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   24-JAN-2024, entry version 135.
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   GlyCosmos; Q8BX51; 2 sites, No reported glycans.
DR   GlyGen; Q8BX51; 2 sites.
DR   PhosphoSitePlus; Q8BX51; -.
DR   PaxDb; 10090-ENSMUSP00000113912; -.
DR   ProteomicsDB; 257216; -. [Q8BX51-1]
DR   ProteomicsDB; 257217; -. [Q8BX51-2]
DR   Antibodypedia; 2695; 26 antibodies from 12 providers.
DR   DNASU; 244431; -.
DR   Ensembl; ENSMUST00000118896.2; ENSMUSP00000113912.2; ENSMUSG00000039539.14. [Q8BX51-1]
DR   GeneID; 244431; -.
DR   KEGG; mmu:244431; -.
DR   UCSC; uc009lme.2; mouse. [Q8BX51-1]
DR   AGR; MGI:2388820; -.
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; FQMTREQ; -.
DR   OrthoDB; 2913504at2759; -.
DR   PhylomeDB; Q8BX51; -.
DR   TreeFam; TF313538; -.
DR   BioGRID-ORCS; 244431; 2 hits in 76 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 cell types or 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: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   PANTHER; PTHR12939; SARCOGLYCAN; 1.
DR   PANTHER; PTHR12939:SF5; ZETA-SARCOGLYCAN; 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
//