SIP3_YEAST
ID SIP3_YEAST Reviewed; 1229 AA.
AC P38717; D6W0T6;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Membrane-anchored lipid-binding protein SIP3 {ECO:0000303|PubMed:26001273};
DE AltName: Full=Lipid transfer protein anchored at membrane contact sites 3 {ECO:0000303|PubMed:26001273};
DE AltName: Full=SNF1-interacting protein 3 {ECO:0000303|PubMed:8127709};
GN Name=SIP3 {ECO:0000303|PubMed:8127709};
GN Synonyms=LAM3 {ECO:0000303|PubMed:26001273};
GN OrderedLocusNames=YNL257C {ECO:0000312|SGD:S000005201}; ORFNames=N0844;
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], AND INTERACTION WITH SNF1.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8127709; DOI=10.1093/nar/22.4.597;
RA Lesage P., Yang X., Carlson M.;
RT "Analysis of the SIP3 protein identified in a two-hybrid screen for
RT interaction with the SNF1 protein kinase.";
RL Nucleic Acids Res. 22:597-603(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9234673;
RX DOI=10.1002/(sici)1097-0061(199707)13:9<849::aid-yea106>3.0.co;2-n;
RA Sen-Gupta M., Gueldener U., Beinhauer J.D., Fiedler T.A., Hegemann J.H.;
RT "Sequence analysis of the 33 kb long region between ORC5 and SUI1 from the
RT left arm of chromosome XIV from Saccharomyces cerevisiae.";
RL Yeast 13:849-860(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [4]
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 [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
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).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=26001273; DOI=10.7554/elife.07253;
RA Gatta A.T., Wong L.H., Sere Y.Y., Calderon-Norena D.M., Cockcroft S.,
RA Menon A.K., Levine T.P.;
RT "A new family of StART domain proteins at membrane contact sites has a role
RT in ER-PM sterol transport.";
RL Elife 4:E07253-E07253(2015).
CC -!- FUNCTION: May be involved in sterol transfer between intracellular
CC membranes. {ECO:0000269|PubMed:26001273}.
CC -!- SUBUNIT: Interacts with SNF1. {ECO:0000269|PubMed:8127709}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:26001273}; Single-pass membrane protein
CC {ECO:0000255}. Note=Localizes to puncta in the cell periphery
CC representing cortical endoplasmic reticulum (cER)-plasma membrane (PM)
CC membrane contact sites. {ECO:0000269|PubMed:26001273}.
CC -!- DOMAIN: The VASt domain bind sterols. {ECO:0000250|UniProtKB:P38800}.
CC -!- MISCELLANEOUS: Present with 432 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SIP3 family. {ECO:0000305}.
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DR EMBL; U03376; AAA17885.1; -; Genomic_DNA.
DR EMBL; X96722; CAA65487.1; -; Genomic_DNA.
DR EMBL; Z71533; CAA96164.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10302.1; -; Genomic_DNA.
DR PIR; S42391; S42391.
DR RefSeq; NP_014142.1; NM_001183095.1.
DR AlphaFoldDB; P38717; -.
DR BioGRID; 35582; 68.
DR DIP; DIP-780N; -.
DR STRING; 4932.YNL257C; -.
DR TCDB; 9.B.198.1.2; the membrane-anchored lipid-binding protein (lam) family.
DR iPTMnet; P38717; -.
DR MaxQB; P38717; -.
DR PaxDb; P38717; -.
DR PRIDE; P38717; -.
DR EnsemblFungi; YNL257C_mRNA; YNL257C; YNL257C.
DR GeneID; 855464; -.
DR KEGG; sce:YNL257C; -.
DR SGD; S000005201; SIP3.
DR VEuPathDB; FungiDB:YNL257C; -.
DR eggNOG; ENOG502QU87; Eukaryota.
DR GeneTree; ENSGT00940000154453; -.
DR HOGENOM; CLU_001720_0_0_1; -.
DR InParanoid; P38717; -.
DR OMA; APGRDCD; -.
DR BioCyc; YEAST:G3O-33253-MON; -.
