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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
 
 
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