P38163 (SRO77_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lethal(2) giant larvae protein homolog SRO77

Alternative name(s):
Sodium protection protein 2
Suppressor of RHO3 protein 77

Gene names

Name:	SRO77
Synonyms:	SNI2, SOP2
Ordered Locus Names:	YBL106C
ORF Names:	YBL0806

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	1010 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acts as an allosteric regulator of polarized exocytosis by promoting the targeted fusion of vesicles with the plasma membrane. Involved in maintenance of ion homeostasis in cells exposed to NaCl stress. May be involved in the targeting of the myosin proteins to their intrinsic pathways. Multicopy suppressor of RHO3. May also participate in the maintenance of cell polarity and bud growth. Ref.5 Ref.6
Subunit structure	Interacts with SEC9. Ref.5
Sequence similarities	Belongs to the WD repeat L(2)GL family. Contains 14 WD repeats.

Ontologies

Keywords
Biological process	Exocytosis
Domain	Repeat WD repeat
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	Golgi to plasma membrane transport Inferred from physical interaction Ref.5. Source: SGD exocytosis Inferred from genetic interaction Ref.5. Source: SGD
Cellular component	plasma membrane Inferred from physical interaction Ref.5. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1010	1010	Lethal(2) giant larvae protein homolog SRO77		PRO_0000051221
Regions
	Repeat	47 – 80	34	WD 1
	Repeat	87 – 122	36	WD 2
	Repeat	127 – 163	37	WD 3
	Repeat	182 – 215	34	WD 4
	Repeat	240 – 275	36	WD 5
	Repeat	299 – 364	66	WD 6
	Repeat	372 – 407	36	WD 7
	Repeat	431 – 504	74	WD 8
	Repeat	518 – 595	78	WD 9
	Repeat	602 – 637	36	WD 10
	Repeat	649 – 700	52	WD 11
	Repeat	709 – 763	55	WD 12
	Repeat	768 – 815	48	WD 13
	Repeat	829 – 852	24	WD 14
Amino acid modifications
	Modified residue	744	1	Phosphoserine Ref.7
Experimental info
	Sequence conflict	130	1	I → F in CAA55989. Ref.1
	Sequence conflict	130	1	I → F in CAA84933. Ref.2
	Sequence conflict	135	1	S → P in CAA55989. Ref.1
	Sequence conflict	135	1	S → P in CAA84933. Ref.2
	Sequence conflict	260	1	S → A in CAA55989. Ref.1
	Sequence conflict	260	1	S → A in CAA84933. Ref.2
	Sequence conflict	834	1	G → V in CAA55989. Ref.1
	Sequence conflict	834	1	G → V in CAA84933. Ref.2
	Sequence conflict	858	1	T → S in CAA55989. Ref.1
	Sequence conflict	858	1	T → S in CAA84933. Ref.2
	Sequence conflict	943	1	E → K in CAA55989. Ref.1
	Sequence conflict	943	1	E → K in CAA84933. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P38163 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: 3547845334179A40	FASTA	1,010	111,623
	10 20 30 40 50 60 MFKKSRHLKN VSNAIKSARV HDVSNGINSK FFDTKKICTY GINGRITVTT FDYTQSLLAV 70 80 90 100 110 120 ATTAGEIHVY GQKQIEVVFT LKNRPQIKHM RFIKGIYLIA VDEKSNIIVL SVHSKQILTT 130 140 150 160 170 180 VFCPNSITCI ETDPSLDWML IGLESGSILI YDVDRNQMSK LKIENFQKSV FLPKERLSPV 190 200 210 220 230 240 ISIQWNPRDI GTILISYEHI TVIYSFIDYK VKQHFFYQLE PYAPGGDLST NIEKKRTPKV 250 260 270 280 290 300 IQSLYHPNSL HILTVHEDNS LVFWDVNSGK LIHARSIFET HVNFPNPALK DCSFTETPAI 310 320 330 340 350 360 FKVSWLCQRN PEYTSLLIAT KATENPCLPQ EITMIDLGGT PMYSVTSFDA MSKYYAKPVQ 370 380 390 400 410 420 QKLFSLIGKA PLINFLPLPK ASPYFGGCHD TNLILLLLED GELETLIYPA GSFSSKASIF 430 440 450 460 470 480 PRSLAWVRPT VTTCIAQSVQ KNLWLGMMTI AQSESFLKGG IPATRNIRRH ETRSALLTGH 490 500 510 520 530 540 SNGSVRIWDA SHSEVTDNAV FEVNTAKVLN RATNLAIKNI SFASETLELA VSSEVGDVIL 550 560 570 580 590 600 FKFETNKFYG QLPKSDALQL KFSRFSLDDS KTILVDVSDR GPTNVKQGFI PSTVIHAKKG 610 620 630 640 650 660 AVSAIMNSNI GFVAVGFIEG TLIILDRRGP AIIFNENIRV ISKAGSSYVS TVHFCVMEYG 670 680 690 700 710 720 DDGFSSILML CGTDIGELMT FKILPATNGR FEVKFTDATK TNNQGKILGI NSFAKDTGYS 730 740 750 760 770 780 CSATISKMQG