ORML1_MOUSE
ID ORML1_MOUSE Reviewed; 153 AA.
AC Q921I0; Q8BK13;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=ORM1-like protein 1;
GN Name=Ormdl1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Negative regulator of sphingolipid synthesis. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ORM family. {ECO:0000305}.
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DR EMBL; AK050385; BAC34226.1; -; mRNA.
DR EMBL; AK077562; BAC36865.1; -; mRNA.
DR EMBL; BC012315; AAH12315.1; -; mRNA.
DR EMBL; BC023695; AAH23695.1; -; mRNA.
DR EMBL; BC025572; AAH25572.1; -; mRNA.
DR CCDS; CCDS14952.1; -.
DR RefSeq; NP_663492.3; NM_145517.4.
DR AlphaFoldDB; Q921I0; -.
DR SMR; Q921I0; -.
DR BioGRID; 230590; 8.
DR IntAct; Q921I0; 1.
DR STRING; 10090.ENSMUSP00000027266; -.
DR PhosphoSitePlus; Q921I0; -.
DR jPOST; Q921I0; -.
DR MaxQB; Q921I0; -.
DR PaxDb; Q921I0; -.
DR PeptideAtlas; Q921I0; -.
DR PRIDE; Q921I0; -.
DR ProteomicsDB; 294346; -.
DR DNASU; 227102; -.
DR Ensembl; ENSMUST00000027266; ENSMUSP00000027266; ENSMUSG00000026097.
DR GeneID; 227102; -.
DR KEGG; mmu:227102; -.
DR UCSC; uc011wks.1; mouse.
DR CTD; 94101; -.
DR MGI; MGI:2181669; Ormdl1.
DR VEuPathDB; HostDB:ENSMUSG00000026097; -.
DR eggNOG; KOG3319; Eukaryota.
DR GeneTree; ENSGT00950000183178; -.
DR HOGENOM; CLU_072117_3_0_1; -.
DR InParanoid; Q921I0; -.
DR OMA; DPTHFII; -.
DR OrthoDB; 1405600at2759; -.
DR PhylomeDB; Q921I0; -.
DR TreeFam; TF323369; -.
DR Reactome; R-MMU-1660661; Sphingolipid de novo biosynthesis.
DR BioGRID-ORCS; 227102; 2 hits in 70 CRISPR screens.
DR PRO; PR:Q921I0; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q921I0; protein.
DR Bgee; ENSMUSG00000026097; Expressed in urinary bladder urothelium and 252 other tissues.
DR Genevisible; Q921I0; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0035339; C:SPOTS complex; IBA:GO_Central.
DR GO; GO:0090156; P:cellular sphingolipid homeostasis; IBA:GO_Central.
DR GO; GO:0006672; P:ceramide metabolic process; ISS:UniProtKB.
DR GO; GO:0061744; P:motor behavior; IGI:MGI.
DR GO; GO:0042552; P:myelination; IGI:MGI.
DR GO; GO:1900060; P:negative regulation of ceramide biosynthetic process; ISO:MGI.
DR GO; GO:2000303; P:regulation of ceramide biosynthetic process; IGI:MGI.
DR GO; GO:0090153; P:regulation of sphingolipid biosynthetic process; IGI:MGI.
DR GO; GO:0006686; P:sphingomyelin biosynthetic process; IGI:MGI.
DR InterPro; IPR007203; ORMDL.
DR InterPro; IPR029884; ORML1.
DR PANTHER; PTHR12665; PTHR12665; 1.
DR PANTHER; PTHR12665:SF12; PTHR12665:SF12; 1.
DR Pfam; PF04061; ORMDL; 1.
DR PIRSF; PIRSF018147; ORMDL; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..153
FT /note="ORM1-like protein 1"
FT /id="PRO_0000215631"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 123
FT /note="H -> N (in Ref. 1; BAC36865)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 153 AA; 17355 MW; A592BCA2BEB1AC6B CRC64;
MNVGVAHSEV NPNTRVMNSR GMWLTYALGV GLLHIVLLSI PFCSVPVAWT LTNIIHNLGM
YVFLHAVKGT PFETPDQGRA RLLTHWEQLD YGVQFTSSRK FFTISPIILY FLASFYTKYD
PTHFILNTAS LLSVLIPKMP QLHGVRIFGI NKY
