ID   SARCO_HUMAN             Reviewed;          31 AA.
AC   O00631; Q6ICV3;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 154.
DE   RecName: Full=Sarcolipin {ECO:0000305};
GN   Name=SLN {ECO:0000312|HGNC:HGNC:11089};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   PubMed=9367679; DOI=10.1006/geno.1997.4967;
RA   Odermatt A., Taschner P.E.M., Scherer S.W., Beatty B., Khanna V.K.,
RA   Cornblath D.R., Chaudhry V., Yee W.-C., Schrank B., Karpati G.,
RA   Breuning M.H., Knoers N., Maclennan D.H.;
RT   "Characterization of the gene encoding human sarcolipin (SLN), a
RT   proteolipid associated with SERCA1: absence of structural mutations in five
RT   patients with Brody disease.";
RL   Genomics 45:541-553(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Skeletal muscle;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=PNS;
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   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX   PubMed=9575189; DOI=10.1074/jbc.273.20.12360;
RA   Odermatt A., Becker S., Khanna V.K., Kurzydlowski K., Leisner E., Pette D.,
RA   MacLennan D.H.;
RT   "Sarcolipin regulates the activity of SERCA1, the fast-twitch skeletal
RT   muscle sarcoplasmic reticulum Ca2+-ATPase.";
RL   J. Biol. Chem. 273:12360-12369(1998).
RN   [6]
RP   INTERACTION WITH ATP2A2 AND VMP1, AND FUNCTION.
RX   PubMed=28890335; DOI=10.1016/j.molcel.2017.08.005;
RA   Zhao Y.G., Chen Y., Miao G., Zhao H., Qu W., Li D., Wang Z., Liu N., Li L.,
RA   Chen S., Liu P., Feng D., Zhang H.;
RT   "The ER-Localized Transmembrane Protein EPG-3/VMP1 Regulates SERCA Activity
RT   to Control ER-Isolation Membrane Contacts for Autophagosome Formation.";
RL   Mol. Cell 67:974.e6-989.e6(2017).
RN   [7]
RP   STRUCTURE BY NMR, FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=11781085; DOI=10.1021/bi011243m;
RA   Mascioni A., Karim C., Barany G., Thomas D.D., Veglia G.;
RT   "Structure and orientation of sarcolipin in lipid environments.";
RL   Biochemistry 41:475-482(2002).
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. Required
CC       for muscle-based, non-shivering thermogenesis (By similarity).
CC       {ECO:0000250|UniProtKB:Q9CQD6, ECO:0000269|PubMed:11781085,
CC       ECO:0000269|PubMed:9575189}.
CC   -!- SUBUNIT: Interacts with calcium ATPase ATP2A1/SERCA1. Interact with
CC       ATP2A2; the inhibition decreases ATP2A1 Ca(2+) affinity
CC       (PubMed:28890335). Interacts with VMP1; VMP1 competes with PLN and SLN
CC       to prevent them from forming an inhibitory complex with ATP2A2
CC       (PubMed:28890335). {ECO:0000250|UniProtKB:P42532,
CC       ECO:0000269|PubMed:28890335}.
CC   -!- INTERACTION:
CC       O00631; Q8N6L0: KASH5; NbExp=3; IntAct=EBI-10180786, EBI-749265;
CC       O00631; Q8N205: SYNE4; NbExp=3; IntAct=EBI-10180786, EBI-7131783;
CC       O00631; Q9BSE2: TMEM79; NbExp=4; IntAct=EBI-10180786, EBI-8649725;
CC   -!- SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:11781085, ECO:0000269|PubMed:9575189}; Single-pass
CC       membrane protein {ECO:0000255}. Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P42532}; Single-pass membrane protein
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the sarcolipin family. {ECO:0000305}.
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DR   EMBL; U96094; AAB86981.1; -; mRNA.
DR   EMBL; U96093; AAB86980.1; -; Genomic_DNA.
DR   EMBL; AK312097; BAG35033.1; -; mRNA.
DR   EMBL; CR450290; CAG29286.1; -; mRNA.
DR   EMBL; BC094685; AAH94685.1; -; mRNA.
DR   EMBL; BC104150; AAI04151.1; -; mRNA.
DR   EMBL; BC104185; AAI04186.1; -; mRNA.
DR   EMBL; BC113930; AAI13931.1; -; mRNA.
DR   EMBL; BC113987; AAI13988.1; -; mRNA.
DR   CCDS; CCDS31667.1; -.
DR   RefSeq; NP_003054.1; NM_003063.2.
DR   PDB; 1JDM; NMR; -; A=1-31.
DR   PDBsum; 1JDM; -.
DR   AlphaFoldDB; O00631; -.
DR   SMR; O00631; -.
DR   BioGRID; 112474; 9.
DR   CORUM; O00631; -.
DR   DIP; DIP-61731N; -.
DR   IntAct; O00631; 5.
DR   STRING; 9606.ENSP00000435380; -.
DR   TCDB; 1.A.50.2.1; the phospholamban (ca(2+)-channel and ca(2+)-atpase regulator) (plb) family.
