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   24-JAN-2024, entry version 128.
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   TCDB; 3.A.34.1.1; the sorting nexins of the escrt complexes (sn-escrt).
DR   PhosphoSitePlus; Q8R3Q0; -.
DR   EPD; Q8R3Q0; -.
DR   MaxQB; Q8R3Q0; -.
DR   PaxDb; 10090-ENSMUSP00000033933; -.
DR   PeptideAtlas; Q8R3Q0; -.
DR   ProteomicsDB; 256917; -.
DR   Pumba; Q8R3Q0; -.
DR   Antibodypedia; 23198; 126 antibodies from 18 providers.
DR   DNASU; 67887; -.
DR   Ensembl; ENSMUST00000033933.8; ENSMUSP00000033933.7; ENSMUSG00000031532.8.
DR   GeneID; 67887; -.
DR   KEGG; mmu:67887; -.
DR   UCSC; uc012gci.1; mouse.
DR   AGR; MGI:1915137; -.
DR   CTD; 51669; -.
DR   MGI; MGI:1915137; Saraf.
DR   VEuPathDB; HostDB:ENSMUSG00000031532; -.
DR   eggNOG; ENOG502QT6Y; Eukaryota.
DR   GeneTree; ENSGT00390000013419; -.
DR   InParanoid; Q8R3Q0; -.
DR   OMA; WILKGSC; -.
DR   OrthoDB; 5402569at2759; -.
DR   PhylomeDB; Q8R3Q0; -.
DR   TreeFam; TF314811; -.
DR   BioGRID-ORCS; 67887; 5 hits in 77 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 271 other cell types or tissues.
DR   ExpressionAtlas; Q8R3Q0; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
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: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:SF0; STORE-OPERATED CALCIUM ENTRY-ASSOCIATED REGULATORY FACTOR; 1.
DR   PANTHER; PTHR15929; UNCHARACTERIZED; 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
//