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O00631 (SARCO_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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+. Required for muscle-based, non-shivering thermogenesis By similarity. Modulates calcium re-uptake during muscle relaxation and plays an important role in calcium homeostasis in muscle. Ref.5 Ref.6

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 Ref.5 Ref.6.

Sequence similarities

Belongs to the sarcolipin family.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Membrane
Sarcoplasmic reticulum
   DomainTransmembrane
Transmembrane helix
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcalcium ion transport

Non-traceable author statement Ref.1. Source: UniProtKB

negative regulation of calcium ion binding

Inferred from sequence or structural similarity PubMed 12032137. Source: BHF-UCL

negative regulation of calcium ion import

Inferred from sequence or structural similarity PubMed 12032137. Source: BHF-UCL

negative regulation of calcium ion transmembrane transporter activity

Inferred from sequence or structural similarity PubMed 12032137. Source: BHF-UCL

negative regulation of catalytic activity

Inferred from sequence or structural similarity PubMed 12032137. Source: BHF-UCL

negative regulation of protein complex disassembly

Inferred from sequence or structural similarity PubMed 12032137. Source: BHF-UCL

positive regulation of protein depolymerization

Inferred from sequence or structural similarity PubMed 12032137. Source: BHF-UCL

regulation of calcium ion transport

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of calcium-transporting ATPase activity

Inferred from direct assay Ref.6. Source: UniProtKB

regulation of relaxation of muscle

Inferred from sequence or structural similarity. Source: UniProtKB

sarcoplasmic reticulum calcium ion transport

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentintegral component of membrane

Non-traceable author statement Ref.1. Source: UniProtKB

sarcoplasmic reticulum

Inferred from direct assay Ref.5. Source: UniProtKB

sarcoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATPase binding

Inferred from sequence or structural similarity PubMed 12032137. Source: BHF-UCL

enzyme inhibitor activity

Inferred from sequence or structural similarity PubMed 12032137. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Peptide1 – 3131Sarcolipin
PRO_0000045898

Regions

Topological domain1 – 77Cytoplasmic Ref.5
Transmembrane8 – 2619Helical
Topological domain27 – 315Lumenal Ref.5

Secondary structure

.... 31
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O00631 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 9B245D9ACD26C58F

FASTA313,762
        10         20         30 
MGINTRELFL NFTIVLITVI LMWLLVRSYQ Y 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of the gene encoding human sarcolipin (SLN), a proteolipid associated with SERCA1: absence of structural mutations in five patients with Brody disease."
Odermatt A., Taschner P.E.M., Scherer S.W., Beatty B., Khanna V.K., Cornblath D.R., Chaudhry V., Yee W.-C., Schrank B., Karpati G., Breuning M.H., Knoers N., Maclennan D.H.
Genomics 45:541-553(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Skeletal muscle.
[3]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"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: PNS.
[5]"Sarcolipin regulates the activity of SERCA1, the fast-twitch skeletal muscle sarcoplasmic reticulum Ca2+-ATPase."
Odermatt A., Becker S., Khanna V.K., Kurzydlowski K., Leisner E., Pette D., MacLennan D.H.
J. Biol. Chem. 273:12360-12369(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY.
[6]"Structure and orientation of sarcolipin in lipid environments."
Mascioni A., Karim C., Barany G., Thomas D.D., Veglia G.
Biochemistry 41:475-482(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR, FUNCTION, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U96094 mRNA. Translation: AAB86981.1.
U96093 Genomic DNA. Translation: AAB86980.1.
AK312097 mRNA. Translation: BAG35033.1.
CR450290 mRNA. Translation: CAG29286.1.
BC094685 mRNA. Translation: AAH94685.1.
BC104150 mRNA. Translation: AAI04151.1.
BC104185 mRNA. Translation: AAI04186.1.
BC113930 mRNA. Translation: AAI13931.1.
BC113987 mRNA. Translation: AAI13988.1.
CCDSCCDS31667.1.
RefSeqNP_003054.1. NM_003063.2.
UniGeneHs.334629.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JDMNMR-A1-31[»]
ProteinModelPortalO00631.
SMRO00631. Positions 1-31.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112474. 3 interactions.
STRING9606.ENSP00000304707.

Protein family/group databases

TCDB1.A.50.2.1. the phospholamban (ca(2+)-channel and ca(2+)-atpase regulator) (plb) family.

PTM databases

PhosphoSiteO00631.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000305991; ENSP00000304707; ENSG00000170290.
ENST00000525934; ENSP00000434189; ENSG00000170290.
ENST00000531293; ENSP00000435380; ENSG00000170290.
GeneID6588.
KEGGhsa:6588.
UCSCuc001pjp.3. human.

Organism-specific databases

CTD6588.
GeneCardsGC11M107612.
H-InvDBHIX0010086.
HGNCHGNC:11089. SLN.
HPACAB011628.
MIM602203. gene.
neXtProtNX_O00631.
PharmGKBPA35942.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG140204.
HOGENOMHOG000142457.
InParanoidO00631.
OMAALHAWGR.
OrthoDBEOG7XH6TJ.
PhylomeDBO00631.

Gene expression databases

BgeeO00631.
CleanExHS_SLN.
GenevestigatorO00631.

Family and domain databases

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

Other

EvolutionaryTraceO00631.
GeneWikiSarcolipin.
GenomeRNAi6588.
NextBio25633.
PROO00631.
SOURCESearch...

Entry information

Entry nameSARCO_HUMAN
AccessionPrimary (citable) accession number: O00631
Secondary accession number(s): Q6ICV3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 1, 1997
Last modified: July 9, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM