ID   MESH_BOMMO              Reviewed;        1583 AA.
AC   H9JIQ1;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2012, sequence version 1.
DT   25-MAY-2022, entry version 38.
DE   RecName: Full=Protein mesh {ECO:0000303|PubMed:22854041};
DE   Flags: Precursor;
OS   Bombyx mori (Silk moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Bombycidae; Bombycinae; Bombyx.
OX   NCBI_TaxID=7091;
RN   [1] {ECO:0000312|EnsemblMetazoa:BGIBMGA009402-TA}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=p50T {ECO:0000312|EnsemblMetazoa:BGIBMGA009402-TA};
RX   PubMed=19121390; DOI=10.1016/j.ibmb.2008.11.004;
RG   International Silkworm Genome Consortium;
RT   "The genome of a lepidopteran model insect, the silkworm Bombyx mori.";
RL   Insect Biochem. Mol. Biol. 38:1036-1045(2008).
RN   [2] {ECO:0000305}
RP   IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=22854041; DOI=10.1242/jcs.112243;
RA   Izumi Y., Yanagihashi Y., Furuse M.;
RT   "A novel protein complex, Mesh-Ssk, is required for septate junction
RT   formation in the Drosophila midgut.";
RL   J. Cell Sci. 125:4923-4933(2012).
CC   -!- FUNCTION: May be required for the proper organization of smooth septate
CC       junctions and for the barrier function of the midgut epithelium.
CC       {ECO:0000250|UniProtKB:Q0KHY3}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}. Cell junction, septate junction
CC       {ECO:0000250|UniProtKB:Q0KHY3, ECO:0000255}. Lateral cell membrane
CC       {ECO:0000269|PubMed:22854041}.
CC   -!- TISSUE SPECIFICITY: In fifth instar larvae, expressed in midgut
CC       epithelial cells (at protein level). {ECO:0000269|PubMed:22854041}.
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DR   AlphaFoldDB; H9JIQ1; -.
DR   STRING; 7091.BGIBMGA009402-TA; -.
DR   EnsemblMetazoa; BGIBMGA009402-RA; BGIBMGA009402-TA; BGIBMGA009402.
DR   eggNOG; KOG4291; Eukaryota.
DR   HOGENOM; CLU_003648_1_0_1; -.
DR   InParanoid; H9JIQ1; -.
DR   OMA; VHERYPP; -.
DR   Proteomes; UP000005204; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016328; C:lateral plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005918; C:septate junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0007160; P:cell-matrix adhesion; IEA:InterPro.
DR   CDD; cd00033; CCP; 1.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR005533; AMOP_dom.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR003886; NIDO_dom.
DR   InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR   InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR   InterPro; IPR001846; VWF_type-D.
DR   Pfam; PF03782; AMOP; 1.
DR   Pfam; PF06119; NIDO; 1.
DR   Pfam; PF00084; Sushi; 1.
DR   Pfam; PF00094; VWD; 1.
DR   SMART; SM00723; AMOP; 1.
DR   SMART; SM00032; CCP; 1.
DR   SMART; SM00539; NIDO; 1.
DR   SMART; SM00216; VWD; 1.
DR   SUPFAM; SSF57535; SSF57535; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
DR   PROSITE; PS50856; AMOP; 1.
DR   PROSITE; PS51220; NIDO; 1.
DR   PROSITE; PS50923; SUSHI; 1.
