SPO71_YEAST
ID SPO71_YEAST Reviewed; 1245 AA.
AC Q03868; D6VS90;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Prospore membrane adapter protein SPO71 {ECO:0000305};
DE AltName: Full=Sporulation-specific protein 71;
GN Name=SPO71; OrderedLocusNames=YDR104C; ORFNames=YD8557.13c;
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=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 DEVELOPMENTAL STAGE.
RX PubMed=9784122; DOI=10.1126/science.282.5389.699;
RA Chu S., DeRisi J., Eisen M., Mulholland J., Botstein D., Brown P.O.,
RA Herskowitz I.;
RT "The transcriptional program of sporulation in budding yeast.";
RL Science 282:699-705(1998).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=22611022; DOI=10.1128/ec.00076-12;
RA Parodi E.M., Baker C.S., Tetzlaff C., Villahermosa S., Huang L.S.;
RT "SPO71 mediates prospore membrane size and maturation in Saccharomyces
RT cerevisiae.";
RL Eukaryot. Cell 11:1191-1200(2012).
RN [5]
RP FUNCTION, INTERACTION WITH VPS13, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=24036347; DOI=10.1128/ec.00239-13;
RA Park J.S., Okumura Y., Tachikawa H., Neiman A.M.;
RT "SPO71 encodes a developmental stage-specific partner for Vps13 in
RT Saccharomyces cerevisiae.";
RL Eukaryot. Cell 12:1530-1537(2013).
RN [6]
RP INTERACTION WITH VPS13, AND MUTAGENESIS OF 384-PHE--LEU-395 AND
RP 390-PRO--PRO-392.
RX PubMed=30018089; DOI=10.1083/jcb.201804111;
RA Bean B.D.M., Dziurdzik S.K., Kolehmainen K.L., Fowler C.M.S., Kwong W.K.,
RA Grad L.I., Davey M., Schluter C., Conibear E.;
RT "Competitive organelle-specific adaptors recruit Vps13 to membrane contact
RT sites.";
RL J. Cell Biol. 217:3593-3607(2018).
CC -!- FUNCTION: Recruits the lipid transfer protein VPS13 to the prospore
CC membrane during sporulation, thereby aiding prospore membrane
CC formation. {ECO:0000269|PubMed:22611022, ECO:0000269|PubMed:24036347}.
CC -!- SUBUNIT: Interacts (via PxP motif) with VPS13 (via SHR-BD domain);
CC during prospore membrane formation. {ECO:0000269|PubMed:24036347,
CC ECO:0000269|PubMed:30018089}.
CC -!- SUBCELLULAR LOCATION: Prospore membrane {ECO:0000269|PubMed:24036347,
CC ECO:0000305|PubMed:22611022}; Peripheral membrane protein
CC {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expressed during sexual reproduction; expression
CC increases during meiosis II (at protein level).
CC {ECO:0000269|PubMed:22611022, ECO:0000269|PubMed:9784122}.
CC -!- DISRUPTION PHENOTYPE: Abnormal prospore membrane formation
CC (PubMed:22611022, PubMed:24036347). Abolishes localization of VPS13 to
CC the prospore membrane (PubMed:24036347). Accumulation of vesicles
CC within the prospore membrane lumen and reduction of
CC phosphatidylinositol in the membrane (PubMed:24036347). Abnormal spore
CC wall formation; the first three layers are synthesized but abnormally
CC deposited and the dityrosine layer is missing (PubMed:22611022).
CC Sporulation specific septins are mislocalized (PubMed:22611022).
CC {ECO:0000269|PubMed:22611022, ECO:0000269|PubMed:24036347}.
CC -!- SIMILARITY: Belongs to the SPO71 family. {ECO:0000305}.
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DR EMBL; Z47746; CAA87680.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11950.1; -; Genomic_DNA.
DR PIR; S51255; S51255.
DR RefSeq; NP_010389.3; NM_001180412.3.
DR AlphaFoldDB; Q03868; -.
DR BioGRID; 32161; 58.
DR IntAct; Q03868; 4.
DR MINT; Q03868; -.
DR STRING; 4932.YDR104C; -.
DR iPTMnet; Q03868; -.
DR PaxDb; Q03868; -.
DR PRIDE; Q03868; -.
DR EnsemblFungi; YDR104C_mRNA; YDR104C; YDR104C.
DR GeneID; 851681; -.
DR KEGG; sce:YDR104C; -.
DR SGD; S000002511; SPO71.
DR VEuPathDB; FungiDB:YDR104C; -.
DR eggNOG; ENOG502QRAT; Eukaryota.
DR HOGENOM; CLU_003938_1_0_1; -.
DR InParanoid; Q03868; -.
DR OMA; GRSMVFM; -.
DR BioCyc; YEAST:G3O-29706-MON; -.
