SEC39_YEAST
ID SEC39_YEAST Reviewed; 709 AA.
AC Q12745; D6VZ75; Q7LHI0;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Protein transport protein SEC39;
DE AltName: Full=Dependent on SLY1-20 protein 3;
GN Name=SEC39 {ECO:0000312|EMBL:AAB67520.1}; Synonyms=DSL3;
GN OrderedLocusNames=YLR440C;
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] {ECO:0000312|EMBL:AAB67520.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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] {ECO:0000305, ECO:0000312|EMBL:CAA83058.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 548-709.
RC STRAIN=07173 {ECO:0000312|EMBL:CAA83058.1};
RX PubMed=7828914; DOI=10.1016/0378-1119(94)00633-4;
RA Graack H.-R., Grohmann L., Kitakawa M., Goldschmidt-Reisin S.;
RT "Gene MRP-L4, encoding mitochondrial ribosomal protein YmL4, is
RT indispensable for proper non-respiratory cell functions in yeast.";
RL Gene 152:107-112(1995).
RN [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=15242642; DOI=10.1016/j.cell.2004.06.013;
RA Mnaimneh S., Davierwala A.P., Haynes J., Moffat J., Peng W.-T., Zhang W.,
RA Yang X., Pootoolal J., Chua G., Lopez A., Trochesset M., Morse D.,
RA Krogan N.J., Hiley S.L., Li Z., Morris Q., Grigull J., Mitsakakis N.,
RA Roberts C.J., Greenblatt J.F., Boone C., Kaiser C.A., Andrews B.J.,
RA Hughes T.R.;
RT "Exploration of essential gene functions via titratable promoter alleles.";
RL Cell 118:31-44(2004).
RN [5] {ECO:0000305}
RP INTERACTION WITH TIP20.
RX PubMed=15942868; DOI=10.2323/jgam.51.73;
RA Ishikawa T., Unno K., Nonaka G., Nakajima H., Kitamoto K.;
RT "Isolation of Saccharomyces cerevisiae RNase T1 hypersensitive (rns)
RT mutants and genetic analysis of the RNS1/DSL1 gene.";
RL J. Gen. Appl. Microbiol. 51:73-82(2005).
RN [6] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH DSL1; TIP20; SEC20; USE1 AND
RP UFE1, AND SUBCELLULAR LOCATION.
RX PubMed=15958492; DOI=10.1091/mbc.e05-01-0056;
RA Kraynack B.A., Chan A., Rosenthal E., Essid M., Umansky B., Waters M.G.,
RA Schmitt H.D.;
RT "Dsl1p, Tip20p, and the novel Dsl3(Sec39) protein are required for the
RT stability of the Q/t-SNARE complex at the endoplasmic reticulum in yeast.";
RL Mol. Biol. Cell 16:3963-3977(2005).
RN [7] {ECO:0000305}
RP IDENTIFICATION IN A COMPLEX WITH DSL1; TIP20; SEC20; UFE1; USE1 AND SEC22.
RX PubMed=16429126; DOI=10.1038/nature04532;
RA Gavin A.-C., Aloy P., Grandi P., Krause R., Boesche M., Marzioch M.,
RA Rau C., Jensen L.J., Bastuck S., Duempelfeld B., Edelmann A.,
RA Heurtier M.-A., Hoffman V., Hoefert C., Klein K., Hudak M., Michon A.-M.,
RA Schelder M., Schirle M., Remor M., Rudi T., Hooper S., Bauer A.,
RA Bouwmeester T., Casari G., Drewes G., Neubauer G., Rick J.M., Kuster B.,
RA Bork P., Russell R.B., Superti-Furga G.;
RT "Proteome survey reveals modularity of the yeast cell machinery.";
RL Nature 440:631-636(2006).
CC -!- FUNCTION: Required for protein transport between the Golgi and the
CC endoplasmic reticulum. May contribute to tethering of coatomer-coated
CC retrograde transport vesicles to the ER membrane through interaction
CC with and stabilization of the SNARE complex.
CC {ECO:0000269|PubMed:15242642, ECO:0000269|PubMed:15958492}.
CC -!- SUBUNIT: Component of a peripheral membrane protein complex consisting
CC of DSL1, SEC39/DSL3 and TIP20. Bound to a SNARE complex consisting of
CC UFE1, USE1, SEC20 and SEC22 or YKT6 through direct interaction of TIP20
CC with SEC20. Interacts with TIP20 and DSL1.
