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TMN2_YEAST
ID   TMN2_YEAST              Reviewed;         672 AA.
AC   Q04562; D6VS93;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Transmembrane 9 superfamily member 2;
DE   Flags: Precursor;
GN   Name=TMN2; OrderedLocusNames=YDR107C;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [2]
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   [3]
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   [4]
RP   FUNCTION.
RX   PubMed=18178563; DOI=10.1074/jbc.m704484200;
RA   Froquet R., Cherix N., Birke R., Benghezal M., Cameroni E., Letourneur F.,
RA   Moesch H.-U., De Virgilio C., Cosson P.;
RT   "Control of cellular physiology by TM9 proteins in yeast and
RT   Dictyostelium.";
RL   J. Biol. Chem. 283:6764-6772(2008).
RN   [5]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=20681974; DOI=10.1111/j.1399-3054.2010.01404.x;
RA   Hegelund J.N., Jahn T.P., Baekgaard L., Palmgren M.G., Schjoerring J.K.;
RT   "Transmembrane nine proteins in yeast and Arabidopsis affect cellular metal
RT   contents without changing vacuolar morphology.";
RL   Physiol. Plantarum 140:355-367(2010).
CC   -!- FUNCTION: With EMP70 and TMN3, plays a critical role in the late stages
CC       of a nutrient-controlled pathway notably regulating FLO11 gene
CC       expression. Acts downstream of RAS2 and TOR. Essential for cell
CC       adhesion and filamentous growth. May play a role as effector of
CC       cellular copper homeostasis. {ECO:0000269|PubMed:18178563,
CC       ECO:0000269|PubMed:20681974}.
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the nonaspanin (TM9SF) (TC 9.A.2) family.
CC       {ECO:0000305}.
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DR   EMBL; Z48758; CAA88661.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA11953.1; -; Genomic_DNA.
DR   PIR; S52673; S52673.
DR   RefSeq; NP_010392.1; NM_001180415.1.
DR   AlphaFoldDB; Q04562; -.
DR   BioGRID; 32165; 55.
DR   DIP; DIP-4247N; -.
DR   IntAct; Q04562; 3.
DR   MINT; Q04562; -.
DR   STRING; 4932.YDR107C; -.
DR   iPTMnet; Q04562; -.
DR   MaxQB; Q04562; -.
DR   PaxDb; Q04562; -.
DR   PRIDE; Q04562; -.
DR   EnsemblFungi; YDR107C_mRNA; YDR107C; YDR107C.
DR   GeneID; 851685; -.
DR   KEGG; sce:YDR107C; -.
DR   SGD; S000002514; TMN2.
DR   VEuPathDB; FungiDB:YDR107C; -.
DR   eggNOG; KOG1278; Eukaryota.
DR   GeneTree; ENSGT00940000172441; -.
DR   HOGENOM; CLU_010714_4_1_1; -.
DR   InParanoid; Q04562; -.
DR   OMA; CYPKNGT; -.
DR   BioCyc; YEAST:G3O-29709-MON; -.
DR   PRO; PR:Q04562; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; Q04562; protein.
DR   GO; GO:0005768; C:endosome; IBA:GO_Central.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0006878; P:cellular copper ion homeostasis; IDA:UniProtKB.
DR   GO; GO:0001403; P:invasive growth in response to glucose limitation; IMP:SGD.
DR   GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0072657; P:protein localization to membrane; IBA:GO_Central.
DR   GO; GO:0007124; P:pseudohyphal growth; IGI:SGD.
DR   GO; GO:0007034; P:vacuolar transport; IGI:SGD.
DR   InterPro; IPR004240; EMP70.
DR   PANTHER; PTHR10766; PTHR10766; 1.
DR   Pfam; PF02990; EMP70; 1.
PE   1: Evidence at protein level;
KW   Ion transport; Membrane; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix; Transport; Vacuole.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..672
FT                   /note="Transmembrane 9 superfamily member 2"
FT                   /id="PRO_0000244444"
FT   TOPO_DOM        19..307
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        308..328
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        329..383
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        384..404
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        405..410
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        411..431
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        432..447
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        448..468
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        469..479
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        480..500
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        501..532
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        533..553
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        554..565
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        566..586
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        587..601
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        602..622
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        623..628
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        629..649
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        650..672
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   672 AA;  76347 MW;  172855FA4B29BA13 CRC64;
     MKRGVWLLIY CYATLTKGFS LPGLSPTTYH SGDEIPLLVN RLTPSIYFQH QDEEGNDVSG
     DKEHFLYSYD YYNKRFHFCR PEHVEKQPES LGSVIFGDRI YNSPFQLNML EEKECVALCK
     STIPGKDAKF INTLIKSGFF QNWLVDGLPA ARKAYDSRTK TNYYGTGFEL GFTDVKQTVD
     GKAVPSTMEE LTSEASNEDV ILDARLPKNV KPNLVKTVEL PYFVNHFDIE VEFHDRGNDN
     YRVVGVIVNP VSIERSSPGA CSTTGKPLIL DEDKDNEVYF TYSVKFVASD TVWATRWDKY
     LHIYDPQIQW FSLINFSVIV ILLSSVVMHS LLRALKSDLA RYNELNLDNE FHEDSGWKLG
     HGDVFRTPSK SMLLSILVGS GMQLFLMVMC SIFFAAVGLV SPVSRGSLPT VMFVLYALFG
     FVGSYASMGV YKFFRGPYWK ANMILTPILL PGAIFLLIVI MNFFLLFAHS SGVIPARSLF
     FIILLWFLVS VPLSFAGSIV AHKQCNWDEH PTKTNQIARQ IPYQPWYLRT AQATLIAGIF
     SFGSIAVELY FIYSSLWFNK IFYMFGFLLF SFLLLTLTTS LVTILITYYS LCLENWLWQW
     RSFIIGGLGC SIYTFIHSIL FTKFKLGGVI TVVLYLGYSL IISALCCVVT GAIGFFSSMF
     FIRKIYSAIK VE
 
 
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