SARAF_MOUSE
ID SARAF_MOUSE Reviewed; 334 AA.
AC Q8R3Q0; Q8C2F1; Q8C6G7; Q8N9S4; Q8R233; Q9D8R1;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Store-operated calcium entry-associated regulatory factor;
DE Short=SARAF;
DE Short=SOCE-associated regulatory factor;
DE AltName: Full=Transmembrane protein 66;
DE Flags: Precursor;
GN Name=Saraf; Synonyms=Tmem66;
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].
RA Suzuki O., Sasaki N., Aotsuka S., Shoji T., Ichihara T., Shiohata N.,
RA Matsumoto K., Hirano M., Sano S., Nomura R., Yoshikawa Y., Matsumura Y.,
RA Moriya S., Chiba E., Momiyama H., Onogawa S., Kaeriyama S., Satoh N.,
RA Matsunawa H., Takahashi E., Kataoka R., Kuga N., Kuroda A., Satoh I.,
RA Kamata K., Takami S., Terashima Y., Watanabe M., Sugiyama T., Irie R.,
RA Otsuki T., Sato H., Ota T., Wakamatsu A., Ishii S., Yamamoto J., Isono Y.,
RA Kawai-Hio Y., Saito K., Nishikawa T., Kimura K., Yamashita H., Matsuo K.,
RA Nakamura Y., Sekine M., Kikuchi H., Kanda K., Wagatsuma M., Murakawa K.,
RA Kanehori K., Takahashi-Fujii A., Oshima A., Sugiyama A., Kawakami B.,
RA Suzuki Y., Sugano S., Nagahari K., Masuho Y., Nagai K., Isogai T.;
RT "NEDO cDNA sequencing project.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Egg, Pancreas, Placenta, and Thymus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor, and Salivary gland;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Negative regulator of store-operated Ca(2+) entry (SOCE)
CC involved in protecting cells from Ca(2+) overfilling. In response to
CC cytosolic Ca(2+) elevation after endoplasmic reticulum Ca(2+)
CC refilling, promotes a slow inactivation of STIM (STIM1 or STIM2)-
CC dependent SOCE activity: possibly act by facilitating the
CC deoligomerization of STIM to efficiently turn off ORAI when the
CC endoplasmic reticulum lumen is filled with the appropriate Ca(2+)
CC levels, and thus preventing the overload of the cell with excessive
CC Ca(2+) ions (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with STIM1; the interaction is inhibit by th
CC interaction of STIM1 with EFHB. {ECO:0000250|UniProtKB:Q96BY9}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass type I membrane protein {ECO:0000250}. Note=Translocates to
CC the endoplasmic reticulum-plasma membrane (ER-PM) region in a STIM1-
CC dependent manner following cytosolic Ca(2+) elevation. {ECO:0000250}.
CC -!- DOMAIN: The cytoplasmic C-terminal region mediates interaction with
CC STIM1, while the N-terminal lumenal region mediates regulation of SOCE
CC activity. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SARAF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH13497.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH22616.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH24888.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB25254.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC04255.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC40531.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE37240.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK093942; BAC04255.1; ALT_INIT; mRNA.
DR EMBL; AK007787; BAB25254.1; ALT_INIT; mRNA.
DR EMBL; AK075744; BAC35924.1; -; mRNA.
DR EMBL; AK088728; BAC40531.1; ALT_INIT; mRNA.
DR EMBL; AK163218; BAE37240.1; ALT_INIT; mRNA.
DR EMBL; BC013497; AAH13497.1; ALT_INIT; mRNA.
DR EMBL; BC022616; AAH22616.1; ALT_INIT; mRNA.
DR EMBL; BC024888; AAH24888.1; ALT_INIT; mRNA.
DR CCDS; CCDS22240.1; -.
DR RefSeq; NP_080708.3; NM_026432.3.
DR AlphaFoldDB; Q8R3Q0; -.
DR SMR; Q8R3Q0; -.
DR BioGRID; 212511; 2.
DR IntAct; Q8R3Q0; 1.
DR STRING; 10090.ENSMUSP00000033933; -.
DR PhosphoSitePlus; Q8R3Q0; -.
DR EPD; Q8R3Q0; -.
DR MaxQB; Q8R3Q0; -.
DR PaxDb; Q8R3Q0; -.
DR PeptideAtlas; Q8R3Q0; -.
DR PRIDE; Q8R3Q0; -.
DR ProteomicsDB; 256917; -.
DR Antibodypedia; 23198; 115 antibodies from 17 providers.
DR DNASU; 67887; -.
DR Ensembl; ENSMUST00000033933; ENSMUSP00000033933; ENSMUSG00000031532.
DR GeneID; 67887; -.
DR KEGG; mmu:67887; -.
DR UCSC; uc012gci.1; mouse.
DR CTD; 51669; -.
DR MGI; MGI:1915137; Saraf.
DR VEuPathDB; HostDB:ENSMUSG00000031532; -.
DR eggNOG; ENOG502QT6Y; Eukaryota.
DR GeneTree; ENSGT00390000013419; -.
DR InParanoid; Q8R3Q0; -.
DR OMA; DKWVLKG; -.
DR OrthoDB; 1402326at2759; -.
DR PhylomeDB; Q8R3Q0; -.
DR TreeFam; TF314811; -.
DR BioGRID-ORCS; 67887; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Saraf; mouse.
DR PRO; PR:Q8R3Q0; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8R3Q0; protein.
DR Bgee; ENSMUSG00000031532; Expressed in olfactory epithelium and 267 other tissues.
DR ExpressionAtlas; Q8R3Q0; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0140268; C:endoplasmic reticulum-plasma membrane contact site; ISS:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0006816; P:calcium ion transport; IEA:UniProtKB-KW.
DR GO; GO:2001256; P:regulation of store-operated calcium entry; ISS:UniProtKB.
DR InterPro; IPR009567; SARAF.
DR PANTHER; PTHR15929; PTHR15929; 1.
DR Pfam; PF06682; SARAF; 1.
PE 1: Evidence at protein level;
KW Calcium; Calcium transport; Endoplasmic reticulum; Ion transport; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..334
FT /note="Store-operated calcium entry-associated regulatory
FT factor"
FT /id="PRO_0000045486"
FT TOPO_DOM 32..168
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 190..334
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 198..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 12
FT /note="L -> V (in Ref. 2; BAC04255/BAC40531 and 3;
FT AAH24888)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="G -> V (in Ref. 3; AAH22616)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 334 AA; 35856 MW; EA12FE138052BCC4 CRC64;
MAVAAVGRPR ALRCPLLLLL SLLLVAGPAL GWNDPDRILL RDVKALTLYS DRYTTSRRLD
PIPQLKCVGG TAGCEAYTPR VIQCQNKGWD GYDVQWECKT DLDIAYKFGK TVVSCEGYES
SEDQYVLRGS CGLEYNLDYT ELGLKKLKES GKHQGFSDYY HKLYSSDSCG FITIAVLFVL
AFAVYKLFLS DGQGSPPPYS EHPPYSEHSQ RFASAAGAPP PGFKSEFTGP QNTGYGASSG
FGSAFGGQGY GSSGPGFWSG LGAGGLLGYL FGSNRAATPF SDSWYHPAYP PSHSGAWNSR
AYSPLGGGAG SYCASSNADS RTRTASGYGG TRRR
