SGCE_HUMAN
ID SGCE_HUMAN Reviewed; 437 AA.
AC O43556; B2R8N2; D6W5Q8; E9PF60; G5E9K6; Q6L8P0; Q75MH8; Q8NFG8; Q8WW28;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 6.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Epsilon-sarcoglycan;
DE Short=Epsilon-SG;
GN Name=SGCE; Synonyms=ESG; ORFNames=UNQ433/PRO840;
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 [MRNA] (ISOFORM 1).
RC TISSUE=Heart;
RX PubMed=9475163; DOI=10.1016/s0014-5793(97)01593-7;
RA McNally E.M., Ly C.T., Kunkel L.M.;
RT "Human epsilon-sarcoglycan is highly related to alpha-sarcoglycan
RT (adhalin), the limb girdle muscular dystrophy 2D gene.";
RL FEBS Lett. 422:27-32(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Heart;
RA Nigro V.;
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Dagvadorj A.;
RT "Epsilon-sarcoglycan mutations in three ethnically diverse families
RT segregating Myoclonus-Dystonia.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain cortex;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS SER-49 AND
RP HIS-399.
RC TISSUE=Testis;
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 [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 14-437 (ISOFORM 2), AND ALTERNATIVE SPLICING.
RC TISSUE=Brain;
RX PubMed=15193417; DOI=10.1016/j.molbrainres.2004.01.012;
RA Nishiyama A., Endo T., Takeda S., Imamura M.;
RT "Identification and characterization of epsilon-sarcoglycans in the central
RT nervous system.";
RL Brain Res. Mol. Brain Res. 125:1-12(2004).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 293-437 (ISOFORM 1).
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 [11]
RP ERRATUM OF PUBMED:9405466.
RA Ettinger A.J., Feng G., Sanes J.R.;
RL J. Biol. Chem. 273:19922-19922(1998).
RN [12]
RP INVOLVEMENT IN DYT11.
RX PubMed=11528394; DOI=10.1038/ng709;
RA Zimprich A., Grabowski M., Asmus F., Naumann M., Berg D., Bertram M.,
RA Scheidtmann K., Kern P., Winkelmann J., Muller-Myhsok B., Riedel L.,
RA Bauer M., Muller T., Castro M., Meitinger T., Strom T.M., Gasser T.;
RT "Mutations in the gene encoding epsilon-sarcoglycan cause myoclonus-
RT dystonia syndrome.";
RL Nat. Genet. 29:66-69(2001).
RN [13]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-200.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [14]
RP VARIANT DYT11 ARG-196.
RX PubMed=12402271; DOI=10.1002/ana.10358;
RA Klein C., Liu L., Doheny D., Kock N., Muller B., de Carvalho Aguiar P.,
RA Leung J., de Leon D., Bressman S.B., Silverman J., Smith C., Danisi F.,
RA Morrison C., Walker R.H., Velickovic M., Schwinger E., Kramer P.L.,
RA Breakefield X.O., Brin M.F., Ozelius L.J.;
RT "Epsilon-sarcoglycan mutations found in combination with other dystonia
RT gene mutations.";
RL Ann. Neurol. 52:675-679(2002).
RN [15]
RP VARIANT DYT11 ARG-60.
RX PubMed=15258227; DOI=10.1136/jnnp.2003.027177;
RA Schule B., Kock N., Svetel M., Dragasevic N., Hedrich K.,
RA De Carvalho Aguiar P., Liu L., Kabakci K., Garrels J., Meyer E.M.,
RA Berisavac I., Schwinger E., Kramer P.L., Ozelius L.J., Klein C., Kostic V.;
RT "Genetic heterogeneity in ten families with myoclonus-dystonia.";
RL J. Neurol. Neurosurg. Psych. 75:1181-1185(2004).
RN [16]
RP VARIANT DYT11 PRO-60.
