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Q9CQD6 (SARCO_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sarcolipin
Gene names
Name:Sln
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length31 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Reversibly inhibits the activity of ATP2A1 in sarcoplasmic reticulum by decreasing the apparent affinity of the ATPase for Ca2+. Modulates calcium re-uptake during muscle relaxation and plays an important role in calcium homeostasis in muscle. Required for muscle-based, non-shivering thermogenesis. Ref.3 Ref.4

Subunit structure

Interacts with calcium ATPase ATP2A1/SERCA1.

Subcellular location

Sarcoplasmic reticulum membrane; Single-pass membrane protein. Endoplasmic reticulum membrane; Single-pass membrane protein By similarity.

Tissue specificity

Highly expressed in heart atrium, red gastrocnemius muscle and soleus. Detected at lower levels in the extensor digitorum longus muscle (at protein level). Ref.3

Disruption phenotype

No visible phenotype at 22 degrees Celsius. Increased heat-loss and failure to maintain body temperature at 4 degrees Celsius when the shivering response is prevented. Mice show increased weight gain and obesity when kept on a high-fat diet. Mice display faster muscle relaxation rates in soleus due to an increase in the affinity of ATP2A1 for Ca2+. Ref.3 Ref.4

Sequence similarities

Belongs to the sarcolipin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Peptide1 – 3131Sarcolipin
PRO_0000045899

Regions

Topological domain1 – 77Cytoplasmic By similarity
Transmembrane8 – 2619Helical; By similarity
Topological domain27 – 315Lumenal By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9CQD6 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 9B310161575EF81D

FASTA313,808
        10         20         30 
MERSTQELFI NFTVVLITVL LMWLLVRSYQ Y 

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Stomach and Tongue.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Mammary gland.
[3]"Enhanced Ca2+ transport and muscle relaxation in skeletal muscle from sarcolipin-null mice."
Tupling A.R., Bombardier E., Gupta S.C., Hussain D., Vigna C., Bloemberg D., Quadrilatero J., Trivieri M.G., Babu G.J., Backx P.H., Periasamy M., MacLennan D.H., Gramolini A.O.
Am. J. Physiol. 301:C841-C849(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY.
[4]"Sarcolipin is a newly identified regulator of muscle-based thermogenesis in mammals."
Bal N.C., Maurya S.K., Sopariwala D.H., Sahoo S.K., Gupta S.C., Shaikh S.A., Pant M., Rowland L.A., Bombardier E., Goonasekera S.A., Tupling A.R., Molkentin J.D., Periasamy M.
Nat. Med. 18:1575-1579(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK008863 mRNA. No translation available.
AK008896 mRNA. Translation: BAB25959.1.
AK009005 mRNA. Translation: BAB26019.1.
AK009809 mRNA. Translation: BAB26516.1.
BC028496 mRNA. Translation: AAH28496.1.
CCDSCCDS40640.1.
RefSeqNP_079816.1. NM_025540.2.
UniGeneMm.29132.

3D structure databases

ProteinModelPortalQ9CQD6.
SMRQ9CQD6. Positions 1-31.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000036950.

PTM databases

PhosphoSiteQ9CQD6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000048485; ENSMUSP00000036950; ENSMUSG00000042045.
GeneID66402.
KEGGmmu:66402.
UCSCuc009pmp.1. mouse.

Organism-specific databases

CTD6588.
MGIMGI:1913652. Sln.

Phylogenomic databases

eggNOGNOG140204.
GeneTreeENSGT00530000064724.
HOGENOMHOG000142457.
HOVERGENHBG079165.
InParanoidQ9CQD6.
OrthoDBEOG7T7GXN.
PhylomeDBQ9CQD6.

Gene expression databases

BgeeQ9CQD6.
CleanExMM_SLN.
GenevestigatorQ9CQD6.

Family and domain databases

InterProIPR008028. Sarcolipin.
[Graphical view]
PfamPF05366. Sarcolipin. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSLN. mouse.
NextBio321575.
PROQ9CQD6.
SOURCESearch...

Entry information

Entry nameSARCO_MOUSE
AccessionPrimary (citable) accession number: Q9CQD6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 13, 2002
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot