SGCE_MOUSE
ID SGCE_MOUSE Reviewed; 437 AA.
AC O70258; Q921G2;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Epsilon-sarcoglycan;
DE Short=Epsilon-SG;
GN Name=Sgce;
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] (ISOFORM 1).
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-437 (ISOFORM 1).
RC TISSUE=Lung;
RX PubMed=9405466; DOI=10.1074/jbc.272.51.32534;
RA Ettinger A.J., Feng G., Sanes J.R.;
RT "Epsilon-sarcoglycan, a broadly expressed homologue of the gene mutated in
RT limb-girdle muscular dystrophy 2D.";
RL J. Biol. Chem. 272:32534-32538(1997).
RN [3]
RP ERRATUM OF PUBMED:9405466.
RA Ettinger A.J., Feng G., Sanes J.R.;
RL J. Biol. Chem. 273:19922-19922(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 22-437 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 27-437 (ISOFORM 2).
RC TISSUE=Lung;
RX PubMed=10488149; DOI=10.1074/jbc.274.39.27989;
RA Straub V., Ettinger A.J., Durbeej M., Venzke D.P., Cutshall S., Sanes J.R.,
RA Campbell K.P.;
RT "Epsilon-sarcoglycan replaces alpha-sarcoglycan in smooth muscle to form a
RT unique dystrophin-glycoprotein complex.";
RL J. Biol. Chem. 274:27989-27996(1999).
RN [6]
RP SUBCELLULAR LOCATION, GLYCOSYLATION, UBIQUITINATION, AND MUTAGENESIS OF
RP HIS-60 AND LEU-196.
RX PubMed=17200151; DOI=10.1093/hmg/ddl472;
RA Esapa C.T., Waite A., Locke M., Benson M.A., Kraus M., McIlhinney R.A.,
RA Sillitoe R.V., Beesley P.W., Blake D.J.;
RT "SGCE missense mutations that cause myoclonus-dystonia syndrome impair
RT epsilon-sarcoglycan trafficking to the plasma membrane: modulation by
RT ubiquitination and torsinA.";
RL Hum. Mol. Genet. 16:327-342(2007).
CC -!- FUNCTION: Component of the sarcoglycan complex, a subcomplex of the
CC dystrophin-glycoprotein complex which forms a link between the F-actin
CC cytoskeleton and the extracellular matrix.
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
CC {ECO:0000269|PubMed:17200151}; Single-pass membrane protein
CC {ECO:0000269|PubMed:17200151}. Golgi apparatus
CC {ECO:0000269|PubMed:17200151}. Cell projection, dendrite
CC {ECO:0000269|PubMed:17200151}. Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O70258-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O70258-2; Sequence=VSP_006019;
CC -!- TISSUE SPECIFICITY: Identified in all tissues tested. Expression
CC highest in lung and placenta, moderate in brain, heart and skeletal
CC muscle, low in kidney and liver. Also detected in embryo.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:17200151}.
CC -!- PTM: Ubiquitinated, leading to its degradation by the proteasome.
CC {ECO:0000269|PubMed:17200151}.
CC -!- SIMILARITY: Belongs to the sarcoglycan alpha/epsilon family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC14020.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH12665.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC36184.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC012665; AAH12665.1; ALT_INIT; mRNA.
DR EMBL; AF031919; AAC14020.1; ALT_INIT; mRNA.
DR EMBL; AK076102; BAC36184.1; ALT_INIT; mRNA.
DR EMBL; AF103877; AAF21895.1; -; mRNA.
DR CCDS; CCDS51716.1; -. [O70258-1]
DR CCDS; CCDS51718.1; -. [O70258-2]
DR RefSeq; NP_001123660.1; NM_001130188.1. [O70258-2]
DR RefSeq; NP_001123661.1; NM_001130189.1.
DR RefSeq; NP_001123662.1; NM_001130190.1.
DR RefSeq; NP_035490.3; NM_011360.3. [O70258-1]
DR AlphaFoldDB; O70258; -.
DR SMR; O70258; -.
DR BioGRID; 203196; 1.
DR CORUM; O70258; -.
DR STRING; 10090.ENSMUSP00000111242; -.
DR GlyConnect; 2298; 1 N-Linked glycan (1 site).
DR GlyGen; O70258; 1 site, 1 N-linked glycan (1 site).
DR iPTMnet; O70258; -.
DR PhosphoSitePlus; O70258; -.
DR MaxQB; O70258; -.