RX PubMed=15079037; DOI=10.1212/01.wnl.0000118286.75059.35;
RA Hedrich K., Meyer E.M., Schule B., Kock N., de Carvalho Aguiar P.,
RA Wiegers K., Koelman J.H., Garrels J., Durr R., Liu L., Schwinger E.,
RA Ozelius L.J., Landwehrmeyer B., Stoessl A.J., Tijssen M.A., Klein C.;
RT "Myoclonus-dystonia: detection of novel, recurrent, and de novo SGCE
RT mutations.";
RL Neurology 62:1229-1231(2004).
RN [17]
RP VARIANTS DYT11 THR-92; CYS-115 AND TYR-271.
RX PubMed=16227522; DOI=10.1136/jmg.2005.036780;
RA Tezenas du Montcel S., Clot F., Vidailhet M., Roze E., Damier P.,
RA Jedynak C.P., Camuzat A., Lagueny A., Vercueil L., Doummar D.,
RA Guyant-Marechal L., Houeto J.L., Ponsot G., Thobois S., Cournelle M.A.,
RA Durr A., Durif F., Echenne B., Hannequin D., Tranchant C., Brice A.;
RT "Epsilon sarcoglycan mutations and phenotype in French patients with
RT myoclonic syndromes.";
RL J. Med. Genet. 43:394-400(2006).
RN [18]
RP VARIANT DYT11 ARG-112.
RX PubMed=17853490; DOI=10.1002/mds.21715;
RA Nardocci N., Zorzi G., Barzaghi C., Zibordi F., Ciano C., Ghezzi D.,
RA Garavaglia B.;
RT "Myoclonus-dystonia syndrome: clinical presentation, disease course, and
RT genetic features in 11 families.";
RL Mov. Disord. 23:28-34(2008).
RN [19]
RP VARIANTS DYT11 ARG-36 AND PRO-184.
RX PubMed=18175340; DOI=10.1002/mds.21785;
RA Raymond D., Saunders-Pullman R., de Carvalho Aguiar P., Schule B., Kock N.,
RA Friedman J., Harris J., Ford B., Frucht S., Heiman G.A., Jennings D.,
RA Doheny D., Brin M.F., de Leon Brin D., Multhaupt-Buell T., Lang A.E.,
RA Kurlan R., Klein C., Ozelius L., Bressman S.;
RT "Phenotypic spectrum and sex effects in eleven myoclonus-dystonia families
RT with epsilon-sarcoglycan mutations.";
RL Mov. Disord. 23:588-592(2008).
RN [20]
RP VARIANTS DYT11 GLY-100 AND CYS-115.
RX PubMed=18362280; DOI=10.1212/01.wnl.0000297516.98574.c0;
RA Roze E., Apartis E., Clot F., Dorison N., Thobois S., Guyant-Marechal L.,
RA Tranchant C., Damier P., Doummar D., Bahi-Buisson N., Andre-Obadia N.,
RA Maltete D., Echaniz-Laguna A., Pereon Y., Beaugendre Y., Dupont S.,
RA De Greslan T., Jedynak C.P., Ponsot G., Dussaule J.C., Brice A., Durr A.,
RA Vidailhet M.;
RT "Myoclonus-dystonia: clinical and electrophysiologic pattern related to
RT SGCE mutations.";
RL Neurology 70:1010-1016(2008).
RN [21]
RP VARIANTS DYT11 SER-175; CYS-177 AND ARG-270.
RX PubMed=19066193; DOI=10.1136/jnnp.2008.162099;
RA Ritz K., Gerrits M.C., Foncke E.M., van Ruissen F., van der Linden C.,
RA Vergouwen M.D., Bloem B.R., Vandenberghe W., Crols R., Speelman J.D.,
RA Baas F., Tijssen M.A.;
RT "Myoclonus-dystonia: clinical and genetic evaluation of a large cohort.";
RL J. Neurol. Neurosurg. Psych. 80:653-658(2009).
RN [22]
RP CHARACTERIZATION OF VARIANTS DYT11 ARG-60; PRO-60; THR-92; CYS-115; ARG-270
RP AND TYR-271.
