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Protein

Epsilon-sarcoglycan

Gene

Sgce

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the sarcoglycan complex, a subcomplex of the dystrophin-glycoprotein complex which forms a link between the F-actin cytoskeleton and the extracellular matrix.

Names & Taxonomyi

Protein namesi
Recommended name:
Epsilon-sarcoglycan
Short name:
Epsilon-SG
Gene namesi
Name:Sgce
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1329042. Sgce.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 317317ExtracellularSequence AnalysisAdd
BLAST
Transmembranei318 – 33821HelicalSequence AnalysisAdd
BLAST
Topological domaini339 – 43799CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • cytoskeleton Source: UniProtKB-SubCell
  • dendrite Source: UniProtKB-SubCell
  • dendrite membrane Source: UniProtKB
  • dystrophin-associated glycoprotein complex Source: MGI
  • Golgi apparatus Source: UniProtKB
  • integral component of plasma membrane Source: MGI
  • plasma membrane Source: UniProtKB
  • sarcoglycan complex Source: InterPro
  • sarcolemma Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi60 – 601H → P or R: Misfolded, leading to the interaction with TOR1A, ubiquitination and a decrease of the half-life. Impairs intracellular transport. No effect on glycosylation. 1 Publication
Mutagenesisi196 – 1961L → R: Misfolded, leading to the interaction with TOR1A, ubiquitination and a decrease of the half-life. Impairs intracellular transport. No effect on glycosylation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 437437Epsilon-sarcoglycanPRO_0000031678Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi200 – 2001N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

N-glycosylated.1 Publication
Ubiquitinated, leading to its degradation by the proteasome.1 Publication

Keywords - PTMi

Glycoprotein, Ubl conjugation

Proteomic databases

MaxQBiO70258.
PaxDbiO70258.
PRIDEiO70258.

PTM databases

PhosphoSiteiO70258.

Expressioni

Tissue specificityi

Identified in all tissues tested. Expression highest in lung and placenta, moderate in brain, heart and skeletal muscle, low in kidney and liver. Also detected in embryo.

Gene expression databases

BgeeiO70258.
CleanExiMM_SGCE.
ExpressionAtlasiO70258. baseline and differential.
GenevisibleiO70258. MM.

Interactioni

Protein-protein interaction databases

BioGridi203196. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliO70258.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi235 – 341107Cys-richAdd
BLAST

Sequence similaritiesi

Belongs to the sarcoglycan alpha/epsilon family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG323743.
GeneTreeiENSGT00390000005672.
HOGENOMiHOG000074154.
HOVERGENiHBG006891.
InParanoidiO70258.
OMAiVEKRNMQ.
OrthoDBiEOG7MD4PV.
PhylomeDBiO70258.
TreeFamiTF314655.

Family and domain databases

InterProiIPR006644. Cadg.
IPR008908. Sarcoglycan_alpha/epsilon.
IPR030775. SGCE.
[Graphical view]
PANTHERiPTHR10132. PTHR10132. 1 hit.
PTHR10132:SF13. PTHR10132:SF13. 1 hit.
PfamiPF05510. Sarcoglycan_2. 1 hit.
[Graphical view]
SMARTiSM00736. CADG. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O70258-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLLFWWWELG DPCAWTGKGR GTLKMSPATT GTFLLTVYTL FSKVHSDRNV
60 70 80 90 100
YPSAGVLFVH VLEREYFKGE FPPYPKPGEV SNDPITFNTN LMGYPDRPGW
110 120 130 140 150
LRYIQRTPYS DGVLYGSPTA ENVGKPTIIE ITAYNRRTFE TARHNLIINI
160 170 180 190 200
MSAEEFPLPY QAEFFIKNMN VEEMLASEVL GDFLGAVKNV WQPERLNAIN
210 220 230 240 250
ITSALDRGGR VPLPINDMKE GVYVMVGADV AFSSCLREVE NPQNQLRCSQ
260 270 280 290 300
EMEPVITCDK KFRTHFHIDW CKISLVDKTK QVSTYQEVVR GEGILPDGGE
310 320 330 340 350
YKPPSDSLKS RDYYTDFLVT LAVPSAVALV LFLILAYIMC CRREGVEKRD
360 370 380 390 400
MQTPDIQLVH HSSIQKSTKE LRDMSKNREI AWPLSTLPVF HPVTGEVIPP
410 420 430
THTDNYDSTN MPLMQAQQNL PHQTQIPQPQ TTGKWYP
Length:437
Mass (Da):49,736
Last modified:July 7, 2009 - v2
Checksum:iA294007261593637
GO
Isoform 2 (identifier: O70258-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     36-36: T → TAFLLSCADGINGTVNWKTKQASSFSISRKLAAGKKD

Show »
Length:473
Mass (Da):53,532
Checksum:iDCAE4D4FFA879CA6
GO

Sequence cautioni

The sequence AAC14020.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH12665.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAC36184.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti401 – 4011T → M in AAH12665 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei36 – 361T → TAFLLSCADGINGTVNWKTK QASSFSISRKLAAGKKD in isoform 2. 1 PublicationVSP_006019

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC012665 mRNA. Translation: AAH12665.1. Different initiation.
AF031919 mRNA. Translation: AAC14020.1. Different initiation.
AK076102 mRNA. Translation: BAC36184.1. Different initiation.
AF103877 mRNA. Translation: AAF21895.1.
CCDSiCCDS51716.1. [O70258-1]
CCDS51718.1. [O70258-2]
RefSeqiNP_001123660.1. NM_001130188.1. [O70258-2]
NP_001123661.1. NM_001130189.1.
NP_001123662.1. NM_001130190.1.
NP_035490.3. NM_011360.3. [O70258-1]
UniGeneiMm.8739.