DR   PROSITE; PS51233; VWFD; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Cell membrane; Disulfide bond; Membrane; Phosphoprotein;
KW   Reference proteome; Signal; Sushi; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..1583
FT                   /note="Protein mesh"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000423947"
FT   TOPO_DOM        22..1182
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1183..1203
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1204..1472
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1473..1493
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1494..1583
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          260..415
FT                   /note="NIDO"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00570"
FT   DOMAIN          647..798
FT                   /note="AMOP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00347"
FT   DOMAIN          811..1019
FT                   /note="VWFD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   DOMAIN          1110..1170
FT                   /note="Sushi"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   REGION          1232..1448
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1521..1583
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1232..1255
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1293..1315
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1341..1363
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1370..1388
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1404..1439
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1521..1543
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        1112..1152
FT                   /evidence="ECO:0000250|UniProtKB:Q0KHY3"
FT   DISULFID        1138..1168
FT                   /evidence="ECO:0000250|UniProtKB:Q0KHY3"
SQ   SEQUENCE   1583 AA;  180588 MW;  A8EF77955E425EEC CRC64;
     MGVKIKLVLA VVLILSANVL GQDEIVNDTE STVSVTEAQV VELETDVKEK EDETFEETSP
     VELLPDTENL EVRSGKYQLN DGLVGEEPVN LEAVDFNSNN VESEKQLLSP PSTTVVTGTD
     YSYIDGRVLP ATTYQNNGQP YVITTQRLQQ IRSNFMYWFY DQGGSDNIGD YQRDIHTSTP
     QIHKNFNFQL PFFGFRFNYT RISMNGYIYF SDPPDHYTYP LSFPVRDWPN INDPSFIGIF
     FSKCRIGNMR PEEPDPRRPG IYFRLDRDLQ TRTDQLGVEM RERVTWDIRE GVIGSETFFP
     KHTITITWKN MSFAGGIDNS LFMTNTFQMV LATDEVFTYA IFNYLEINWS SHTEAGGDTT
     TGEGGIPAYI GFNAGNGTRS YEYKPYSQAS VLRDLTGRGW ANGFPGRHIF RIDENILMGT
     CNKDIDGANL PLMFAPESGN MLGGTIVNIT GPCFNPNDRI TCRFDTESVL GAVVDVNRAI
     CVQPRFWHNG YARFEVAINN EPYKWKGRYF VETPATATEK IFFPDNSVHE RYPPEVRITW
     DRFNLTTNLN VQLQISLWGY KEVTIRPQLE YIDMIEVGVA NTGEYVINPQ NFRNRENIMH
     NDMQFGFLQI NLTTPEVFKG VPISPILWSR PIPLGWYFAP QWERLHGQRW SNSMCNNWLR
     TDRFLKNFAA QVWVCPCTLE HALLDKGRFM PDLDCDRDTN PTCRYHWGGI HCVRSGAPSS
     EGSGQQCCYD KNGFLMLSYD QMWGSKPSRS HDFGFTPYNE ANKVPSLSRW FHDMIPFYQC
     CLWQEEQAVG CETFRFERRP SQDCVAYQSP GVAGIFGDPH IVTFDDLQYT FNGKGEYVLV
     RVDHSQLKLD VQGRFEQVPR NIHGAVNATH LTSVVAASNN SQTIEVRLRP QHAQWRYRLD
     VFANGKRVYF DRTALRVQYF PGVTVYQPMY VLNQSEIVVM FSSGAGLEVV ENRGFMTARV
     YLPWTFMNQT RGLFGNWSLD VNDDFTRPDG TLASVDLNNF QSAHRDFAQH WQLTDREQRD
     IGVAMFVREY GRTAAYYNDN EFIPNFIREP ANFLPVNRSH DVTRAIEICQ DSYQCRYDYG
     MTLNRDMAEF TKNYLSSITN IKEQNARRVI SCGILETPRF GRKSNFFFTP GTRVNFECNQ
     DFILTGDKRR VCEDNGRWNL PDYGYTECLR QQEFSQRALF LTWGVIVAVI LPLGLLICLL
     WFWCWHKPRS EGKEGFRFED LPRSKSASRL NLRSSSMGNI TDTMKSSTIP GSEKKSPETP
     TEETPARIVG RSVLAPPADG DSSGIGYPDS GKSDSGKSDK SSGLPKKRRA YDKTYRTNEP
     LPNAPDVEFP EKLWDLSEED LLSLTSPSDS ESNRDSTLTR PAKDIQYLNK PRQTGRQAIP
     SDSGYSTKEG SEDPYAPKFD DQYSPIPSQY SPTYSEIYSP PISPASDSSP RNTYNNPGIP
     EAPKSAPVDG IKTFTMPTNK GKQEYSSRTL GATWGIISAV MLPIIIILIC VAWRILQRRK
     AEEREENEFL DVKTRAIDPD DSVKVTSDDE SIPYKKDVTE ETPEPTEGVQ AVEPSNPNYN
     YGRPYVDLQP GQPRQWGGET EIN