RX PubMed=21796726; DOI=10.1002/humu.21561;
RA Waite A., De Rosa M.C., Brancaccio A., Blake D.J.;
RT "A gain-of-glycosylation mutation associated with myoclonus-dystonia
RT syndrome affects trafficking and processing of mouse epsilon-sarcoglycan in
RT the late secretory pathway.";
RL Hum. Mutat. 32:1246-1258(2011).
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 {ECO:0000250}; Single-
CC pass membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Golgi apparatus
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=epsilon-SG1;
CC IsoId=O43556-1; Sequence=Displayed;
CC Name=2; Synonyms=epsilon-SG2;
CC IsoId=O43556-3; Sequence=VSP_045092, VSP_045093;
CC Name=3;
CC IsoId=O43556-4; Sequence=VSP_054079;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- PTM: Ubiquitinated, leading to its degradation by the proteasome.
CC {ECO:0000250}.
CC -!- DISEASE: Dystonia 11, myoclonic (DYT11) [MIM:159900]: A myoclonic
CC dystonia. Dystonia is defined by the presence of sustained involuntary
CC muscle contractions, often leading to abnormal postures. DYT11 is
CC characterized by involuntary lightning jerks and dystonic movements and
CC postures alleviated by alcohol. Inheritance is autosomal dominant. The
CC age of onset, pattern of body involvement, presence of myoclonus and
CC response to alcohol are all variable. {ECO:0000269|PubMed:11528394,
CC ECO:0000269|PubMed:12402271, ECO:0000269|PubMed:15079037,
CC ECO:0000269|PubMed:15258227, ECO:0000269|PubMed:16227522,
CC ECO:0000269|PubMed:17853490, ECO:0000269|PubMed:18175340,
CC ECO:0000269|PubMed:18362280, ECO:0000269|PubMed:19066193,
CC ECO:0000269|PubMed:21796726}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 2]: Brain-specific. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the sarcoglycan alpha/epsilon family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC04368.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD21206.1; 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; AF036364; AAC04368.1; ALT_INIT; mRNA.
DR EMBL; AJ000534; CAA04167.1; -; mRNA.
DR EMBL; AF516515; AAM64204.1; -; mRNA.
DR EMBL; AY359042; AAQ89401.1; -; mRNA.
DR EMBL; AK313438; BAG36229.1; -; mRNA.
DR EMBL; AC069292; AAS07485.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76784.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76785.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76786.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76788.1; -; Genomic_DNA.
DR EMBL; BC021709; AAH21709.1; -; mRNA.
DR EMBL; AB117974; BAD21206.1; ALT_INIT; mRNA.
DR EMBL; AF031920; AAC14021.1; -; mRNA.
DR CCDS; CCDS47642.1; -. [O43556-3]
DR CCDS; CCDS47643.1; -. [O43556-4]
DR CCDS; CCDS5637.1; -. [O43556-1]
DR RefSeq; NP_001092870.1; NM_001099400.1. [O43556-3]
DR RefSeq; NP_001092871.1; NM_001099401.1. [O43556-4]
DR RefSeq; NP_001288068.1; NM_001301139.1.
DR RefSeq; NP_003910.1; NM_003919.2. [O43556-1]
DR AlphaFoldDB; O43556; -.
DR BioGRID; 114424; 22.
DR CORUM; O43556; -.
DR IntAct; O43556; 11.
DR STRING; 9606.ENSP00000398930; -.
DR GlyConnect; 1218; 2 N-Linked glycans (1 site).
DR GlyGen; O43556; 1 site, 2 N-linked glycans (1 site).
DR iPTMnet; O43556; -.
DR PhosphoSitePlus; O43556; -.
DR SwissPalm; O43556; -.
DR BioMuta; SGCE; -.
DR EPD; O43556; -.
DR jPOST; O43556; -.
DR MassIVE; O43556; -.
DR MaxQB; O43556; -.
DR PeptideAtlas; O43556; -.
DR PRIDE; O43556; -.
DR ProteomicsDB; 20035; -.
DR ProteomicsDB; 33967; -.
