ID   SARAF_RAT               Reviewed;         334 AA.
AC   Q6AYN2;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 89.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Brown Norway; TISSUE=Testis;
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 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}.
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DR   EMBL; BC078979; AAH78979.1; -; mRNA.
DR   RefSeq; NP_001004213.1; NM_001004213.1.
DR   AlphaFoldDB; Q6AYN2; -.
DR   SMR; Q6AYN2; -.
DR   STRING; 10116.ENSRNOP00000016792; -.
DR   PhosphoSitePlus; Q6AYN2; -.
DR   jPOST; Q6AYN2; -.
DR   PaxDb; Q6AYN2; -.
DR   PRIDE; Q6AYN2; -.
DR   GeneID; 290796; -.
DR   KEGG; rno:290796; -.
DR   CTD; 51669; -.
DR   RGD; 1303011; Saraf.
DR   VEuPathDB; HostDB:ENSRNOG00000012329; -.
DR   eggNOG; ENOG502QT6Y; Eukaryota.
DR   HOGENOM; CLU_046802_0_1_1; -.
DR   InParanoid; Q6AYN2; -.
DR   OMA; DKWVLKG; -.
DR   OrthoDB; 1402326at2759; -.
DR   PhylomeDB; Q6AYN2; -.
DR   PRO; PR:Q6AYN2; -.
DR   Proteomes; UP000002494; Chromosome 16.
DR   Bgee; ENSRNOG00000012329; Expressed in Ammon's horn and 20 other tissues.
DR   Genevisible; Q6AYN2; RN.
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   2: Evidence at transcript 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_0000045488"
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          308..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        310..327
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   334 AA;  35885 MW;  6812CFBA88D352DC CRC64;
     MAVAAVGRPR AVRCLLLLLL SFLLVAGPAL CWKNPDRILL RDVEALTLYS DRYTTSRRLD
     PIPQLKCVGG TAGCDAYTPK VVQCQNKGWD GYDVQWECKT DLDIAYKFGK TVVSCEGYDS
     SEDQYILRGS CGLEYNLDYT ELGLSKLKES GKHQSFSDYY HKLSSVDSCG LVTVAVLFVL
     AFVVYKLFLS DGQGSPPPYS EHPPYSQHSQ RFAGTAGAPP PGFKSDFTGP QSTSYGASSG
     FGSAFGGQSY ASSGPGFWSG LGAGGLLGYL FGSNRAATPF SGSWYHPSYP SSYAGAWNSH
     AYSPLGGGAG RYSASSNTES RTRTTSGYGG TRRR