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SMA2_YEAST
ID   SMA2_YEAST              Reviewed;         369 AA.
AC   Q04658; D6VZA7;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Spore membrane assembly protein 2;
GN   Name=SMA2; OrderedLocusNames=YML066C;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(1997).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [4]
RP   FUNCTION.
RX   PubMed=11470404; DOI=10.1016/s0960-9822(01)00274-3;
RA   Rabitsch K.P., Toth A., Galova M., Schleiffer A., Schaffner G., Aigner E.,
RA   Rupp C., Penkner A.M., Moreno-Borchart A.C., Primig M., Esposito R.E.,
RA   Klein F., Knop M., Nasmyth K.;
RT   "A screen for genes required for meiosis and spore formation based on
RT   whole-genome expression.";
RL   Curr. Biol. 11:1001-1009(2001).
RN   [5]
RP   FUNCTION.
RX   PubMed=12432101; DOI=10.1073/pnas.202604399;
RA   Deutschbauer A.M., Williams R.M., Chu A.M., Davis R.W.;
RT   "Parallel phenotypic analysis of sporulation and postgermination growth in
RT   Saccharomyces cerevisiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:15530-15535(2002).
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).
RN   [7]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=17298976; DOI=10.1242/jcs.03405;
RA   Nakanishi H., Suda Y., Neiman A.M.;
RT   "Erv14 family cargo receptors are necessary for ER exit during sporulation
RT   in Saccharomyces cerevisiae.";
RL   J. Cell Sci. 120:908-916(2007).
CC   -!- FUNCTION: Involved in spore and ascus formation. Required for the
CC       efficient assembly of the precursors of the prospore membrane to a
CC       continuous prospore membrane. {ECO:0000269|PubMed:11470404,
CC       ECO:0000269|PubMed:12432101, ECO:0000269|PubMed:17298976}.
CC   -!- SUBCELLULAR LOCATION: Prospore membrane {ECO:0000269|PubMed:17298976};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:17298976}. Endoplasmic
CC       reticulum {ECO:0000269|PubMed:17298976}. Note=Localizes to prospore
CC       membrane, and accumulates in the endoplasmic reticulum in vegetative
CC       and sporulating ERV14-deleted cells.
CC   -!- SIMILARITY: Belongs to the SMA2 family. {ECO:0000305}.
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DR   EMBL; Z38114; CAA86255.1; -; Genomic_DNA.
DR   EMBL; AY557993; AAS56319.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA09831.1; -; Genomic_DNA.
DR   PIR; S48332; S48332.
DR   RefSeq; NP_013645.1; NM_001182425.1.
DR   AlphaFoldDB; Q04658; -.
DR   BioGRID; 35100; 220.
DR   IntAct; Q04658; 3.
DR   MINT; Q04658; -.
DR   STRING; 4932.YML066C; -.
DR   PaxDb; Q04658; -.
DR   PRIDE; Q04658; -.
DR   EnsemblFungi; YML066C_mRNA; YML066C; YML066C.
DR   GeneID; 854936; -.
DR   KEGG; sce:YML066C; -.
DR   SGD; S000004531; SMA2.
DR   VEuPathDB; FungiDB:YML066C; -.
DR   eggNOG; ENOG502QW7F; Eukaryota.
DR   HOGENOM; CLU_776604_0_0_1; -.
DR   InParanoid; Q04658; -.
DR   OMA; TIDMGWS; -.
DR   BioCyc; YEAST:G3O-32661-MON; -.
DR   PRO; PR:Q04658; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; Q04658; protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; HDA:SGD.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005628; C:prospore membrane; IDA:SGD.
DR   GO; GO:0032120; P:ascospore-type prospore membrane formation; IMP:SGD.
DR   GO; GO:0070583; P:spore membrane bending pathway; IMP:SGD.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Membrane; Reference proteome; Sporulation;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..369
FT                   /note="Spore membrane assembly protein 2"
FT                   /id="PRO_0000203252"
FT   TOPO_DOM        1..6
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        28..220
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        221..241
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        242..265
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        266..286
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        287..319
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        320..340
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        341..369
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          348..369
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   369 AA;  40872 MW;  37CA79238F4CCAEF CRC64;
     MLFPKRLIVW GVLLILSLSQ FVLYLPATTC TNSKGLRLCA PQFTITVIGG SSTANEFIAS
     VREFLRLISY LTIDMGWSNE FTDPSVYEDE NLVDTFQPDK VFELNYFGFC KRSNKSKVYC
     TSNENYGMDV LEVLVRDVGI QLGNISTTRS NETKKFGDSL VLTYRLALTS IRDFLKHDKH
     TGNALSKALI GSPDPNVKGV SPTKNYLKGV NLAFILMMFN GMVFYFAVLE IIVGFLSICV
     VSAFGGALSV GKRHRLFPML LKSSSSILVV IATLTILCNI VYLIALKTLE PEEVTDVGSD
     NAAVHTTGWE LLKVNVGSGF IMGLARYAIQ WVLLVLAFLA ANHYKAKPKK SDKYTEDTSN
     SPSPDLMEK
 
 
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