SLP1_YEAST
ID SLP1_YEAST Reviewed; 587 AA.
AC Q12232; D6W2L1;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Uncharacterized protein SLP1 {ECO:0000305};
DE AltName: Full=SUN-like protein 1 {ECO:0000303|PubMed:16923827};
DE Flags: Precursor;
GN Name=SLP1 {ECO:0000303|PubMed:16923827};
GN OrderedLocusNames=YOR154W {ECO:0000312|SGD:S000005680}; ORFNames=O3545;
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=S288c / FY1678;
RX PubMed=9046089;
RX DOI=10.1002/(sici)1097-0061(199701)13:1<73::aid-yea52>3.0.co;2-m;
RA Bordonne R., Camasses A., Madania A., Poch O., Tarassov I.A., Winsor B.,
RA Martin R.P.;
RT "Analysis of a 35.6 kb region on the right arm of Saccharomyces cerevisiae
RT chromosome XV.";
RL Yeast 13:73-83(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
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 SUBCELLULAR LOCATION.
RX PubMed=11935221; DOI=10.1007/s00294-001-0264-9;
RA Terashima H., Fukuchi S., Nakai K., Arisawa M., Hamada K., Yabuki N.,
RA Kitada K.;
RT "Sequence-based approach for identification of cell wall proteins in
RT Saccharomyces cerevisiae.";
RL Curr. Genet. 40:311-316(2002).
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 GENE NAME.
RX PubMed=16923827; DOI=10.1083/jcb.200601062;
RA Jaspersen S.L., Martin A.E., Glazko G., Giddings T.H. Jr., Morgan G.,
RA Mushegian A., Winey M.;
RT "The Sad1-UNC-84 homology domain in Mps3 interacts with Mps2 to connect the
RT spindle pole body with the nuclear envelope.";
RL J. Cell Biol. 174:665-675(2006).
RN [7]
RP FUNCTION.
RX PubMed=19325107; DOI=10.1126/science.1167983;
RA Jonikas M.C., Collins S.R., Denic V., Oh E., Quan E.M., Schmid V.,
RA Weibezahn J., Schwappach B., Walter P., Weissman J.S., Schuldiner M.;
RT "Comprehensive characterization of genes required for protein folding in
RT the endoplasmic reticulum.";
RL Science 323:1693-1697(2009).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH EMP56.
RX PubMed=23275891; DOI=10.1534/g3.112.004614;
RA Friederichs J.M., Gardner J.M., Smoyer C.J., Whetstine C.R., Gogol M.,
RA Slaughter B.D., Jaspersen S.L.;
RT "Genetic analysis of Mps3 SUN domain mutants in Saccharomyces cerevisiae
RT reveals an interaction with the SUN-like protein Slp1.";
RL G3 (Bethesda) 2:1703-1718(2012).
CC -!- FUNCTION: May be involved in membrane protein folding
CC (PubMed:19325107). Required for localization of MPS3 to the nuclear
CC envelope (PubMed:23275891). {ECO:0000269|PubMed:19325107,
CC ECO:0000269|PubMed:23275891}.
CC -!- SUBUNIT: Interacts with EMP65. {ECO:0000269|PubMed:23275891}.
CC -!- INTERACTION:
CC Q12232; P40085: EMP65; NbExp=3; IntAct=EBI-35990, EBI-22717;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:11935221, ECO:0000269|PubMed:23275891}; Single-pass
CC type I membrane protein {ECO:0000255}.
CC -!- MISCELLANEOUS: Present with 3250 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SLP1 family. {ECO:0000305}.
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DR EMBL; U55020; AAC49640.1; -; Genomic_DNA.
DR EMBL; Z75062; CAA99360.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10927.1; -; Genomic_DNA.
DR PIR; S67042; S67042.
DR RefSeq; NP_014797.1; NM_001183573.1.
DR AlphaFoldDB; Q12232; -.
DR SMR; Q12232; -.
DR BioGRID; 34550; 109.
DR DIP; DIP-3829N; -.
DR IntAct; Q12232; 2.
DR STRING; 4932.YOR154W; -.
DR MaxQB; Q12232; -.
DR PaxDb; Q12232; -.
DR PRIDE; Q12232; -.
DR EnsemblFungi; YOR154W_mRNA; YOR154W; YOR154W.
DR GeneID; 854325; -.
DR KEGG; sce:YOR154W; -.
DR SGD; S000005680; SLP1.
DR VEuPathDB; FungiDB:YOR154W; -.
DR eggNOG; KOG1396; Eukaryota.
DR GeneTree; ENSGT00390000013502; -.
DR HOGENOM; CLU_006633_4_1_1; -.
DR InParanoid; Q12232; -.
DR OMA; YVIIELC; -.
DR BioCyc; YEAST:G3O-33671-MON; -.
DR PRO; PR:Q12232; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12232; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0034975; P:protein folding in endoplasmic reticulum; HGI:SGD.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR045120; Suco/Slp1-like.
DR InterPro; IPR012919; SUN_dom.
DR PANTHER; PTHR12953; PTHR12953; 2.
DR Pfam; PF07738; Sad1_UNC; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR PROSITE; PS51469; SUN; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..587
FT /note="Uncharacterized protein SLP1"
FT /id="PRO_0000237659"
FT TOPO_DOM 22..541
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:23275891"
FT TRANSMEM 542..562
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 563..587
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:23275891"
FT DOMAIN 163..331
FT /note="SUN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00802"
FT REGION 44..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 448
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 486
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 587 AA; 67452 MW; 4A457C95124FD0B8 CRC64;
MANRLLIYGL ILWVSIIGSF ALDRNKTAQN AKIGLHDTTV ITTGSTTNVQ KEHSSPLSTG
SLRTHDFRQA SKVDIRQADI RENGERKEQD ALTQPATPRN PGDSSNSFLS FDEWKKVKSK
EHSSGPERHL SRVREPVDPS CYKEKECIGE ELEIDLGFLT NKNEWSEREE NQKGFNEEKD
IEKVYKKKFN YASLDCAATI VKSNPEAIGA TSTLIESKDK YLLNPCSAPQ QFIVIELCED
ILVEEIEIAN YEFFSSTFKR FRVSVSDRIP MVKNEWTILG EFEARNSREL QKFQIHNPQI
WASYLKIEIL SHYEDEFYCP ISLIKVYGKS MMDEFKIDQL KAQEDKEQSI GTNNINNLNE
QNIQDRCNNI ETRLETPNTS NLSDLAGALS CTSKLIPLKF DEFFKVLNAS FCPSKQMISS
SSSSAVPVIP EESIFKNIMK RLSQLETNSS LTVSYIEEQS KLLSKSFEQL EMAHEAKFSH
LVTIFNETMM SNLDLLNNFA NQLKDQSLRI LEEQKLENDK FTNRHLLHLE RLEKEVSFQR
RIVYASFFAF VGLISYLLIT RELYFEDFEE SKNGAIEKAD IVQQAIR