DR ProteomicsDB; 49048; -. [O43556-1]
DR Antibodypedia; 30109; 151 antibodies from 26 providers.
DR DNASU; 8910; -.
DR Ensembl; ENST00000445866.7; ENSP00000398930.2; ENSG00000127990.19. [O43556-4]
DR Ensembl; ENST00000642933.1; ENSP00000496237.1; ENSG00000127990.19. [O43556-3]
DR Ensembl; ENST00000648936.2; ENSP00000497130.1; ENSG00000127990.19. [O43556-1]
DR GeneID; 8910; -.
DR KEGG; hsa:8910; -.
DR MANE-Select; ENST00000648936.2; ENSP00000497130.1; NM_003919.3; NP_003910.1.
DR UCSC; uc003unl.3; human. [O43556-1]
DR CTD; 8910; -.
DR DisGeNET; 8910; -.
DR GeneCards; SGCE; -.
DR GeneReviews; SGCE; -.
DR HGNC; HGNC:10808; SGCE.
DR HPA; ENSG00000127990; Low tissue specificity.
DR MalaCards; SGCE; -.
DR MIM; 159900; phenotype.
DR MIM; 604149; gene.
DR neXtProt; NX_O43556; -.
DR OpenTargets; ENSG00000127990; -.
DR Orphanet; 36899; Myoclonus-dystonia syndrome.
DR PharmGKB; PA35719; -.
DR VEuPathDB; HostDB:ENSG00000127990; -.
DR eggNOG; KOG4482; Eukaryota.
DR GeneTree; ENSGT00390000005672; -.
DR InParanoid; O43556; -.
DR OrthoDB; 534519at2759; -.
DR PhylomeDB; O43556; -.
DR TreeFam; TF314655; -.
DR PathwayCommons; O43556; -.
DR SignaLink; O43556; -.
DR BioGRID-ORCS; 8910; 38 hits in 1074 CRISPR screens.
DR ChiTaRS; SGCE; human.
DR GeneWiki; SGCE; -.
DR GenomeRNAi; 8910; -.
DR Pharos; O43556; Tbio.
DR PRO; PR:O43556; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; O43556; protein.
DR Bgee; ENSG00000127990; Expressed in tendon of biceps brachii and 205 other tissues.
DR ExpressionAtlas; O43556; baseline and differential.
DR Genevisible; O43556; HS.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0032590; C:dendrite membrane; ISS:UniProtKB.
DR GO; GO:0016010; C:dystrophin-associated glycoprotein complex; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0016012; C:sarcoglycan complex; IBA:GO_Central.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0007160; P:cell-matrix adhesion; TAS:ProtInc.
DR GO; GO:0007517; P:muscle organ development; TAS:ProtInc.
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; Disease variant; Dystonia; Glycoprotein; Golgi apparatus;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT CHAIN 1..437
FT /note="Epsilon-sarcoglycan"
FT /id="PRO_0000031677"
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:0000269|PubMed:19159218"
FT VAR_SEQ 347..355
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15193417"
FT /id="VSP_045092"
FT VAR_SEQ 418
FT /note="Q -> QWSFAPVAQAGVQWSDLGSLQPPPPR (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_054079"
FT VAR_SEQ 434..437
FT /note="KWYP -> DFRLTTFQRFEVNGIPEERKLTEAMNL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15193417"
FT /id="VSP_045093"
FT VARIANT 36
FT /note="T -> R (in DYT11)"
FT /evidence="ECO:0000269|PubMed:18175340"
FT /id="VAR_066732"
FT VARIANT 49
FT /note="N -> S (in dbSNP:rs11548284)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_058088"
FT VARIANT 60
FT /note="H -> P (in DYT11; affects protein stability; the
