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MST27_YEAST
ID   MST27_YEAST             Reviewed;         234 AA.
AC   P53176; D6VU89;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=Multicopy suppressor of SEC21 protein 27;
DE   AltName: Full=DUP240 protein MST27;
DE            Short=Protein DUP2;
GN   Name=MST27; Synonyms=DUP2; OrderedLocusNames=YGL051W;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9234674;
RX   DOI=10.1002/(sici)1097-0061(199707)13:9<861::aid-yea125>3.0.co;2-9;
RA   Feuermann M., de Montigny J., Potier S., Souciet J.-L.;
RT   "The characterization of two new clusters of duplicated genes suggests a
RT   'Lego' organization of the yeast Saccharomyces cerevisiae chromosomes.";
RL   Yeast 13:861-869(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   SUBCELLULAR LOCATION.
RX   PubMed=12101299; DOI=10.1099/00221287-148-7-2111;
RA   Poirey R., Despons L., Leh V., Lafuente M.-J., Potier S., Souciet J.-L.,
RA   Jauniaux J.-C.;
RT   "Functional analysis of the Saccharomyces cerevisiae DUP240 multigene
RT   family reveals membrane-associated proteins that are not essential for cell
RT   viability.";
RL   Microbiology 148:2111-2123(2002).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF 231-LYS-LYS-232, AND
RP   INTERACTION WITH MST28.
RX   PubMed=12925749; DOI=10.1091/mbc.e02-11-0736;
RA   Sandmann T., Herrmann J.M., Dengjel J., Schwarz H., Spang A.;
RT   "Suppression of coatomer mutants by a new protein family with COPI and
RT   COPII binding motifs in Saccharomyces cerevisiae.";
RL   Mol. Biol. Cell 14:3097-3113(2003).
RN   [6]
RP   TOPOLOGY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 208353 / W303-1A;
RX   PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA   Kim H., Melen K., Oesterberg M., von Heijne G.;
RT   "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
CC   -!- FUNCTION: Involved in protein trafficking vesicle formation, probably
CC       by stabilizing of coatomer at the Golgi membrane and thus allowing the
CC       efficient formation of COPI coated vesicles.
CC       {ECO:0000269|PubMed:12925749}.
CC   -!- SUBUNIT: Interacts with MST28. Binds to coatomer proteins of COPI and
CC       SEC23/SEC24 of COPII coated vesicles. {ECO:0000269|PubMed:12925749}.
CC   -!- INTERACTION:
CC       P53176; P39552: MST28; NbExp=4; IntAct=EBI-6205, EBI-20785;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000269|PubMed:12101299, ECO:0000269|PubMed:12925749}. Golgi
CC       apparatus {ECO:0000269|PubMed:12925749}. Cytoplasmic vesicle, COPI-
CC       coated vesicle membrane {ECO:0000269|PubMed:12925749}; Multi-pass
CC       membrane protein {ECO:0000269|PubMed:12925749}. Cytoplasmic vesicle,
CC       COPII-coated vesicle membrane {ECO:0000269|PubMed:12925749}; Multi-pass
CC       membrane protein {ECO:0000269|PubMed:12925749}.
CC   -!- MISCELLANEOUS: Members of the DUP240 multigene family are specific to
CC       S.cerevisiae sensu strictu. Cells lacking all 10 DUP240 proteins show
CC       no obvious alterations in mating, sporulation and cell growth.
CC   -!- SIMILARITY: Belongs to the DUP/COS family. {ECO:0000305}.
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DR   EMBL; Z72574; CAA96754.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08050.1; -; Genomic_DNA.
DR   PIR; S64055; S64055.
DR   RefSeq; NP_011464.1; NM_001180916.1.
DR   AlphaFoldDB; P53176; -.
DR   BioGRID; 33196; 81.
DR   ComplexPortal; CPX-1303; MST27-MST28 vesicle formation complex.
DR   DIP; DIP-1852N; -.
DR   IntAct; P53176; 16.
DR   MINT; P53176; -.
DR   STRING; 4932.YGL051W; -.
DR   MaxQB; P53176; -.
DR   PaxDb; P53176; -.
DR   PRIDE; P53176; -.
DR   EnsemblFungi; YGL051W_mRNA; YGL051W; YGL051W.
DR   GeneID; 852830; -.
DR   KEGG; sce:YGL051W; -.
DR   SGD; S000003019; MST27.
DR   VEuPathDB; FungiDB:YGL051W; -.
DR   eggNOG; ENOG502SSNW; Eukaryota.
DR   GeneTree; ENSGT00940000176285; -.
DR   HOGENOM; CLU_081384_0_1_1; -.
DR   InParanoid; P53176; -.
DR   OMA; IRCHRIA; -.
DR   BioCyc; YEAST:G3O-30561-MON; -.
DR   PRO; PR:P53176; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P53176; protein.
DR   GO; GO:0030663; C:COPI-coated vesicle membrane; IDA:ComplexPortal.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR   GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
DR   GO; GO:0016021; C:integral component of membrane; IDA:SGD.
DR   GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR   GO; GO:0005886; C:plasma membrane; IMP:SGD.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IGI:SGD.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IGI:SGD.
DR   GO; GO:0016050; P:vesicle organization; IDA:ComplexPortal.
DR   InterPro; IPR001142; DUP/COS.
DR   Pfam; PF00674; DUP; 1.
PE   1: Evidence at protein level;
KW   Cytoplasmic vesicle; Endoplasmic reticulum; ER-Golgi transport;
KW   Golgi apparatus; Membrane; Phosphoprotein; Protein transport;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..234
FT                   /note="Multicopy suppressor of SEC21 protein 27"
FT                   /id="PRO_0000207525"
FT   TOPO_DOM        1..47
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        48..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        69..72
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        73..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        94..234
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          231..234
FT                   /note="COPI binding"
FT   MOD_RES         3
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P39552"
FT   MUTAGEN         231..232
FT                   /note="KK->AA: Abolishes binding to COPI coatomer complex."
FT                   /evidence="ECO:0000269|PubMed:12925749"
SQ   SEQUENCE   234 AA;  27241 MW;  ACABFFB30C3C23D2 CRC64;
     MQTPLESTDV KLDTLNEPSA HLIEKNVALP KDIFRSYLSY WIYEIARYTP VMILSLVIGV
     LVLLIIFFND NEACVFNSAY YAYLSLVVLL IILGDGNPKL VSRRNFRTEL LVDVITRKPA
     VEGKEWRIIT YNMNQYLFNH GQWHTPYYFY SDEDCYRYFL RLVEGVTPKK QTATSIGNSP
     VTAKPEDAIE SASPSSRLNY RNFLLKAAEI ERQAQENYWR RRHPNIDALL KKTE
 
 
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