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Protein mesh

 MESH_DROME              Reviewed;        1454 AA.
Q0KHY3; B3DNA3; E1JJ26; E1JJ27; E2QD49; Q6NND0; Q8MR59;
16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
16-OCT-2013, sequence version 2.
23-MAY-2018, entry version 99.
RecName: Full=Protein mesh;
Flags: Precursor;
Name=mesh; ORFNames=CG31004;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
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.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[2]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=Berkeley; TISSUE=Embryo;
Stapleton M., Carlson J.W., Booth B., Chavez C., Frise E.,
George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M.,
Celniker S.E.;
Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 217-1431 (ISOFORM 1).
STRAIN=Berkeley; TISSUE=Head;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
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.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[5]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-888, AND IDENTIFICATION BY
MASS SPECTROMETRY.
STRAIN=Oregon-R; TISSUE=Head;
PubMed=17893096; DOI=10.1093/glycob/cwm097;
Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,
Panin V.;
"Identification of N-glycosylated proteins from the central nervous
system of Drosophila melanogaster.";
Glycobiology 17:1388-1403(2007).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1249; THR-1251;
SER-1254; THR-1295 AND SER-1297, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Embryo;
PubMed=18327897; DOI=10.1021/pr700696a;
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
[7]
FUNCTION, INTERACTION WITH SSK, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
PubMed=22854041; DOI=10.1242/jcs.112243;
Izumi Y., Yanagihashi Y., Furuse M.;
"A novel protein complex, Mesh-Ssk, is required for septate junction
formation in the Drosophila midgut.";
J. Cell Sci. 125:4923-4933(2012).
[8]
FUNCTION, IDENTIFICATION IN A COMPLEX WITH SSK AND TSP2A, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
PubMed=26848177; DOI=10.1242/jcs.180448;
Izumi Y., Motoishi M., Furuse K., Furuse M.;
"A tetraspanin regulates septate junction formation in Drosophila
midgut.";
J. Cell Sci. 129:1155-1164(2016).
-!- FUNCTION: Required, together with Ssk and Tsp2A, for the proper
organization of smooth septate junctions (sSJs), probably by
mediating cell adhesion via its homophilic interaction
(PubMed:22854041, PubMed:26848177). Also required for the correct
subcellular localization of several sSJ components, such as Ssk,
cora and l(2)gl, and for the barrier function of the midgut
epithelium (PubMed:22854041). Required for maintaining the three-
layered structure of the proventriculus (PubMed:22854041).
{ECO:0000269|PubMed:22854041}.
-!- SUBUNIT: Forms a complex with Ssk and Tsp2A (PubMed:26848177).
Interacts with Ssk; the interaction may be necessary for the
localization of both proteins to the cell apicolateral region
(PubMed:22854041). {ECO:0000269|PubMed:22854041,
ECO:0000269|PubMed:26848177}.
-!- SUBCELLULAR LOCATION: Cell junction, septate junction
{ECO:0000269|PubMed:22854041, ECO:0000269|PubMed:26848177}.
Apicolateral cell membrane {ECO:0000269|PubMed:22854041,
ECO:0000269|PubMed:26848177}; Single-pass type I membrane protein
{ECO:0000269|PubMed:22854041}. Note=Colocalizes with Ssk, cora,
dlg1, l(2)gl and Fas3 at the apicolateral region of epithelial
cells in the midgut. Also localizes to the apicolateral region of
epithelial cells in the outer epithelial layer of the
proventriculus and Malpighian tubules.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=3; Synonyms=D;
IsoId=Q0KHY3-3; Sequence=Displayed;
Note=No experimental confirmation available.;
Name=1; Synonyms=B;
IsoId=Q0KHY3-1; Sequence=VSP_053282;
Name=2; Synonyms=C;
IsoId=Q0KHY3-2; Sequence=VSP_035956;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: At embryonic stage 12, expressed in endoderm-
derived tissues (at protein level) (PubMed:22854041). In late-
stage embryos, third-instar larvae and adult flies, expressed in
the midgut, outer epithelial layer of the proventriculus and
Malpighian tubules, but not expressed in the foregut and hindgut
(at protein level) (PubMed:22854041, PubMed:26848177).
