CC -!- PTM: O-glycosylation by pgant3 is required for proper secretion and
CC localization to the basal cell layer interface during wing development.
CC {ECO:0000269|PubMed:18835818, ECO:0000269|PubMed:20371600}.
CC -!- DISRUPTION PHENOTYPE: Pupal lethal with about 1% escapers. In mutant
CC larvae, muscles 6 and 7 appear stringy and not anchored to other
CC muscles or the epidermis, often these muscles are missing or
CC unrecognizable. Sites where muscles 3, 4, 5, 8 and 16 come together are
CC rarely recognizable and large gaps between muscles 9 and 10 can be
CC observed. Muscle contraction waves that transverse the length of the
CC larvae and are responsible for locomotion are much slower in mutant
CC larvae. Mutant pupae are longer than wild type pupae. Mutant adult
CC flies present elongated abdomen and wings with altered shapes and
CC sizes. {ECO:0000269|PubMed:11034900, ECO:0000269|PubMed:9521906}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ23578.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U09506; AAA56998.1; -; mRNA.
DR EMBL; AE014134; AAF52380.2; -; Genomic_DNA.
DR EMBL; BT010260; AAQ23578.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001285670.1; NM_001298741.1.
DR RefSeq; NP_477033.1; NM_057685.4.
DR AlphaFoldDB; Q9VMD9; -.
DR SMR; Q9VMD9; -.
DR BioGRID; 60053; 4.
DR IntAct; Q9VMD9; 12.
DR STRING; 7227.FBpp0078905; -.
DR PaxDb; Q9VMD9; -.
DR PRIDE; Q9VMD9; -.
DR EnsemblMetazoa; FBtr0079275; FBpp0078905; FBgn0011722.
DR EnsemblMetazoa; FBtr0343152; FBpp0309850; FBgn0011722.
DR GeneID; 33896; -.
DR KEGG; dme:Dmel_CG11527; -.
DR UCSC; CG11527-RA; d. melanogaster.
DR CTD; 33896; -.
DR FlyBase; FBgn0011722; Tig.
DR VEuPathDB; VectorBase:FBgn0011722; -.
DR eggNOG; ENOG502S4BN; Eukaryota.
DR HOGENOM; CLU_231371_0_0_1; -.
DR InParanoid; Q9VMD9; -.
DR OMA; KDREHMQ; -.
DR OrthoDB; 16764at2759; -.
DR PhylomeDB; Q9VMD9; -.
DR SignaLink; Q9VMD9; -.
DR BioGRID-ORCS; 33896; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 33896; -.
DR PRO; PR:Q9VMD9; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0011722; Expressed in embryonic/larval hemocyte (Drosophila) and 18 other tissues.
DR ExpressionAtlas; Q9VMD9; baseline and differential.
DR Genevisible; Q9VMD9; DM.
DR GO; GO:0005604; C:basement membrane; IDA:FlyBase.
DR GO; GO:0031012; C:extracellular matrix; IDA:FlyBase.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005178; F:integrin binding; IPI:FlyBase.
DR GO; GO:0007411; P:axon guidance; IMP:FlyBase.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IDA:FlyBase.
DR GO; GO:0031589; P:cell-substrate adhesion; IMP:FlyBase.
DR GO; GO:0072499; P:photoreceptor cell axon guidance; IMP:FlyBase.
DR GO; GO:0033628; P:regulation of cell adhesion mediated by integrin; IGI:FlyBase.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IDA:FlyBase.
DR InterPro; IPR016084; Haem_Oase-like_multi-hlx.
DR SUPFAM; SSF48613; SSF48613; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Developmental protein; Direct protein sequencing;
KW Extracellular matrix; Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:7924982"
FT CHAIN 19..2188
FT /note="Tiggrin"
FT /evidence="ECO:0000269|PubMed:7924982"
FT /id="PRO_5000144152"
FT REGION 1984..2188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 570..635
FT /evidence="ECO:0000255"
FT COILED 1009..1050
FT /evidence="ECO:0000255"
FT COILED 1312..1343
FT /evidence="ECO:0000255"
FT COILED 1613..1641
FT /evidence="ECO:0000255"
FT MOTIF 1989..1991
FT /note="Cell attachment site"
FT /evidence="ECO:0000269|PubMed:9521906,
FT ECO:0000269|PubMed:9660786"
FT COMPBIAS 1988..2012
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2014..2035
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2053..2080
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2112..2172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 1989..1991
FT /note="RGD->LGA: Partially rescues muscle function and
FT structure defects in the null mutant. Fails to interact
FT with alpha-PS2/beta-PS."
