STIMA_MOUSE
ID STIMA_MOUSE Reviewed; 288 AA.
AC Q3UF25; Q3U2J0; Q8C691; Q8R3U0; Q9D7D4; Q9D8S1;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Store-operated calcium entry regulator STIMATE {ECO:0000250|UniProtKB:Q86TL2};
DE AltName: Full=STIM-activating enhancer encoded by TMEM110 {ECO:0000250|UniProtKB:Q86TL2};
DE AltName: Full=Transmembrane protein 110 {ECO:0000305};
GN Name=Stimate {ECO:0000250|UniProtKB:Q86TL2};
GN Synonyms=Tmem110 {ECO:0000312|MGI:MGI:1921500};
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, and NOD;
RC TISSUE=Pancreas, Skin, Sympathetic ganglion, and Tongue;
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] OF 115-288.
RC STRAIN=Czech II; 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).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=26322679; DOI=10.1038/ncb3234;
RA Jing J., He L., Sun A., Quintana A., Ding Y., Ma G., Tan P., Liang X.,
RA Zheng X., Chen L., Shi X., Zhang S.L., Zhong L., Huang Y., Dong M.Q.,
RA Walker C.L., Hogan P.G., Wang Y., Zhou Y.;
RT "Proteomic mapping of ER-PM junctions identifies STIMATE as a regulator of
RT Ca(2+) influx.";
RL Nat. Cell Biol. 17:1339-1347(2015).
CC -!- FUNCTION: Acts as a regulator of store-operated Ca(2+) entry (SOCE) at
CC junctional sites that connect the endoplasmic reticulum (ER) and plasma
CC membrane (PM), called ER-plasma membrane (ER-PM) junction or cortical
CC ER. SOCE is a Ca(2+) influx following depletion of intracellular Ca(2+)
CC stores. Acts by interacting with STIM1, promoting STIM1 conformational
CC switch. Involved in STIM1 relocalization to ER-PM junctions.
CC Contributes to the maintenance and reorganization of store-dependent
CC ER-PM junctions. {ECO:0000250|UniProtKB:Q86TL2}.
CC -!- SUBUNIT: Homooligomer. Interacts with STIM1.
CC {ECO:0000250|UniProtKB:Q86TL2}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q86TL2}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q86TL2}. Note=Colocalizes with STIM1 at ER-
CC plasma membrane (ER-PM) junctions, also called cortical endoplasmic
CC reticulum (ER), in store-depleted calcium cells. May translocate to ER-
CC PM junctions in a STIM1-dependent manner in store-depleted cells.
CC {ECO:0000250|UniProtKB:Q86TL2}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:26322679}.
CC -!- DOMAIN: The GXXXG motif may mediate oligomerization. The C-terminus is
CC necessary for its localization at ER-plasma membrane (ER-PM) junctions
CC as well as for the store-dependent rearrangement of ER-PM junctions.
CC {ECO:0000250|UniProtKB:Q86TL2}.
CC -!- SIMILARITY: Belongs to the STIMATE family. {ECO:0000305}.
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DR EMBL; AK007740; BAB25227.1; -; mRNA.
DR EMBL; AK009341; BAB26228.1; -; mRNA.
DR EMBL; AK076341; BAC36304.1; -; mRNA.
DR EMBL; AK149088; BAE28736.1; -; mRNA.
DR EMBL; AK155257; BAE33150.1; -; mRNA.
DR EMBL; BC024583; AAH24583.1; -; mRNA.
DR CCDS; CCDS26899.1; -.
DR RefSeq; NP_083115.3; NM_028839.4.
DR AlphaFoldDB; Q3UF25; -.
DR STRING; 10090.ENSMUSP00000006701; -.
DR iPTMnet; Q3UF25; -.
DR PhosphoSitePlus; Q3UF25; -.
DR PaxDb; Q3UF25; -.
DR PRIDE; Q3UF25; -.
DR ProteomicsDB; 257492; -.
DR Ensembl; ENSMUST00000006701; ENSMUSP00000006701; ENSMUSG00000006526.
DR GeneID; 69179; -.
DR KEGG; mmu:69179; -.
DR UCSC; uc007svt.2; mouse.
DR CTD; 375346; -.
DR MGI; MGI:1921500; Stimate.
DR VEuPathDB; HostDB:ENSMUSG00000006526; -.
DR eggNOG; ENOG502S1HE; Eukaryota.
DR GeneTree; ENSGT00940000153920; -.
DR HOGENOM; CLU_040321_1_0_1; -.
DR InParanoid; Q3UF25; -.
DR OMA; LQCGAWA; -.
DR OrthoDB; 897391at2759; -.
DR PhylomeDB; Q3UF25; -.
DR TreeFam; TF324457; -.
DR BioGRID-ORCS; 69179; 2 hits in 72 CRISPR screens.
DR PRO; PR:Q3UF25; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q3UF25; protein.
DR Bgee; ENSMUSG00000006526; Expressed in internal carotid artery and 216 other tissues.
DR ExpressionAtlas; Q3UF25; baseline and differential.
DR Genevisible; Q3UF25; MM.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0140268; C:endoplasmic reticulum-plasma membrane contact site; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005246; F:calcium channel regulator activity; ISS:UniProtKB.
DR GO; GO:0032237; P:activation of store-operated calcium channel activity; ISS:UniProtKB.
DR GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; ISS:UniProtKB.
DR GO; GO:0070886; P:positive regulation of calcineurin-NFAT signaling cascade; ISS:UniProtKB.
DR InterPro; IPR022127; STIMATE/YPL162C.
DR PANTHER; PTHR31735; PTHR31735; 1.
DR Pfam; PF12400; STIMATE; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..288
FT /note="Store-operated calcium entry regulator STIMATE"
FT /id="PRO_0000243916"
FT TOPO_DOM 1..28
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q86TL2"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215..288
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q86TL2"
FT REGION 228..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..246
FT /note="Required for localization in the endoplasmic
FT reticulum"
FT /evidence="ECO:0000250|UniProtKB:Q86TL2"
FT MOTIF 149..153
FT /note="GXXXG motif"
FT /evidence="ECO:0000250|UniProtKB:Q86TL2"
FT COMPBIAS 228..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 8
FT /note="V -> L (in Ref. 1; BAB25227)"
FT /evidence="ECO:0000305"
FT CONFLICT 23
FT /note="G -> E (in Ref. 1; BAB25227)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="V -> A (in Ref. 1; BAC36304)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="F -> L (in Ref. 1; BAC36304)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="I -> M (in Ref. 1; BAC36304)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="E -> K (in Ref. 1; BAC36304)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="E -> G (in Ref. 1; BAE33150)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="D -> Y (in Ref. 1; BAB26228)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 288 AA; 32500 MW; 2B30815B4CCD5784 CRC64;
MQGPGGNVSR GLPSGPASTV ASGAGRCESG ALMHSFGIFL QGLLGVVAFS TLMLKRFREP
KHERRPWRIW FLDTSKQAIG MLFIHFANVY LADLTEEDPC SLYLINFLLD ATVGMLLIYV
GVRAVGVLVE WQQWESLRFG EYGDPLQCGA WVGQCALYIV IMIFEKSVVF IVLLILQWKK
VALLNPIENP DLKLAIVMLI VPFFVNAFMF WVVDNFLMRK GKTKAKLEER GANQDSRNGS
KVRYRRAASH EESESEILIS ADDEMEESDA EEDLRRPVKK KHRFGLPV