{ECO:0000269|PubMed:22854041, ECO:0000269|PubMed:26848177}.
-!- DEVELOPMENTAL STAGE: Expressed throughout embryonic, larval and
adult stages (at protein level). {ECO:0000269|PubMed:22854041}.
-!- DISRUPTION PHENOTYPE: Homozygous larval lethal. Mutant embryos
hatch into the first instar larvae, but die within 1 day. In
mutant larvae midgut, a few septa are present at the cell contacts
but large gaps between the lateral membranes of adjacent
epithelial cells are frequently observed. Mutant larvae lack the
three-layered structure of the proventriculus.
{ECO:0000269|PubMed:22854041}.
-!- SEQUENCE CAUTION:
Sequence=AAM52621.1; Type=Frameshift; Positions=547; Evidence={ECO:0000305};
Sequence=AAR96152.1; Type=Frameshift; Positions=1224, 1226; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AE014297; AAF57124.2; -; Genomic_DNA.
EMBL; AE014297; ACZ95074.1; -; Genomic_DNA.
EMBL; AE014297; ACZ95075.1; -; Genomic_DNA.
EMBL; AE014297; AAF57123.2; -; Genomic_DNA.
EMBL; BT032891; ACD99455.1; -; mRNA.
EMBL; BT133164; AEZ02857.1; -; mRNA.
EMBL; BT011360; AAR96152.1; ALT_FRAME; mRNA.
EMBL; AY122109; AAM52621.1; ALT_FRAME; mRNA.
RefSeq; NP_001163781.1; NM_001170310.1. [Q0KHY3-2]
RefSeq; NP_001163782.1; NM_001170311.1. [Q0KHY3-3]
RefSeq; NP_001287618.1; NM_001300689.1. [Q0KHY3-2]
RefSeq; NP_733418.1; NM_170539.1. [Q0KHY3-1]
RefSeq; NP_733419.1; NM_170540.1. [Q0KHY3-1]
UniGene; Dm.10424; -.
ProteinModelPortal; Q0KHY3; -.
SMR; Q0KHY3; -.
BioGrid; 68533; 2.
IntAct; Q0KHY3; 1.
STRING; 7227.FBpp0290183; -.
iPTMnet; Q0KHY3; -.
PaxDb; Q0KHY3; -.
PRIDE; Q0KHY3; -.
EnsemblMetazoa; FBtr0085779; FBpp0085140; FBgn0051004. [Q0KHY3-1]
EnsemblMetazoa; FBtr0085780; FBpp0085141; FBgn0051004. [Q0KHY3-1]
EnsemblMetazoa; FBtr0300960; FBpp0290182; FBgn0051004. [Q0KHY3-2]
EnsemblMetazoa; FBtr0300961; FBpp0290183; FBgn0051004. [Q0KHY3-3]
EnsemblMetazoa; FBtr0344066; FBpp0310483; FBgn0051004. [Q0KHY3-2]
GeneID; 43688; -.
KEGG; dme:Dmel_CG31004; -.
UCSC; CG31004-RA; d. melanogaster. [Q0KHY3-3]
UCSC; CG31004-RB; d. melanogaster.
CTD; 43688; -.
FlyBase; FBgn0051004; mesh.
eggNOG; KOG4291; Eukaryota.
eggNOG; ENOG410YZ7Z; LUCA.
GeneTree; ENSGT00730000110943; -.
InParanoid; Q0KHY3; -.
OMA; MSSYYAN; -.
OrthoDB; EOG091G01S5; -.
PhylomeDB; Q0KHY3; -.
Reactome; R-DME-913709; O-linked glycosylation of mucins.
Reactome; R-DME-977068; Termination of O-glycan biosynthesis.
GenomeRNAi; 43688; -.
PRO; PR:Q0KHY3; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0051004; -.
ExpressionAtlas; Q0KHY3; baseline and differential.