DR   iPTMnet; O00631; -.
DR   PhosphoSitePlus; O00631; -.
DR   BioMuta; SLN; -.
DR   PaxDb; O00631; -.
DR   PeptideAtlas; O00631; -.
DR   PRIDE; O00631; -.
DR   Antibodypedia; 45530; 70 antibodies from 13 providers.
DR   DNASU; 6588; -.
DR   Ensembl; ENST00000305991.3; ENSP00000304707.2; ENSG00000170290.4.
DR   Ensembl; ENST00000525934.1; ENSP00000434189.1; ENSG00000170290.4.
DR   Ensembl; ENST00000531293.1; ENSP00000435380.1; ENSG00000170290.4.
DR   GeneID; 6588; -.
DR   KEGG; hsa:6588; -.
DR   MANE-Select; ENST00000305991.3; ENSP00000304707.2; NM_003063.3; NP_003054.1.
DR   UCSC; uc001pjp.4; human.
DR   CTD; 6588; -.
DR   DisGeNET; 6588; -.
DR   GeneCards; SLN; -.
DR   HGNC; HGNC:11089; SLN.
DR   HPA; ENSG00000170290; Group enriched (skeletal muscle, tongue).
DR   MIM; 602203; gene.
DR   neXtProt; NX_O00631; -.
DR   OpenTargets; ENSG00000170290; -.
DR   PharmGKB; PA35942; -.
DR   VEuPathDB; HostDB:ENSG00000170290; -.
DR   eggNOG; ENOG502TD28; Eukaryota.
DR   GeneTree; ENSGT01040000240931; -.
DR   HOGENOM; CLU_221275_0_0_1; -.
DR   InParanoid; O00631; -.
DR   OrthoDB; 1647338at2759; -.
DR   PhylomeDB; O00631; -.
DR   PathwayCommons; O00631; -.
DR   Reactome; R-HSA-5578775; Ion homeostasis.
DR   Reactome; R-HSA-936837; Ion transport by P-type ATPases.
DR   SignaLink; O00631; -.
DR   SIGNOR; O00631; -.
DR   BioGRID-ORCS; 6588; 12 hits in 641 CRISPR screens.
DR   EvolutionaryTrace; O00631; -.
DR   GeneWiki; Sarcolipin; -.
DR   GenomeRNAi; 6588; -.
DR   Pharos; O00631; Tbio.
DR   PRO; PR:O00631; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   Bgee; ENSG00000170290; Expressed in diaphragm and 136 other tissues.
DR   ExpressionAtlas; O00631; baseline and differential.
DR   Genevisible; O00631; HS.
DR   GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR   GO; GO:0016529; C:sarcoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0033017; C:sarcoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0051117; F:ATPase binding; ISS:BHF-UCL.
DR   GO; GO:0004857; F:enzyme inhibitor activity; ISS:BHF-UCL.
DR   GO; GO:0006816; P:calcium ion transport; NAS:UniProtKB.
DR   GO; GO:1901895; P:negative regulation of ATPase-coupled calcium transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:1901877; P:negative regulation of calcium ion binding; ISS:BHF-UCL.
DR   GO; GO:0090281; P:negative regulation of calcium ion import; ISS:BHF-UCL.
DR   GO; GO:1901020; P:negative regulation of calcium ion transmembrane transporter activity; ISS:BHF-UCL.
DR   GO; GO:0043086; P:negative regulation of catalytic activity; ISS:BHF-UCL.
DR   GO; GO:0043242; P:negative regulation of protein-containing complex disassembly; ISS:BHF-UCL.
DR   GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR   GO; GO:1901881; P:positive regulation of protein depolymerization; ISS:BHF-UCL.
DR   GO; GO:1901894; P:regulation of ATPase-coupled calcium transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0051924; P:regulation of calcium ion transport; ISS:UniProtKB.
DR   GO; GO:1901077; P:regulation of relaxation of muscle; ISS:UniProtKB.
DR   GO; GO:0070296; P:sarcoplasmic reticulum calcium ion transport; ISS:UniProtKB.
DR   InterPro; IPR008028; Sarcolipin.
DR   Pfam; PF05366; Sarcolipin; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Endoplasmic reticulum; Membrane; Reference proteome;
KW   Sarcoplasmic reticulum; Transmembrane; Transmembrane helix.
FT   PEPTIDE         1..31
FT                   /note="Sarcolipin"
FT                   /id="PRO_0000045898"
FT   TOPO_DOM        1..7
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:9575189"
FT   TRANSMEM        8..26
FT                   /note="Helical"
FT   TOPO_DOM        27..31
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000269|PubMed:9575189"
FT   STRAND          5..8
FT                   /evidence="ECO:0007829|PDB:1JDM"
FT   HELIX           9..25
FT                   /evidence="ECO:0007829|PDB:1JDM"
SQ   SEQUENCE   31 AA;  3762 MW;  9B245D9ACD26C58F CRC64;
     MGINTRELFL NFTIVLITVI LMWLLVRSYQ Y