Genome annotation databases

EnsembliENSMUST00000115577; ENSMUSP00000111240; ENSMUSG00000004631. [O70258-2]
ENSMUST00000115579; ENSMUSP00000111242; ENSMUSG00000004631. [O70258-1]
GeneIDi20392.
KEGGimmu:20392.
UCSCiuc009avp.2. mouse. [O70258-1]
uc009avq.2. mouse. [O70258-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC012665 mRNA. Translation: AAH12665.1. Different initiation.
AF031919 mRNA. Translation: AAC14020.1. Different initiation.
AK076102 mRNA. Translation: BAC36184.1. Different initiation.
AF103877 mRNA. Translation: AAF21895.1.
CCDSiCCDS51716.1. [O70258-1]
CCDS51718.1. [O70258-2]
RefSeqiNP_001123660.1. NM_001130188.1. [O70258-2]
NP_001123661.1. NM_001130189.1.
NP_001123662.1. NM_001130190.1.
NP_035490.3. NM_011360.3. [O70258-1]
UniGeneiMm.8739.

3D structure databases

ProteinModelPortaliO70258.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203196. 1 interaction.

PTM databases

PhosphoSiteiO70258.

Proteomic databases

MaxQBiO70258.
PaxDbiO70258.
PRIDEiO70258.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000115577; ENSMUSP00000111240; ENSMUSG00000004631. [O70258-2]
ENSMUST00000115579; ENSMUSP00000111242; ENSMUSG00000004631. [O70258-1]
GeneIDi20392.
KEGGimmu:20392.
UCSCiuc009avp.2. mouse. [O70258-1]
uc009avq.2. mouse. [O70258-2]

Organism-specific databases

CTDi8910.
MGIiMGI:1329042. Sgce.

Phylogenomic databases

eggNOGiNOG323743.
GeneTreeiENSGT00390000005672.
HOGENOMiHOG000074154.
HOVERGENiHBG006891.
InParanoidiO70258.
OMAiVEKRNMQ.
OrthoDBiEOG7MD4PV.
PhylomeDBiO70258.
TreeFamiTF314655.

Miscellaneous databases

NextBioi298334.
PROiO70258.
SOURCEiSearch...

Gene expression databases

BgeeiO70258.
CleanExiMM_SGCE.
ExpressionAtlasiO70258. baseline and differential.
GenevisibleiO70258. MM.

Family and domain databases

InterProiIPR006644. Cadg.
IPR008908. Sarcoglycan_alpha/epsilon.
IPR030775. SGCE.
[Graphical view]
PANTHERiPTHR10132. PTHR10132. 1 hit.
PTHR10132:SF13. PTHR10132:SF13. 1 hit.
PfamiPF05510. Sarcoglycan_2. 1 hit.
[Graphical view]
SMARTiSM00736. CADG. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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] (ISOFORM 1).
    Strain: Czech II.
    Tissue: Mammary tumor.
  2. "Epsilon-sarcoglycan, a broadly expressed homologue of the gene mutated in limb-girdle muscular dystrophy 2D."
    Ettinger A.J., Feng G., Sanes J.R.
    J. Biol. Chem. 272:32534-32538(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-437 (ISOFORM 1).
    Tissue: Lung.
  3. Erratum
    Ettinger A.J., Feng G., Sanes J.R.
    J. Biol. Chem. 273:19922-19922(1998)
  4. "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.
    , 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] OF 22-437 (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Embryo.
  5. "Epsilon-sarcoglycan replaces alpha-sarcoglycan in smooth muscle to form a unique dystrophin-glycoprotein complex."
    Straub V., Ettinger A.J., Durbeej M., Venzke D.P., Cutshall S., Sanes J.R., Campbell K.P.
    J. Biol. Chem. 274:27989-27996(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 27-437 (ISOFORM 2).
    Tissue: Lung.
  6. "SGCE missense mutations that cause myoclonus-dystonia syndrome impair epsilon-sarcoglycan trafficking to the plasma membrane: modulation by ubiquitination and torsinA."
    Esapa C.T., Waite A., Locke M., Benson M.A., Kraus M., McIlhinney R.A., Sillitoe R.V., Beesley P.W., Blake D.J.
    Hum. Mol. Genet. 16:327-342(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, GLYCOSYLATION, UBIQUITINATION, MUTAGENESIS OF HIS-60 AND LEU-196.

Entry informationi

Entry nameiSGCE_MOUSE
AccessioniPrimary (citable) accession number: O70258
Secondary accession number(s): Q921G2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: July 7, 2009
Last modified: July 22, 2015
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.