SGCE_PONAB
ID SGCE_PONAB Reviewed; 437 AA.
AC Q5RAP2;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=Epsilon-sarcoglycan {ECO:0000250|UniProtKB:O43556};
DE Short=Epsilon-SG {ECO:0000250|UniProtKB:O43556};
GN Name=SGCE {ECO:0000250|UniProtKB:O43556};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1] {ECO:0000312|EMBL:CAH91168.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney {ECO:0000312|EMBL:CAH91168.1};
RG The German cDNA Consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000250|UniProtKB:O43556}.
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000250}; Single-
CC pass membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P82350}. Cell projection, dendrite
CC {ECO:0000250}. Golgi apparatus {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- PTM: Ubiquitinated, leading to its degradation by the proteasome.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the sarcoglycan alpha/epsilon family.
CC {ECO:0000255}.
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DR EMBL; CR858973; CAH91168.1; -; mRNA.
DR RefSeq; NP_001125684.1; NM_001132212.1.
DR AlphaFoldDB; Q5RAP2; -.
DR SMR; Q5RAP2; -.
DR STRING; 9601.ENSPPYP00000024315; -.
DR GeneID; 100172605; -.
DR KEGG; pon:100172605; -.
DR CTD; 8910; -.
DR eggNOG; KOG4482; Eukaryota.
DR InParanoid; Q5RAP2; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0032590; C:dendrite membrane; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0016012; C:sarcoglycan complex; IEA:InterPro.
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 2: Evidence at transcript level;
KW Cell membrane; Cell projection; Cytoplasm; Cytoskeleton; Glycoprotein;
KW Golgi apparatus; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Ubl conjugation.
FT CHAIN 1..437
FT /note="Epsilon-sarcoglycan"
FT /id="PRO_0000378623"
FT TOPO_DOM 1..317
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:O43556, ECO:0000255"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 339..437
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O43556, ECO:0000255"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 437 AA; 49855 MW; AF85EE96B7B4EE43 CRC64;
MQLPRWWELG DPCAWTGQGR GTRRMSPATT GTFLLTVYSI FSKVHSDRNV YPSAGVLFVH
VLEREYFKGE FPPYPKPGEI SNDPITFNTN LMGYPDRPGW LRYIQRTPYS DGVLYGSPTA
ENVGKPTIIE ITAYNRRTFE TARHNLIINV MSAEDFPLPY QAEFFIKNMN VEEMLASEVL
GDFLGAVKNV WQPERLNAIN ITSALDRGGR VPLPINDLKE GVYVMVGADV PFSSCLREVE
NPQNQLRCSQ EMEPVITCDK KFRTQFYIDW CKISLVDKTK QVSTYQEVIR GEGILPDGGE
YKPPSDSLKS RDYYTDFLIT LAVPSAVALV LFLILAYIMC CRREGVEKRN MQTPDIQLVH
HSAIQKSTKE LRDMSKNREI AWPLSTLPVF HPVTGEMIPP LHTDNYDSTN MPLMQTQQNL
PHQTQIPQQQ TTGKWYP