DR PRIDE; O70258; -.
DR ProteomicsDB; 261334; -. [O70258-1]
DR ProteomicsDB; 261335; -. [O70258-2]
DR Antibodypedia; 30109; 151 antibodies from 26 providers.
DR DNASU; 20392; -.
DR Ensembl; ENSMUST00000115577; ENSMUSP00000111240; ENSMUSG00000004631. [O70258-2]
DR Ensembl; ENSMUST00000115579; ENSMUSP00000111242; ENSMUSG00000004631. [O70258-1]
DR GeneID; 20392; -.
DR KEGG; mmu:20392; -.
DR UCSC; uc009avp.2; mouse. [O70258-1]
DR UCSC; uc009avq.2; mouse. [O70258-2]
DR CTD; 8910; -.
DR MGI; MGI:1329042; Sgce.
DR VEuPathDB; HostDB:ENSMUSG00000004631; -.
DR eggNOG; KOG4482; Eukaryota.
DR GeneTree; ENSGT00390000005672; -.
DR InParanoid; O70258; -.
DR OMA; FWESFLM; -.
DR OrthoDB; 534519at2759; -.
DR PhylomeDB; O70258; -.
DR TreeFam; TF314655; -.
DR BioGRID-ORCS; 20392; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Sgce; mouse.
DR PRO; PR:O70258; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; O70258; protein.
DR Bgee; ENSMUSG00000004631; Expressed in placenta labyrinth and 252 other tissues.
DR ExpressionAtlas; O70258; baseline and differential.
DR Genevisible; O70258; MM.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0032590; C:dendrite membrane; IDA:UniProtKB.
DR GO; GO:0016010; C:dystrophin-associated glycoprotein complex; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0016012; C:sarcoglycan complex; IBA:GO_Central.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR InterPro; IPR006644; Cadg.
DR InterPro; IPR008908; Sarcoglycan_alpha/epsilon.
DR InterPro; IPR030775; SGCE.
DR PANTHER; PTHR10132; PTHR10132; 1.
DR PANTHER; PTHR10132:SF17; PTHR10132:SF17; 1.
DR Pfam; PF05510; Sarcoglycan_2; 1.
DR SMART; SM00736; CADG; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Cytoplasm;
KW Cytoskeleton; Glycoprotein; Golgi apparatus; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Ubl conjugation.
FT CHAIN 1..437
FT /note="Epsilon-sarcoglycan"
FT /id="PRO_0000031678"
FT TOPO_DOM 1..317
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 339..437
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 36
FT /note="T -> TAFLLSCADGINGTVNWKTKQASSFSISRKLAAGKKD (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:10488149"
FT /id="VSP_006019"
FT MUTAGEN 60
FT /note="H->P,R: Misfolded, leading to the interaction with
FT TOR1A, ubiquitination and a decrease of the half-life.
FT Impairs intracellular transport. No effect on
FT glycosylation."
FT /evidence="ECO:0000269|PubMed:17200151"
FT MUTAGEN 196
FT /note="L->R: Misfolded, leading to the interaction with
FT TOR1A, ubiquitination and a decrease of the half-life.
FT Impairs intracellular transport. No effect on
FT glycosylation."
FT /evidence="ECO:0000269|PubMed:17200151"
FT CONFLICT 401
FT /note="T -> M (in Ref. 1; AAH12665)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 437 AA; 49736 MW; A294007261593637 CRC64;
MLLFWWWELG DPCAWTGKGR GTLKMSPATT GTFLLTVYTL FSKVHSDRNV YPSAGVLFVH
VLEREYFKGE FPPYPKPGEV SNDPITFNTN LMGYPDRPGW LRYIQRTPYS DGVLYGSPTA
ENVGKPTIIE ITAYNRRTFE TARHNLIINI MSAEEFPLPY QAEFFIKNMN VEEMLASEVL
GDFLGAVKNV WQPERLNAIN ITSALDRGGR VPLPINDMKE GVYVMVGADV AFSSCLREVE
NPQNQLRCSQ EMEPVITCDK KFRTHFHIDW CKISLVDKTK QVSTYQEVVR GEGILPDGGE
YKPPSDSLKS RDYYTDFLVT LAVPSAVALV LFLILAYIMC CRREGVEKRD MQTPDIQLVH
HSSIQKSTKE LRDMSKNREI AWPLSTLPVF HPVTGEVIPP THTDNYDSTN MPLMQAQQNL
PHQTQIPQPQ TTGKWYP
