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Database: UniProt
Entry: A0A3Q3FX38_KRYMA
LinkDB: A0A3Q3FX38_KRYMA
Original site: A0A3Q3FX38_KRYMA 
ID   A0A3Q3FX38_KRYMA        Unreviewed;       222 AA.
AC   A0A3Q3FX38;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   18-JUN-2025, entry version 31.
DE   RecName: Full=Insulin-induced gene protein {ECO:0000256|RuleBase:RU241113};
OS   Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX   NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000016852.1, ECO:0000313|Proteomes:UP000264800};
RN   [1] {ECO:0000313|Ensembl:ENSKMAP00000016852.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2025) to UniProtKB.
CC   -!- FUNCTION: Mediates feedback control of cholesterol synthesis.
CC       {ECO:0000256|RuleBase:RU241113}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004477}.
CC   -!- SIMILARITY: Belongs to the INSIG family.
CC       {ECO:0000256|ARBA:ARBA00007475, ECO:0000256|RuleBase:RU241113}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU241113}.
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DR   AlphaFoldDB; A0A3Q3FX38; -.
DR   Ensembl; ENSKMAT00000017086.1; ENSKMAP00000016852.1; ENSKMAG00000012561.1.
DR   GeneTree; ENSGT00580000081600; -.
DR   OMA; ENHTWSC; -.
DR   Proteomes; UP000264800; Unplaced.
DR   GO; GO:0032937; C:SREBP-SCAP-Insig complex; IEA:TreeGrafter.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0032869; P:cellular response to insulin stimulus; IEA:TreeGrafter.
DR   GO; GO:0006695; P:cholesterol biosynthetic process; IEA:TreeGrafter.
DR   GO; GO:0032933; P:SREBP signaling pathway; IEA:TreeGrafter.
DR   GO; GO:0036316; P:SREBP-SCAP complex retention in endoplasmic reticulum; IEA:TreeGrafter.
DR   InterPro; IPR025929; INSIG_fam.
DR   PANTHER; PTHR15301; INSULIN-INDUCED GENE 1; 1.
DR   PANTHER; PTHR15301:SF11; INSULIN-INDUCED GENE 1 PROTEIN; 1.
DR   Pfam; PF07281; INSIG; 1.
PE   3: Inferred from homology;
KW   Cholesterol metabolism {ECO:0000256|ARBA:ARBA00022548,
KW   ECO:0000256|RuleBase:RU241113};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW   ECO:0000256|RuleBase:RU241113};
KW   Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU241113};
KW   Reference proteome {ECO:0000313|Proteomes:UP000264800};
KW   Steroid metabolism {ECO:0000256|ARBA:ARBA00023221,
KW   ECO:0000256|RuleBase:RU241113};
KW   Sterol metabolism {ECO:0000256|ARBA:ARBA00023166};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU241113};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU241113}.
FT   TRANSMEM        34..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU241113"
FT   TRANSMEM        72..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU241113"
FT   TRANSMEM        104..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU241113"
FT   TRANSMEM        130..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU241113"
FT   TRANSMEM        156..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU241113"
FT   TRANSMEM        187..208
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU241113"
SQ   SEQUENCE   222 AA;  24418 MW;  773A71CFB3E53AAC CRC64;
     MYMKDKNCSP GPILVCAYGS LHCGRVANLV RRGLVLFTVG VFLALVLNLL QIQRNVTLFP
     EEVMTTLFSS AWWIPPCCGT GAAVVGLLYP CLDSHLGEPH KFKREWASVM RCIAVFVGIN
     HASAKLDFDN NVQLSLTLAA LSLGLWWTFD RSRSGFGLGI TTAFLATVIT QLLVYNGVYQ
     YTSPDFLYVR SWLPCIFFSG GVTVGNIGRQ LAMGGSEKPH MD
//
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