DFM1_YEAST
ID DFM1_YEAST Reviewed; 341 AA.
AC Q12743; D6VT43; Q7LIJ5;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=DER1-like family member protein 1;
GN Name=DFM1; OrderedLocusNames=YDR411C; ORFNames=D9461.2;
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 NUCLEOTIDE SEQUENCE OF 233-341.
RC STRAIN=JRY3205;
RX PubMed=8212897; DOI=10.1002/yea.320090810;
RA Ashby M.N., Errada P.R., Boyartchuk V.L., Rine J.;
RT "Isolation and DNA sequence of the STE14 gene encoding farnesyl cysteine:
RT carboxyl methyltransferase.";
RL Yeast 9:907-913(1993).
RN [4]
RP INDUCTION.
RX PubMed=10847680; DOI=10.1016/s0092-8674(00)80835-1;
RA Travers K.J., Patil C.K., Wodicka L., Lockhart D.J., Weissman J.S.,
RA Walter P.;
RT "Functional and genomic analyses reveal an essential coordination between
RT the unfolded protein response and ER-associated degradation.";
RL Cell 101:249-258(2000).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND MEMBRANE TOPOLOGY.
RX PubMed=15093775; DOI=10.1016/j.femsyr.2004.02.003;
RA Hitt R., Wolf D.H.;
RT "Der1p, a protein required for degradation of malfolded soluble proteins of
RT the endoplasmic reticulum: topology and Der1-like proteins.";
RL FEMS Yeast Res. 4:721-729(2004).
RN [6]
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 [7]
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: May be involved in the degradation process of some misfolded
CC endoplasmic reticulum (ER) luminal proteins. Its precise role is
CC however unclear and its inability to complement der1 mutations,
CC suggests either that it is not involved in degradation process of
CC misfolded proteins, or that it participates in the destruction of
CC specific misfolded ER luminal proteins. {ECO:0000269|PubMed:15093775}.
CC -!- INTERACTION:
CC Q12743; P34223: SHP1; NbExp=2; IntAct=EBI-33192, EBI-17093;
CC Q12743; P38349: UBX7; NbExp=3; IntAct=EBI-33192, EBI-21157;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15093775}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:15093775}.
CC -!- INDUCTION: By endoplasmic reticulum stress.
CC {ECO:0000269|PubMed:10847680}.
CC -!- SIMILARITY: Belongs to the derlin family. {ECO:0000305}.
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DR EMBL; U33007; AAB64889.1; -; Genomic_DNA.
DR EMBL; L07952; AAA16518.1; -; Unassigned_DNA.
DR EMBL; BK006938; DAA12253.1; -; Genomic_DNA.
DR PIR; S69696; S69696.
DR RefSeq; NP_010699.1; NM_001180719.1.
DR AlphaFoldDB; Q12743; -.
DR BioGRID; 32471; 87.
DR IntAct; Q12743; 15.
DR MINT; Q12743; -.
DR STRING; 4932.YDR411C; -.
DR TCDB; 3.A.16.1.2; the endoplasmic reticular retrotranslocon (er-rt) family.
DR iPTMnet; Q12743; -.
DR PaxDb; Q12743; -.
DR PRIDE; Q12743; -.
DR EnsemblFungi; YDR411C_mRNA; YDR411C; YDR411C.
DR GeneID; 852020; -.
DR KEGG; sce:YDR411C; -.
DR SGD; S000002819; DFM1.
DR VEuPathDB; FungiDB:YDR411C; -.
DR eggNOG; KOG0858; Eukaryota.
DR GeneTree; ENSGT00530000063156; -.
DR HOGENOM; CLU_059047_0_0_1; -.
DR InParanoid; Q12743; -.
DR OMA; YLPWAFL; -.
DR BioCyc; YEAST:G3O-29954-MON; -.
DR PRO; PR:Q12743; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q12743; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0000839; C:Hrd1p ubiquitin ligase ERAD-L complex; IBA:GO_Central.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:SGD.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IMP:SGD.
DR GO; GO:1904152; P:regulation of retrograde protein transport, ER to cytosol; IMP:SGD.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:SGD.
DR InterPro; IPR007599; DER1.
DR InterPro; IPR035952; Rhomboid-like_sf.
DR Pfam; PF04511; DER1; 1.
DR SUPFAM; SSF144091; SSF144091; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Membrane; Reference proteome; Stress response;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..341
FT /note="DER1-like family member protein 1"
FT /id="PRO_0000219054"
FT TOPO_DOM 1..41
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..122
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 144..170
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 214..341
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 276..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 341 AA; 38131 MW; 771CD4C0947FBD89 CRC64;
MAGPRNVRTL HGNGGRNNDV MGPKEFWLNI PPITRTLFTL AIVMTIVGRL NLINPWYFIY
VWNLTFKKVQ IWRLLTSCVM LSSRAMPALM ELYSIYDRSS QLERGHFGPG LSNRRGPMVT
VDYAYYLCFC ILAITTATTI IYGSYYPVVL TSGFISCITY TWSIDNANVQ IMFYGLIPVW
GKYFPLIQLF ISFVFNEGDF VISLIGFTTG YLYTCLDTHT LGPIWGMISR KADPTYGISP
NGKFSTPWWF TSLYARITGA HNETATFNNN FANVPSSQRE TRTFSGRGQR LGTAPATLSQ
TSGTDSGRAS GSQLRSGPSN LNQFQGRGQR VGQTNSPSDS Q
