ID   SARCO_MOUSE             Reviewed;          31 AA.
AC   Q9CQD6;
DT   13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   24-JAN-2024, entry version 132.
DE   RecName: Full=Sarcolipin {ECO:0000303|PubMed:21697544};
GN   Name=Sln {ECO:0000312|MGI:MGI:1913652};
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; TISSUE=Stomach, 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].
RC   TISSUE=Mammary 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   [3]
RP   DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=21697544; DOI=10.1152/ajpcell.00409.2010;
RA   Tupling A.R., Bombardier E., Gupta S.C., Hussain D., Vigna C.,
RA   Bloemberg D., Quadrilatero J., Trivieri M.G., Babu G.J., Backx P.H.,
RA   Periasamy M., MacLennan D.H., Gramolini A.O.;
RT   "Enhanced Ca2+ transport and muscle relaxation in skeletal muscle from
RT   sarcolipin-null mice.";
RL   Am. J. Physiol. 301:C841-C849(2011).
RN   [4]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=22961106; DOI=10.1038/nm.2897;
RA   Bal N.C., Maurya S.K., Sopariwala D.H., Sahoo S.K., Gupta S.C.,
RA   Shaikh S.A., Pant M., Rowland L.A., Bombardier E., Goonasekera S.A.,
RA   Tupling A.R., Molkentin J.D., Periasamy M.;
RT   "Sarcolipin is a newly identified regulator of muscle-based thermogenesis
RT   in mammals.";
RL   Nat. Med. 18:1575-1579(2012).
RN   [5]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=26816378; DOI=10.1126/science.aad4076;
RA   Nelson B.R., Makarewich C.A., Anderson D.M., Winders B.R., Troupes C.D.,
RA   Wu F., Reese A.L., McAnally J.R., Chen X., Kavalali E.T., Cannon S.C.,
RA   Houser S.R., Bassel-Duby R., Olson E.N.;
RT   "Muscle physiology. A peptide encoded by a transcript annotated as long
RT   noncoding RNA enhances SERCA activity in muscle.";
RL   Science 351:271-275(2016).
CC   -!- FUNCTION: Reversibly inhibits the activity of ATP2A1 and ATP2A2 in
CC       sarcoplasmic reticulum by decreasing the apparent affinity of the
CC       ATPase for Ca(2+). Modulates calcium re-uptake during muscle relaxation
CC       and plays an important role in calcium homeostasis in muscle
CC       (PubMed:21697544, PubMed:26816378). Required for muscle-based, non-
CC       shivering thermogenesis (PubMed:22961106).
CC       {ECO:0000269|PubMed:21697544, ECO:0000269|PubMed:22961106,
CC       ECO:0000269|PubMed:26816378}.
CC   -!- SUBUNIT: Interacts with calcium ATPase ATP2A1/SERCA1. Interact with
CC       ATP2A2; the inhibition decreases ATP2A1 Ca(2+) affinity. Interacts with
CC       VMP1; VMP1 competes with PLN and SLN to prevent them from forming an
CC       inhibitory complex with ATP2A2 (By similarity).
CC       {ECO:0000250|UniProtKB:O00631, ECO:0000250|UniProtKB:P42532}.
CC   -!- SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:26816378}; Single-pass membrane protein
CC       {ECO:0000255}. Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P42532}; Single-pass membrane protein
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in heart atrium, red gastrocnemius
CC       muscle and soleus. Detected at lower levels in the extensor digitorum
CC       longus muscle (at protein level). {ECO:0000269|PubMed:21697544}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype at 22 degrees Celsius.
CC       Increased heat-loss and failure to maintain body temperature at 4
CC       degrees Celsius when the shivering response is prevented. Mice show
CC       increased weight gain and obesity when kept on a high-fat diet. Mice
CC       display faster muscle relaxation rates in soleus due to an increase in
CC       the affinity of ATP2A1 for Ca(2+). {ECO:0000269|PubMed:21697544,
CC       ECO:0000269|PubMed:22961106}.
CC   -!- SIMILARITY: Belongs to the sarcolipin family. {ECO:0000305}.
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DR   EMBL; AK008863; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK008896; BAB25959.1; -; mRNA.
DR   EMBL; AK009005; BAB26019.1; -; mRNA.
DR   EMBL; AK009809; BAB26516.1; -; mRNA.
DR   EMBL; BC028496; AAH28496.1; -; mRNA.
DR   CCDS; CCDS40640.1; -.
DR   RefSeq; NP_079816.1; NM_025540.2.
DR   AlphaFoldDB; Q9CQD6; -.
DR   SMR; Q9CQD6; -.
DR   STRING; 10090.ENSMUSP00000036950; -.
DR   iPTMnet; Q9CQD6; -.
DR   PhosphoSitePlus; Q9CQD6; -.
DR   PaxDb; 10090-ENSMUSP00000036950; -.
DR   DNASU; 66402; -.
DR   Ensembl; ENSMUST00000048485.7; ENSMUSP00000036950.6; ENSMUSG00000042045.7.
DR   GeneID; 66402; -.
DR   KEGG; mmu:66402; -.
DR   UCSC; uc009pmp.1; mouse.
DR   AGR; MGI:1913652; -.
DR   CTD; 6588; -.
DR   MGI; MGI:1913652; Sln.
DR   VEuPathDB; HostDB:ENSMUSG00000042045; -.
DR   eggNOG; ENOG502TD27; Eukaryota.
DR   GeneTree; ENSGT01100000263709; -.
DR   HOGENOM; CLU_221275_0_0_1; -.
DR   InParanoid; Q9CQD6; -.
DR   OrthoDB; 4630259at2759; -.
DR   PhylomeDB; Q9CQD6; -.
DR   BioGRID-ORCS; 66402; 3 hits in 70 CRISPR screens.
DR   ChiTaRS; Sln; mouse.
DR   PRO; PR:Q9CQD6; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   Bgee; ENSMUSG00000042045; Expressed in atrioventricular valve and 88 other cell types or tissues.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:MGI.
DR   GO; GO:0016529; C:sarcoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0033017; C:sarcoplasmic reticulum membrane; IDA:UniProtKB.
DR   GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
DR   GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR   GO; GO:1901894; P:regulation of ATPase-coupled calcium transmembrane transporter activity; IMP:UniProtKB.
DR   GO; GO:0051924; P:regulation of calcium ion transport; ISS:UniProtKB.
DR   GO; GO:1901077; P:regulation of relaxation of muscle; IMP:UniProtKB.
DR   GO; GO:0070296; P:sarcoplasmic reticulum calcium ion transport; IMP:UniProtKB.
DR   CDD; cd20253; Sarcolipin; 1.
DR   Gene3D; 1.20.5.510; Single helix bin; 1.
DR   InterPro; IPR008028; Sarcolipin.
DR   Pfam; PF05366; Sarcolipin; 1.
DR   Genevisible; Q9CQD6; MM.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Membrane; Reference proteome;
KW   Sarcoplasmic reticulum; Transmembrane; Transmembrane helix.
FT   PEPTIDE         1..31
FT                   /note="Sarcolipin"
FT                   /id="PRO_0000045899"
FT   TOPO_DOM        1..7
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        8..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        27..31
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   31 AA;  3808 MW;  9B310161575EF81D CRC64;
     MERSTQELFI NFTVVLITVL LMWLLVRSYQ Y
//