INSIG_MYCVP
ID INSIG_MYCVP Reviewed; 204 AA.
AC A1T557;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=INSIG protein homolog {ECO:0000303|PubMed:26160948};
DE Short=MvINS {ECO:0000303|PubMed:26160948};
GN OrderedLocusNames=Mvan_1475 {ECO:0000312|EMBL:ABM12307.1};
OS Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350058;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC PYR-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Anderson I.J., Miller C., Richardson P.;
RT "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007744|PDB:4XU4, ECO:0007744|PDB:4XU5, ECO:0007744|PDB:4XU6}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH DIACYLGLYCEROL,
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=26160948; DOI=10.1126/science.aab1091;
RA Ren R., Zhou X., He Y., Ke M., Wu J., Liu X., Yan C., Wu Y., Gong X.,
RA Lei X., Yan S.F., Radhakrishnan A., Yan N.;
RT "Crystal structure of a mycobacterial Insig homolog provides insight into
RT how these sensors monitor sterol levels.";
RL Science 349:187-191(2015).
CC -!- FUNCTION: Diacylglycerol-binding protein.
CC {ECO:0000269|PubMed:26160948}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:26160948}.
CC -!- INTERACTION:
CC A1T557; A1T557: Mvan_1475; NbExp=3; IntAct=EBI-16163958, EBI-16163958;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:26160948}; Multi-
CC pass membrane protein {ECO:0000269|PubMed:26160948}.
CC -!- DOMAIN: The KxHxx motif mediates association with the coatomer complex.
CC {ECO:0000250|UniProtKB:Q9Y5U4}.
CC -!- SIMILARITY: Belongs to the INSIG family. {ECO:0000305}.
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DR EMBL; CP000511; ABM12307.1; -; Genomic_DNA.
DR RefSeq; WP_011778733.1; NC_008726.1.
DR PDB; 4XU4; X-ray; 1.90 A; A=1-204.
DR PDB; 4XU5; X-ray; 2.10 A; A=1-204.
DR PDB; 4XU6; X-ray; 1.90 A; A=1-204.
DR PDBsum; 4XU4; -.
DR PDBsum; 4XU5; -.
DR PDBsum; 4XU6; -.
DR AlphaFoldDB; A1T557; -.
DR SMR; A1T557; -.
DR DIP; DIP-61665N; -.
DR STRING; 350058.Mvan_1475; -.
DR EnsemblBacteria; ABM12307; ABM12307; Mvan_1475.
DR KEGG; mva:Mvan_1475; -.
DR eggNOG; ENOG5031FRC; Bacteria.
DR HOGENOM; CLU_1407438_0_0_11; -.
DR OMA; DHSHVVT; -.
DR OrthoDB; 1586171at2; -.
DR Proteomes; UP000009159; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW 3D-structure; Lipid-binding; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..204
FT /note="INSIG protein homolog"
FT /id="PRO_0000450693"
FT TRANSMEM 5..27
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:26160948,
FT ECO:0007744|PDB:4XU4, ECO:0007744|PDB:4XU5,
FT ECO:0007744|PDB:4XU6"
FT TRANSMEM 47..64
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:26160948,
FT ECO:0007744|PDB:4XU4, ECO:0007744|PDB:4XU5,
FT ECO:0007744|PDB:4XU6"
FT TRANSMEM 76..97
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:26160948,
FT ECO:0007744|PDB:4XU4, ECO:0007744|PDB:4XU5,
FT ECO:0007744|PDB:4XU6"
FT TRANSMEM 101..118
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:26160948,
FT ECO:0007744|PDB:4XU4, ECO:0007744|PDB:4XU5,
FT ECO:0007744|PDB:4XU6"
FT TRANSMEM 124..145
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:26160948,
FT ECO:0007744|PDB:4XU4, ECO:0007744|PDB:4XU5,
FT ECO:0007744|PDB:4XU6"
FT TRANSMEM 162..179
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:26160948,
FT ECO:0007744|PDB:4XU4, ECO:0007744|PDB:4XU5,
FT ECO:0007744|PDB:4XU6"
FT BINDING 26
FT /ligand="a 1,2-diacyl-sn-glycerol"
FT /ligand_id="ChEBI:CHEBI:17815"
FT /evidence="ECO:0000269|PubMed:26160948,
FT ECO:0007744|PDB:4XU5"
FT BINDING 150
FT /ligand="a 1,2-diacyl-sn-glycerol"
FT /ligand_id="ChEBI:CHEBI:17815"
FT /evidence="ECO:0000269|PubMed:26160948,
FT ECO:0007744|PDB:4XU5"
FT HELIX 5..28
FT /evidence="ECO:0007829|PDB:4XU6"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:4XU6"
FT HELIX 48..64
FT /evidence="ECO:0007829|PDB:4XU6"
FT HELIX 76..96
FT /evidence="ECO:0007829|PDB:4XU6"
FT HELIX 101..119
FT /evidence="ECO:0007829|PDB:4XU6"
FT HELIX 122..144
FT /evidence="ECO:0007829|PDB:4XU6"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:4XU6"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:4XU6"
FT HELIX 164..184
FT /evidence="ECO:0007829|PDB:4XU6"
SQ SEQUENCE 204 AA; 20710 MW; 94A82D1E31C18345 CRC64;
MRLRISEAVV LFLLGAVAAL IGDHSHVVTG TTVYHTDAVP FVWSSPFWFP ILVGAATASL
AELRLHLPAP RDGVTARQAL GGVAAVVGTY VTTALVHAFP VVPVTALVCA AAAITWCVLG
DGPGAACGVV IAVIGPAVEI ALVQLGVFAY HPDSDGLFGV APFLAPLYFA FGVVAALLGE
LAVARRPQLG PPVCDTVSRG PGAG