CC {ECO:0000269|PubMed:15942868, ECO:0000269|PubMed:15958492,
CC ECO:0000269|PubMed:16429126}.
CC -!- INTERACTION:
CC Q12745; P53847: DSL1; NbExp=14; IntAct=EBI-31898, EBI-29249;
CC Q12745; P33891: TIP20; NbExp=4; IntAct=EBI-31898, EBI-19396;
CC Q12745; P53146: USE1; NbExp=4; IntAct=EBI-31898, EBI-23881;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:15958492}; Peripheral membrane protein
CC {ECO:0000269|PubMed:15958492}.
CC -!- MISCELLANEOUS: Cells with a reduced level of SEC39 show a defect in
CC post-translational processing of PRC1/CPY.
CC -!- SIMILARITY: Belongs to the SEC39 family. {ECO:0000305}.
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DR EMBL; U21094; AAB67520.1; -; Genomic_DNA.
DR EMBL; Z30582; CAA83058.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09741.1; -; Genomic_DNA.
DR PIR; S59408; S59408.
DR RefSeq; NP_013545.3; NM_001182328.3.
DR PDB; 3K8P; X-ray; 2.60 A; D=1-709.
DR PDBsum; 3K8P; -.
DR AlphaFoldDB; Q12745; -.
DR SMR; Q12745; -.
DR BioGRID; 31699; 381.
DR ComplexPortal; CPX-1786; Dsl1 tethering complex.
DR DIP; DIP-941N; -.
DR IntAct; Q12745; 16.
DR STRING; 4932.YLR440C; -.
DR MaxQB; Q12745; -.
DR PaxDb; Q12745; -.
DR PRIDE; Q12745; -.
DR EnsemblFungi; YLR440C_mRNA; YLR440C; YLR440C.
DR GeneID; 851161; -.
DR KEGG; sce:YLR440C; -.
DR SGD; S000004432; SEC39.
DR VEuPathDB; FungiDB:YLR440C; -.
DR eggNOG; ENOG502RS0W; Eukaryota.
DR HOGENOM; CLU_389403_0_0_1; -.
DR InParanoid; Q12745; -.
DR OMA; WPELDDP; -.
DR BioCyc; YEAST:G3O-32496-MON; -.
DR EvolutionaryTrace; Q12745; -.
DR PRO; PR:Q12745; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q12745; protein.
DR GO; GO:0070939; C:Dsl1/NZR complex; IDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0005635; C:nuclear envelope; IDA:SGD.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0032581; P:ER-dependent peroxisome organization; IMP:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IDA:ComplexPortal.
DR GO; GO:0016192; P:vesicle-mediated transport; IMP:SGD.
DR InterPro; IPR013244; Sec39_domain.
DR Pfam; PF08314; Sec39; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endoplasmic reticulum; ER-Golgi transport; Membrane;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..709
FT /note="Protein transport protein SEC39"
FT /id="PRO_0000234109"
FT HELIX 33..42
FT /evidence="ECO:0007829|PDB:3K8P"
FT HELIX 49..53
FT /evidence="ECO:0007829|PDB:3K8P"
FT HELIX 54..60
FT /evidence="ECO:0007829|PDB:3K8P"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:3K8P"
FT HELIX 105..111
FT /evidence="ECO:0007829|PDB:3K8P"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:3K8P"
FT HELIX 120..132
FT /evidence="ECO:0007829|PDB:3K8P"
FT TURN 139..142
FT /evidence="ECO:0007829|PDB:3K8P"
FT HELIX 143..147
FT /evidence="ECO:0007829|PDB:3K8P"
FT HELIX 156..164
