SGCZ_MOUSE
ID SGCZ_MOUSE Reviewed; 311 AA.
AC Q8BX51; Q3UVZ2; Q8K1E7;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Zeta-sarcoglycan;
DE Short=Zeta-SG;
DE AltName: Full=ZSG1;
GN Name=Sgcz;
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 [MRNA] (ISOFORMS 1 AND 2), AND ALTERNATIVE INITIATION.
RC STRAIN=C57BL/6J; TISSUE=Heart, and Skeletal muscle;
RX PubMed=12189167; DOI=10.1093/hmg/11.18.2147;
RA Wheeler M.T., Zarnegar S., McNally E.M.;
RT "Zeta-sarcoglycan, a novel component of the sarcoglycan complex, is reduced
RT in muscular dystrophy.";
RL Hum. Mol. Genet. 11:2147-2154(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Svensson R.U., Groh S.C., Campbell K.P.;
RT "Cloning and characterization of zeta-sarcoglycan: new insights into the
RT structure of the sarcoglycan complex.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Diencephalon;
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).
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. May play a role in the
CC maintenance of striated muscle membrane stability.
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BX51-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BX51-2; Sequence=VSP_018885;
CC -!- TISSUE SPECIFICITY: Expressed in the heart, skeletal muscle and
CC arterial vascular smooth muscle.
CC -!- SIMILARITY: Belongs to the sarcoglycan beta/delta/gamma/zeta family.
CC {ECO:0000305}.
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DR EMBL; AY095374; AAM23275.1; -; mRNA.
DR EMBL; AY250713; AAP76378.1; -; mRNA.
DR EMBL; AK048960; BAC33500.1; -; mRNA.
DR EMBL; AK136779; BAE23127.1; -; mRNA.
DR CCDS; CCDS22251.2; -. [Q8BX51-1]
DR RefSeq; NP_665840.2; NM_145841.2. [Q8BX51-1]
DR RefSeq; XP_006509183.1; XM_006509120.3. [Q8BX51-1]
DR RefSeq; XP_011240440.1; XM_011242138.1. [Q8BX51-2]
DR AlphaFoldDB; Q8BX51; -.
DR BioGRID; 232651; 2.
DR CORUM; Q8BX51; -.
DR STRING; 10090.ENSMUSP00000113912; -.
DR GlyGen; Q8BX51; 2 sites.
DR PhosphoSitePlus; Q8BX51; -.
DR PaxDb; Q8BX51; -.
DR PRIDE; Q8BX51; -.
DR ProteomicsDB; 257216; -. [Q8BX51-1]
DR ProteomicsDB; 257217; -. [Q8BX51-2]
DR Antibodypedia; 2695; 21 antibodies from 11 providers.
DR DNASU; 244431; -.
DR Ensembl; ENSMUST00000118896; ENSMUSP00000113912; ENSMUSG00000039539. [Q8BX51-1]
DR GeneID; 244431; -.
DR KEGG; mmu:244431; -.
DR UCSC; uc009lme.2; mouse. [Q8BX51-1]
DR CTD; 137868; -.
DR MGI; MGI:2388820; Sgcz.
DR VEuPathDB; HostDB:ENSMUSG00000039539; -.
DR eggNOG; KOG3950; Eukaryota.
DR GeneTree; ENSGT00940000157146; -.
DR HOGENOM; CLU_043450_0_0_1; -.
DR InParanoid; Q8BX51; -.
DR OMA; NHLPRTE; -.
DR OrthoDB; 1407024at2759; -.
DR PhylomeDB; Q8BX51; -.
DR TreeFam; TF313538; -.
DR BioGRID-ORCS; 244431; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Sgcz; mouse.
DR PRO; PR:Q8BX51; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8BX51; protein.
DR Bgee; ENSMUSG00000039539; Expressed in striatum and 17 other tissues.
DR ExpressionAtlas; Q8BX51; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0016012; C:sarcoglycan complex; IDA:MGI.
DR GO; GO:0042383; C:sarcolemma; IBA:GO_Central.
DR GO; GO:0048738; P:cardiac muscle tissue development; IBA:GO_Central.
DR GO; GO:0060047; P:heart contraction; IBA:GO_Central.
DR GO; GO:0061024; P:membrane organization; TAS:MGI.
DR InterPro; IPR006875; Sarcoglycan.
DR InterPro; IPR039972; Sarcoglycan_gamma/delta/zeta.
DR InterPro; IPR027662; Sgcz.
DR PANTHER; PTHR12939; PTHR12939; 1.
DR PANTHER; PTHR12939:SF5; PTHR12939:SF5; 1.
DR Pfam; PF04790; Sarcoglycan_1; 1.
PE 2: Evidence at transcript level;
KW Alternative initiation; Cell membrane; Cytoplasm; Cytoskeleton;
KW Disulfide bond; Glycoprotein; Membrane; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..311
FT /note="Zeta-sarcoglycan"
FT /id="PRO_0000031679"
FT TOPO_DOM 1..50
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 51..71
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 72..311
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 285..301
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..13
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12189167,
FT ECO:0000303|PubMed:16141072, ECO:0000303|Ref.2"
FT /id="VSP_018885"
FT CONFLICT 274
FT /note="N -> D (in Ref. 1; AAM23275)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 311 AA; 34461 MW; 1F85C0B347810E2B CRC64;
MDRSTDLDIQ ELKMTREQYI LATQQNNLPR PENAQLYPVG IYGWRKRCLY FFVLLLLVTM
IVNLAMTIWI LKVMNFTVDG MGNLRVTKKG IRLEGISEFL LPLYVKEIHS RKDSPLVLQS
DRNVTVNARN HMGQLTGQLT VGAEAVEAQC KRFEVRASED GRVLFSADED EITIGAEKLK
VTGTEGAVFG HSVETPHIRA EPSQDLRLES PTRSLKMEAP RGVQVSAAAG DFKATCRKEL
HLQSTEGEIF LNADSIRLGN LPIGSFSSST SSSNSRQTVY ELCVCPNGKL YLSPAGVGST
CQSSSSICLW N