FT /evidence="ECO:0000269|PubMed:9521906"
FT CONFLICT 7
FT /note="I -> V (in Ref. 1; AAA56998)"
FT /evidence="ECO:0000305"
FT CONFLICT 77
FT /note="A -> G (in Ref. 1; AAA56998)"
FT /evidence="ECO:0000305"
FT CONFLICT 381
FT /note="E -> Q (in Ref. 1; AAA56998)"
FT /evidence="ECO:0000305"
FT CONFLICT 869
FT /note="N -> S (in Ref. 1; AAA56998)"
FT /evidence="ECO:0000305"
FT CONFLICT 2157..2158
FT /note="Missing (in Ref. 1; AAA56998)"
FT /evidence="ECO:0000305"
FT CONFLICT 2185
FT /note="E -> G (in Ref. 1; AAA56998)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2188 AA; 257446 MW; FFD4715696C33E9E CRC64;
MRALGGITLL LAVAICQGYE TYQRSSFRSS SSSSYGGGQT VPQLNSFASA HFNEVRELAN
QLKQKFNVLS QGSTNFAYTS PWSASILDLS GKSTLQLDQL SSEISRQLVQ DMREGITNYH
TIAQPNFFEA KAAELLERYS GAESASLQQT VGLGPYQPVD LSGFDEVKNY AYPAEVKVID
GKTYVVHRNC TEATKLSDYG SSGQLNSGFL GHQQTSLPLS STTTTITRKK TIHDWVRENM
EPSVVGYNSV VKLDGQLRNS ALNQMVPLSP GSNVVIHRFN KTITTNPDGT SSVGGSEWQQ
RWQDGKLVYD HQQPFGQSTI PRDEQWKREE RERLFWYLTT PQRLDDWQQQ QEERLLGVVQ
RYQVSLPVLK EFHRRELARY EALLGQYQSR VQDTSSWQRQ ERGRLDWLIH QNGFTVQDIE
RWQNENARKL AEAARQHGIS QNQLQQFQRE ELQRLYVHFN QVNESLAPQV PSVPQTTYNY
QSSSSLTEDN TKEQQRLEEL IRQHNATIAA LQNSIKTDQQ RLKNLSIKYQ GDMQSQTQWL
RGEVARIGDL IKEQNEQVSK ITAWQSSERS RLENILLQHR GSVEEVQQRI NMDRNYLQNL
ATKYQVSVEE LEKWQKEELE RLQVRGQQQL EEHIKDWQIS VSSNLRDIAT QNKLTIDEFQ
NYIINDRSHL EEMARLYKVK VEEIEQWIKS ELKKFQSEGL LKGVEQELIQ WQQKERERLQ
AIVQQNSLTV EQLEVRIKND QDHFFKLADK YKINVEDIQD WLKKELLRLQ SEGLVKAETL
KEWQQQERAQ ISLLVQQNKY SLDEFERKML ADRARLQELS NTYNVKVSEI EQWIKSEGDR
LQHEGQLRME SQLNNWQKIE RQRLLDLINK NNLSIEEIES KISKDQTHLY SLAQQHQVRV
EEIEQWIRQQ IQKLQDQGLI EMQKLKNWQL EWRGNLTNMV QDRDFTVEEF HKWLLKDREQ
LQSLAMQHNV QIEEIEQFVK KEEQRFIGMG LLKPSEKLTN WQEVERLHLK NLAQQQYKST
EQLEARLRQD RELLERLARQ YSVQVEEIES WMKQELARMR DEGQLQIDNL TSWQLAERER
LEALIKQNKQ WSAEELRAEL EKDREHMQTM AFQYHTSVEE IEKWLQSEIE RLKQQGKLNI
EQLTAWQRTE QQRILSLLQQ HSNITLEQFQ AKVHNDRRFL MNLAEQHHVH IEEVDNYVKQ
VIEDLRKNGQ FEIEQLQTWQ RVERDYIKSL ISEYKNSLST AEYEEKLLAD RAHLKHLADQ
YRINVEQIEE WMIAELKRLR GSTEETLKSL SAWQVSELER LQNLVKQQNH LTFVEFEMEL
NQERDRLQKL ANQYSVNVVE IEEWLRQQLI NLRTTGQAKV ENLSKWQVEE QQRLIEMLLK
KQQEMPYEQV ERELTQDHAR LQSLSQTHHV DIDHVDHWLR EELRRLQSSG LVQIEQQTQW
QQKISNGFNN WLEQQRNGAS YQDFVDFLKR DKQRMDGIAT DYHVTVEQVE KWVQKEAARL
SLIGVIERPE NNLKYEDISN IWVGDQTDSW KNELVTRLRS VTRQRPFTRQ EFESYLIRNK
PIFEQIARQY HVTIEDIHLW LDQSAKNEGL VTTEWQAKER LHIDNLINQQ LRKQQRWTIE
ELELRLNNDQ KHLQDAVAQY HVTVEELKVW YKDELNRLLE QRRIDRGSGI SWQNIESQRI
YLAIVNNPGI SRQALENRLF RDVHVRASQY QITVEELRQF ILSQLRRFSD MGLIVDNGRQ
ANNWHDQERK RLREVVKGVV ITEQELLDFI SQDTSFQTQL AQSYQVGLEQ LAPVQRIFIG
NLAREQLLEQ RRLNHLTTWQ QRERDRLYEF IGNQNMTQTE LKTWQIQDSK LLAEFAKRYE
ISVQQLSDWQ KKELARINQL ARYYGMSQSD LQQFREGELR QLAYINHRQL LSAAEAQKWE
KRHQWTLSRL QSRYGKFGQE LVAWRRTLYL LSQGLIDLPA DSGSNGGYVV DAGSTNATAV
YKPIFSKDRG DQPPHTYDES FVEGDEPGLE GETARPRPPN PAPIVSTPKP PLPYSRGGPS
GGFEYRRQDY TFNVPVGSAS ASASGGPTGS SASASASLGK WNRASGDEPL QQEVDLGQQQ
QIEELGWNEK LEDLGQQTQV EDTDWNQQAE DLGQQQQVQV EDDLHFDQTQ GHSSSSNSRS
QPLQQATKVE VEATSEPSFW EKLKEKLG