Genevisible; Q0KHY3; DM.
GO; GO:0016327; C:apicolateral plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005920; C:smooth septate junction; IDA:FlyBase.
GO; GO:0007160; P:cell-matrix adhesion; IEA:InterPro.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
GO; GO:0090528; P:smooth septate junction assembly; IMP:FlyBase.
CDD; cd00033; CCP; 1.
Gene3D; 2.60.40.10; -; 1.
InterPro; IPR005533; AMOP_dom.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR003886; NIDO_dom.
InterPro; IPR035976; Sushi/SCR/CCP_sf.
InterPro; IPR000436; Sushi_SCR_CCP_dom.
InterPro; IPR001846; VWF_type-D.
Pfam; PF03782; AMOP; 1.
Pfam; PF06119; NIDO; 1.
Pfam; PF00084; Sushi; 1.
Pfam; PF00094; VWD; 1.
SMART; SM00723; AMOP; 1.
SMART; SM00032; CCP; 1.
SMART; SM00539; NIDO; 1.
SMART; SM00216; VWD; 1.
SUPFAM; SSF57535; SSF57535; 1.
SUPFAM; SSF81296; SSF81296; 1.
PROSITE; PS50856; AMOP; 1.
PROSITE; PS51220; NIDO; 1.
PROSITE; PS50923; SUSHI; 1.
PROSITE; PS51233; VWFD; 1.
1: Evidence at protein level;
Alternative splicing; Cell adhesion; Cell junction; Cell membrane;
Complete proteome; Developmental protein; Disulfide bond;
Glycoprotein; Membrane; Phosphoprotein; Reference proteome; Signal;
Sushi; Transmembrane; Transmembrane helix.
SIGNAL 1 21 {ECO:0000255}.
CHAIN 22 1454 Protein mesh.
/FTId=PRO_0000355637.
TOPO_DOM 22 1186 Extracellular. {ECO:0000255}.
TRANSMEM 1187 1207 Helical. {ECO:0000255}.
TOPO_DOM 1208 1454 Cytoplasmic. {ECO:0000255}.
DOMAIN 259 425 NIDO. {ECO:0000255|PROSITE-
ProRule:PRU00570}.
DOMAIN 656 807 AMOP. {ECO:0000255|PROSITE-
ProRule:PRU00347}.
DOMAIN 821 1052 VWFD. {ECO:0000255|PROSITE-
ProRule:PRU00580}.
DOMAIN 1119 1179 Sushi. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
MOD_RES 1249 1249 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 1251 1251 Phosphothreonine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 1254 1254 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 1295 1295 Phosphothreonine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 1297 1297 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
CARBOHYD 24 24 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 208 208 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 320 320 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 386 386 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 458 458 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 554 554 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 620 620 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 888 888 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17893096}.
CARBOHYD 942 942 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 977 977 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 985 985 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1048 1048 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1066 1066 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 1121 1161 {ECO:0000250}.
DISULFID 1147 1177 {ECO:0000250}.
VAR_SEQ 1180 1454 EVYYTRRVAFIAIGIIFLVICPLMLCIVCGVYRYRQKQLKE
DPQWQMPMLPRSRASSARNLRTLNYDDDSDTDASTLKKSRS
YDKVYRTNEPLPGKPQIDFPAKKWDLDENDEDVTSSEGEKP
KQLGRRSLHSASGTELDQHGSPVDGDHPDEDDDFDEADVHT
GTTHPVGYHQPLSPEEADQLHRQQYSPTFSGLDSRTSGASS
INYTPQAATQNRFGGVPVLPSNTQYYSRPPSSVNTVPLRTA
PTPLTQDTGLPSPPLATSPTPSVQKSTEV -> HEERSARV
ASISLGMVLLILIPCLLLLVCGASYWIRERIAREEEEAAQA
LLPKSKWQQSKQHVI (in isoform 2).
{ECO:0000303|Ref.3}.
/FTId=VSP_035956.