DR PRO; PR:Q03868; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q03868; protein.
DR GO; GO:0005628; C:prospore membrane; IDA:SGD.
DR GO; GO:0043495; F:protein-membrane adaptor activity; IMP:UniProtKB.
DR GO; GO:0032120; P:ascospore-type prospore membrane formation; IMP:UniProtKB.
DR GO; GO:1902657; P:protein localization to prospore membrane; IDA:SGD.
DR InterPro; IPR040345; Mug56/Spo71.
DR InterPro; IPR039486; Mug56/Spo71_PH.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR029217; Spo7_2_N.
DR PANTHER; PTHR28076; PTHR28076; 1.
DR Pfam; PF15404; PH_4; 1.
DR Pfam; PF15407; Spo7_2_N; 1.
DR SMART; SM00233; PH; 2.
DR SMART; SM01316; Spo7_2_N; 1.
PE 1: Evidence at protein level;
KW Membrane; Reference proteome; Sporulation.
FT CHAIN 1..1245
FT /note="Prospore membrane adapter protein SPO71"
FT /id="PRO_0000072140"
FT DOMAIN 1030..1229
FT /note="PH"
FT REGION 207..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1154..1192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 385..399
FT /note="PxP"
FT /evidence="ECO:0000269|PubMed:30018089"
FT COMPBIAS 207..246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1177..1192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 384..395
FT /note="Missing: Disrupts interaction with VPS13."
FT /evidence="ECO:0000269|PubMed:30018089"
FT MUTAGEN 390..392
FT /note="PWP->AWA: Disrupts interaction with VPS13."
FT /evidence="ECO:0000269|PubMed:30018089"
SQ SEQUENCE 1245 AA; 145181 MW; 39B1FD4192BF4692 CRC64;
MDSIVNVVED DVKYAQRVTS FSSPQNANVK VFTIPRHSFT AFRLSYVSPT ELSACSQVTL
LGGIPKQWYA DQNNQVWKLL TKISLRKVRK QSDMLRRYGY GTIYKKRVGK IPTALYLRKH
FTWSYEDNTS IHNGHRLKEA EMEMKRTRSS PVQKSEYKLS LPRRCRSSSD QNFMRQELLK
EKKSELSRNN SLPLIDTAQA VDIHPVLHEE DQENTNKRNK SLLSNLKRKD LGESKSISRK
DYSHFDRIPS PSSARSVGET DFNYNREPSE DTLRYPDSII EVTNRTSPAP NSILSRSGQF
VNSNDLSDGF STSNTINNVG LNANEKIFFN ALQSMEKENL MLWKTSQKYG TYLDERRKSA
DAFQKRERGS CVDIGKLHSS HLPFINILPP WPTELTEEER IIHDRLASKH SHHIRKHVHN
ARNKTSCKIK DSVGTFLGMT NSLTNKATVK KRTGQILKKE KMLVMVKEAI QNKVPLPNFS
ENECFDTRVS ERWKEYIVIA RSTGRFDPPI LLQFYRHRHI PEIEDISSIA TKYHRNPLDF
FLSRNCIVKF YSSLDKTISI QKPDKRLGGF IDESIEKKDE LKHYSPIKIF ILRCSSIRSS
GRWYKFLLES LDRQLFTPAI NLKIPLTEIS IKINLNEIIF QKLIDLGKQE KDRLKICFLQ
RGYKIFQHPI LRYFTVAILE KLKLAHYDYL IRKWDTENPV LGCALKRYDR LEWIPCDEDS
LVTGIFAFCQ SHLIQYRPIA NRLRETKSLE GKCLKEPTPI EGFLIRLTDK YGSARTNFGK
YSISTAYFFT CENLLFSMKA YRANPPLPID SMIDDTSTEI EKEEIWKQWK KIPEVYEQQP
YPLDTNDHIE WMNCQTTQSE YDSRDFYAFH CFHRRIDQIL KTDNVIDLTE VKDIYQGTRT
DYEADKIKYG VYKEASEIFW HRNYEIDDVS RSVINIETSN GLLLKLLATS ATVAEEWVIK
LKQMISYWKN KQREDTERLL KIRRSNAGLL MLNGEEETKI GENTLRWIVE HGRADEQTFN
ANGISLSRPL IQKGPLYQKP HKHSVFSKYY VVLISGFIVL FHCFHRSTTG FAKEVLEYAH
YVTIPIDDCY LYSGTTTELD LLQRDRTFDE INYGSHALPR VYGDGWRSVE DESSRCFTLW
FGTRRALSSN RLQKKGNEKQ YTQDYGRQDN NIDPPSAPEA DLNNSNVPSN TDKIHFTKKL
GVSGKSMVFM ARSRQERDLW VMSIYYELER LRRTASTSNS RNQTM
