SPO75_YEAST
ID SPO75_YEAST Reviewed; 868 AA.
AC Q07798; D6VXZ8;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Sporulation-specific protein 75;
GN Name=SPO75; OrderedLocusNames=YLL005C; ORFNames=L1361;
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].
RX PubMed=8810043;
RX DOI=10.1002/(sici)1097-0061(19960615)12:7<693::aid-yea956>3.0.co;2-g;
RA Miosga T., Zimmermann F.K.;
RT "Sequence analysis of the CEN12 region of Saccharomyces cerevisiae on a
RT 43.7 kb fragment of chromosome XII including an open reading frame
RT homologous to the human cystic fibrosis transmembrane conductance regulator
RT protein CFTR.";
RL Yeast 12:693-708(1996).
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
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=15590821; DOI=10.1128/ec.3.6.1464-1475.2004;
RA Coluccio A., Bogengruber E., Conrad M.N., Dresser M.E., Briza P.,
RA Neiman A.M.;
RT "Morphogenetic pathway of spore wall assembly in Saccharomyces
RT cerevisiae.";
RL Eukaryot. Cell 3:1464-1475(2004).
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: Acts as an osmosensitive calcium-permeable cation channel (By
CC similarity). Required for spore wall assembly and ascus formation.
CC {ECO:0000250, ECO:0000269|PubMed:11470404,
CC ECO:0000269|PubMed:15590821}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the CSC1 (TC 1.A.17) family. {ECO:0000305}.
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DR EMBL; X91488; CAA62764.1; -; Genomic_DNA.
DR EMBL; Z73110; CAA97448.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09314.1; -; Genomic_DNA.
DR PIR; S64747; S64747.
DR RefSeq; NP_013096.1; NM_001181825.1.
DR AlphaFoldDB; Q07798; -.
DR SMR; Q07798; -.
DR BioGRID; 31246; 90.
DR DIP; DIP-8843N; -.
DR IntAct; Q07798; 3.
DR MINT; Q07798; -.
DR STRING; 4932.YLL005C; -.
DR TCDB; 1.A.17.5.7; the calcium-dependent chloride channel (ca-clc) family.
DR PaxDb; Q07798; -.
DR PRIDE; Q07798; -.
DR EnsemblFungi; YLL005C_mRNA; YLL005C; YLL005C.
DR GeneID; 850655; -.
DR KEGG; sce:YLL005C; -.
DR SGD; S000003928; SPO75.
DR VEuPathDB; FungiDB:YLL005C; -.
DR eggNOG; KOG1134; Eukaryota.
DR HOGENOM; CLU_002458_2_0_1; -.
DR InParanoid; Q07798; -.
DR OMA; WINIVGR; -.
DR BioCyc; YEAST:G3O-32110-MON; -.
DR PRO; PR:Q07798; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q07798; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005227; F:calcium activated cation channel activity; IBA:GO_Central.
DR GO; GO:0030437; P:ascospore formation; IMP:SGD.
DR GO; GO:0030476; P:ascospore wall assembly; IMP:SGD.
DR InterPro; IPR045122; Csc1-like.
DR InterPro; IPR032880; Csc1_N.
DR InterPro; IPR003864; RSN1_7TM.
DR PANTHER; PTHR13018; PTHR13018; 1.
DR Pfam; PF02714; RSN1_7TM; 1.
DR Pfam; PF13967; RSN1_TM; 1.
PE 1: Evidence at protein level;
KW Calcium; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Reference proteome; Sporulation; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..868
FT /note="Sporulation-specific protein 75"
FT /id="PRO_0000072143"
FT TOPO_DOM 1..34
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 56..127
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 149..187
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..481
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 482..502
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 503..527
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 528..548
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 549..569
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 570..590
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 591..611
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 612..632
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 633..660
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 661..683
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 684..692
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 693..713
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 714..730
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 731..751
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 752..753
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 754..774
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 775..868
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 2
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 503
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 868 AA; 102170 MW; 10E4B5B8C7580653 CRC64;
MNATKELTFN LLNKFQDKER FGSAQRHAGI SLKGFISGIL FSFLYFLFQL SLFIILRSRF
KTIYQANVVL KIHPGSKVCF AKKKIKNYWS LFAFLKQLPG RMLDPMEKFE RNERYGLDNY
LFLRFLKLLI FFFAVLSIIN IPILIPIHYF SRDILKENEG ERYEQSFRTT SKLDKWTMSN
LSPNSSNTLI CHLFLSIFVV LWFHFILSSE LRFVNRLGYS VLTKSKYQNI LYLEGFSSKL
VTQSISLETF FQPLHSDCFG VTHFIPKNLK KVHKLEIKLN KLQKSKEQII FEIILEKYFR
RVSIHRHLIA NHKRFFFSKL KNHLLFQYKK LVFLTQFRIS YYCTKIRLRW KKSSIFPLYY
PKLYVNTETI LERKYRILDK IIRKEKLIKF QVNSLKATSE TKQALPDDLS SGTDIYMDKM
FITFKSTLLS NVIGELLSYR LPTQNLKVII GPNVNDIIWR NILDSSPLWK SAKYFSANIL
RIFVIIGWIL PVAFLGLISQ IPNISSLIPF TKIIHFQSPF IREVAKNLIP IVTLIIIIEI
VPYFFRWLSY LRGLKTGAQI EADVQNWYFV FVFIHLFVVV TISSGFSIII ERLLNNPVSI
PALLANDLPK CANFFCSFVL IRGMAYAGGN LLRIKELLFE LFYYKWKRST PHAQFKRLKT
SLFFQLGSIY PIFSVLGCIG IIYSVVAPII LLLCCISFSM VFFSFSYLFK YQYNKENYSE
TFGKLYIQAL MQLYAGIYFM EFCLLGLFTL FDQYTLSTIM LVVFALTVIT HSKISKQIKS
KPQRIPTLEY LSNLTEERKD QFCQESYTFH DIFSICRNSD EIWLPRDKLG ISEEEQSFLE
KSYHLKFDLN MYSMNLFGDC HLENSHLH