VAR_SEQ 1259 1282 SRSYDKVYRTNEPLPGKPQIDFPA -> T (in isoform
1). {ECO:0000303|PubMed:12537569,
ECO:0000303|Ref.3}.
/FTId=VSP_053282.
CONFLICT 686 686 C -> Y (in Ref. 4; AAM52621).
{ECO:0000305}.
SEQUENCE 1454 AA; 165038 MW; 2C8C1239C69EA6F8 CRC64;
MRFKLFVVCA LACGFMAFVL ANENISTEEF EDQIINAVPE PVKVTKPKAQ AEFVEVPKAT
PAPKKAEADN PKTKPLALQK PTLIPVVHVS SRGTDDILTV AGLKPEKMFG ALIMPNDYLG
ELYDVDNSGY NWDPNNNVAP PTTYSTAAGG YTITAARLAE LRSNFMYWYF DKDMYGGRGD
YQFDIHASMT QLHKNLNFQL PFYGFRFNYT RLSLNGYLEF SDPPEYLTYP LVFPIKDWPA
KRDPSFMGIF FSKCRVGRIY PSDIDQRTPG VYFRVERDLM GRTDRFGVEV RERTMWDIRQ
GVVGADTFIP KHVVIATWKN VSFAGGIDNS LYTTNTFQMV LATDEVYTYI IFNYAVLNWL
SHTEAGGDTT KGEGGVPAYV GFNAGNGTQA YEYNPYSQNM VIRDLANRGW ANGFPGRHIF
RVDEQILIGS CNKDIDAALL PLTFAPESGN MLGGQVVNIT GPCFDPAIRV TCHFDTESVL
GTYVDRNRVI CVQPYLKAEG YIRFQISVGT QRFKWRGKYF VETPAAATEK IFFTTDDVHK
KNPAEIRITW NQYNLTSNAN ANVMISLWGY RETKIEPQLE YIDVIEASYS NSGSYVITPS
NYINRNNINR DMQFGFLQIN LTQPDQYSGL AISPVLWSRP IPLAWYMAPQ WERQHGKRWA
RALCDNWIRA DRFLRNFAAD LPLCPCTLDQ AVLDKGRFRP DRECDKDSNP SCLRHRGAIH
CVVSGTPVAQ GAEQQCCYDR YGFLMLTYDQ MWGSRPRRVH NLGKMPWNEA SKVPSLSMWF
HDMRPFYSCC YWQEEQAVGC ETYRFERRPS QDCVAYQAPG IAGVFGDPHF VTFDGTAYTF
NGLGEFVLAR SVDESNKFEV QGRFEQLPVN YYGEVKATQL TAVAMRGNTT TTIEVRLRPL
HARWRYRLDV LADGRRVYFD RESLKFQHFD GVTVYTPTYL LNQSQVVVQF DAGIGVEVVE
NEGYMTGRVF LPWKFINKTA GLFGNWSFNK LDDFMLPNGQ VAQLNLNDLR SIHTNFGIKW
MLTDREVPGV GAALFKREFG RMSGYYANAT FQPNYVLDPA DFLPANRSYD LERAEELCGE
CMQCQYDYAM TLNRDLAHFT KNYYDTIVNM QAENAVRVVS CGVLQTPRFG RKLSFDFMPG
AKVSFECNEG FILIGDQRRE CLSNGLWNIP EYGYTECLRE VYYTRRVAFI AIGIIFLVIC
PLMLCIVCGV YRYRQKQLKE DPQWQMPMLP RSRASSARNL RTLNYDDDSD TDASTLKKSR
SYDKVYRTNE PLPGKPQIDF PAKKWDLDEN DEDVTSSEGE KPKQLGRRSL HSASGTELDQ
HGSPVDGDHP DEDDDFDEAD VHTGTTHPVG YHQPLSPEEA DQLHRQQYSP TFSGLDSRTS
GASSINYTPQ AATQNRFGGV PVLPSNTQYY SRPPSSVNTV PLRTAPTPLT QDTGLPSPPL
ATSPTPSVQK STEV


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