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LST4_YEAST
ID   LST4_YEAST              Reviewed;         828 AA.
AC   P34239; D6VX24;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Protein LST4;
DE   AltName: Full=Lethal with SEC30 protein 4;
GN   Name=LST4; OrderedLocusNames=YKL176C; ORFNames=YKL642;
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=8154185; DOI=10.1002/yea.320091208;
RA   Wiemann S., Voss H., Schwager C., Rupp T., Stegemann J., Zimmermann J.,
RA   Grothues D., Sensen C., Erfle H., Hewitt N., Banrevi A., Ansorge W.;
RT   "Sequencing and analysis of 51.6 kilobases on the left arm of chromosome XI
RT   from Saccharomyces cerevisiae reveals 23 open reading frames including the
RT   FAS1 gene.";
RL   Yeast 9:1343-1348(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8196765; DOI=10.1038/369371a0;
RA   Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA   Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA   Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA   Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA   Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA   Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA   Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA   Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA   Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA   Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA   Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA   Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA   Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA   Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA   Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA   Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA   Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA   Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA   Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA   van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA   von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA   Becker I., Mewes H.-W.;
RT   "Complete DNA sequence of yeast chromosome XI.";
RL   Nature 369:371-378(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 1-306.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8091858; DOI=10.1002/yea.320100004;
RA   Vandenbol M., Bolle P.-A., Dion C., Portetelle D., Hilger F.;
RT   "Sequencing and analysis of a 20.5 kb DNA segment located on the left arm
RT   of yeast chromosome XI.";
RL   Yeast 10:S25-S33(1994).
RN   [5]
RP   FUNCTION.
RX   PubMed=9409822; DOI=10.1093/genetics/147.4.1569;
RA   Roberg K.J., Bickel S., Rowley N., Kaiser C.A.;
RT   "Control of amino acid permease sorting in the late secretory pathway of
RT   Saccharomyces cerevisiae by SEC13, LST4, LST7 and LST8.";
RL   Genetics 147:1569-1584(1997).
RN   [6]
RP   FUNCTION.
RX   PubMed=11352928; DOI=10.1083/jcb.153.4.649;
RA   Helliwell S.B., Losko S., Kaiser C.A.;
RT   "Components of a ubiquitin ligase complex specify polyubiquitination and
RT   intracellular trafficking of the general amino acid permease.";
RL   J. Cell Biol. 153:649-662(2001).
RN   [7]
RP   FUNCTION.
RX   PubMed=16641373; DOI=10.1091/mbc.e05-07-0669;
RA   Rubio-Texeira M., Kaiser C.A.;
RT   "Amino acids regulate retrieval of the yeast general amino acid permease
RT   from the vacuolar targeting pathway.";
RL   Mol. Biol. Cell 17:3031-3050(2006).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
RN   [10]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=32801125; DOI=10.1242/jcs.245555;
RA   Uemura S., Mochizuki T., Amemiya K., Kurosaka G., Yazawa M., Nakamoto K.,
RA   Ishikawa Y., Izawa S., Abe F.;
RT   "Amino acid homeostatic control by TORC1 in Saccharomyces cerevisiae under
RT   high hydrostatic pressure.";
RL   J. Cell Sci. 133:jcs245555-jcs245555(2020).
CC   -!- FUNCTION: Involved in extracellular amino acid uptake. Required for the
CC       trafficking of the GAP1 nitrogen-regulated general amino acid permease
CC       from the Golgi to the plasma membrane. {ECO:0000269|PubMed:11352928,
CC       ECO:0000269|PubMed:16641373, ECO:0000269|PubMed:9409822}.
CC   -!- DISRUPTION PHENOTYPE: Sensitive to high hydrostatic pressure
CC       (mechanical stress). {ECO:0000269|PubMed:32801125}.
CC   -!- SIMILARITY: Belongs to the LST4 family. {ECO:0000305}.
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DR   EMBL; X74151; CAA52262.1; -; Genomic_DNA.
DR   EMBL; Z26878; CAA81509.1; -; Genomic_DNA.
DR   EMBL; Z28176; CAA82018.1; -; Genomic_DNA.
DR   EMBL; BK006944; DAA08990.1; -; Genomic_DNA.
DR   PIR; S34695; S34695.
DR   RefSeq; NP_012745.1; NM_001179742.1.
DR   AlphaFoldDB; P34239; -.
DR   SMR; P34239; -.
DR   BioGRID; 33962; 294.
