ID A0A5F4CJH1_CANLF Unreviewed; 310 AA. AC A0A5F4CJH1; DT 11-DEC-2019, integrated into UniProtKB/TrEMBL. DT 11-DEC-2019, sequence version 1. DT 07-APR-2021, entry version 7. DE RecName: Full=Insulin-induced gene protein {ECO:0000256|RuleBase:RU241113}; GN Name=INSIG2 {ECO:0000313|Ensembl:ENSCAFP00000054398, GN ECO:0000313|VGNC:VGNC:42040}; OS Canis lupus familiaris (Dog) (Canis familiaris). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis. OX NCBI_TaxID=9615 {ECO:0000313|Ensembl:ENSCAFP00000054398, ECO:0000313|Proteomes:UP000002254}; RN [1] {ECO:0000313|Ensembl:ENSCAFP00000054398, ECO:0000313|Proteomes:UP000002254} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000054398, RC ECO:0000313|Proteomes:UP000002254}; RX PubMed=16341006; DOI=10.1038/nature04338; RG Broad Sequencing Platform; RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B., RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E., RA Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F., RA Smith D.R., deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W., RA Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S., RA Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A., RA Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P., RA Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A., RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P., RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P., RA Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B., RA Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A., RA Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M., RA Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., RA Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., RA Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S., RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C., RA Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G., RA Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N., RA Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A., RA Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A., RA Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M., RA Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., RA LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A., RA Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S., RA Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., RA Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., RA Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N., RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S., RA Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M., RA Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F., RA Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T., RA Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C., RA Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C., RA Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D., RA Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H., RA Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J., RA Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J., RA Zembek L., Zimmer A., Lander E.S.; RT "Genome sequence, comparative analysis and haplotype structure of the RT domestic dog."; RL Nature 438:803-819(2005). RN [2] {ECO:0000313|Ensembl:ENSCAFP00000054398} RP IDENTIFICATION. RC STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000054398}; RG Ensembl; RL Submitted (OCT-2019) 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, ECO:0000256|RuleBase:RU241113}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004477, CC ECO:0000256|RuleBase:RU241113}. Membrane CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141}. CC -!- SIMILARITY: Belongs to the INSIG family. CC {ECO:0000256|ARBA:ARBA00007475, ECO:0000256|RuleBase:RU241113}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AAEX03011883; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSCAFT00000060104; ENSCAFP00000054398; ENSCAFG00000030843. DR VGNC; VGNC:42040; INSIG2. DR GeneTree; ENSGT00580000081600; -. DR Proteomes; UP000002254; Chromosome 19. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW. DR GO; GO:0006695; P:cholesterol biosynthetic process; IEA:Ensembl. DR GO; GO:0060363; P:cranial suture morphogenesis; IEA:Ensembl. DR GO; GO:0042472; P:inner ear morphogenesis; IEA:Ensembl. DR GO; GO:0042474; P:middle ear morphogenesis; IEA:Ensembl. DR GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; IEA:Ensembl. DR GO; GO:0010894; P:negative regulation of steroid biosynthetic process; IEA:Ensembl. DR GO; GO:0006991; P:response to sterol depletion; IEA:Ensembl. DR GO; GO:0060021; P:roof of mouth development; IEA:Ensembl. DR GO; GO:0006641; P:triglyceride metabolic process; IEA:Ensembl. DR InterPro; IPR025929; INSIG_fam. DR PANTHER; PTHR15301; PTHR15301; 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 ECO:0000256|RuleBase:RU241113}; KW Lipid metabolism {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:UP000002254}; 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 28..49 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU241113" FT TRANSMEM 69..88 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU241113" FT TRANSMEM 131..148 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU241113" FT TRANSMEM 155..174 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU241113" FT TRANSMEM 227..246 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU241113" SQ SEQUENCE 310 AA; 35470 MW; 7947727EFDADEDE3 CRC64; MAEEETESPG PKKRGPYISS VTSRSVNLMI RGVVLFFIGV FLALVLNLLQ IQRNVTLFPP DVIASIFSSA WWVPPCCGTA SAVIGLLYPC IDRHLGEPHK FKREWSSVMR CVAVFVGINH ASAKVDFDNN IQLSLTLAAL SIGLWWTFDR SRSGFGLGVG IAFLATLVTQ LLVYNGVYHM NVKLLQKNLI RNEEAKIYLL YKKQEEKGME MITISKLWTV KLPGCSFPLD WCIHICVCVC VCMRIYRHKY IRIHTHICMH ICIHMHIHIY YYITAICDCF ICKSVTNLDV FDLNNYKIYI CTTLNMFINR //