SCS22_YEAST
ID SCS22_YEAST Reviewed; 175 AA.
AC Q6Q595; D6VPR2;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Vesicle-associated membrane protein-associated protein SCS22;
DE Short=VAMP-associated protein SCS22;
DE AltName: Full=VAP homolog 2;
GN Name=SCS22; OrderedLocusNames=YBL091C-A;
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].
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.
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 77-175.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP REVISION OF GENE MODEL.
RX PubMed=12844361; DOI=10.1186/gb-2003-4-7-r45;
RA Brachat S., Dietrich F.S., Voegeli S., Zhang Z., Stuart L., Lerch A.,
RA Gates K., Gaffney T.D., Philippsen P.;
RT "Reinvestigation of the Saccharomyces cerevisiae genome annotation by
RT comparison to the genome of a related fungus: Ashbya gossypii.";
RL Genome Biol. 4:R45.1-R45.13(2003).
RN [6]
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 [7]
RP FUNCTION.
RX PubMed=15668246; DOI=10.1074/jbc.m500147200;
RA Loewen C.J.R., Levine T.P.;
RT "A highly conserved binding site in vesicle-associated membrane protein-
RT associated protein (VAP) for the FFAT motif of lipid-binding proteins.";
RL J. Biol. Chem. 280:14097-14104(2005).
CC -!- FUNCTION: Targets proteins containing a FFAT motif to membranes (By
CC similarity). Involved in regulation of phospholipid metabolism.
CC {ECO:0000250, ECO:0000269|PubMed:15668246}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type IV
CC membrane protein {ECO:0000305}.
CC -!- DOMAIN: The MSP domain is required for binding to the FFAT motif of
CC target proteins. {ECO:0000250}.
CC -!- MISCELLANEOUS: Present with 358 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the VAMP-associated protein (VAP) (TC 9.B.17)
CC family. {ECO:0000305}.
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DR EMBL; X79489; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z35852; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z35853; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY558293; AAS56619.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07032.1; -; Genomic_DNA.
DR RefSeq; NP_009461.2; NM_001184321.1.
DR AlphaFoldDB; Q6Q595; -.
DR SMR; Q6Q595; -.
DR BioGRID; 32612; 111.
DR IntAct; Q6Q595; 6.
DR STRING; 4932.YBL091C-A; -.
DR MaxQB; Q6Q595; -.
DR PaxDb; Q6Q595; -.
DR PRIDE; Q6Q595; -.
DR EnsemblFungi; YBL091C-A_mRNA; YBL091C-A; YBL091C-A.
DR GeneID; 852186; -.
DR KEGG; sce:YBL091C-A; -.
DR SGD; S000007228; SCS22.
DR VEuPathDB; FungiDB:YBL091C-A; -.
DR GeneTree; ENSGT00940000172509; -.
DR HOGENOM; CLU_032848_4_0_1; -.
DR InParanoid; Q6Q595; -.
DR OMA; MIEIVPD; -.
DR BioCyc; YEAST:G3O-29247-MON; -.
DR Reactome; R-SCE-9013106; RHOC GTPase cycle.
DR PRO; PR:Q6Q595; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; Q6Q595; protein.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
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:0033149; F:FFAT motif binding; IBA:GO_Central.
DR GO; GO:0090158; P:endoplasmic reticulum membrane organization; IGI:SGD.
DR GO; GO:0061817; P:endoplasmic reticulum-plasma membrane tethering; IBA:GO_Central.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IGI:SGD.
DR GO; GO:0060304; P:regulation of phosphatidylinositol dephosphorylation; IGI:SGD.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR000535; MSP_dom.
DR InterPro; IPR008962; PapD-like_sf.
DR InterPro; IPR016763; VAP.
DR PANTHER; PTHR10809; PTHR10809; 1.
DR Pfam; PF00635; Motile_Sperm; 1.
DR SUPFAM; SSF49354; SSF49354; 1.
DR PROSITE; PS50202; MSP; 1.
PE 1: Evidence at protein level;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..175
FT /note="Vesicle-associated membrane protein-associated
FT protein SCS22"
FT /id="PRO_0000213468"
FT TOPO_DOM 1..154
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT DOMAIN 1..125
FT /note="MSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00132"
FT REGION 133..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 169
FT /note="L -> P (in Ref. 4; AAS56619)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 175 AA; 19678 MW; F738A09B9F94489D CRC64;
MRIVPEKLVF KAPLNKQSTE YIKLENDGEK RVIFKVRTSA PTKYCVRPNV AIIGAHESVN
VQIVFLGLPK STADDEMDQK RDKFLIVTLP IPAAYQNVED GELLSDWPNL EEQYKDDIVF
KKIKIFHSVL PKRKPSGNHD AESARAPSAG NGQSLSSRAL LIITVIALLV GWIYY
