SMA2_YEAS7
ID SMA2_YEAS7 Reviewed; 369 AA.
AC A6ZLZ9;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 37.
DE RecName: Full=Spore membrane assembly protein 2;
GN Name=SMA2; ORFNames=SCY_4111;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Prospore membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}.
CC Note=Localizes to prospore membrane, and accumulates in the endoplasmic
CC reticulum in vegetative and sporulating ERV14-deleted cells.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SMA2 family. {ECO:0000305}.
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DR EMBL; AAFW02000020; EDN64329.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZLZ9; -.
DR EnsemblFungi; EDN64329; EDN64329; SCY_4111.
DR HOGENOM; CLU_776604_0_0_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005628; C:prospore membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Membrane; Sporulation; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..369
FT /note="Spore membrane assembly protein 2"
FT /id="PRO_0000324504"
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; 40826 MW; ACAD49EA08E734BC CRC64;
MLFPKRLIVW GVLLILSLSQ FVLYLPATTC TNSKGLRLCA PQFTITVIGG SSTANEFIAS
VREFLRLISY LTIDMGWSNE FTDPSVYEDE NLVDTFQPDK VFELNYFGFC KRSNKSKVYC
TSNENYGMDV LEVLVRDVGI QLGNISTTRS NETKKFGDSL VLTYRLALTS IRDFLKHDKH
TGNALSKALI GSPDPNVKGA SPTKNYLKGV NLAFILMMFN GMVFYFAVLE IIVGFLSICV
VSAFGGALSV GKRHRLFPIL LKSSSSILVV IATLTILCNI VYLIALKTLE PEEVTDVGSD
NAAVHTTGWE LLKVNVGSGF IMGLARYAIQ WVLLVLAFLA ANHYKAKPKK SDKYTEDTSN
SPSPDLMEK