DR   DIP; DIP-2882N; -.
DR   IntAct; P34239; 4.
DR   MINT; P34239; -.
DR   STRING; 4932.YKL176C; -.
DR   iPTMnet; P34239; -.
DR   MaxQB; P34239; -.
DR   PaxDb; P34239; -.
DR   PRIDE; P34239; -.
DR   EnsemblFungi; YKL176C_mRNA; YKL176C; YKL176C.
DR   GeneID; 853678; -.
DR   KEGG; sce:YKL176C; -.
DR   SGD; S000001659; LST4.
DR   VEuPathDB; FungiDB:YKL176C; -.
DR   eggNOG; ENOG502QPJF; Eukaryota.
DR   HOGENOM; CLU_010482_0_0_1; -.
DR   InParanoid; P34239; -.
DR   OMA; NMVVANK; -.
DR   BioCyc; YEAST:G3O-31943-MON; -.
DR   PRO; PR:P34239; -.
DR   Proteomes; UP000002311; Chromosome XI.
DR   RNAct; P34239; protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005829; C:cytosol; HDA:SGD.
DR   GO; GO:1990877; C:FNIP-folliculin RagC/D GAP; IDA:SGD.
DR   GO; GO:0005774; C:vacuolar membrane; IDA:SGD.
DR   GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR   GO; GO:0043547; P:positive regulation of GTPase activity; IDA:SGD.
DR   GO; GO:1904263; P:positive regulation of TORC1 signaling; IMP:SGD.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR037545; DENN_FNIP1/2.
DR   InterPro; IPR041153; Longin_2.
DR   Pfam; PF18639; Longin_2; 1.
DR   PROSITE; PS51836; DENN_FNIP12; 1.
PE   1: Evidence at protein level;
KW   Amino-acid transport; Phosphoprotein; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..828
FT                   /note="Protein LST4"
FT                   /id="PRO_0000203139"
FT   DOMAIN          114..302
FT                   /note="uDENN FNIP1/2-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01180"
FT   DOMAIN          310..712
FT                   /note="cDENN FNIP1/2-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01180"
FT   DOMAIN          718..825
FT                   /note="dDENN FNIP1/2-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01180"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          392..411
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          423..444
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          538..569
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         401
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   828 AA;  93359 MW;  4CE2DEA23B0A18F8 CRC64;
     MLGNLLRNKT SSSGFEKSSE HSDFSSVVPN VPVYCKAAST GTTKTAAGAL LDTAVNVEKP
     SEMLSTTSPP ILDHISDDLK LKLFGSRDIP YSRPIDTLQN NGGLGTDKIT SINEKTYAFR
     ILIIEEAGQM ACRNNYRDIF DYTTSKISNS MEQIRPSELK EYIFGSPVRS SDLTQCDKIR
     TIPNSDLVLI TRIFYYTHQY NRIAISLCIP RILLPVVAES WSSISSWLTQ TQKMLIGFLT
     KNRIMQENTG NYSNNSVIKL SNIDIRTHYP KEIEIMVQTL QKRVIPGLRS MSEIPRLFLY
     PETFKEFVHV WFKSIFNWIE IKDGPKLGFL PLLMAMIISD YRHTIRELKT SKIVILSGNM
     VVANKLLFIL SALLEPKYKG QITIRRENIR SDSSAVSRNK SNNNFVDKPE TELSTLTSTD
     NLLSRTENNS NHNYNNSNVS SNSIGSPNFH SLRKGWQIPN RRNSNTSVSV SSSESLAEVI
     QPSSFKSGSS SLHYLSSSIS SQPGSYGSWF NKRPTISQFF QPSPSLKHNE SWERLQTTAG
     NMQRTSSSSS LQQATSRLSL TTPQQSPSIS EYDEYPWMGT PGSPNVGDVS HAPPLVKNIS
     YKFPLKNVEL KRDCQRISQD DLLDEAFERI CQPSLADLNS TYEIFPGNSS YADILTTDSD
     IDDGLMNKPL ELLPKYTMYL THFNNFFQLQ ACPAGQESES RITNSMKIDL LKADYTRSLL
     VSLRSRDIRD VALKREFTGN NNNNSNQNIY DENFVGKRKY VLKQKTRKIF SCGKIGKLST
     SLENCVNFVE NSIKSAMMLY DDNGIDSELR DSEALRIFSS LVHYCNAG
 
 
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