SARCO_MOUSE
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 03-AUG-2022, entry version 126.
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; Q9CQD6; -.
DR PRIDE; Q9CQD6; -.
DR DNASU; 66402; -.
DR Ensembl; ENSMUST00000048485; ENSMUSP00000036950; ENSMUSG00000042045.
DR GeneID; 66402; -.
DR KEGG; mmu:66402; -.
DR UCSC; uc009pmp.1; mouse.
DR CTD; 6588; -.
DR MGI; MGI:1913652; Sln.
DR VEuPathDB; HostDB:ENSMUSG00000042045; -.
DR eggNOG; ENOG502TD27; Eukaryota.
DR GeneTree; ENSGT00990000204194; -.
DR HOGENOM; CLU_221275_0_0_1; -.
DR InParanoid; Q9CQD6; -.
DR OrthoDB; 1647338at2759; -.
DR PhylomeDB; Q9CQD6; -.
DR BioGRID-ORCS; 66402; 3 hits in 65 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 tissues.
DR Genevisible; Q9CQD6; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:1901895; P:negative regulation of ATPase-coupled calcium transmembrane transporter activity; IDA:MGI.
DR GO; GO:1901877; P:negative regulation of calcium ion binding; IDA:MGI.
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 InterPro; IPR008028; Sarcolipin.
DR Pfam; PF05366; Sarcolipin; 1.
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
