SRO77_YEAST
ID SRO77_YEAST Reviewed; 1010 AA.
AC P38163; D6VPP7;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Lethal(2) giant larvae protein homolog SRO77;
DE AltName: Full=Sodium protection protein 2;
DE AltName: Full=Suppressor of RHO3 protein 77;
GN Name=SRO77; Synonyms=SNI2, SOP2; OrderedLocusNames=YBL106C;
GN ORFNames=YBL0806;
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=7502586; DOI=10.1002/yea.320111112;
RA Obermaier B., Gassenhuber J., Piravandi E., Domdey H.;
RT "Sequence analysis of a 78.6 kb segment of the left end of Saccharomyces
RT cerevisiae chromosome II.";
RL Yeast 11:1103-1112(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [3]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 130; 135; 260; 834; 858 AND
RP 943.
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 CHARACTERIZATION.
RX PubMed=9691031; DOI=10.1093/genetics/149.4.1717;
RA Kagami M., Toh-e A., Matsui Y.;
RT "Sro7p, a Saccharomyces cerevisiae counterpart of the tumor suppressor
RT l(2)gl protein, is related to myosins in function.";
RL Genetics 149:1717-1727(1998).
RN [5]
RP FUNCTION, AND INTERACTION WITH SEC9.
RX PubMed=10402465; DOI=10.1083/jcb.146.1.125;
RA Lehman K., Rossi G., Adamo J.E., Brennwald P.;
RT "Yeast homologues of tomosyn and lethal giant larvae function in exocytosis
RT and are associated with the plasma membrane SNARE, Sec9.";
RL J. Cell Biol. 146:125-140(1999).
RN [6]
RP FUNCTION.
RX PubMed=9837945; DOI=10.1074/jbc.273.50.33610;
RA Larsson K., Bohl F., Sjostrom I., Akhtar N., Strand D., Mechler B.M.,
RA Grabowski R., Adler L.;
RT "The Saccharomyces cerevisiae SOP1 and SOP2 genes, which act in cation
RT homeostasis, can be functionally substituted by the Drosophila
RT lethal(2)giant larvae tumor suppressor gene.";
RL J. Biol. Chem. 273:33610-33618(1998).
CC -!- FUNCTION: Acts as an allosteric regulator of polarized exocytosis by
CC promoting the targeted fusion of vesicles with the plasma membrane.
CC Involved in maintenance of ion homeostasis in cells exposed to NaCl
CC stress. May be involved in the targeting of the myosin proteins to
CC their intrinsic pathways. Multicopy suppressor of RHO3. May also
CC participate in the maintenance of cell polarity and bud growth.
CC {ECO:0000269|PubMed:10402465, ECO:0000269|PubMed:9837945}.
CC -!- SUBUNIT: Interacts with SEC9. {ECO:0000269|PubMed:10402465}.
CC -!- SIMILARITY: Belongs to the WD repeat L(2)GL family. {ECO:0000305}.
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DR EMBL; X79489; CAA55989.1; -; Genomic_DNA.
DR EMBL; Z35867; CAA84933.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07017.2; -; Genomic_DNA.
DR PIR; S45389; S45389.
DR RefSeq; NP_009444.2; NM_001178346.2.
DR AlphaFoldDB; P38163; -.
DR SMR; P38163; -.
DR BioGRID; 32597; 83.
DR DIP; DIP-2947N; -.
DR IntAct; P38163; 11.
DR MINT; P38163; -.
DR STRING; 4932.YBL106C; -.
DR iPTMnet; P38163; -.
DR MaxQB; P38163; -.
DR PaxDb; P38163; -.
DR PRIDE; P38163; -.
DR EnsemblFungi; YBL106C_mRNA; YBL106C; YBL106C.
DR GeneID; 852168; -.
DR KEGG; sce:YBL106C; -.
DR SGD; S000000202; SRO77.
DR VEuPathDB; FungiDB:YBL106C; -.
DR eggNOG; KOG1983; Eukaryota.
DR GeneTree; ENSGT00950000182906; -.
DR HOGENOM; CLU_006030_0_0_1; -.
DR InParanoid; P38163; -.
DR OMA; NSITCIE; -.
DR BioCyc; YEAST:G3O-28990-MON; -.
DR PRO; PR:P38163; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38163; protein.
DR GO; GO:0005935; C:cellular bud neck; HDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IPI:SGD.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0045159; F:myosin II binding; IBA:GO_Central.
DR GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
DR GO; GO:0030010; P:establishment of cell polarity; IBA:GO_Central.