FT /evidence="ECO:0007829|PDB:3K8P"
FT HELIX 166..175
FT /evidence="ECO:0007829|PDB:3K8P"
FT HELIX 182..187
FT /evidence="ECO:0007829|PDB:3K8P"
FT HELIX 190..197
FT /evidence="ECO:0007829|PDB:3K8P"
FT HELIX 212..216
FT /evidence="ECO:0007829|PDB:3K8P"
FT HELIX 218..225
FT /evidence="ECO:0007829|PDB:3K8P"
FT HELIX 228..235
FT /evidence="ECO:0007829|PDB:3K8P"
FT TURN 238..240
FT /evidence="ECO:0007829|PDB:3K8P"
FT HELIX 246..261
FT /evidence="ECO:0007829|PDB:3K8P"
FT HELIX 270..289
FT /evidence="ECO:0007829|PDB:3K8P"
FT HELIX 294..305
FT /evidence="ECO:0007829|PDB:3K8P"
FT STRAND 310..314
FT /evidence="ECO:0007829|PDB:3K8P"
FT TURN 315..317
FT /evidence="ECO:0007829|PDB:3K8P"
FT STRAND 318..321
FT /evidence="ECO:0007829|PDB:3K8P"
FT HELIX 322..334
FT /evidence="ECO:0007829|PDB:3K8P"
FT HELIX 341..348
FT /evidence="ECO:0007829|PDB:3K8P"
FT HELIX 352..367
FT /evidence="ECO:0007829|PDB:3K8P"
FT HELIX 373..382
FT /evidence="ECO:0007829|PDB:3K8P"
FT TURN 383..385
FT /evidence="ECO:0007829|PDB:3K8P"
FT STRAND 392..394
FT /evidence="ECO:0007829|PDB:3K8P"
FT HELIX 399..412
FT /evidence="ECO:0007829|PDB:3K8P"
FT HELIX 416..425
FT /evidence="ECO:0007829|PDB:3K8P"
FT HELIX 432..448
FT /evidence="ECO:0007829|PDB:3K8P"
FT HELIX 457..477
FT /evidence="ECO:0007829|PDB:3K8P"
FT HELIX 479..494
FT /evidence="ECO:0007829|PDB:3K8P"
FT HELIX 515..520
FT /evidence="ECO:0007829|PDB:3K8P"
FT TURN 521..523
FT /evidence="ECO:0007829|PDB:3K8P"
FT HELIX 526..535
FT /evidence="ECO:0007829|PDB:3K8P"
FT HELIX 539..541
FT /evidence="ECO:0007829|PDB:3K8P"
FT HELIX 543..556
FT /evidence="ECO:0007829|PDB:3K8P"
FT HELIX 565..582
FT /evidence="ECO:0007829|PDB:3K8P"
FT HELIX 586..603
FT /evidence="ECO:0007829|PDB:3K8P"
FT HELIX 605..624
FT /evidence="ECO:0007829|PDB:3K8P"
FT HELIX 631..633
FT /evidence="ECO:0007829|PDB:3K8P"
FT HELIX 637..653
FT /evidence="ECO:0007829|PDB:3K8P"
FT HELIX 656..658
FT /evidence="ECO:0007829|PDB:3K8P"
FT HELIX 659..673
FT /evidence="ECO:0007829|PDB:3K8P"
SQ SEQUENCE 709 AA; 82396 MW; 8ABD59328A006863 CRC64;
MLEEQLYLLA CIFASRADTR NIKKLSTRLG SQSKYLEILC VLWPELDDPK NLLFLRELEE
EVQSPEGEET TDEDVIVELL ESDSSLIPLI ESDTTTRSNR YHELQEFISK KLNNKTLENF
EEWLRERILI CNEMIPETPL LYSVLWETAK SKVLSTKFIG WVEGVLKPLD HLNKRLHLIF
KINEWEKMPD SELFKIIFDG VEDMQGYIGI ADVIEDELAP TLSYGKKWET FITEFFNKQQ
FSLKSDTNYQ LFIKLYYSLE KGVKDNSEAS RKLQSNVVDI LFHNSENLFN LSSLTHKLDE
LWSILSGFPD EITIEEQKTI TALEMKQFME FFIKCSTKFS FKEIFAITQE EESAQLAHFS
SLCHEEFNKA NEISSFLQAM YETVLDISKD DKIFTRISMD EKLYSILEIL LQMNEFAYIE
AIIERFDYSN NTQIYELLVK FFWHFFNNAS NGLRKEPEMK KASQTLQIIQ KHMSQRAGTN
LTKLEVLLEI SDKLSHYSIN LNKSHNGARD TAFKPSNILE YRDCPLDIIS NLLELNPRLY
KDLPTTKSLL FGIYDSLSIN REGQTGKVEV DLMVLHIDYA LVNLDFGTAY ELGKQVFEIC
QEAGQHMMKA LGDEHWLTFY QMGKFVDPNW VDNEIPTEII VLQMSILGRL LEVCPLEEVE
IVTSQWSTLE LELSARDLVK DKYALDGQND NKSKVGGIAR EIFHNVTNF
