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P82349 (SGCB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Beta-sarcoglycan

Short name=Beta-SG
Alternative name(s):
43 kDa dystrophin-associated glycoprotein
Short name=43DAG
Gene names
Name:Sgcb
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length320 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

Cross-link to form 2 major subcomplexes: one consisting of SGCB, SGCD and SGCG and the other consisting of SGCB and SGCD. The association between SGCB and SGCG is particularly strong while SGCA is loosely associated with the other sarcoglycans. Ref.4

Subcellular location

Cell membranesarcolemma; Single-pass type II membrane protein. Cytoplasmcytoskeleton Ref.4.

Tissue specificity

Most strongly expressed in skeletal and heart muscle. Also detected in proliferating myoblasts.

Post-translational modification

Disulfide bonds are present.

Sequence similarities

Belongs to the sarcoglycan beta/delta/gamma/zeta family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 320320Beta-sarcoglycan
PRO_0000175244

Regions

Topological domain1 – 6767Cytoplasmic Potential
Transmembrane68 – 8821Helical; Signal-anchor for type II membrane protein; Potential
Topological domain89 – 320232Extracellular Potential

Amino acid modifications

Glycosylation1601N-linked (GlcNAc...) Potential
Glycosylation2131N-linked (GlcNAc...) Potential
Glycosylation2601N-linked (GlcNAc...) Potential
Disulfide bond290 ↔ 316 Potential
Disulfide bond292 ↔ 309 Potential

Sequences

Sequence LengthMass (Da)Tools
P82349 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: AFA5E28496003618

FASTA32034,873
        10         20         30         40         50         60 
MAAAAAAAAA TEQQGSNGPV KKSMREKAVE RRNVNKEHNS NFKAGYIPID EDRLHKTGLR 

        70         80         90        100        110        120 
GRKGNLAICV IVLLFILAVI NLLITLVIWA VIRIGPNGCD SMEFHESGLL RFKQVSDMGV 

       130        140        150        160        170        180 
IHPLYKSTVG GRRNENLVIT GNNQPIVFQQ GTTKLSVEKN KTSITSDIGM QFFDPRTHNI 

       190        200        210        220        230        240 
LFSTDYETHE FHLPSGVKSL NVQKASTERI TSNATSDLNI KVDGRAIVRG NEGVFIMGKT 

       250        260        270        280        290        300 
IEFHMGGDVE LKAENSIILN GTVMVSPTRL PSSSSGDQSG SGDWVRYKLC MCADGTLFKV 

       310        320 
QVTGHNMGCQ VSDNPCGNTH 

« Hide

References

« Hide 'large scale' references
[1]"Disruption of the beta-sarcoglycan gene reveals pathogenetic complexity of limb-girdle muscular dystrophy type 2E."
Durbeej M., Campbell K.P.
Mol. Cell 5:141-151(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Developmental expression of sarcoglycan gene products in cultured myocytes."
Noguchi S., Wakabayashi E., Imamura M., Yoshida M., Ozawa E.
Biochem. Biophys. Res. Commun. 262:88-93(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Skeletal muscle.
[3]"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. expand/collapse author list , 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].
Strain: C57BL/6J.
Tissue: Head.
[4]"Molecular organization of sarcoglycan complex in mouse myotubes in culture."
Chan Y.-M., Boennemann C.G., Lidov H.G.W., Kunkel L.M.
J. Cell Biol. 143:2033-2044(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, SUBUNIT, DISULFIDE BONDS.
[5]"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: Testis.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF169288 Genomic DNA. Translation: AAF28458.1.
AB024921 mRNA. Translation: BAA83492.1.
AK014381 mRNA. Translation: BAB29310.1.
AK132306 mRNA. Translation: BAE21093.1.
AK169403 mRNA. Translation: BAE41149.1.
BC052349 mRNA. Translation: AAH52349.1.
RefSeqNP_036020.1. NM_011890.4.
UniGeneMm.89310.

3D structure databases

ProteinModelPortalP82349.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204864. 7 interactions.
IntActP82349. 1 interaction.
MINTMINT-4134438.

PTM databases

PhosphoSiteP82349.

Proteomic databases

PaxDbP82349.
PRIDEP82349.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000081170; ENSMUSP00000079937; ENSMUSG00000029156.
GeneID24051.
KEGGmmu:24051.
UCSCuc008xtb.1. mouse.

Organism-specific databases

CTD6443.
MGIMGI:1346523. Sgcb.

Phylogenomic databases

eggNOGNOG84633.
GeneTreeENSGT00390000008110.
HOGENOMHOG000133159.
HOVERGENHBG004508.
KOK12566.
OMANMGCQTS.
OrthoDBEOG74R1R4.
PhylomeDBP82349.
TreeFamTF313538.

Gene expression databases

BgeeP82349.
GenevestigatorP82349.

Family and domain databases

InterProIPR006875. Sarcoglycan.
IPR027659. Sgcb.
[Graphical view]
PANTHERPTHR21142. PTHR21142. 1 hit.
PfamPF04790. Sarcoglycan_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio303987.
PROP82349.
SOURCESearch...

Entry information

Entry nameSGCB_MOUSE
AccessionPrimary (citable) accession number: P82349
Secondary accession number(s): Q3TEU9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot