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YNT4_YEAST
ID   YNT4_YEAST              Reviewed;         301 AA.
AC   P40169; D6W0Z3;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Uncharacterized plasma membrane protein YNL194C;
GN   OrderedLocusNames=YNL194C; ORFNames=N1394;
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=ATCC 96604 / S288c / FY1679;
RX   PubMed=7725799; DOI=10.1002/yea.320101213;
RA   Jonniaux J.-L., Coster F., Purnelle B., Goffeau A.;
RT   "A 21.7 kb DNA segment on the left arm of yeast chromosome XIV carries
RT   WHI3, GCR2, SPX18, SPX19, an homologue to the heat shock gene SSB1 and 8
RT   new open reading frames of unknown function.";
RL   Yeast 10:1639-1645(1994).
RN   [2]
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   [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   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=11784867; DOI=10.1128/mcb.22.3.927-934.2002;
RA   Young M.E., Karpova T.S., Bruegger B., Moschenross D.M., Wang G.K.,
RA   Schneiter R., Wieland F.T., Cooper J.A.;
RT   "The Sur7p family defines novel cortical domains in Saccharomyces
RT   cerevisiae, affects sphingolipid metabolism, and is involved in
RT   sporulation.";
RL   Mol. Cell. Biol. 22:927-934(2002).
RN   [5]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(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).
CC   -!- FUNCTION: Involved in sporulation and affects the sphingolipid
CC       composition of the plasma membrane. {ECO:0000269|PubMed:11784867}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11784867,
CC       ECO:0000269|PubMed:14562095}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:11784867, ECO:0000269|PubMed:14562095}.
CC   -!- SIMILARITY: Belongs to the SUR7 family. {ECO:0000305}.
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DR   EMBL; X78898; CAA55514.1; -; Genomic_DNA.
DR   EMBL; Z71470; CAA96088.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10359.1; -; Genomic_DNA.
DR   PIR; S50737; S50737.
DR   RefSeq; NP_014205.1; NM_001183032.1.
DR   AlphaFoldDB; P40169; -.
DR   BioGRID; 35639; 88.
DR   DIP; DIP-4465N; -.
DR   IntAct; P40169; 2.
DR   MINT; P40169; -.
DR   STRING; 4932.YNL194C; -.
DR   PaxDb; P40169; -.
DR   PRIDE; P40169; -.
DR   EnsemblFungi; YNL194C_mRNA; YNL194C; YNL194C.
DR   GeneID; 855527; -.
DR   KEGG; sce:YNL194C; -.
DR   SGD; S000005138; YNL194C.
DR   VEuPathDB; FungiDB:YNL194C; -.
DR   eggNOG; ENOG502RKFF; Eukaryota.
DR   GeneTree; ENSGT00940000176556; -.
DR   HOGENOM; CLU_059603_0_0_1; -.
DR   InParanoid; P40169; -.
DR   OMA; WIALTFQ; -.
DR   BioCyc; YEAST:G3O-33204-MON; -.
DR   PRO; PR:P40169; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P40169; protein.
DR   GO; GO:0005938; C:cell cortex; IDA:SGD.
DR   GO; GO:0071944; C:cell periphery; HDA:SGD.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045121; C:membrane raft; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; HDA:SGD.
DR   GO; GO:0030437; P:ascospore formation; IMP:SGD.
DR   GO; GO:0030866; P:cortical actin cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR   GO; GO:0031505; P:fungal-type cell wall organization; IBA:GO_Central.
DR   GO; GO:0032185; P:septin cytoskeleton organization; IBA:GO_Central.
DR   InterPro; IPR009571; SUR7/Rim9-like_fungi.
DR   Pfam; PF06687; SUR7; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..301
FT                   /note="Uncharacterized plasma membrane protein YNL194C"
FT                   /id="PRO_0000203399"
FT   TOPO_DOM        1..5
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        27..112
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        113..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        134..143
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        144..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        165..191
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        192..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        213..301
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          254..301
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        274..291
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   301 AA;  34081 MW;  A62F153F41B36174 CRC64;
     MSYKKFVYFI NLFFLLGATL LTFFLILAGG RTTGVLKNFY WFQASTSGFN SAPSVTRWYN
     YNWCGWESRG IAVNCSSKMA AQPFSPRDNF GSSPLMPSTF LNNRNAYYYL SRVGWAMLLI
     GLFFLLITLV SVIASLIRYN RRTAALATAM SWITLFFITL SACLYTGCYA KAVKAFHHEN
     RDARLGPKNF GLIWTTVFLL IVNAICCTIM VATHKRNEYI YDRSFASTKT VDSQTPTPVP
     TNGGIPSSVP VTEVQQSQSH QNHRFFKKLR TKKRTVTSAG DEPDRVQEER VYTEQNVPVV
     S
 
 
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