LSKGIAIPGF VTISGANDIR LVSPGKSKDT HALFKYPIAT SGLSFIPIID 790 800 810 820 830 840 GKGERKLSTI MIVLLINGDI KVLTVPELKE VKNLRCPVPL SAQYVENSSI LENGDIVIRT 850 860 870 880 890 900 GKFQASLISV LNESATGTNH TADISQHTPI DTLYNPDLKI GYRPQVNSLQ WARGTIYCTP 910 920 930 940 950 960 YQLDELLGGI ERPESKYEES AIARGCISSS SSNAARKLPP GTEDHRYARP VRSSGRSNGY 970 980 990 1000 1010 GVLKSVSRAI ETRLDTVETT INDYATTMGQ TMNDAMEETG RDMMKSAVGF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence analysis of a 78.6 kb segment of the left end of Saccharomyces cerevisiae chromosome II." Obermaier B., Gassenhuber J., Piravandi E., Domdey H. Yeast 11:1103-1112(1995) [PubMed: 7502586] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	"Complete DNA sequence of yeast chromosome II." Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K. EMBO J. 13:5795-5809(1994) [PubMed: 7813418] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	Saccharomyces Genome Database Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 130; 135; 260; 834; 858 AND 943. Strain: ATCC 204508 / S288c.
[4]	"Sro7p, a Saccharomyces cerevisiae counterpart of the tumor suppressor l(2)gl protein, is related to myosins in function." Kagami M., Toh-e A., Matsui Y. Genetics 149:1717-1727(1998) [PubMed: 9691031] [Abstract] Cited for: CHARACTERIZATION.
[5]	"Yeast homologues of tomosyn and lethal giant larvae function in exocytosis and are associated with the plasma membrane SNARE, Sec9." Lehman K., Rossi G., Adamo J.E., Brennwald P. J. Cell Biol. 146:125-140(1999) [PubMed: 10402465] [Abstract] Cited for: FUNCTION, INTERACTION WITH SEC9.
[6]	"The Saccharomyces cerevisiae SOP1 and SOP2 genes, which act in cation homeostasis, can be functionally substituted by the Drosophila lethal(2)giant larvae tumor suppressor gene." Larsson K., Bohl F., Sjostrom I., Akhtar N., Strand D., Mechler B.M., Grabowski R., Adler L. J. Biol. Chem. 273:33610-33618(1998) [PubMed: 9837945] [Abstract] Cited for: FUNCTION.
[7]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-744, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X79489 Genomic DNA. Translation: CAA55989.1. Z35867 Genomic DNA. Translation: CAA84933.1. BK006936 Genomic DNA. Translation: DAA07017.2.
PIR	S45389.
RefSeq	NP_009444.2. NM_001178346.2.
3D structure databases
ProteinModelPortal	P38163.
SMR	P38163. Positions 28-924.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2947N.
IntAct	P38163. 11 interactions.
MINT	MINT-583073.
STRING	P38163.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	852168.
KEGG	sce:YBL106C.
NMPDR	fig|4932.3.peg.129.
Organism-specific databases
CYGD	YBL106c.
SGD	S000000202. SRO77.
Phylogenomic databases
eggNOG	fuNOG05052.
GeneTree	EFGT00050000006429.
HOGENOM	HBG331004.
OMA	RPPSKRM.
OrthoDB	EOG42Z7ZC.
Gene expression databases
ArrayExpress	P38163.
Genevestigator	P38163.
GermOnline	YBL106C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR013905. Lgl_C. IPR015943. WD40/YVTN_repeat-like_dom. IPR001680. WD40_repeat. IPR011046. WD40_repeat-like_dom. IPR019775. WD40_repeat_CS. IPR017986. WD40_repeat_dom. [Graphical view]
Gene3D	G3DSA:2.130.10.10. WD40/YVTN_repeat-like. 4 hits.
Pfam	PF08596. Lgl_C. 1 hit. [Graphical view]
SMART	SM00320. WD40. 5 hits. [Graphical view]
SUPFAM	SSF50978. WD40_like. 2 hits.
PROSITE	PS00678. WD_REPEATS_1. 2 hits. PS50082. WD_REPEATS_2. 2 hits. PS50294. WD_REPEATS_REGION. 2 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	970611.

Entry information

Entry name

SRO77_YEAST

Accession

Primary (citable) accession number: P38163
Secondary accession number(s): D6VPP7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	July 27, 2011
Last modified:	January 25, 2012
This is version 90 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program