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Protein mesh

 MESH_BOMMO              Reviewed;        1583 AA.
H9JIQ1;
16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
16-MAY-2012, sequence version 1.
25-OCT-2017, entry version 25.
RecName: Full=Protein mesh {ECO:0000303|PubMed:22854041};
Flags: Precursor;
Bombyx mori (Silk moth).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Lepidoptera; Glossata; Ditrysia;
Bombycoidea; Bombycidae; Bombycinae; Bombyx.
NCBI_TaxID=7091;
[1] {ECO:0000312|EnsemblMetazoa:BGIBMGA009402-TA}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=p50T {ECO:0000312|EnsemblMetazoa:BGIBMGA009402-TA};
PubMed=19121390; DOI=10.1016/j.ibmb.2008.11.004;
International Silkworm Genome Consortium;
"The genome of a lepidopteran model insect, the silkworm Bombyx
mori.";
Insect Biochem. Mol. Biol. 38:1036-1045(2008).
[2] {ECO:0000305}
IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
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).
-!- FUNCTION: May be required for the proper organization of smooth
septate junctions and for the barrier function of the midgut
epithelium. {ECO:0000250|UniProtKB:Q0KHY3}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
protein {ECO:0000255}. Cell junction, septate junction
{ECO:0000250|UniProtKB:Q0KHY3, ECO:0000255}. Lateral cell membrane
{ECO:0000269|PubMed:22854041}.
-!- TISSUE SPECIFICITY: In fifth instar larvae, expressed in midgut
epithelial cells (at protein level).
{ECO:0000269|PubMed:22854041}.
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SMR; H9JIQ1; -.
EnsemblMetazoa; BGIBMGA009402-RA; BGIBMGA009402-TA; BGIBMGA009402.
eggNOG; KOG4291; Eukaryota.
eggNOG; ENOG410YZ7Z; LUCA.
InParanoid; H9JIQ1; -.
OMA; VSFECNE; -.
Proteomes; UP000005204; Unassembled WGS sequence.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016328; C:lateral plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005918; C:septate junction; IEA:UniProtKB-SubCell.
GO; GO:0007160; P:cell-matrix adhesion; IEA:InterPro.
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;
Cell junction; Cell membrane; Complete proteome; Disulfide bond;
Membrane; Phosphoprotein; Reference proteome; Signal; Sushi;
Transmembrane; Transmembrane helix.
SIGNAL 1 21 {ECO:0000255}.
CHAIN 22 1583 Protein mesh. {ECO:0000255}.
/FTId=PRO_0000423947.
TOPO_DOM 22 1182 Extracellular. {ECO:0000255}.
TRANSMEM 1183 1203 Helical. {ECO:0000255}.
TOPO_DOM 1204 1472 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1473 1493 Helical. {ECO:0000255}.
TOPO_DOM 1494 1583 Extracellular. {ECO:0000255}.
DOMAIN 260 415 NIDO. {ECO:0000255|PROSITE-
ProRule:PRU00570}.
DOMAIN 647 798 AMOP. {ECO:0000255|PROSITE-
ProRule:PRU00347}.
DOMAIN 812 1054 VWFD. {ECO:0000255|PROSITE-
ProRule:PRU00580}.
DOMAIN 1110 1170 Sushi. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DISULFID 1112 1152 {ECO:0000250|UniProtKB:Q0KHY3}.
DISULFID 1138 1168 {ECO:0000250|UniProtKB:Q0KHY3}.
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


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