DR PRO; PR:P38717; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P38717; protein.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:SGD.
DR GO; GO:0003712; F:transcription coregulator activity; IDA:SGD.
DR GO; GO:0032366; P:intracellular sterol transport; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:SGD.
DR CDD; cd07609; BAR_SIP3_fungi; 1.
DR CDD; cd13280; PH_SIP3; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR039463; Sip3/Lam1_BAR.
DR InterPro; IPR042067; Sip3_PH.
DR InterPro; IPR031968; VASt.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF16016; VASt; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS51778; VAST; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..1229
FT /note="Membrane-anchored lipid-binding protein SIP3"
FT /id="PRO_0000097765"
FT TOPO_DOM 1..1066
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258,
FT ECO:0000305|PubMed:26001273"
FT TRANSMEM 1067..1087
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1088..1229
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:16847258"
FT DOMAIN 309..423
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 771..976
FT /note="VASt"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01114"
FT CARBOHYD 1206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1229 AA; 142820 MW; 977995219282CD65 CRC64;
MSVHGRDPKK RQLRLISVAF KEASIDSPSF RASVNFFQTR VDALEDWIEK TVDFFDQKYK
VSFEDFRRAK ETLLSQLLPP PALLSNGFVS NQSFTPRLID SFNKDYYDFS MKLLQIVKGD
DSSHSTALLE LMTTAIEPYR NVRKNFDFYQ GKYDSMLASY QAIRISKTSL EPSSIKSDAL
QLFEVQKNYL KASLDLISAI SAVKLSLDKF ILESMKVLKS RSIFITKDSG RKIDLSPCIN
EYLDNYAIWV ENSIEGSKVL DSDISNAKKQ AYRYTLKRIT PSSDTSDYNI RSIHSSKLLS
KDTQVPPKSP EKSGWLYMKT QVGKPTREIW VRRWCFLKNA VFGMFLLSPS KTYVEETDKF
GVFLTNVRYD PEEDRKFCFE VKIFGNKVTE AHDNMSKDIT LVFQTSNYLD LKSWLIAFEA
TKKYVMSIQH DSLEYELAFK RFSPKFFEFA SSTTTSIDQL ITTFDKETES LYETLNCSIS
EYDILTLGEE KVFQFQMPTT PISTKMTQLA ILSNFLTKGS WFPNAVLANI WGTTDWSEYT
ILPGKGKKPS SLLTIDGKRL PIRNSTIYPQ YYSNELKVLD LQFKSLVFSP DQRLEKLPEE
LLLFKFEALW CPNKKQKFSA TCFCTKDYIY CYMNSMEFIC LTKISLSEIV SVEADRSSKK
TLKLYDASGL QMKAIVLFSD YKLIASKLQY LLENKAIKNP NSNEEILVKF EQMEKESQEK
KQEELYKIEQ ENSFDRKATS VSKIIKSRVT FWEMSDDAST LLNRLKKLQT EYSITYNHEY
EISSKGLAHI LFGDKSNAFP KCLFLARKDG EEHGKRFWYK NKDINGKSQL VRKIPFRLDM
TGNFLNTGKY HRDKESKMIF ATQRIVKIVD NKYYEVDLDP FFVKVPFCHL LKLSIKFVIT
ESYDVDNHLE IKLNMTASSS SLHVLYKLEY IDSRTGKTIE KLSLAEIICQ TWALKFAHSE
FLLIRRVLRY YLEKIGKHGK VIKAIKLCGI LGVLSNKSEE PATEKNGNSK ESESMQYDIR
YSCTILFLVF IKLMVYRVTN LTFVFFRILI GILLLCAEKF SRINRMMVVG LLASIMINIL
LSEKASVPYW SIKRAEKLFH DRLGSDKFTM QRAIYISDSD LLSSQLSVPS NNPIFEKFSE
DNFNKDYQYS ETRKQLAMRR NELLIELRIL QDMEKQLVHD DYEKFLLEEV NKCSMVSIEM
TDLWFNDTQL QNYCSICNEE LEKLRPPIT