DR GO; GO:0006887; P:exocytosis; IGI:SGD.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; IGI:SGD.
DR GO; GO:0017157; P:regulation of exocytosis; IBA:GO_Central.
DR GO; GO:0050708; P:regulation of protein secretion; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR013905; Lgl_C_dom.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF08596; Lgl_C; 1.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 2.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 1: Evidence at protein level;
KW Exocytosis; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..1010
FT /note="Lethal(2) giant larvae protein homolog SRO77"
FT /id="PRO_0000051221"
FT REPEAT 47..80
FT /note="WD 1"
FT REPEAT 87..122
FT /note="WD 2"
FT REPEAT 127..163
FT /note="WD 3"
FT REPEAT 182..215
FT /note="WD 4"
FT REPEAT 240..275
FT /note="WD 5"
FT REPEAT 299..364
FT /note="WD 6"
FT REPEAT 372..407
FT /note="WD 7"
FT REPEAT 431..504
FT /note="WD 8"
FT REPEAT 518..595
FT /note="WD 9"
FT REPEAT 602..637
FT /note="WD 10"
FT REPEAT 649..700
FT /note="WD 11"
FT REPEAT 709..763
FT /note="WD 12"
FT REPEAT 768..815
FT /note="WD 13"
FT REPEAT 829..852
FT /note="WD 14"
FT REGION 932..958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 130
FT /note="I -> F (in Ref. 1; CAA55989 and 2; CAA84933)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="S -> P (in Ref. 1; CAA55989 and 2; CAA84933)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="S -> A (in Ref. 1; CAA55989 and 2; CAA84933)"
FT /evidence="ECO:0000305"
FT CONFLICT 834
FT /note="G -> V (in Ref. 1; CAA55989 and 2; CAA84933)"
FT /evidence="ECO:0000305"
FT CONFLICT 858
FT /note="T -> S (in Ref. 1; CAA55989 and 2; CAA84933)"
FT /evidence="ECO:0000305"
FT CONFLICT 943
FT /note="E -> K (in Ref. 1; CAA55989 and 2; CAA84933)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1010 AA; 111623 MW; 3547845334179A40 CRC64;
MFKKSRHLKN VSNAIKSARV HDVSNGINSK FFDTKKICTY GINGRITVTT FDYTQSLLAV
ATTAGEIHVY GQKQIEVVFT LKNRPQIKHM RFIKGIYLIA VDEKSNIIVL SVHSKQILTT
VFCPNSITCI ETDPSLDWML IGLESGSILI YDVDRNQMSK LKIENFQKSV FLPKERLSPV
ISIQWNPRDI GTILISYEHI TVIYSFIDYK VKQHFFYQLE PYAPGGDLST NIEKKRTPKV
IQSLYHPNSL HILTVHEDNS LVFWDVNSGK LIHARSIFET HVNFPNPALK DCSFTETPAI
FKVSWLCQRN PEYTSLLIAT KATENPCLPQ EITMIDLGGT PMYSVTSFDA MSKYYAKPVQ
QKLFSLIGKA PLINFLPLPK ASPYFGGCHD TNLILLLLED GELETLIYPA GSFSSKASIF
PRSLAWVRPT VTTCIAQSVQ KNLWLGMMTI AQSESFLKGG IPATRNIRRH ETRSALLTGH
SNGSVRIWDA SHSEVTDNAV FEVNTAKVLN RATNLAIKNI SFASETLELA VSSEVGDVIL
FKFETNKFYG QLPKSDALQL KFSRFSLDDS KTILVDVSDR GPTNVKQGFI PSTVIHAKKG
AVSAIMNSNI GFVAVGFIEG TLIILDRRGP AIIFNENIRV ISKAGSSYVS TVHFCVMEYG
DDGFSSILML CGTDIGELMT FKILPATNGR FEVKFTDATK TNNQGKILGI NSFAKDTGYS
CSATISKMQG LSKGIAIPGF VTISGANDIR LVSPGKSKDT HALFKYPIAT SGLSFIPIID
GKGERKLSTI MIVLLINGDI KVLTVPELKE VKNLRCPVPL SAQYVENSSI LENGDIVIRT
GKFQASLISV LNESATGTNH TADISQHTPI DTLYNPDLKI GYRPQVNSLQ WARGTIYCTP
YQLDELLGGI ERPESKYEES AIARGCISSS SSNAARKLPP GTEDHRYARP VRSSGRSNGY
GVLKSVSRAI ETRLDTVETT INDYATTMGQ TMNDAMEETG RDMMKSAVGF