FT mutant undergoes endoplasmic reticulum-associated
FT degradation)"
FT /evidence="ECO:0000269|PubMed:15079037,
FT ECO:0000269|PubMed:21796726"
FT /id="VAR_066733"
FT VARIANT 60
FT /note="H -> R (in DYT11; affects protein stability; the
FT mutant undergoes endoplasmic reticulum-associated
FT degradation)"
FT /evidence="ECO:0000269|PubMed:15258227,
FT ECO:0000269|PubMed:21796726"
FT /id="VAR_066734"
FT VARIANT 92
FT /note="M -> T (in DYT11; results in gain-of-glycosylation;
FT the mutant is targeted to the plasma membrane at reduced
FT levels compared to wild-type)"
FT /evidence="ECO:0000269|PubMed:16227522,
FT ECO:0000269|PubMed:21796726"
FT /id="VAR_066735"
FT VARIANT 100
FT /note="W -> G (in DYT11)"
FT /evidence="ECO:0000269|PubMed:18362280"
FT /id="VAR_066736"
FT VARIANT 112
FT /note="G -> R (in DYT11)"
FT /evidence="ECO:0000269|PubMed:17853490"
FT /id="VAR_066737"
FT VARIANT 115
FT /note="Y -> C (in DYT11; affects protein stability; the
FT mutant undergoes endoplasmic reticulum-associated
FT degradation)"
FT /evidence="ECO:0000269|PubMed:16227522,
FT ECO:0000269|PubMed:18362280, ECO:0000269|PubMed:21796726"
FT /id="VAR_066738"
FT VARIANT 175
FT /note="L -> S (in DYT11)"
FT /evidence="ECO:0000269|PubMed:19066193"
FT /id="VAR_066739"
FT VARIANT 177
FT /note="S -> C (in DYT11)"
FT /evidence="ECO:0000269|PubMed:19066193"
FT /id="VAR_066740"
FT VARIANT 184
FT /note="L -> P (in DYT11; affects protein stability; the
FT mutant undergoes endoplasmic reticulum-associated
FT degradation; dbSNP:rs1064794321)"
FT /evidence="ECO:0000269|PubMed:18175340"
FT /id="VAR_066741"
FT VARIANT 196
FT /note="L -> R (in DYT11; dbSNP:rs121908491)"
FT /evidence="ECO:0000269|PubMed:12402271"
FT /id="VAR_026750"
FT VARIANT 270
FT /note="W -> R (in DYT11; affects protein stability; the
FT mutant undergoes endoplasmic reticulum-associated
FT degradation)"
FT /evidence="ECO:0000269|PubMed:19066193,
FT ECO:0000269|PubMed:21796726"
FT /id="VAR_066742"
FT VARIANT 271
FT /note="C -> Y (in DYT11; affects protein stability; the
FT mutant undergoes endoplasmic reticulum-associated
FT degradation; dbSNP:rs372686312)"
FT /evidence="ECO:0000269|PubMed:16227522,
FT ECO:0000269|PubMed:21796726"
FT /id="VAR_066743"
FT VARIANT 399
FT /note="P -> H (in dbSNP:rs17851923)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_058089"
FT CONFLICT 78
FT /note="G -> S (in Ref. 3; AAM64204)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 437 AA; 49851 MW; 0996CB18272DED44 CRC64;
MQLPRWWELG DPCAWTGQGR GTRRMSPATT GTFLLTVYSI FSKVHSDRNV YPSAGVLFVH
VLEREYFKGE FPPYPKPGEI SNDPITFNTN LMGYPDRPGW LRYIQRTPYS DGVLYGSPTA
ENVGKPTIIE ITAYNRRTFE TARHNLIINI MSAEDFPLPY QAEFFIKNMN VEEMLASEVL
GDFLGAVKNV WQPERLNAIN ITSALDRGGR VPLPINDLKE GVYVMVGADV PFSSCLREVE
NPQNQLRCSQ EMEPVITCDK KFRTQFYIDW CKISLVDKTK QVSTYQEVIR GEGILPDGGE
YKPPSDSLKS RDYYTDFLIT LAVPSAVALV LFLILAYIMC CRREGVEKRN MQTPDIQLVH
HSAIQKSTKE LRDMSKNREI AWPLSTLPVF HPVTGEIIPP LHTDNYDSTN MPLMQTQQNL
PHQTQIPQQQ TTGKWYP
